title: Quantitative proteomics of kinase inhibitor targets and mechanisms.
abstract: Small molecule inhibitors of protein kinases are key tools for signal transduction research and represent a major class of targeted drugs. Recent developments in quantitative proteomics enable an unbiased view on kinase inhibitor selectivity and modes of action in the biological context. While chemical proteomics techniques utilizing quantitative mass spectrometry interrogate both target specificity and affinity in cellular extracts, proteome-wide phosphorylation analyses upon kinase inhibitor treatment identify signal transduction pathway and network regulation in an unbiased manner. Thus, critical information is provided to promote new insights into mechanisms of kinase signaling and their relevance for kinase inhibitor drug discovery.
authors.affiliation: Evotec (München) GmbH , Am Klopferspitz 19a, 82152 Martinsried, Germany.
authors.forename: Henrik
authors.initials: H
authors.lastname: Daub
mesh_terms: D000818:Animals; D055808:Drug Discovery / Q000379:methods*; D004800:Enzymes, Immobilized / Q000737:chemistry; D006801:Humans; D010766:Phosphorylation; D011485:Protein Binding; D047428:Protein Kinase Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction; D054852:Small Molecule Libraries / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D004800:Enzymes, Immobilized; D047428:Protein Kinase Inhibitors; D054852:Small Molecule Libraries; D011494:Protein Kinases