%0 Figure %A Sanvitale, Caroline E. %A Kerr, Georgina %A Chaikuad, Apirat %A Ramel, Marie-Christine %A H. Mohedas, Agustin %A Reichert, Sabine %A Wang, You %A Triffitt, James T. %A Cuny, Gregory D. %A Yu, Paul B. %A S. Hill, Caroline %A Bullock, Alex N. %D 2013 %T Kinome-wide selectivity of K02288 and LDN-193189. %U https://plos.figshare.com/articles/figure/_Kinome_wide_selectivity_of_K02288_and_LDN_193189_/694794 %R 10.1371/journal.pone.0062721.g002 %2 https://plos.figshare.com/ndownloader/files/1049679 %K Biochemistry %K chemical biology %K drug discovery %K proteins %K Small molecules %K biophysics %K Biomacromolecule-ligand interactions %K Protein chemistry %K developmental biology %K morphogenesis %K Molecular cell biology %K Signal transduction %K Signaling cascades %K Protein kinase signaling cascade %K TGF-beta signaling cascade %K Membrane receptor signaling %K Signaling pathways %K medicinal chemistry %K selectivity %K k02288 %X

(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).

%I PLOS ONE