HMS Dataset ID,Dataset Title,Publication(s) Using Dataset,Project Summary Page(s),Assay Description,Assay Protocol Reference,HMS Dataset Type,Usage Message,Date Publicly Available,Most Recent Update
20000,Target Affinity Spectrum (TAS) vectors for compounds in the HMS LINCS small molecule library.,,,"The target affinity spectrum (TAS) is a vector of binding assertions based on dose-response affinity constants, one-dose percent inhibition data and manual literature curation.","Moret, N., Clark, N., Hafner, M., Wang, Y., Lounkine, E., Medvedovic, M., Wang, J., Gray, N., Jenkins, J., and Sorger, P. (2019). Cheminformatics tools for analyzing and designing optimized small molecule libraries. CellChemBio. In press.",Analysis,The original dataset #20000 (LINCS Compound Protein Targets and Concentrations) with kinase inhibitor target information has been replaced with Target Affinity Spectrum binding information for small molecules in the HMS-LINCS database (March 2019).,2019-03-29,2019-03-29
20001,Moerke 2 Color Apoptosis,,"lincs.hms.harvard.edu/tang-jbiomolscreen-2013","Moerke 2 Color Apoptosis: IA-LM, IST-MEL1, NCI-H1648, PC-9 and SK-LMS-1 cells. Dose response of anti-mitotic compounds in human cancer cell lines at 24, 48, and 72 hours to determine their effects on apoptosis. In this assay, the cell-permeable DNA dye Hoechst 33342 is used to stain the nuclei of all cells. The fluorescent caspase 3 reporter NucView488 stains the nuclei of cells undergoing apoptosis (in which caspase 3 is active).","Cen H, Mao F, Aronchik I, Fuentes RJ, Firestone GL. DEVD-NucView488: a novel class of enzyme substrates for real-time detection of caspase-3 activity in live cells. FASEB J. 2008 Jul;22(7):2243-52.
http://www.biotium.com/product/applications/Cell_Biology/price_and_info.asp?item=30029&layer1=A;&layer2=A02;&layer3=A0203;",Microscopy/Imaging,,2011-07-15,2016-07-12
20002,Moerke 3 Color Apoptosis,,"lincs.hms.harvard.edu/tang-jbiomolscreen-2013","Moerke 3 Color Apoptosis: Dose response of anti-mitotic compounds in human cancer cell lines at 24 and 48 hours to determine their effects on apoptosis and cell death. In this assay, the cell-permeable DNA dye Hoechst 33342 is used to stain the nuclei of all cells. The fluorescent caspase 3 reporter NucView488 stains the nuclei of cells undergoing apoptosis (in which caspase 3 is active), and the cell-impermeable DNA dye TO-PRO3 stains only the nuclei of dead or dying cells in which membrane integrity is compromised.","Cen H, Mao F, Aronchik I, Fuentes RJ, Firestone GL. DEVD-NucView488: a novel class of enzyme substrates for real-time detection of caspase-3 activity in live cells. FASEB J. 2008 Jul;22(7):2243-52.
http://www.biotium.com/product/applications/Cell_Biology/price_and_info.asp?item=30029&layer1=A;&layer2=A02;&layer3=A0203;",Microscopy/Imaging,,2011-07-15,2016-07-12
20003,Tang Mitosis/Apoptosis ver. II,"PMID: 23788527","lincs.hms.harvard.edu/tang-jbiomolscreen-2013","Tang Mitosis/Apoptosis ver.II: Dose response of anti-mitotic compounds in human cancer cell lines at 24, 48 and 72 hours to determine effect on apoptosis, mitosis and cell death.
In screening for small-molecule compounds that are effective at killing cancer cells, one-dimensional readout GI50, which is the EC50 value of growth inhibition, is usually used as the only criterion. A major problem with this one-readout approach is that other useful information is discarded, which could be critical for understanding the action of the compounds. In this screen, we use a single-cell-based imaging assay that can report multi-dimensional physiological responses in cells treated with small molecule kinase inhibitors. The data in this dataset are described in PMID: 23788527: Differential Determinants of Cancer Cell Insensitivity to Antimitotic Drugs Discriminated by a One-Step Cell Imaging Assay (J. Biomolecular Screening, 2013). The image analysis algorithm is available at https://github.com/xietiao/Tang_et_al_LINCS_cell_scoring.","Protocols and data are published in Tang Y, Xie T, Florian S, Moerke N, Shamu C, Benes C, Mitchison TJ. Differential Determinants of Cancer Cell Insensitivity to Antimitotic Drugs Discriminated by a One-Step Cell Imaging Assay. J Biomol Screen. 2013 Jun 20. PMID: 23788527.
Image analysis algorithm (MATLAB code) is available at https://github.com/xietiao/Tang_et_al_LINCS_cell_scoring
Reference for NucView:
Cen H, Mao F, Aronchik I, Fuentes RJ, Firestone GL. DEVD-NucView488: a novel class of enzyme substrates for real-time detection of caspase-3 activity in live cells. FASEB J. 2008 Jul;22(7):2243-52.",Microscopy/Imaging,,2011-07-15,2016-07-12
20004,Tang Proliferation/Mitosis,,"lincs.hms.harvard.edu/tang-jbiomolscreen-2013","Tang Proliferation/Mitosis: Dose response of anti-mitotic compounds in human cancer cell lines at 24, 48 and 72 hours to determine effect on cell proliferation and mitosis.","Reference for EdU labeling:
Salic A, Mitchison TJ. A chemical method for fast and sensitive detection of DNA synthesis in vivo. Proc Natl Acad Sci USA. 2008 Feb 19;105(7):2415-20.",Microscopy/Imaging,,2011-10-11,2016-08-24
20020,Sorafenib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-09-25
20021,HG-6-64-1 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20022,GW-5074 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20023,SB590885 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20024,PLX-4720 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20025,AZ-628 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20026,PLX4032 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20027,AZD7762 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20028,CP466722 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20029,CP724714 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20030,GSK429286A KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20031,GSK461364 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20032,GW843682 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20033,PF02341066 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20034,BMS345541 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20035,AS601245 KINOMEscan,,,"The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,"The data for this assay have been removed permanently. Other information about this dataset have been left in this database for the record, instead of deleting the dataset entirely (April 2015).",2011-07-15,2018-03-27
20036,WH-4-023 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20037,BX-912 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20038,AZD-6482 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20039,TAK-715 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20040,NU7441 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20041,KIN001-220 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20042,MLN8054 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20043,AZD1152-HQPA KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20044,PD0332991 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20045,THZ-2-98-01 KINOMEscan,,,"The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,"The data for this assay have been removed permanently. Other information about this dataset have been left in this database for the record, instead of deleting the dataset entirely (April 2015).",2011-07-15,2018-03-27
20046,JWE-035 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20047,ZM-447439 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20048,JNK-9L KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-07-15,2015-10-06
20049,ALW-II-38-3 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2016-03-03
20050,ALW-II-49-7 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2016-03-03
20051,HG-5-113-01 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20052,HG-5-88-01 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20053,HKI-272 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20054,CGP60474 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20055,PD173074 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20056,WH-4-025 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20057,BI-2536 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20058,KIN001-127 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20059,A443654 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20060,GDC-0941 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20061,NPK76-II-72-1 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20062,QL-X-138 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20063,QL-XI-92 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20064,Torin1 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20065,Torin2 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20066,WZ-4-145 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20067,WZ-7043 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,LCMS has shown evidence of significant degradation of original compound (March 2015),2011-11-21,2015-10-06
20068,WZ3105 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20069,WZ4002 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20070,XMD11-50 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20071,XMD11-85h KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20072,XMD13-2 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20073,XMD14-99 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20074,XMD15-27 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20075,XMD16-144 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20076,XMD8-85 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20077,XMD8-92 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20078,ZG-10 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2011-11-21,2015-10-06
20079,WYE-125132 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2012-04-30,2015-10-06
20080,PD0325901 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2012-04-30,2015-10-06
20081,JNK-IN-5A KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2012-04-30,2015-10-06
20082,CYT387 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2012-08-10,2015-10-06
20083,Sigma A6730 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2012-08-10,2015-10-06
20084,GSK2126458 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2012-08-10,2015-10-06
20085,GSK1059615 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2012-08-10,2015-10-06
20086,AG1478 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2012-08-10,2015-10-06
20087,Sorafenib KiNativ -- dose response experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2011-07-15,2016-09-09
20088,GW-5074 KiNativ -- dose response experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2011-07-15,2016-09-09
20089,SB590885 KiNativ -- dose response experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2011-07-15,2016-09-09
20090,PLX-4720 KiNativ -- dose response experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2011-07-15,2016-09-09
20091,AZ-628 KiNativ -- dose response experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2011-07-15,2016-09-09
20092,PLX4032 KiNativ -- dose response experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2011-07-15,2016-09-09
20093,HG-6-64-01 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2012-05-09,2016-09-09
20094,Torin1 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2012-05-09,2016-09-09
20095,Torin2 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2012-05-09,2016-09-09
20096,BEZ235 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-01-11,2015-10-06
20097,XMD11-50 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20098,XMD11-85h KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20099,XMD16-144 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20100,JWE-035 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20101,XMD8-85 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20102,XMD8-92 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20103,XMD-12 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20104,NVP-BHG712 KiNativ -- multiple dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20105,CH5424802 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20106,NPK76-II-72-1 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP or ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2013-01-10,2016-09-09
20107,Lapatinib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-02-08,2015-10-06
20108,JW-7-24-1 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20109,NVP-TAE684 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20110,R406 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20111,SP600125 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20112,BMS-536924 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20113,A770041 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20114,CG-930 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20115,XMD-12 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20116,Bosutinib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,"The data for this assay have been removed permanently. Other information about this dataset have been left in this database for the record, instead of deleting the dataset entirely (June 2016).",2013-04-01,2018-03-27
20117,KU63794 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20118,CI-1033 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20119,WZ-1-84 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-04-01,2015-10-06
20120,Metrics other than potency reveal systematic variation in responses to cancer drugs,"PMID: 24013279","lincs.hms.harvard.edu/fallahi-sichani-nchembio-2013","The following is the abstract from Fallahi-Sichani et al. (2013) Nature Chemical Biology: Large-scale analysis of cellular response to anticancer drugs typically focuses on variation in potency (half-maximum inhibitory concentration, (IC50)), assuming that it is the most important difference between effective and ineffective drugs or sensitive and resistant cells. We took a multiparametric approach involving analysis of the slope of the dose-response curve, the area under the curve and the maximum effect (Emax). We found that some of these parameters vary systematically with cell line and others with drug class. For cell-cycle inhibitors, Emax often but not always correlated with cell proliferation rate. For drugs targeting the Akt/PI3K/mTOR pathway, dose-response curves were unusually shallow. Classical pharmacology has no ready explanation for this phenomenon, but single-cell analysis showed that it correlated with significant and heritable cell-to-cell variability in the extent of target inhibition. We conclude that parameters other than potency should be considered in the comparative analysis of drug response, particularly at clinically relevant concentrations near and above the IC50.
Heiser LM, Sadanandam A, Kuo WL, Benz SC, Goldstein TC, Ng S, Gibb WJ, Wang NJ, Ziyad S, Tong F, Bayani N, Hu Z, Billig JI, Dueregger A, Lewis S, Jakkula L, Korkola JE, Durinck S, Pepin F, Guan Y, Purdom E, Neuvial P, Bengtsson H, Wood KW, Smith PG, Vassilev LT, Hennessy BT, Greshock J, Bachman KE, Hardwicke MA, Park JW, Marton LJ, Wolf DM, Collisson EA, Neve RM, Mills GB, Speed TP, Feiler HS, Wooster RF, Haussler D, Stuart JM, Gray JW, Spellman PT. Subtype and pathway specific responses to anticancer compounds in breast cancer. Proc Natl Acad Sci U S A. 2012 Feb 21;109(8):2724-9. PMID: 22003129",Analysis,,2013-08-01,2016-08-24
20121,A549 cells -- High-throughput Secretomic Analysis of Single Cells,"PMID: 23339603",,This micro-fluidics assay is performed using a microchip developed by the Yale LINCS U01 team. This microchip consists of a PDMS microwell array containing >5000 single-cell trapping chambers and a high-density antibody barcode array fabricated by Yale LINCS’ flow patterning method. The assay does not require external fluid handling equipment and can be performed anywhere in a typical cell biology lab.,,Microfluidics,,2013-06-10,2016-08-24
20122,U87 cells -- High-throughput Secretomic Analysis of Single Cells,"PMID: 23339603",,This micro-fluidics assay is performed using a microchip developed by the Yale LINCS U01 team. This microchip consists of a PDMS microwell array containing >5000 single-cell trapping chambers and a high-density antibody barcode array fabricated by Yale LINCS’ flow patterning method. The assay does not require external fluid handling equipment and can be performed anywhere in a typical cell biology lab.,,Microfluidics,,2013-06-10,2016-08-24
20123,U937 cells -- High-throughput Secretomic Analysis of Single Cells,"PMID: 23339603",,This micro-fluidics assay is performed using a microchip developed by the Yale LINCS U01 team. This microchip consists of a PDMS microwell array containing >5000 single-cell trapping chambers and a high-density antibody barcode array fabricated by Yale LINCS’ flow patterning method. The assay does not require external fluid handling equipment and can be performed anywhere in a typical cell biology lab.,,Microfluidics,,2013-06-10,2016-08-24
20124,(R)-Roscovitine KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20125,PHA-793887 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20126,PHA-767491 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20127,BS-181 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20128,Dinaciclib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20129,AZD4547 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20130,OTSSP167 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20131,Dabrafenib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20132,HG-9-91-01 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20133,HG-14-8-02 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20134,HG-14-10-04 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20135,AZD 5438 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-07-08,2015-10-06
20136,Breast cell line dose response to target inhibition measured by high throughput microscopy,"PMID: 24013279","lincs.hms.harvard.edu/fallahi-sichani-nchembio-2013","To investigate how a shallow dose-response curve might arise (as seen in data analyzed in Fallahi-Sichani et al. (2013) Nature Chemical Biology. PMID: 24013279), this assay focuses on drugs inhibiting the PI3K/Akt/mTOR pathway that varied widely in Hill slope (HS) and Emax values independent of proliferation rate. For six compounds with varying HS, target inhibition was measured by immunofluorescence microscopy and cell killing in four breast cell lines (HER2-amplified AU565 and HCC1954 cancer cells, hormone receptor-positive T47D cancer cells, and non-transformed MCF10A cells). The effects of the mTOR inhibitor PP242, PI3K inhibitor GSK1059615, dual specificity mTOR/PI3K inhibitor dactolisib (BEZ235), Akt inhibitors MK2206 and triciribine, and also an EGFR inhibitor gefitinib were probed 6 hr and 24 hr after drug exposure in 9-point dose-response assays using antibodies specific for p-ERK (Thr202/Tyr204), p-Akt (Ser473), p-4EBP1 (Thr37/46), and p-S6 (Ser235/236). A shallow dose-response curve is correlated with high cell-to-cell variability in target (p-4EBP1) inhibition by PP242 and dactolisib as compared to drugs for which HS ~ 1 or HS > 1 (in four of four cell lines tested). This dataset refers to data shown in Figure 5 and Supplementary Figures 5, 7, 8 and 9 of the paper.","Fallahi-Sichani M, Honarnejad, S Heiser, LM, Gray JW and Sorger PK. Metrics other than potency reveal systematic variation in responses to cancer drugs. Nature Chemical Biology, 2013. doi:10.1038/nchembio.1337. PMID: 24013279. Please refer to Figure 5 and Supplementary Figures 5, 7, 8 and 9.",Microscopy/Imaging,,2014-01-24,2016-08-24
20137,Basal profile of receptor tyrosine kinase signaling network measured by ELISA,"PMID: 24065145; PMID: 24655548","lincs.hms.harvard.edu/niepel_scisignal_2013; lincs.hms.harvard.edu/niepel-bmcbiol-2014","Here, basal profiles for cells are the data for the abundance and basal phosphorylation of 22 receptors and 3 downstream kinases, as well as for the abundance of estrogen receptor (ER) and progesterone receptor (PR). In this dataset, basal profiles were obtained for approximately 40 breast cancer cell lines. All basal phosphorylation and protein abundance data were obtained by ELISA and, where possible, we estimated steady-state levels of molecules per cell using calibrated, recombinant standards. For the receptor tyrosine kinase phosphorylation data, we measured the amount of total phosphotyrosine rather than of individual phosphorylation sites, with the exception of IGF1R, for which we measured phosphorylation of Tyr1131.","Niepel M, Hafner M, Pace EA, Chung M, Chai DH, Zhou L, Schoeberl B, Sorger PK. Profiles of basal and stimulated receptor signaling networks predict drug response in breast cancer lines..Sci Signal. 2013 Sep 24;6(294):ra84. doi: 10.1126/scisignal.2004379. PMID: 24065145",ELISA,,2013-09-24,2016-11-08
20138,Cell signaling response to growth factors measured by high throughput microscopy,"PMID: 24065145","lincs.hms.harvard.edu/niepel_scisignal_2013","To generate the growth factor “signaling profile” set, we exposed approximately 40 breast cancer cell lines individually to fifteen different growth factors (protein ligands) for 10, 30, or 90 min. We monitored the response by measuring the phosphorylation state of ERK1/2, Akt, p38, and JNK using high throughput immunofluorescence microscopy.","Niepel M, Hafner M, Pace EA, Chung M, Chai DH, Zhou L, Schoeberl B, Sorger PK. Profiles of basal and stimulated receptor signaling networks predict drug response in breast cancer lines..Sci Signal. 2013 Sep 24;6(294):ra84. doi: 10.1126/scisignal.2004379. PMID: 24065145",Microscopy/Imaging,,2013-09-24,2016-11-08
20139,Cell signaling response to cytokines measured by high throughput microscopy,"PMID: 24065145","lincs.hms.harvard.edu/niepel_scisignal_2013","To generate the cytokine “signaling profile” set, we exposed approximately 40 breast cancer cell lines individually to seven different cytokines (protein ligands or LPS) for 10, 30, or 90 min. We monitored the response by measuring the phosphorylation state of ERK1/2, STAT1, and STAT3 and the nuclear translocation of NF-kappaB using high throughput immunofluorescence microscopy.","Niepel M, Hafner M, Pace EA, Chung M, Chai DH, Zhou L, Schoeberl B, Sorger PK. Profiles of basal and stimulated receptor signaling networks predict drug response in breast cancer lines..Sci Signal. 2013 Sep 24;6(294):ra84. doi: 10.1126/scisignal.2004379. PMID: 24065145",Microscopy/Imaging,,2013-09-24,2017-10-16
20140,Cell signaling response to growth factors measured by ELISA,"PMID: 24065145; PMID: 24655548","lincs.hms.harvard.edu/niepel_scisignal_2013; lincs.hms.harvard.edu/niepel-bmcbiol-2014","To generate the growth factor “signaling profile” set, we exposed approximately 40 breast cancer cell lines individually to fifteen different growth factors (protein ligands) for 10, 30, or 90 min. We monitored the response by measuring the phosphorylation state of ERK1/2 and Akt using ELISA.","Niepel M, Hafner M, Pace EA, Chung M, Chai DH, Zhou L, Schoeberl B, Sorger PK. Profiles of basal and stimulated receptor signaling networks predict drug response in breast cancer lines..Sci Signal. 2013 Sep 24;6(294):ra84. doi: 10.1126/scisignal.2004379. PMID: 24065145",ELISA,,2013-09-24,2016-11-08
20146,BMS-345541 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20147,AC220 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20148,R406 KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20149,BI-2536 KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20150,AMG-706 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20151,BIRB-796 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,The small molecule associated with this KINOMEscan dataset was erroneously assigned as HMS LINCS ID 10044-101 at the time of data release. The assignment was corrected to HMS LINCS 10169-999 on 2016-06-03.,2013-10-16,2016-06-03
20152,GDC-0941 KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20153,CI-1040 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20154,PLX-4720 KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20155,Lapatinib KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20156,AZD-6244 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20157,MLN-8054 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20158,AZD-1152HQPA KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20159,LY-317615 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20160,Erlotinib KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20161,Gefitinib KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20162,Nilotinib KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20163,Pazopanib KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20164,CI-1033 KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20165,SGX-523 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20166,PHA-665752 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20167,PI-103 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20168,TKI-258 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20169,GSK-690693 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20170,AB-1010 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20171,BMS-387032 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20172,BIBW-2992 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20173,INCB018424 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20174,TG-101348 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20175,BIBF-1120 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20176,GSK-1363089 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20177,SB-203580 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20178,VX-745 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20179,Sunitinib KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20180,BMS-540215 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20181,GDC-0879 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20182,ABT-869 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20183,Ki-20227 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20184,SKI-606 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20185,KW-2449 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20186,Vandetanib KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20187,PKC-412 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20188,CP-690550 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20189,CEP-701 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20190,GSK-1838705A KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20191,AT-7519 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20192,Sorafenib KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20193,Flavopiridol KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20194,GSK-461364A KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20195,HKI-272 KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20196,Dasatinib KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20197,VX-680 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20198,Imatinib KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20199,TAE-684 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20200,Crizotinib KINOMEscan-2,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2013-10-16,2016-06-03
20201,RAF-265 KINOMEscan,"PMID: 22037378","lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 442 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Kd values (nM) reported for each compound were determined using 11 serial threefold dilutions of test compound and a DMSO control. A null result means no inhibition of kinase binding to the ligand in the presence of the compound and low Kd means strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2014-03-10,2016-06-03
20202,RO-3306 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2014-03-10,2015-10-08
20203,CGP74514A KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2014-03-10,2015-10-08
20204,QL-X-138 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2014-06-26,2016-09-09
20205,QL-XII-47 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2016-03-04,2016-09-09
20206,PCI-32765 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2014-06-26,2016-08-24
20207,BX795 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,"The data for this assay have been removed permanently. Other information about this dataset have been left in this database for the record, instead of deleting the dataset entirely (June 2016).",2014-06-26,2018-03-27
20209,OTSSP167 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2014-06-26,2016-08-24
20210,DCC-2036 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2014-06-26,2016-08-24
20211,5z-7-oxozeaenol KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2014-06-26,2015-10-08
20212,JNK-IN-8 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition. The KINOMEscan data are presented graphically on TREEspot Kinase Dendrograms (http://www.kinomescan.com/Tools---Resources/Study-Reports---Data-Analysis). For this study, HMS LINCS investigators have graphed results for kinases classified as 35 ""percent of control"" (in the presence of the compound, the kinase is 35% as active for binding ligand in the presence of DMSO), 5 ""percent of control"" and 1 ""percent of control"".","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-10-08,2015-10-08
20213,JNK-IN-8 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2015-10-08,2016-09-09
20214,Ibrutinib KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2016-03-04,2016-09-09
20215,Sensitivity measures of MDA-MB-231 and HME-1 cell lines to LINCS Pilot Phase TransCenter Project kinase inhibitors,,,"To generate measures of the sensitivities of two cell lines to LINCS Pilot Phase TransCenter Project kinase inhibitors we treated cells with single drugs and measured the cell number after three days of drug exposure. This dataset is experimental data. Calculated metrics (IC50, GI50, EC50, Hill coefficient and Einf; see Fallahi-Sichani et al. Nat Chem Biol (2013) 9, p.708–714) from this data are available in HMS-LINCS dataset 20216.",,Microscopy/Imaging,,2014-12-10,2016-09-09
20216,Metrics for growth responses of MDA-MB-231 and HME-1 cell lines to LINCS Pilot Phase TransCenter Project kinase inhibitors,,,"This dataset presents calculated metrics (IC50, GI50, EC50, Hill coefficient and Einf) for the data in HMS-LINCS dataset #20215. The data in 20215 are measures of the sensitivities of two cell lines to the LINCS Pilot Phase TransCenter kinase inhibitors -- cells were treated with single drugs and cell number was measured after three days of drug exposure.","Fallahi-Sichani M, Honarnejad, S Heiser, LM, Gray JW and Sorger PK. Metrics other than potency reveal systematic variation in responses to cancer drugs. Nature Chemical Biology, 2013. doi:10.1038/nchembio.1337. PMID: 24013279.",Analysis,,2014-12-10,2016-09-09
20217,Viability and apoptosis in BRAF(V600E/D) melanoma cell lines monitored by imaging,"PMID: 25814555","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2015","Dose response of a set of anti-cancer compounds, including five RAF/MEK inhibitors, in human melanoma cell lines at 24, 48, and 72 hours to determine their effects on apoptosis and viability. Cells were treated in 4 replicates using Hewlett-Packard (HP) D300 Digital Dispenser with either seven or nine doses (in 1:3.16 or 1:2.5 dilution ratios, respectively) of each compound for 24, 48 and 72 h. To score viability and apoptosis, a dye-based imaging assay was used; the cell-permeable DNA dye Hoechst 33342 was used to mark nuclei and DEVD-NucView488 caspase-3 substrate was used to mark apoptosis (stains nuclei of cells undergoing apoptosis, in which caspase 3 is active). The data from this dataset and from the related HMS dataset #20218 were used to generate the signatures presented in HMS datasets #20229-20231.","Cen H, Mao F, Aronchik I, Fuentes RJ, Firestone GL. DEVD-NucView488: a novel class of enzyme substrates for real-time detection of caspase-3 activity in live cells. FASEB J. 2008 Jul;22(7):2243-52. PMID: 18263700",Microscopy/Imaging,,2015-01-23,2016-10-28
20218,Phosphorylation state and protein levels measured in BRAF(V600E/D) melanoma cell lines monitored by Reverse Phase Protein Arrays (RPPA),"PMID: 25814555","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2015","This assay measures phosphorylation state and protein levels in BRAF(V600E/D) melanoma cell lines monitored by Reverse Phase Protein Arrays (RPPA). Cells were plated in 4 replicates at 20,000 (or 15,000) cells per well density in 96-well plates, treated with different doses of each compound for 1, 5, 10, 24 and 48 hr. Plates for RPPA assays were treated with drugs using previously prepared 384-well dilution plates and a Seiko pin transfer robot system. Lysates were collected at the designated time-points (1, 5, 10, 24, 48 hr) post drug treatment. To generate reverse phase arrays, lysates were printed on nitrocellulose coated glass slides on a 2470 Arrayer. The data from this dataset and from the related HMS dataset #20217 were used to generate the signatures presented in HMS datasets #20229-20231.","1) Fallahi-Sichani, et al. (2015) Molecular Systems Biology. PMID: 25814555)
2) Sevecka et al. (2011) Lysate microarrays enable high-throughput, quantitative investigations of cellular signaling. Mol Cell Proteomics. Apr;10(4). PMID: 21296872",Reverse Phase Protein Array,"August 25, 2015: The data file for this dataset was updated to include additional DMSO control data that were inadvertently omitted from the original version. The Assay Protocol description of how experimental data were normalized to DMSO control data also was clarified (point 9).",2015-01-23,2016-10-28
20219,Phosphorylation state and protein levels measured in BRAF(V600E/D) melanoma cell lines monitored by imaging,"PMID: 25814555","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2015","This is the numerical data extracted from microscopy images measuring the mean intensity for 7 signals in multiple replicates across 4 cell lines and 3 treatment conditions (10 drug doses). Each data row reports the mean intensity of three fluorescent channels (Alexa 488, Alexa 568 and Alexa 647) for each measured protein (or phospho protein). Cells were seeded at the following densities in 96-well plates in full growth media for 24 hr: WM115 (10,000 cells per well), WM1552C (7,000 cells per well), COLO858 and LOXIMVI (5,000 cells per well). Cells were then treated in duplicates using Hewlett-Packard (HP) D300 Digital Dispenser with nine doses of vemurafenib, JNK-IN-8 or their combination for 24 hr. When combined, drugs were added at a 1:1 ratio at indicated doses. Several related HMS datasets from the same project also are available: experimental data in #20217 and #20218 and signature data in #20229, #20230, and #20231.",,Microscopy/Imaging,,2015-01-23,2016-10-28
20220,ZSTK474 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-04-17,2015-10-08
20221,MPS-1-IN-1 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-04-17,2015-10-08
20222,Ibrutinib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-04-17,2015-10-08
20223,TGX221 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-04-17,2015-10-08
20224,BGJ398 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-04-17,2015-10-08
20225,CGP082996 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-04-17,2015-10-08
20227,Baricitinib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-04-17,2015-10-08
20228,MRT67307 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2015-04-17,2015-10-08
20229,PLSR model loadings (pMEK and pERK included) from analysis of the covariation of molecular signals with cell viability and apoptosis fraction in BRAF(V600E/D) melanoma cell lines,"PMID: 25814555","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2015",This analysis dataset presents partial-least-squares regression (PLSR) model loadings arising from analysis of HMS LINCS datasets #20217 and 20218 for covariation of molecular signals (measured by RPPA; dataset #20218) with cellular responses (relative viability and apoptotic fractions; datasets #20217) when pMEK and pERK signals are included.,"Geladi P, Kowalski BR (1986) Partial least-squares regression: a tutorial. Anal Chim Acta 185:1-17.
Janes KA, Yaffe MB (2006) Data-driven modelling of signal-transduction networks. Nat Rev Mol Cell Biol 7:820-828.",Analysis,,2015-04-17,2015-09-23
20230,PLSR model loadings (pMEK and pERK excluded) from analysis of the covariation of molecular signals with cell viability and apoptosis fraction in BRAF(V600E/D) melanoma cell lines,"PMID: 25814555","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2015",This analysis dataset presents partial-least-squares regression (PLSR) model loadings arising from analysis of HMS LINCS datasets #20217 and 20218 for covariation of molecular signals (measured by RPPA; dataset #20218) with cellular responses (relative viability and apoptotic fractions; datasets #20217) when pMEK and pERK signals are excluded.,"Geladi P, Kowalski BR (1986) Partial least-squares regression: a tutorial. Anal Chim Acta 185:1-17.
Janes KA, Yaffe MB (2006) Data-driven modelling of signal-transduction networks. Nat Rev Mol Cell Biol 7:820-828.",Analysis,,2015-04-17,2015-09-23
20231,Average variable importance in the projection (VIP) scores from the PLSR models analyzing the covariation of molecular signals with cell viability and apoptosis fraction in BRAF(V600E/D) melanoma cell lines,"PMID: 25814555","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2015","This dataset presents an analysis of the variable importance in the projection (VIP) scores for each variable in the partial-least-squares regression (PLSR) models arising from analysis of HMS LINCS datasets #20217 and 20218, which assess covariation of molecular signals (measured by RPPA; dataset #20218) with cellular responses (relative viability and apoptotic fractions; dataset #20217). pMEK and pERK signals were excluded from the analysis.","Janes KA, Reinhardt HC, Yaffe MB (2008) Cytokine-induced signaling networks prioritize dynamic range over signal strength. Cell 135:343-354.
Wold S (1994) Exponentially weighted moving principal components analysis and projections to latent structures. Chemometrics Intellig Lab Syst 23:149-161.",Analysis,,2015-04-17,2015-09-23
20232,Live-cell imaging of cell-to-cell variability in caspase-8 FRET reporter activity and cell fate trajectory modeling,"PMID: 25953765","lincs.hms.harvard.edu/roux-molsystbiol-2015","This analysis dataset presents calculated parameters fit to a phenomenological model that defines an initiator caspase threshold that underlies cell-to-cell variability in cell killing by TRAIL (TNF10) and therapeutic antibody TRAIL receptor agonists. The analysis is based on live-cell, microscopy-based fate tracking of cells following perturbation with TRAIL, therapeutic antibody TRAIL receptor agonists, and other agents that modulate the cellular fate decision.",,Analysis,,2015-07-02,2016-03-22
20233,Synovial Fibroblast 1: Secretion response of primary human synovial fibroblast samples from one healthy and one rheumatoid arthritis donor to a panel of 10 stimuli and 10 small molecule inhibitors,"PMID: 27820799","lincs.hms.harvard.edu/jones-natchembiol-2016","Supernatant levels of 48 cytokines, chemokines, and growth factors were measured using a multiplexed bead-based sandwich immunoassay to quantify the secretion response of two primary human synovial fibroblast donor samples exposed to 10 different stimuli in the presence or absence of 1 of 10 small molecule kinase inhibitors. Two related datasets from the same project also are available: #20234 and #20235.","Rosengren, S., Boyle, D. L. & Firestein, G. S. (2007) Acquisition, culture, and phenotyping of synovial fibroblasts. Methods Mol. Med. 135, 365–375.",Bead-based immunoassay,,2015-08-27,2017-10-16
20234,Synovial Fibroblast 3.1: Secretion response of seven primary human synovial fibroblast samples from healthy and rheumatoid arthritis donors to a panel of 3 stimuli and 5 small molecule inhibitors (replicate 1 of 2),"PMID: 27820799","lincs.hms.harvard.edu/jones-natchembiol-2016","Supernatant levels of 51 cytokines, chemokines, growth factors, and proteases were measured using a multiplexed bead-based sandwich immunoassay to quantify the secretion response of 7 primary human synovial fibroblast samples from healthy and rheumatoid arthritis-diagnosed donors exposed to 3 different stimuli in the presence or absence of 1 of 5 small molecule kinase inhibitors. A full replicate of this experiment (including cell stimulation, supernatant recovery, and Luminex analysis) was conducted on a separate day and is available in HMS dataset #20235. A third, related dataset from the same project also is available: #20233.","Rosengren, S., Boyle, D. L. & Firestein, G. S. (2007) Acquisition, culture, and phenotyping of synovial fibroblasts. Methods Mol. Med. 135, 365–375.",Bead-based immunoassay,,2015-08-27,2017-10-16
20235,Synovial Fibroblast 3.2: Secretion response of seven primary human synovial fibroblast samples from healthy and rheumatoid arthritis-diagnosed donors to a panel of 3 stimuli and 5 small molecule inhibitors (replicate 2 of 2),"PMID: 27820799","lincs.hms.harvard.edu/jones-natchembiol-2016","Supernatant levels of 51 cytokines, chemokines, growth factors, and proteases were measured using a multiplexed bead-based sandwich immunoassay to quantify the secretion response of 7 primary human synovial fibroblast samples from healthy and rheumatoid arthritis-diagnosed donors exposed to 3 different stimuli in the presence or absence of 1 of 5 small molecule kinase inhibitors. A full replicate of this experiment (including cell stimulation, supernatant recovery, and Luminex analysis) was conducted on a separate day and is available in HMS dataset #20234. A third, related dataset from the same project also is available: #20233.","Rosengren, S., Boyle, D. L. & Firestein, G. S. (2007) Acquisition, culture, and phenotyping of synovial fibroblasts. Methods Mol. Med. 135, 365–375.",Bead-based immunoassay,,2015-08-27,2017-10-16
20236,Highly multiplexed imaging by Cyclic Immunofluorescence (CycIF) of protein levels and protein phosphorylation states in the COLO 858 melanoma cell line,"PMID: 26399630","lincs.hms.harvard.edu/lin-natcommun-2015",Cyclic Immunofluorescence (CycIF) is a novel fluorescence imaging assay used for multiplexed measurement of protein levels and protein phosphorylation states in single cells. COLO 858 melanoma cells plated in 96-well plates were treated with different doses of PLX4032/Vemurafenib for 48 hr before being fixed and subjected to two cycles of CycIF staining according to the protocol described below.,,Microscopy/Imaging,,2015-09-15,2016-08-24
20237,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 1 of 15: Cell count and relative growth within biological replicate 1.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-08-25,2017-03-14
20238,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 2 of 15: Cell count and relative growth within biological replicate 2.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-08-25,2017-03-14
20239,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 3 of 15: Cell count and relative growth within biological replicate 3.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-08-25,2017-03-14
20240,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 4 of 15: Mean cell count and mean growth rate across biological replicate 1.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-08-25,2017-03-14
20241,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 5 of 15: Mean cell count and mean growth rate across biological replicate 2.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-08-25,2017-03-14
20242,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 6 of 15: Mean cell count and mean growth rate across biological replicate 3.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-08-25,2017-03-14
20243,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 7 of 15: Mean cell count and mean growth rate across all replicates.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-08-25,2017-03-14
20244,High-content imaging of six breast cancer cell lines treated with a library of small molecule kinase inhibitors.,,"lincs.hms.harvard.edu/mills-unpubl-2015","To investigate the phenotypic effects that kinase inhibitors have on breast cancer cell lines at the single cell level, five breast cancer cell lines (hormone receptor-positive MCF7 cells, Her2-amplified SK-BR-3 cells, and triple negative BT-20, MDA-MB-231, and Hs 578T cells) and one non-tumorigenic breast cell line (MCF 10A) were treated at three doses with a panel of 105 kinase inhibitors covering a broad range of targets. A panel of twelve control treatments with small molecule and protein perturbagens known to induce particular types of cell stress/death was included for reference. The cells were stained with DRAQ5 (to visualize nuclei and cytoplasm) and TMRE (an indicator of mitochondrial membrane potential). The experiment was performed in biological triplicate. A subset of the data from one of the three biological replicates is presented here to illustrate some of the cellular features assayed. The complete dataset is available at http://lincs.hms.harvard.edu/mills-unpubl-2015/.","Haralick, R.M., Shanmugam, K., and Dinstein, I. (1973) Textural features for image classification. IEEE Trans Syst Man Cybern. SMC-3, 610-621.
Hamilton, N.A. Pantelic, R.S., Hanson, K., and Teasdale, R.D. (2007) Fast automated cell phenotype image classification. BMC Bioinformatics. 8, 110. doi:10.1186/1471-2105-8-110 PMID:17394669 PMCID: PMC1847687",Microscopy/Imaging,,2015-12-16,2016-11-08
20245,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 8 of 15: Cell count and normalized growth rate inhibition values within biological replicate 1.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-12-18,2017-03-14
20246,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 9 of 15: Cell count and normalized growth rate inhibition values within biological replicate 2.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-12-18,2017-03-14
20247,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 10 of 15: Cell count and normalized growth rate inhibition values within biological replicate 3.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-12-18,2017-03-14
20248,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 11 of 15: Mean cell count and mean normalized growth rate inhibition values across biological replicate 1.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-12-18,2017-03-14
20249,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 12 of 15: Mean cell count and mean normalized growth rate inhibition values across biological replicate 2.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-12-18,2017-03-14
20250,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 13 of 15: Mean cell count and mean normalized growth rate inhibition values across biological replicate 3.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-12-18,2017-03-14
20251,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 14 of 15: Mean cell count and mean normalized growth rate inhibition values across all replicates.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Microscopy/Imaging,,2015-12-18,2017-03-14
20252,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (single drug treatments). Dataset 15 of 15: Calculated dose-response metrics.,,,"To generate measures of the sensitivities of six cell lines to a library of small molecule inhibitors, we treated cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measured cell number after three days of drug exposure. This dataset presents the dose-response metrics (GR_AOC) calculated using the normalized growth rate inhibition values reported in HMS LINCS Datasets #20245-20251. As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same set of cells and perturbagens is available at http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE70138.",,Analysis,,2015-12-18,2017-03-14
20253,WZ3105 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2016-01-20,2016-09-09
20254,PF-3758309 KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2016-01-20,2016-09-09
20255,5z-7-oxozeaenol KiNativ -- single dose experiment,,"lincs.hms.harvard.edu/kinativ","The KiNativ assay platform is based on the use of biotinylated acyl phosphates of ATP and ADP that act as probes by reacting with protein kinases on conserved lysine residues in the ATP binding pocket to covalently attach a biotin moiety. Using these probes, cell lysates treated with a kinase inhibitor can be labeled with BHAcATP or BHAcADP, with kinases inhibited by the compound of interest exhibiting reduced or no labeling. This is followed by digestion with trypsin, isolation of biotinylated peptides, and analysis by mass spectrometry to determine the extent of labeling of peptides from each kinase.","KiNativ website: kinativ.com
Patricelli MP, Szardenings AK, Liyanage M, Nomanbhoy TK, Wu M, Weissig H, Aban A, Chun D, Tanner S, Kozarich JW. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry. 2007 Jan 16;46(2):350-8. PMID: 17209545",KiNativ,,2016-01-20,2016-09-09
20256,Breast Cancer Cell Density: Imaging assay of the density- and context-dependence of small molecule perturbagen response in breast cancer cell lines. Dataset 1 of 3: Cell count and normalized growth rate inhibition values.,"PMID: 27135972",,The density- and context-dependent sensitivities of 6 cell lines plated at 6 different cell densities were assayed by measuring cell counts 72 hours after treatment with each of 12 small molecule inhibitors across a 9-point dose range.,,Microscopy/Imaging,,2016-02-04,2017-03-14
20257,Breast Cancer Cell Density: Imaging assay of the density- and context-dependence of small molecule perturbagen response in breast cancer cell lines. Dataset 2 of 3: Mean cell count and mean normalized growth rate inhibition values across all replicates.,"PMID: 27135972",,The density- and context-dependent sensitivities of 6 cell lines plated at 6 different cell densities were assayed by measuring cell counts 72 hours after treatment with each of 12 small molecule inhibitors across a 9-point dose range.,,Microscopy/Imaging,,2016-02-04,2017-03-14
20258,Breast Cancer Cell Density: Imaging assay of the density- and context-dependence of small molecule perturbagen response in breast cancer cell lines. Dataset 3 of 3: Calculated dose-response metrics.,"PMID: 27135972",,The density- and context-dependent sensitivities of 6 cell lines plated at 6 different cell densities were assayed by measuring cell counts 72 hours after treatment with each of 12 small molecule inhibitors across a 9-point dose range. This dataset presents a comparison of the dose-response metrics calculated using the normalized and non-normalized cell count data reported in HMS LINCS Datasets #20256 and 20257.,,Analysis,,2016-02-04,2017-03-14
20259,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (drug combination treatments). Dataset 1 of 2: Cell count and normalized growth rate inhibition values.,,,"As described in HMS LINCS Datasets #20245-20252, measures of the sensitivities of six cell lines to a library of small molecule inhibitors were generated by treating cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measuring cell number after three days of drug exposure. Based on those results, a subset of the drugs was chosen for analysis of combinatorial drug sensitivities in a single cell line (Datasets #20259 and #20260). As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same perturbagen combinations are available at http://projects.lincscloud.org/#LJP.",,Microscopy/Imaging,,2016-04-01,2016-09-09
20260,LINCS Pilot Phase Joint Project: Sensitivity measures of six breast cancer cell lines to a library of small molecule kinase inhibitors (drug combination treatments). Dataset 2 of 2: Mean cell count and mean normalized growth rate inhibition values across technical replicates.,,,"As described in HMS LINCS Datasets #20245-20252, measures of the sensitivities of six cell lines to a library of small molecule inhibitors were generated by treating cells with single drugs at six doses starting at 10 µM in 3x dilution steps and measuring cell number after three days of drug exposure. Based on those results, a subset of the drugs was chosen for analysis of combinatorial drug sensitivities in a single cell line (Datasets #20259 and #20260). As part of this LINCS Pilot Phase Joint Project, L1000 gene expression data generated by the Broad LINCS Center for the same perturbagen combinations are available at http://projects.lincscloud.org/#LJP.",,Microscopy/Imaging,,2016-04-01,2016-09-09
20261,GDC-0941 KINOMEscan-3,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2016-05-26,2016-06-02
20262,Buparlisib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2016-05-26,2016-06-02
20263,BYL719 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2016-05-26,2016-06-02
20264,Taselisib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2016-05-26,2016-06-02
20265,Multiplexed imaging of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with EGF,,,The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of epidermal growth factor (EGF) for 24 hr before being fixed and analyzed by immunofluorescence microscopy according to the protocol described below.,,Microscopy/Imaging,,2016-09-29,2016-09-29
20266,Multiplexed imaging of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with nine kinase inhibitors,,,"The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of one of 9 kinase inhibitors (Getifinib, Erlotinib, Lapatinib, PD0325901, Selumetinib, MK2206, Triciribine, Dactolisib, and Torkinib) for 24 or 48 hr before being fixed and analyzed by immunofluorescence microscopy according to the protocol described below.",,Microscopy/Imaging,,2016-09-29,2016-09-29
20267,Highly-multiplexed imaging by Cyclic Immunofluorescence (CycIF) of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with EGF or four kinase inhibitors,,,"Cyclic Immunofluorescence (CycIF) is a fluorescence imaging assay used for multiplexed measurement of protein levels and protein phosphorylation states in single cells. The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of one of five perturbagens (EGF and the kinase inhibitors Lapatinib, Selumetinib, Dactolisib, and Torkinib) for 24 hr before being fixed and subjected to nine cycles of CycIF staining according to the protocol described below.",,Microscopy/Imaging,,2016-09-29,2016-09-29
20268,Growth rate-corrected (GR) dose-response metrics across a panel of 71 breast cancer cell lines treated with a library of small molecule and antibody perturbagens. Dataset 1 of 4: Relative cell counts and normalized growth rate inhibition values across technical replicates.,"PMID: 27135972",,"Dose-response data were collected for a panel of 73 breast cancer cell lines grown under standard or modified culture conditions and treated with 139 small molecule and antibody perturbagens. A subset of these data was previously described in Heiser et al. (2012) (PMID: 22003129) and Daemen et al. (2013) (PMID: 24176112). Here, the complete dataset was analyzed using the growth rate inhibition (GR) metrics described in Hafner et al. (2016) (PMID: 27135972) to account for differences in growth rates across the cell lines and treatment conditions.","1. Kuo, W.L., Das, D., Ziyad, S., Bhattacharya, S., Gibb, W.J., Heiser, L.M., Sadanandam, A., Fontenay, G.V., Hu, Z., Wang, N.J., Bayani, N., Feiler, H.S., Neve, R.M., Wyrobek, A.J., Spellman, P.T., Marton, L.J., and Gray, J.W. (2009) A systems analysis of the chemosensitivity of breast cancer cells to the polyamine analogue PG-11047. BMC Med. 7:77. doi:10.1186/1741-7015-7-77 PMID: 20003408 PMCID: PMC2803786
2. Heiser, L.M., Sadanandam, A., Kuo, W.L., Benz, S.C., Goldstein, T.C., Ng, S., Gibb, W.J., Wang, N.J., Ziyad, S., Tong, F., Bayani, N., Hu, Z., Billig, J.I., Dueregger, A., Lewis, S., Jakkula, L., Korkola, J.E., Durinck, S., Pepin, F., Guan, Y., Purdom, E., Neuvial, P., Bengtsson, H., Wood, K.W., Smith, P.G., Vassilev, L.T., Hennessy, B.T., Greshock, J., Bachman, K.E., Hardwicke, M.A., Park, J.W., Marton, L.J., Wolf, D.M., Collisson, E.A., Neve, R.M., Mills, G.B., Speed, T.P., Feiler, H.S., Wooster, R.F., Haussler, D., Stuart, J.M., Gray, J.W., and Spellman, P.T. (2012) Subtype and pathway specific responses to anticancer compounds in breast cancer. Proc Natl Acad Sci USA. 109(8):2724-9. doi:10.1073/pnas.1018854108 PMID: 22003129 PMCID: PMC3286973
3. Heiser, L.M., Wang, N.J., Korkola, J.E., and Gray, J.W. (2017) Synapse. doi:10.7303/syn8094063.1
4. Hafner, M., Heiser, L.M., Williams, E.H., Wang, N.J., Korkola, J.E., Gray, J.W., and Sorger, P. K. (2017) Reference file package
5. Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336
",Analysis,,2016-12-22,2017-02-01
20269,Growth rate-corrected (GR) dose-response metrics across a panel of 71 breast cancer cell lines treated with a library of small molecule and antibody perturbagens. Dataset 2 of 4: Calculated dose-response metrics.,"PMID: 27135972",,"Dose-response data were collected for a panel of 73 breast cancer cell lines grown under standard or modified culture conditions and treated with 139 small molecule and antibody perturbagens. A subset of these data was previously described in Heiser et al. (2012) (PMID: 22003129) and Daemen et al. (2013) (PMID: 24176112). Here, the complete dataset was analyzed using the growth rate inhibition (GR) metrics described in Hafner et al. (2016) (PMID: 27135972) to account for differences in growth rates across the cell lines and treatment conditions.","1. Kuo, W.L., Das, D., Ziyad, S., Bhattacharya, S., Gibb, W.J., Heiser, L.M., Sadanandam, A., Fontenay, G.V., Hu, Z., Wang, N.J., Bayani, N., Feiler, H.S., Neve, R.M., Wyrobek, A.J., Spellman, P.T., Marton, L.J., and Gray, J.W. (2009) A systems analysis of the chemosensitivity of breast cancer cells to the polyamine analogue PG-11047. BMC Med. 7:77. doi:10.1186/1741-7015-7-77 PMID: 20003408 PMCID: PMC2803786
2. Heiser, L.M., Sadanandam, A., Kuo, W.L., Benz, S.C., Goldstein, T.C., Ng, S., Gibb, W.J., Wang, N.J., Ziyad, S., Tong, F., Bayani, N., Hu, Z., Billig, J.I., Dueregger, A., Lewis, S., Jakkula, L., Korkola, J.E., Durinck, S., Pepin, F., Guan, Y., Purdom, E., Neuvial, P., Bengtsson, H., Wood, K.W., Smith, P.G., Vassilev, L.T., Hennessy, B.T., Greshock, J., Bachman, K.E., Hardwicke, M.A., Park, J.W., Marton, L.J., Wolf, D.M., Collisson, E.A., Neve, R.M., Mills, G.B., Speed, T.P., Feiler, H.S., Wooster, R.F., Haussler, D., Stuart, J.M., Gray, J.W., and Spellman, P.T. (2012) Subtype and pathway specific responses to anticancer compounds in breast cancer. Proc Natl Acad Sci USA. 109(8):2724-9. doi:10.1073/pnas.1018854108 PMID: 22003129 PMCID: PMC3286973
3. Heiser, L.M., Wang, N.J., Korkola, J.E., and Gray, J.W. (2017) Synapse. doi:10.7303/syn8094063.1
4. Hafner, M., Heiser, L.M., Williams, E.H., Wang, N.J., Korkola, J.E., Gray, J.W., and Sorger, P. K. (2017) Reference file package
5. Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336
",Analysis,,2016-12-22,2017-03-14
20270,"Growth rate-corrected (GR) dose-response metric signatures across a panel of 71 breast cancer cell lines treated with a library of small molecule and antibody perturbagens. Dataset 3 of 4: Median, upper quartile, and lower quartile GR metrics per perturbagen.",,,"Dose-response data were collected for a panel of 73 breast cancer cell lines grown under standard or modified culture conditions and treated with 139 small molecule and antibody perturbagens. A subset of these data was previously described in Heiser et al. (2012) (PMID: 22003129) and Daemen et al. (2013) (PMID: 24176112). Here, the complete dataset was analyzed using the growth rate inhibition (GR) metrics described in Hafner et al. (2016) (PMID: 27135972) to account for differences in growth rates across the cell lines and treatment conditions.","1. Kuo, W.L., Das, D., Ziyad, S., Bhattacharya, S., Gibb, W.J., Heiser, L.M., Sadanandam, A., Fontenay, G.V., Hu, Z., Wang, N.J., Bayani, N., Feiler, H.S., Neve, R.M., Wyrobek, A.J., Spellman, P.T., Marton, L.J., and Gray, J.W. (2009) A systems analysis of the chemosensitivity of breast cancer cells to the polyamine analogue PG-11047. BMC Med. 7:77. doi:10.1186/1741-7015-7-77 PMID: 20003408 PMCID: PMC2803786
2. Heiser, L.M., Sadanandam, A., Kuo, W.L., Benz, S.C., Goldstein, T.C., Ng, S., Gibb, W.J., Wang, N.J., Ziyad, S., Tong, F., Bayani, N., Hu, Z., Billig, J.I., Dueregger, A., Lewis, S., Jakkula, L., Korkola, J.E., Durinck, S., Pepin, F., Guan, Y., Purdom, E., Neuvial, P., Bengtsson, H., Wood, K.W., Smith, P.G., Vassilev, L.T., Hennessy, B.T., Greshock, J., Bachman, K.E., Hardwicke, M.A., Park, J.W., Marton, L.J., Wolf, D.M., Collisson, E.A., Neve, R.M., Mills, G.B., Speed, T.P., Feiler, H.S., Wooster, R.F., Haussler, D., Stuart, J.M., Gray, J.W., and Spellman, P.T. (2012) Subtype and pathway specific responses to anticancer compounds in breast cancer. Proc Natl Acad Sci USA. 109(8):2724-9. doi:10.1073/pnas.1018854108 PMID: 22003129 PMCID: PMC3286973
3. Heiser, L.M., Wang, N.J., Korkola, J.E., and Gray, J.W. (2017) Synapse. doi:10.7303/syn8094063.1
4. Hafner, M., Heiser, L.M., Williams, E.H., Wang, N.J., Korkola, J.E., Gray, J.W., and Sorger, P. K. (2017) Reference file package
5. Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336
",Analysis,,2016-12-22,2017-10-16
20271,"Growth rate-corrected (GR) dose-response metric signatures across a panel of 71 breast cancer cell lines treated with a library of small molecule and antibody perturbagens. Dataset 4 of 4: Median, upper quartile, and lower quartile GR metrics per perturbagen class.",,,"Dose-response data were collected for a panel of 73 breast cancer cell lines grown under standard or modified culture conditions and treated with 139 small molecule and antibody perturbagens. A subset of these data was previously described in Heiser et al. (2012) (PMID: 22003129) and Daemen et al. (2013) (PMID: 24176112). Here, the complete dataset was analyzed using the growth rate inhibition (GR) metrics described in Hafner et al. (2016) (PMID: 27135972) to account for differences in growth rates across the cell lines and treatment conditions.","1. Kuo, W.L., Das, D., Ziyad, S., Bhattacharya, S., Gibb, W.J., Heiser, L.M., Sadanandam, A., Fontenay, G.V., Hu, Z., Wang, N.J., Bayani, N., Feiler, H.S., Neve, R.M., Wyrobek, A.J., Spellman, P.T., Marton, L.J., and Gray, J.W. (2009) A systems analysis of the chemosensitivity of breast cancer cells to the polyamine analogue PG-11047. BMC Med. 7:77. doi:10.1186/1741-7015-7-77 PMID: 20003408 PMCID: PMC2803786
2. Heiser, L.M., Sadanandam, A., Kuo, W.L., Benz, S.C., Goldstein, T.C., Ng, S., Gibb, W.J., Wang, N.J., Ziyad, S., Tong, F., Bayani, N., Hu, Z., Billig, J.I., Dueregger, A., Lewis, S., Jakkula, L., Korkola, J.E., Durinck, S., Pepin, F., Guan, Y., Purdom, E., Neuvial, P., Bengtsson, H., Wood, K.W., Smith, P.G., Vassilev, L.T., Hennessy, B.T., Greshock, J., Bachman, K.E., Hardwicke, M.A., Park, J.W., Marton, L.J., Wolf, D.M., Collisson, E.A., Neve, R.M., Mills, G.B., Speed, T.P., Feiler, H.S., Wooster, R.F., Haussler, D., Stuart, J.M., Gray, J.W., and Spellman, P.T. (2012) Subtype and pathway specific responses to anticancer compounds in breast cancer. Proc Natl Acad Sci USA. 109(8):2724-9. doi:10.1073/pnas.1018854108 PMID: 22003129 PMCID: PMC3286973
3. Heiser, L.M., Wang, N.J., Korkola, J.E., and Gray, J.W. (2017) Synapse. doi:10.7303/syn8094063.1
4. Hafner, M., Heiser, L.M., Williams, E.H., Wang, N.J., Korkola, J.E., Gray, J.W., and Sorger, P. K. (2017) Reference file package
5. Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336
",Analysis,,2016-12-22,2017-02-01
20272,Viability and apoptosis measured by imaging in BRAF(V600E/D) melanoma cell lines following treatment with combinations of two compounds (viability/apoptosis dataset 1 of 2),"PMID: 28069687","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2017","The dose response of human melanoma cell lines in response to Vemurafenib in combination with a second compound was measured at 72 hr to determine their effects on apoptosis and viability. Cells were treated in 3 replicates using a Hewlett-Packard (HP) D300 Digital Dispenser with 4 doses of Vemurafenib (1:3.16 dilution ratios) and 1 or 3 doses of a second compound for 72 hr. To score viability and apoptosis, a dye-based imaging assay was used. The cell-permeable DNA dye Hoechst 33342 was used to mark all nuclei, and DEVD-NucView488 Caspase-3 substrate was used to mark the nuclei of cells undergoing apoptosis (i.e., in which caspase 3 is active).",,Microscopy/Imaging,,2016-12-22,2017-01-20
20273,Viability and apoptosis measured by imaging in BRAF(V600E/D) melanoma cell lines following treatment with combinations of three compounds (viability/apoptosis dataset 2 of 2),"PMID: 28069687","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2017","The dose response of human melanoma cell lines to Vemurafenib in combination with Trametinib and a third compound was measured at 72 hr to determine their effects on apoptosis and viability. Cells were treated in 3 replicates using a Hewlett-Packard (HP) D300 Digital Dispenser with 4 combined doses of Vemurafenib/Trametinib (1:3.16 dilution ratios) and 1 or 3 doses of a third compound for 72 hr. To score viability and apoptosis, a dye-based imaging assay was used. The cell-permeable DNA dye Hoechst 33342 was used to mark all nuclei, and DEVD-NucView488 Caspase-3 substrate was used to mark the nuclei of cells undergoing apoptosis (i.e., in which caspase 3 is active).",,Microscopy/Imaging,,2016-12-22,2017-01-20
20274,Phosphorylation state and protein levels measured by imaging in BRAF(V600E/D) melanoma cell lines following treatment with combinations of two compounds (immunofluorescence dataset 1 of 4),"PMID: 28069687","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2017","Three human melanoma cell lines were treated in 2 replicates with Vemurafenib at 3 doses in combination with DMSO or 2 doses of 9 other compounds. This dataset presents the mean intensity measurements for 6 protein or phosphoprotein readouts (KI-67, Rb (pS807; pS811), NGFR, S6 (pS240; pS244), c-Jun, and c-Jun (pS73)) extracted from microscopy images across each condition.",,Microscopy/Imaging,,2016-12-22,2017-01-20
20275,Phosphorylation state and protein levels measured by imaging in BRAF(V600E/D) melanoma cell lines following treatment with combinations of two compounds (immunofluorescence dataset 2 of 4),"PMID: 28069687","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2017","Three human melanoma cell lines were treated in 2 replicates with Vemurafenib at 3 doses in combination with DMSO or 1 dose of 9 other compounds. This dataset presents the mean intensity measurements for 3 protein or phosphoprotein readouts (KI-67, Rb (pS807; pS811), and ERK-1 (pT202; pY204) / ERK-2 (pT185; pY187) extracted from microscopy images across each condition.",,Microscopy/Imaging,,2016-12-22,2017-01-20
20276,Protein levels measured by imaging in BRAF(V600E/D) melanoma cell lines following treatment with Vemurafenib in combination with chromatin-targeting compounds (immunofluorescence dataset 3 of 4),"PMID: 28069687","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2017",Three human melanoma cell lines were treated in 2 replicates with 1 dose of Vemurafenib in combination with DMSO or 3 doses of each of 41 compounds in a chromatin-targeting library (LINCS 3 Chromatin Targeting Library). This dataset presents the number of nuclei assayed and the mean intensity measurements for 2 protein readouts (KI-67 and NGFR) extracted from microscopy images across each condition.,,Microscopy/Imaging,,2016-12-22,2017-01-20
20277,Phosphorylation state and protein levels measured by imaging in BRAF(V600E/D) melanoma cell lines following treatment with combinations of two compounds (immunofluorescence dataset 4 of 4),"PMID: 28069687","lincs.hms.harvard.edu/fallahi-sichani-molsystbiol-2017","Three human melanoma cell lines were treated in 2 replicates with 5 doses of Vemurafenib in combination with DMSO or 1 dose of 5 other compounds. This dataset presents the mean intensity measurements for 5 protein and phosphoprotein readouts (KI-67, NGFR, S6 (pS240; pS244), ERK-1 (pT202; pY204) / ERK-2 (pT185; pY187), and c-Jun) extracted from microscopy images across each condition.",,Microscopy/Imaging,,2016-12-22,2017-01-20
20278,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 1 of 9: Cell count and normalized growth rate inhibition values for biological replicate 1,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-02-07,2017-02-07
20279,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 2 of 9: Cell count and normalized growth rate inhibition values for biological replicate 2,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-02-07,2017-02-07
20280,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 3 of 9: Cell count and normalized growth rate inhibition values for biological replicate 3,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-02-07,2017-02-07
20281,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 4 of 9: Mean cell count and mean normalized growth rate inhibition values for biological replicate 1,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-02-07,2017-02-07
20282,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 5 of 9: Mean cell count and mean normalized growth rate inhibition values for biological replicate 2,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-02-07,2017-02-07
20283,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 6 of 9: Mean cell count and mean normalized growth rate inhibition values for biological replicate 3,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-02-07,2017-02-07
20284,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 7 of 9: Calculated dose-response metrics for biological replicate 1,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-02-07,2017-03-14
20285,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 8 of 9: Calculated dose-response metrics for biological replicate 2,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-02-07,2017-03-14
20286,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 9 of 9: Calculated dose-response metrics for biological replicate 3,,,"To generate measures of the sensitivities of three independent batches and one derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 9-point dilution series using SQRT(10) dilutions centered around the GR50 but not exceeding 10 µM and then measured cell number after three days of drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-02-07,2017-03-14
20287,FoxO3a nuclear-cytoplasmic pulsing dynamics in a mammary epithelial cell line following growth-factor treatment with varying ERK/AKT activation loads. Dataset 1 of 3: single-cell reporter measurements.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-Venus) expressed in the 184A1 mammary epithelial cell line was assessed at the single-cell level using live imaging of cells that were untreated or treated with one of six growth factors in the absence or presence of an AKT or MEK inhibitor.,,Microscopy/Imaging,,2017-05-02,2017-05-02
20288,FoxO3a nuclear-cytoplasmic pulsing dynamics in a mammary epithelial cell line following growth-factor treatment with varying ERK/AKT activation loads. Dataset 2 of 3: single-cell reporter pulsing metrics.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-Venus) expressed in the 184A1 mammary epithelial cell line was assessed at the single-cell level using live imaging of cells that were untreated or treated with one of six growth factors in the absence or presence of an AKT or MEK inhibitor.,,Analysis,,2017-05-02,2017-05-02
20289,FoxO3a nuclear-cytoplasmic pulsing dynamics in a mammary epithelial cell line following growth-factor treatment with varying ERK/AKT activation loads. Dataset 3 of 3: mean reporter pulsing metrics.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-Venus) expressed in the 184A1 mammary epithelial cell line was assessed at the single-cell level using live imaging of cells that were untreated or treated with one of six growth factors in the absence or presence of an AKT or MEK inhibitor.,,Analysis,,2017-05-02,2017-05-02
20290,Growth factor-induced FoxO3a nuclear-cytoplasmic pulsing dynamics of non-phosphorylatable reporters in mammary epithelial cell lines. Dataset 1 of 3: single-cell reporter measurements.,,,The nuclear-cytoplasmic pulsing behavior of FoxO3a fluorescent reporters (FoxO3aN400-Venus) with or without AKT- and ERK-dependent phosphorylation site mutations was assessed in two mammary epithelial cell lines at the single-cell level using live imaging of cells that were untreated or treated with one of five growth factors.,,Microscopy/Imaging,,2017-05-02,2017-05-02
20291,Growth factor-induced FoxO3a nuclear-cytoplasmic pulsing dynamics of non-phosphorylatable reporters in mammary epithelial cell lines. Dataset 2 of 3: single-cell reporter pulsing metrics.,,,The nuclear-cytoplasmic pulsing behavior of FoxO3a fluorescent reporters (FoxO3aN400-Venus) with or without AKT- and ERK-dependent phosphorylation site mutations was assessed in two mammary epithelial cell lines at the single-cell level using live imaging of cells that were untreated or treated with one of five growth factors.,,Analysis,,2017-05-02,2017-05-02
20292,Growth factor-induced FoxO3a nuclear-cytoplasmic pulsing dynamics of non-phosphorylatable reporters in mammary epithelial cell lines. Dataset 3 of 3: mean reporter pulsing metrics.,,,The nuclear-cytoplasmic pulsing behavior of FoxO3a fluorescent reporters (FoxO3aN400-Venus) with or without AKT- and ERK-dependent phosphorylation site mutations was assessed in two mammary epithelial cell lines at the single-cell level using live imaging of cells that were untreated or treated with one of five growth factors.,,Analysis,,2017-05-02,2017-05-02
20293,IGF-I-induced FoxO3a nuclear-cytoplasmic pulsing dynamics in mammary epithelial cell lines following treatment with increasing doses of an AKT inhibitor. Dataset 1 of 3: single-cell reporter measurements.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-HA-Venus) expressed in two mammary epithelial cell lines was assessed at the single-cell level using live imaging of cells that were untreated or treated with IGF-I in the absence or presence of increasing doses of an AKT inhibitor.,,Microscopy/Imaging,,2017-05-02,2017-05-02
20294,IGF-I-induced FoxO3a nuclear-cytoplasmic pulsing dynamics in mammary epithelial cell lines following treatment with increasing doses of an AKT inhibitor. Dataset 2 of 3: single-cell reporter pulsing metrics.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-HA-Venus) expressed in two mammary epithelial cell lines was assessed at the single-cell level using live imaging of cells that were untreated or treated with IGF-I in the absence or presence of increasing doses of an AKT inhibitor.,,Analysis,,2017-05-02,2017-05-02
20295,IGF-I-induced FoxO3a nuclear-cytoplasmic pulsing dynamics in mammary epithelial cell lines following treatment with increasing doses of an AKT inhibitor. Dataset 3 of 3: mean reporter pulsing metrics.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-HA-Venus) expressed in two mammary epithelial cell lines was assessed at the single-cell level using live imaging of cells that were untreated or treated with IGF-I in the absence or presence of increasing doses of an AKT inhibitor.,,Analysis,,2017-05-02,2017-05-02
20296,EGF-induced FoxO3a nuclear-cytoplasmic pulsing dynamics in mammary epithelial cell lines following treatment with increasing doses of a MEK inhibitor. Dataset 1 of 3: single-cell reporter measurements.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-HA-Venus) expressed in two mammary epithelial cell lines was assessed at the single-cell level using live imaging of cells that were untreated or treated with EGF in the absence or presence of increasing doses of a MEK inhibitor.,,Microscopy/Imaging,,2017-05-02,2017-05-02
20297,EGF-induced FoxO3a nuclear-cytoplasmic pulsing dynamics in mammary epithelial cell lines following treatment with increasing doses of a MEK inhibitor. Dataset 2 of 3: single-cell reporter pulsing metrics.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-HA-Venus) expressed in two mammary epithelial cell lines was assessed at the single-cell level using live imaging of cells that were untreated or treated with EGF in the absence or presence of increasing doses of a MEK inhibitor.,,Analysis,,2017-05-02,2017-05-02
20298,EGF-induced FoxO3a nuclear-cytoplasmic pulsing dynamics in mammary epithelial cell lines following treatment with increasing doses of a MEK inhibitor. Dataset 3 of 3: mean reporter pulsing metrics.,,,The nuclear-cytoplasmic pulsing behavior of a FoxO3a fluorescent reporter (FoxO3aN400-HA-Venus) expressed in two mammary epithelial cell lines was assessed at the single-cell level using live imaging of cells that were untreated or treated with EGF in the absence or presence of increasing doses of a MEK inhibitor.,,Analysis,,2017-05-02,2017-05-02
20299,Growth factor-induced ERK activity and FoxO3a nuclear-cytoplasmic pulsing dynamics in a mammary epithelial cell line. Dataset 1 of 1: single-cell reporter measurements.,,,ERK activity and the nuclear-cytoplasmic pulsing behavior of FoxO3a as measured by a dual fluorescent reporter (EKAREV-FoxO3aN400-mCherry) were assessed in the MCF 10A mammary epithelial cell line at the single-cell level using live imaging of cells that were untreated or treated with one of six growth factors.,,Microscopy/Imaging,,2017-05-02,2017-05-02
20300,Growth factor-induced ERK activity pulsing dynamics in a mammary epithelial cell line. Dataset 1 of 3: single-cell reporter measurements.,,,ERK activity as measured by the EKAREV fluorescent reporter was assessed in the MCF 10A mammary epithelial cell line at the single-cell level using live imaging of cells that were untreated or treated with one of six growth factors.,,Microscopy/Imaging,,2017-05-02,2017-05-02
20301,Growth factor-induced ERK activity pulsing dynamics in a mammary epithelial cell line. Dataset 2 of 3: single-cell reporter pulsing metrics.,,,ERK activity as measured by the EKAREV fluorescent reporter was assessed in the MCF 10A mammary epithelial cell line at the single-cell level using live imaging of cells that were untreated or treated with one of six growth factors.,,Analysis,,2017-05-02,2017-05-02
20302,Growth factor-induced ERK activity pulsing dynamics in a mammary epithelial cell line. Dataset 3 of 3: mean reporter pulsing metrics.,,,ERK activity as measured by the EKAREV fluorescent reporter was assessed in the MCF 10A mammary epithelial cell line at the single-cell level using live imaging of cells that were untreated or treated with one of six growth factors.,,Analysis,,2017-05-02,2017-05-02
20303,LINCS MCF 10A Common Project: Highly-multiplexed imaging by Cyclic Immunofluorescence (CycIF) of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with 8 small molecule perturbagens. Dataset 1 of 6: Cytosolic fluorescent intensity measurements at 24 hr.,,,Cyclic Immunofluorescence (CycIF) is a fluorescence imaging assay used for multiplexed measurement of protein levels and protein phosphorylation states in single cells. The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of one of eight small molecule perturbagens for up to 72 hr before being fixed and subjected to seven cycles of CycIF staining according to the protocol described below.,,Microscopy/Imaging,,2017-05-12,2017-05-12
20304,LINCS MCF 10A Common Project: Highly-multiplexed imaging by Cyclic Immunofluorescence (CycIF) of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with 8 small molecule perturbagens. Dataset 2 of 6: Nuclear fluorescent intensity measurements at 24 hr.,,,Cyclic Immunofluorescence (CycIF) is a fluorescence imaging assay used for multiplexed measurement of protein levels and protein phosphorylation states in single cells. The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of one of eight small molecule perturbagens for up to 72 hr before being fixed and subjected to seven cycles of CycIF staining according to the protocol described below.,,Microscopy/Imaging,,2017-05-12,2017-05-12
20305,LINCS MCF 10A Common Project: Highly-multiplexed imaging by Cyclic Immunofluorescence (CycIF) of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with 8 small molecule perturbagens. Dataset 3 of 6: Cytosolic fluorescent intensity measurements at 48 hr.,,,Cyclic Immunofluorescence (CycIF) is a fluorescence imaging assay used for multiplexed measurement of protein levels and protein phosphorylation states in single cells. The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of one of eight small molecule perturbagens for up to 72 hr before being fixed and subjected to seven cycles of CycIF staining according to the protocol described below.,,Microscopy/Imaging,,2017-05-12,2017-05-12
20306,LINCS MCF 10A Common Project: Highly-multiplexed imaging by Cyclic Immunofluorescence (CycIF) of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with 8 small molecule perturbagens. Dataset 4 of 6: Nuclear fluorescent intensity measurements at 48 hr.,,,Cyclic Immunofluorescence (CycIF) is a fluorescence imaging assay used for multiplexed measurement of protein levels and protein phosphorylation states in single cells. The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of one of eight small molecule perturbagens for up to 72 hr before being fixed and subjected to seven cycles of CycIF staining according to the protocol described below.,,Microscopy/Imaging,,2017-05-12,2017-05-12
20307,LINCS MCF 10A Common Project: Highly-multiplexed imaging by Cyclic Immunofluorescence (CycIF) of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with 8 small molecule perturbagens. Dataset 5 of 6: Cytosolic fluorescent intensity measurements at 72 hr.,,,Cyclic Immunofluorescence (CycIF) is a fluorescence imaging assay used for multiplexed measurement of protein levels and protein phosphorylation states in single cells. The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of one of eight small molecule perturbagens for up to 72 hr before being fixed and subjected to seven cycles of CycIF staining according to the protocol described below.,,Microscopy/Imaging,,2017-05-12,2017-05-12
20308,LINCS MCF 10A Common Project: Highly-multiplexed imaging by Cyclic Immunofluorescence (CycIF) of protein levels and protein phosphorylation states in the MCF 10A breast cell line treated with 8 small molecule perturbagens. Dataset 6 of 6: Nuclear fluorescent intensity measurements at 72 hr.,,,Cyclic Immunofluorescence (CycIF) is a fluorescence imaging assay used for multiplexed measurement of protein levels and protein phosphorylation states in single cells. The MCF 10A breast cell line was plated in 96-well plates and treated with different doses of one of eight small molecule perturbagens for up to 72 hr before being fixed and subjected to seven cycles of CycIF staining according to the protocol described below.,,Microscopy/Imaging,,2017-05-12,2017-05-12
20309,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 1 of 15: End-point cell counts and normalized growth rate inhibition values for all technical replicates of biological replicate 1.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20310,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 2 of 15: End-point cell counts and normalized growth rate inhibition values for all technical replicates of biological replicate 2.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20311,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 3 of 15: End-point cell counts and normalized growth rate inhibition values for all technical replicates of biological replicate 3.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20312,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 4 of 15: End-point mean cell counts and mean normalized growth rate inhibition values for biological replicate 1.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20313,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 5 of 15: End-point mean cell counts and mean normalized growth rate inhibition values for biological replicate 2.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20314,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 6 of 15: End-point mean cell counts and mean normalized growth rate inhibition values for biological replicate 3.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20315,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 7 of 15: End-point dose-response metrics for biological replicate 1.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-05-12,2017-05-12
20316,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 8 of 15: End-point dose-response metrics for biological replicate 2.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-05-12,2017-05-12
20317,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 9 of 15: End-point dose-response metrics for biological replicate 3.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-05-12,2017-05-12
20318,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 10 of 15: Time-dependent mean normalized growth rate inhibition values for biological replicate 1.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20319,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 11 of 15: Time-dependent mean normalized growth rate inhibition values for biological replicate 2.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20320,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 12 of 15: Time-dependent mean normalized growth rate inhibition values for biological replicate 3.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Microscopy/Imaging,,2017-05-12,2017-05-12
20321,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 13 of 15: Time-dependent dose-response metrics for biological replicate 1.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-05-12,2017-05-12
20322,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 14 of 15: Time-dependent dose-response metrics for biological replicate 2.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-05-12,2017-05-12
20323,LINCS MCF 10A Common Project: Rolling-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Dataset 15 of 15: Time-dependent dose-response metrics for biological replicate 3.,,,"To generate measures of the sensitivity of a derivative of the MCF 10A cell line to 8 small molecule perturbagens, we treated cells with single drugs over a minimum 11-point dilution series centered around the GR50 but not exceeding 10 µM and then measured cell number continuously for up to 90 hours after drug exposure.","Hafner, M., Niepel, M., Chung, M., and Sorger, P.K. (2016) Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nat Methods. 13(6):521-527. doi:10.1038/nmeth.3853 PMID: 27135972 PMCID: PMC4887336",Analysis,,2017-05-12,2017-05-12
20324,Tyrosine Kinase Inhibitor-induced cardiotoxicity in hiPSC derived cardiomyocytes - pilot dataset,,,"To define molecular network markers of tyrosine kinase inhibitor-induced cardiotoxicity, we treated human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) with one of four tyrosine kinase inhibitors displaying a range of mild to severe effects on heart function (Erlotinib, Lapatinib, Sorafenib, or Sunitinib) or vehicle control (DMSO). We performed 6 different treatments for each drug, including three doses (1, 3.16 and 10 µM) at 24 hours and the intermediate dose (3.16 µM) for an additional three time points (6h, 72h and 168h). Gene expression changes were assessed at the cell population level using total RNA-Seq, which measured levels of both mRNAs and long non-coding RNAs. Validation of RNA-Seq results was performed by qPCR (HMS-LINCS Dataset #20325).",,RNA-Seq,,2018-03-20,2018-03-23
20325,Tyrosine Kinase Inhibitor-induced cardiotoxicity in hiPSC derived cardiomyocytes - pilot dataset (qPCR validation),,,"To define molecular network markers of tyrosine kinase inhibitor-induced cardiotoxicity, we treated human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) with one of four tyrosine kinase inhibitors displaying a range of mild to severe effects on heart function (Erlotinib, Lapatinib, Sorafenib, or Sunitinib) or vehicle control (DMSO). We performed 3 different treatments for each drug, including two doses (3.16 and 10 µM) at 24 hours and the lower dose (3.16 µM) at 72h. Gene expression changes were assessed at the cell population level using qPCR. This is a validation dataset for RNA-seq HMS-LINCS Dataset #20324.",,qPCR,,2018-03-20,2018-03-23
20326,CH5424802 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20327,BI-D1870 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20328,Torkinib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20329,Ceritinib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20330,Ribociclib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2019-03-15
20331,NG25 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20332,BMX-IN-1 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20333,SCH772984 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20334,THZ1 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20335,JNK-IN-11 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20336,WZ4003 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2017-09-29
20337,ERK5-IN-1 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-09-29,2018-05-31
20338,Abemaciclib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-12-22,2017-12-22
20339,Palbociclib KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-12-22,2017-12-22
20340,QL-XII-47 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-12-22,2017-12-22
20341,AS-252424 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-12-22,2017-12-22
20342,(s)-CR8 KINOMEscan,,"lincs.hms.harvard.edu/kinomescan","The KINOMEscan assay platform is based on a competition binding assay that is run for a compound of interest against each of a panel of 317 to 456 kinases. The assay has three components: a kinase-tagged phage, a test compound, and an immobilized ligand that the compound competes with to displace the kinase. The amount of kinase bound to the immobilized ligand is determined using quantitative PCR of the DNA tag. Results for each kinase are reported as ""Percent of control"", where the control is DMSO and where a 100% result means no inhibition of kinase binding to the ligand in the presence of the compound, and where low percent results mean strong inhibition.","KINOMEscan website: Overview & Assay Principle
Fabian MA, Biggs WH 3rd, Treiber DK, Atteridge CE, Azimioara MD, Benedetti MG, Carter TA, Ciceri P, Edeen PT, Floyd M, Ford JM, Galvin M, Gerlach JL, Grotzfeld RM, Herrgard S, Insko DE, Insko MA, Lai AG, Lelias JM, Mehta SA, Milanov ZV, Velasco AM, Wodicka LM, Patel HK, Zarrinkar PP, Lockhart DJ. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol. 2005 Mar;23(3):329-36. PMID: 15711537",KINOMEscan,,2017-12-22,2017-12-22
20343,"Breast Cancer Profiling Project, Drug Sensitivity phase I: Fixed-cell GR measures of 35 breast cell lines to 34 small molecule perturbagens from library plate I. Dataset 1 of 2: Normalized growth rate inhibition values",,,"We measured the sensitivities of two non-malignant breast cell lines and 33 breast cancer cell lines of which twenty were triple negative, six were hormone receptor positive, four were Her2 amplified, and three were established from triple negative patient-derived xenografts to 34 clinically-relevant small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Microscopy/Imaging,,2018-03-30,2019-05-03
20344,"Breast Cancer Profiling Project, Drug Sensitivity phase I: Fixed-cell GR measures of 35 breast cell lines to 34 small molecule perturbagens from library plate I. Dataset 2 of 2: Calculated dose response metrics",,,"We measured the sensitivities of two non-malignant breast cell lines and 33 breast cancer cell lines of which twenty were triple negative, six were hormone receptor positive, four were Her2 amplified, and three were established from triple negative patient-derived xenografts to 34 clinically-relevant small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Analysis,,2018-03-30,2019-05-03
20345,ReNcell differentiation: Total proteomics during differentiation under basal conditions. Dataset 1 of 3,,,"ReNcell-VM neuroprogenitors were differentiated by growth factor (EGF and FGF) removal for 15 days in culture, giving rise to dopaminergic neurons, astrocytes, and oligodendrocytes. Cells were collected at 10 time points and processed for total proteomics by liquid chromatography mass spectrometry (LC/MS) using 10-plex tandem mass tag (TMT) labelling to achieve deep quantification of proteome dynamics across ~8,900 proteins.",,Proteomics,,2018-06-30,2018-06-30
20346,ReNcell differentiation: Phosphoproteomics during differentiation under basal conditions. Dataset 2 of 3,,,"ReNcell-VM neuroprogenitors were differentiated by growth factor (EGF and FGF) removal for 15 days in culture, giving rise to dopaminergic neurons, astrocytes, and oligodendrocytes. Cells were collected at 10 time points and processed for phosphoproteomics by liquid chromatography mass spectrometry (LC/MS) using 10-plex tandem mass tag (TMT) labelling combined with phosphopeptide enrichment by titanium dioxide (TiO2), allowing deep quantification of proteome dynamics across ~3,500 phospho-proteins (~11,000 sites of phosphorylation).",,Phosphoproteomics,,2018-06-30,2018-06-30
20347,ReNcell differentiation: Total proteomics during differentiation with small molecule perturbagens. Dataset 3 of 3,,,"ReNcell-VM neuroprogenitors were differentiated by growth factor (EGF and FGF) removal for 15 days in culture, giving rise to dopaminergic neurons, astrocytes, and oligodendrocytes. Drugs (Mevastatin and Kenpaullone) previously screened for their promoting effects on neural differentiation or DMSO control were added to the growth factor free maintenance media during the course of differentiation. Cells were collected at 10 time points and processed for total proteomics by liquid chromatography mass spectrometry (LC/MS) using 10-plex tandem mass tag (TMT) labelling to achieve deep quantification of proteome dynamics.",,Proteomics,,2018-06-30,2018-06-30
20348,"Breast Cancer Profiling Project, Gene Expression 1: Baseline mRNA sequencing on 35 breast cell lines",,,"We measured the baseline mRNAseq profiles of two non-malignant breast cell lines and 33 breast cancer cell lines of which twenty were triple negative, six were hormone receptor positive, four were Her2 amplified, and three were established from triple negative patient-derived xenografts.",,RNA-Seq,,2018-07-06,2018-07-06
20349,Tyrosine Kinase Inhibitor-induced cardiotoxicity in hiPSC derived cardiomyocytes - Proteomics,,,"To define protein markers of tyrosine kinase inhibitor-induced cardiotoxicity, we treated human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) with tyrosine kinase inhibitors (TKIs) displaying a range of mild to severe effects on heart function. Two independent cell experiments were performed. In the first experiment, hiPSC-CMs were treated with one of four TKIs (Erlotinib, Lapatinib, Sorafenib and Sunitinib) at 3 μM or a DMSO vehicle-only control in biological replicates (10 samples in total) and harvested at 72 hours for tandem mass tag mass spectrometry. In the second experiment, a different lot of hiPSC-CMs were treated the same way, but samples were collected at both 24 and 72 hours (20 samples in total).
Corresponding gene expression data can be found in datasets 20324 and 20325.",,Proteomics,,2018-07-18,2018-07-18
20350,Breast Cancer Deubiquitinating Enzyme (DUB) Inhibitor Profiling: Fixed-cell GR measures of 21 breast cell lines to 32 small molecule perturbagens. Dataset 1 of 2: Normalized growth rate inhibition values.,,,"We measured the sensitivities of one non-malignant breast cell line and 20 breast cancer cell lines (six triple negative, six hormone receptor positive, five Her2 amplified, and three established from triple negative patient-derived xenografts) to 32 pre-clinical small molecule deubiquitinating enzyme (DUB) inhibitors. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series and then measured cell number and viability after three days of drug exposure.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Microscopy/Imaging,,2018-08-09,2018-08-09
20351,Breast Cancer Deubiquitinating Enzyme (DUB) Inhibitor Profiling: Fixed-cell GR measures of 21 breast cell lines to 32 small molecule perturbagens. Dataset 2 of 2: Calculated dose response metrics.,,,"We measured the sensitivities of one non-malignant breast cell line and 20 breast cancer cell lines (six triple negative, six hormone receptor positive, five Her2 amplified, and three established from triple negative patient-derived xenografts) to 32 pre-clinical small molecule deubiquitinating enzyme (DUB) inhibitors. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series and then measured cell number and viability after three days of drug exposure.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Analysis,,2018-08-09,2018-08-09
20352,Breast Cancer Profiling Project – Proteomics 1: 1 total proteome dataset for a 35-cell line breast cancer panel under basal conditions,,,"We measured the baseline proteomic profiles of two non-malignant breast cell lines and 33 breast cancer cell lines of which twenty were triple negative, six were hormone receptor positive, four were Her2 amplified, and three were established from triple negative patient-derived xenografts.","Rappsilber, J.; Mann, M.; Ishihama, Y., Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nature Protocols 2007, 2 (8), 1896-1906.
Ting, L.; Rad, R.; Gygi, S. P.; Haas, W., MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nature Methods 2011, 8 (11), 937-940.
McAlister, G. C.; Nusinow, D. P.; Jedrychowski, M. P.; Wuhr, M.; Huttlin, E. L.; Erickson, B. K.; Rad, R.; Haas, W.; Gygi, S. P., MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes. Anal Chem 2014, 86 (14), 7150-8.
Eng, J. K.; McCormack, A. L.; Yates, J. R., An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. Journal of the American Society for Mass Spectrometry 1994, 5 (11), 976-989.
",Proteomics,,2018-10-18,2018-12-21
20353,Breast Cancer Profiling Project – Proteomics 2: 1 phosphoproteome dataset (including phosphotyrosine enrichment) for a 35-cell line breast cancer panel under basal conditions,,,"We measured the baseline phosphoproteomic profiles of two non-malignant breast cell lines and 33 breast cancer cell lines of which twenty were triple negative, six were hormone receptor positive, four were Her2 amplified, and three were established from triple negative patient-derived xenografts.","Rappsilber, J.; Mann, M.; Ishihama, Y., Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nature Protocols 2007, 2 (8), 1896-1906.
Ting, L.; Rad, R.; Gygi, S. P.; Haas, W., MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nature Methods 2011, 8 (11), 937-940.
McAlister, G. C.; Nusinow, D. P.; Jedrychowski, M. P.; Wuhr, M.; Huttlin, E. L.; Erickson, B. K.; Rad, R.; Haas, W.; Gygi, S. P., MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes. Anal Chem 2014, 86 (14), 7150-8.
Eng, J. K.; McCormack, A. L.; Yates, J. R., An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. Journal of the American Society for Mass Spectrometry 1994, 5 (11), 976-989.
",Proteomics,,2018-10-18,2018-12-21
20354,"Breast Cancer Profiling Project, Drug Sensitivity phase II: Fixed-cell GR measures of 33 breast cell lines and PDX lines to 16 small molecule perturbagens from library plate II. Dataset 1 of 2: Normalized growth rate inhibition values",,,"We measured the sensitivities of two non-malignant breast cell lines and 31 breast cancer cell lines of which twenty were triple negative, six were hormone receptor positive, five were Her2 amplified, to 16 clinically-relevant small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Microscopy/Imaging,,2019-06-27,2019-06-27
20355,"Breast Cancer Profiling Project, Drug Sensitivity phase II: Fixed-cell GR measures of 33 breast cell lines and PDX lines to 16 small molecule perturbagens from library plate II. Dataset 2 of 2: Calculated dose response metrics",,,"We measured the sensitivities of two non-malignant breast cell lines and 31 breast cancer cell lines of which twenty were triple negative, six were hormone receptor positive, five were Her2 amplified, to 16 clinically-relevant small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Analysis,,2019-06-27,2019-06-27
20358,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Repeat performed by Scientist A in 2019 to assess reproducibility. Dataset 1 of 2: Normalized growth rate inhibition values.,,,"As part of the multi-center study on factors influencing the reproducibility of in vitro drug-response studies, we measured the sensitivities of the MCF 10A cell line to 8 small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure. Replicate experiments were performed at other centers, by the same HMS scientist in 2017 (datasets #20278-20286 ) and by other HMS scientists in 2019 (see datasets #20358-20363). These datasets as well as replicate datasets from other LINCS centers can also be accessed at https://www.synapse.org/#!Synapse:syn18456348/wiki/.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Microscopy/Imaging,,2019-06-27,2019-06-27
20359,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Repeat performed by Scientist B in 2019 to assess reproducibility. Dataset 1 of 2: Normalized growth rate inhibition values.,,,"As part of the multi-center study on factors influencing the reproducibility of in vitro drug-response studies, we measured the sensitivities of the MCF 10A cell line to 8 small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure. Replicate experiments were performed at other centers, and by other HMS scientists in 2017 (datasets #20278-20286 ) and 2019 (datasets #20358-20363). These datasets as well as replicate datasets from other LINCS centers can also be accessed at https://www.synapse.org/#!Synapse:syn18456348/wiki/.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Microscopy/Imaging,,2019-06-27,2019-06-27
20360,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Repeat performed by Scientist C to assess reproducibility. Dataset 1 of 2: Normalized growth rate inhibition values.,,,"As part of the multi-center study on factors influencing the reproducibility of in vitro drug-response studies, we measured the sensitivities of the MCF 10A cell line to 8 small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure. Replicate experiments were performed at other centers, and by other HMS scientists in 2017 (datasets #20278-20286 ) and 2019 (datasets #20358-20363). These datasets as well as replicate datasets from other LINCS centers can also be accessed at https://www.synapse.org/#!Synapse:syn18456348/wiki/.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Microscopy/Imaging,,2019-06-27,2019-06-27
20361,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Repeat performed by Scientist A in 2019 to assess reproducibility. Dataset 2 of 2: Calculated dose response metrics.,,,"As part of the multi-center study on factors influencing the reproducibility of in vitro drug-response studies, we measured the sensitivities of the MCF 10A cell line to 8 small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure. Replicate experiments were performed at other centers, by the same HMS scientist in 2017 (datasets #20278-20286 ) and by other HMS scientists in 2019 (see datasets #20358-20363). These datasets as well as replicate datasets from other LINCS centers can also be accessed at https://www.synapse.org/#!Synapse:syn18456348/wiki/.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Analysis,,2019-06-27,2019-06-27
20362,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Repeat performed by Scientist B in 2019 to assess reproducibility. Dataset 2 of 2: Calculated dose response metrics.,,,"As part of the multi-center study on factors influencing the reproducibility of in vitro drug-response studies, we measured the sensitivities of the MCF 10A cell line to 8 small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure. Replicate experiments were performed at other centers, and by other HMS scientists in 2017 (datasets #20278-20286 ) and 2019 (datasets #20358-20363). These datasets as well as replicate datasets from other LINCS centers can also be accessed at https://www.synapse.org/#!Synapse:syn18456348/wiki/.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Analysis,,2019-06-27,2019-07-10
20363,LINCS MCF 10A Common Project: Fixed-time-point sensitivity measures of the MCF 10A breast cell line to 8 small molecule perturbagens. Repeat performed by Scientist C in 2019 to assess reproducibility. Dataset 2 of 2: Calculated dose response metrics.,,,"As part of the multi-center study on factors influencing the reproducibility of in vitro drug-response studies, we measured the sensitivities of the MCF 10A cell line to 8 small molecule perturbagens. A microscopy-based dose response assay was used to measure drug potency, and to quantify drug efficacy in terms of growth inhibition (GR metrics) and cell death. We treated cells with single drugs over a 9-point ½ log dilution series from a maximum dose not exceeding 10 µM and then measured cell number and viability after three days of drug exposure. Replicate experiments were performed at other centers, and by other HMS scientists in 2017 (datasets #20278-20286 ) and 2019 (datasets #20358-20363). These datasets as well as replicate datasets from other LINCS centers can also be accessed at https://www.synapse.org/#!Synapse:syn18456348/wiki/.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Analysis,,2019-06-27,2019-06-27
20364,Evaluation of the sensitivities of six triple-negative breast cancer (TNBC) cell lines to 23 different PI3K/AKT/mTOR inhibitors or to a MEK inhibitor (trametinib). Dataset 1 of 2: GR values.,,,We measured the sensitivities of six TNBC cell lines to 23 clinical and pre-clinical small molecule inhibitors of kinases in the PI3K/AKT/mTOR signaling pathway and to one inhibitor of MEK. Cells were treated with each drug using a 9-point ½ log dilution series. Live cell counts were measured at the start and end of the 72 hour treatment period using fixed cell microscopy. Drug potency and efficacy were calculated using GR metrics.,"Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Microscopy/Imaging,,2019-11-12,2019-11-12
20365,Evaluation of the sensitivities of six triple-negative breast cancer (TNBC) cell lines to 23 different PI3K/AKT/mTOR inhibitors or to a MEK inhibitor (trametinib). Dataset 2 of 2: GR metrics.,,,We measured the sensitivities of six TNBC cell lines to 23 clinical and pre-clinical small molecule inhibitors of kinases in the PI3K/AKT/mTOR signaling pathway and to one inhibitor of MEK. Cells were treated with each drug using a 9-point ½ log dilution series. Live cell counts were measured at the start and end of the 72 hour treatment period using fixed cell microscopy. Drug potency and efficacy were calculated using GR metrics.,"Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Analysis,,2019-11-12,2019-11-12
20366,"Evaluation of the sensitivity of two triple-negative breast cancer cell lines (HCC1806, HCC70) to a collection of dual mTOR and PI3K-like kinase (PIKK) inhibitors. Dataset 1 of 2: GR values.",,,"We measured the sensitivities of two triple-negative breast cancer cell lines to nine uncharacterized mTOR-PIKK inhibitors, Torin1, Torin2, and the conventional mTOR kinase inhibitor AZD8055 (N=12 drugs). Cells were treated with each drug using a 9-point ½ log dilution series. Live cell counts were measured at the start and end of the 72 hour treatment period using fixed cell microscopy. Drug potency and efficacy were calculated using GR metrics.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Microscopy/Imaging,,2019-11-12,2019-11-12
20367,"Evaluation of the sensitivity of two triple-negative breast cancer cell lines (HCC1806, HCC70) to a collection of dual mTOR and PI3K-like kinase (PIKK) inhibitors. Dataset 2 of 2: GR metrics.",,,"We measured the sensitivities of two triple-negative breast cancer cell lines to nine uncharacterized dual mTOR-PIKK inhibitors, Torin1, Torin2, and the conventional mTOR kinase inhibitor AZD8055 (N=12 drugs). Cells were treated with each drug using a 9-point ½ log dilution series. Live cell counts were measured at the start and end of the 72 hour treatment period using fixed cell microscopy. Drug potency and efficacy were calculated using GR metrics.","Hafner M, Niepel M, Subramanian K, and Sorger PK. Designing drug response experiments and quantifying their results. Curr Protoc Chem Biol 2017 Jun 19;9(2):96-116. doi: 10.1002/cpch.19 PubMed PMID: 28628201.",Analysis,,2019-11-12,2019-11-12
20368,"Targeted metabolomics profiling data (i.e., peak intensity measurements) after acute exposure of BT-549 cells to DMSO or rapamycin, AZD8055 or Torin2 at two doses (100nM, 1000nM) for 6 hours.",,,Recovery and measurement of intracellular polar metabolites from drug-treated breast cancer cells.,"Yuan M, Breitkopf SB, Yang X, Asara JM. A positive/negative ion-switching, targeted mass spectrometry-based metabolomics platform for bodily fluids, cells, and fresh and fixed tissue. Nat Protoc. 2012 Apr 12;7(5):872-81.",Metabolomics,,2019-11-12,2019-11-12
20369,Binding affinity of 6 small molecule JAK inhibitors for 5 kinases,,,"We tested the binding affinity of 6 small molecule JAK inhibitors (Alvocidib, Nintedanib, Bosutinib, Tofacitinib, Baricitinib, and S-Ruxolitinib) for JAK and other kinases (JAK1, JAK2, JAK3, TYK2 and DCLK3).","www.discoverx.com/services/drug-discovery-development-services/kinase-profiling/kinomescan/kdelect",Affinity Data,,2019-10-16,2019-10-16
20370,Breast Cancer Profiling Project – Proteomics 3: 1 total proteome dataset for a 27-cell line breast cancer panel under basal conditions,,,"We measured the baseline proteomic profiles of four non-malignant breast cell lines and 23 breast cancer cell lines of which three were triple negative, ten were hormone receptor positive, nine were Her2 amplified, and one was established from a triple negative patient-derived xenograft.","Rappsilber, J.; Mann, M.; Ishihama, Y., Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nature Protocols 2007, 2 (8), 1896-1906
Ting, L.; Rad, R.; Gygi, S. P.; Haas, W., MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nature Methods 2011, 8 (11), 937-940
McAlister, G. C.; Nusinow, D. P.; Jedrychowski, M. P.; Wuhr, M.; Huttlin, E. L.; Erickson, B. K.; Rad, R.; Haas, W.; Gygi, S. P., MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes. Anal Chem 2014, 86 (14), 7150-8
Eng, J. K.; McCormack, A. L.; Yates, J. R., An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. Journal of the American Society for Mass Spectrometry 1994, 5 (11), 976-989",Proteomics,,2020-03-02,2020-03-02
20371,Quantitative data for differentially expressed phosphopeptides in MCF7 cells treated with palbociclib or abemaciclib at either 0.3 or 3.0 μM and untreated controls,,"Publication Summary","Total phosphoproteomics of MCF7 cells treated with Abemaciclib, Palbociclib (0.3 or 3 µM), or DMSO control for one hour. Log2 fold change data are provided.","Rappsilber, J.; Mann, M.; Ishihama, Y., Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nature Protocols 2007, 2 (8), 1896-1906.
Ting, L.; Rad, R.; Gygi, S. P.; Haas, W., MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nature Methods 2011, 8 (11), 937-940.
McAlister, G. C.; Nusinow, D. P.; Jedrychowski, M. P.; Wuhr, M.; Huttlin, E. L.; Erickson, B. K.; Rad, R.; Haas, W.; Gygi, S. P., MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes. Anal Chem 2014, 86 (14), 7150-8.
Eng, J. K.; McCormack, A. L.; Yates, J. R., An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. Journal of the American Society for Mass Spectrometry 1994, 5 (11), 976-989.",Phosphoproteomics,,2020-06-24,2020-06-24
20372,"mRNA-seq gene expression data for seven cell lines treated with one of three CDK4/6 inhibitors at 0.3, 1.0, or 3.0 μM for 6 or 24 hours",,"Publication Summary","To compare the mechanisms of action of palbociclib, ribociclib, and abemaciclib we performed transcriptional profiling (mRNA-seq) on a panel of seven breast cancer cell lines following 6 or 24 hours of exposure to 0.3, 1, or 3 μM of drug. Log2 fold change data are provided.",,RNA-Seq,,2020-06-24,2020-06-24
20373,"DGE-seq Gene expression data for 7 breast cancer cell lines treated with abemaciclib, palbociclib, ribociclib at 0.1, 0.3, 1, or 3 μM, or alvocidib at 0.1 or 1 μM for 6 hours",,"Publication Summary","We collected mRNA-seq data using the high-throughput, low-cost RNA sequencing method 3’ Digital Gene Expression (DGE-seq) for seven breast cancer cell lines that were exposed for 6 hours to palbociclib, ribociclib, or abemaciclib at four concentrations or to alvocidib at 2 concentrations. Log2 fold change data are provided","Soumillon, M., Cacchiarelli, D., Semrau, S., van Oudenaarden, A., and Mikkelsen, T.S. (2014). Characterization of directed differentiation by high-throughput single-cell RNA-Seq. BioRxiv.",RNA-Seq,,2020-06-24,2020-06-24