A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models

NATURE CHEMICAL BIOLOGY(2015)

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摘要
Protein methyltransferase PRMT5 symmetrically dimethylates arginine residues in proteins, including histones, and has been associated with tumorigenesis. The identification of EPZ015666 as a potent chemical probe of PRMT5 could promote understanding of the role of PRMT5 in human disease both in cells and in vivo .
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nature chemical biology, science
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