Chemical phosphoproteomics reveals kinase network topologies associated to genotypes and phenotypes of cancer cells.

We compare the in vitro specificity profiles of several kinase inhibitors with their effects on cellular phosphoproteomes. For this aim, we developed an algorithm which utilizes information on kinase inhibitor selectivity to determine the most probable kinase(s) acting upstream of phosphorylation sites present in phosphoproteomics data obtained from cancer cells treated with kinase inhibitors.