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J Med Chem. 2015 Feb 26;58(4):1596-629. doi: 10.1021/jm501234a. Epub 2014 Dec 2.

Selective inhibitors of protein methyltransferases.

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Department of Structural and Chemical Biology, ‡Department of Oncological Sciences, §Department of Pharmacology and Systems Therapeutics, Icahn School of Medicine at Mount Sinai , 1425 Madison Avenue, New York, New York 10029, United States.


Mounting evidence suggests that protein methyltransferases (PMTs), which catalyze methylation of histone and nonhistone proteins, play a crucial role in diverse biological processes and human diseases. In particular, PMTs have been recognized as major players in regulating gene expression and chromatin state. PMTs are divided into two categories: protein lysine methyltransferases (PKMTs) and protein arginine methyltransferases (PRMTs). There has been a steadily growing interest in these enzymes as potential therapeutic targets and therefore discovery of PMT inhibitors has also been pursued increasingly over the past decade. Here, we present a perspective on selective, small-molecule inhibitors of PMTs with an emphasis on their discovery, characterization, and applicability as chemical tools for deciphering the target PMTs' physiological functions and involvement in human diseases. We highlight the current state of PMT inhibitors and discuss future directions and opportunities for PMT inhibitor discovery.

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