Figure_2.tif (1.07 MB)
Kinome-wide selectivity of K02288 and LDN-193189.
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posted on 2013-04-30, 01:19 authored by Caroline E. Sanvitale, Georgina Kerr, Apirat Chaikuad, Marie-Christine Ramel, Agustin H. Mohedas, Sabine Reichert, You Wang, James T. Triffitt, Gregory D. Cuny, Paul B. Yu, Caroline S. Hill, Alex N. Bullock(A) Some 200 human kinases were individually ranked according to their enzymatic inhibition by K02288 or LDN-193189 present at 0.1 or 1 µM concentration (screening performed by Nanosyn). Complete screening data are shown in supplemental Table S2. (B) Percent inhibition values for each kinase in the presence of 1 µM K02288 were plotted against those using 1 µM LDN-193189. There is little correlation between those kinases inhibited by K02288 and by LDN-193189. Overall, fewer kinases were inhibited by K02288. (C) Kinome tree visualization of inhibitor profiling showing the appearance of target family clusters (illustration reproduced courtesy of Cell Signaling Technology, Inc.; www.cellsignal.com).
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Biochemistrychemical biologydrug discoveryproteinsSmall moleculesbiophysicsBiomacromolecule-ligand interactionsProtein chemistrydevelopmental biologymorphogenesisMolecular cell biologySignal transductionSignaling cascadesProtein kinase signaling cascadeTGF-beta signaling cascadeMembrane receptor signalingSignaling pathwaysmedicinal chemistryselectivityk02288
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