| Literature DB >> 25399643 |
Rand M Miller1, Jack Taunton2.
Abstract
Protein kinase inhibitors are an important class of therapeutics. In addition, selective kinase inhibitors can often reveal unexpected biological insights, augmenting genetic approaches and playing a decisive role in preclinical target validation studies. Nevertheless, developing protein kinase inhibitors with sufficient selectivity and pharmacodynamic potency presents significant challenges. Targeting noncatalytic cysteines with covalent inhibitors is a powerful approach to address both challenges simultaneously. Here, we describe our efforts to design irreversible and reversible electrophilic inhibitors with varying degrees of kinase selectivity. Highly selective covalent inhibitors have been used to elucidate the roles of p90 ribosomal protein S6 kinases in animal models of atherosclerosis and diabetes. By contrast, semipromiscuous covalent inhibitors have revealed new therapeutic targets in disease-causing parasites and have shown utility as chemoproteomic probes for interrogating kinase occupancy in living cells.Entities:
Keywords: Chemoproteomic; Covalent inhibitors; Cysteine; Hypothemycin; Kinase inhibitors; MSK; RSK; T. brucei
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Year: 2014 PMID: 25399643 PMCID: PMC4265651 DOI: 10.1016/B978-0-12-397918-6.00004-5
Source DB: PubMed Journal: Methods Enzymol ISSN: 0076-6879 Impact factor: 1.600