Sanvitale, Caroline E. Kerr, Georgina Chaikuad, Apirat Ramel, Marie-Christine H. Mohedas, Agustin Reichert, Sabine Wang, You Triffitt, James T. Cuny, Gregory D. Yu, Paul B. S. Hill, Caroline Bullock, Alex N. Kinome-wide selectivity of K02288 and LDN-193189. <p>(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 <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0062721#pone.0062721.s003" target="_blank">Table S2</a>. (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.; <a href="http://www.cellsignal.com" target="_blank">www.cellsignal.com</a>).</p> Biochemistry;chemical biology;drug discovery;proteins;Small molecules;biophysics;Biomacromolecule-ligand interactions;Protein chemistry;developmental biology;morphogenesis;Molecular cell biology;Signal transduction;Signaling cascades;Protein kinase signaling cascade;TGF-beta signaling cascade;Membrane receptor signaling;Signaling pathways;medicinal chemistry;selectivity;k02288 2013-04-30
    https://plos.figshare.com/articles/figure/_Kinome_wide_selectivity_of_K02288_and_LDN_193189_/694794
10.1371/journal.pone.0062721.g002