A Chemical Probe for the Methyl Transferase PRMT5 with a Novel Binding Mode

[Image: see text] Protein arginine methyltransferase 5 (PRMT5) is an enzyme that can symmetrically dimethylate arginine residues in histones and nonhistone proteins by using S-adenosyl methionine (SAM) as the methyl donating cofactor. We have designed a library of SAM analogues and discovered potent...

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Detaylı Bibliyografya
Yayımlandı:ACS Med Chem Lett
Asıl Yazarlar: Pande, Vineet, Sun, Weimei, Beke, Lijs, Berthelot, Didier, Brehmer, Dirk, Brown, David, Corbera, Jordi, Irving, Steve, Meerpoel, Lieven, Nys, Thomas, Parade, Marc, Robinson, Colin, Sommen, Cois, Viellevoye, Marcel, Wu, Tongfei, Thuring, Jan Willem
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: American Chemical Society 2020
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC7667828/
https://ncbi.nlm.nih.gov/pubmed/33214833
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acsmedchemlett.0c00355
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