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• W2330712912 abstract "The protein arginine methyltransferases PRMT7 and PRMT5, respectively, monomethylate and symmetrically dimethylate arginine side-chains of proteins involved in diverse cellular mechanisms, including chromatin-mediated control of gene transcription, splicing, and the RAS to ERK transduction cascade. It is believed that PRMT5 and PRMT7 act in conjunction to methylate their substrates, and genetic deletions support the notion that these enzymes derepress cell proliferation and migration in cancer. Using available structures of PRMT5, we designed DS-437, a PRMT5 inhibitor with an IC50 value of 6 μM against both PRMT5 and PRMT7 that is inactive against 29 other human protein-, DNA-, and RNA-methyltransferases and inhibits symmetrical dimethylation of PRMT5 substrates in cells. This compound behaves as a cofactor competitor and represents a valid scaffold to interrogate the potential of the PRMT5-PRMT7 axis as a target for therapy." @default.
• W2330712912 created "2016-06-24" @default.
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• W2330712912 date "2015-03-05" @default.
• W2330712912 modified "2023-10-16" @default.
• W2330712912 title "Discovery of a Dual PRMT5–PRMT7 Inhibitor" @default.
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• W2330712912 doi "https://doi.org/10.1021/ml500467h" @default.
• W2330712912 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4394339" @default.
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