A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models
NATURE CHEMICAL BIOLOGY(2015)
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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