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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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| Udgivet i: | ACS Med Chem Lett |
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| Main Authors: | , , , , , , , , , , , , , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Chemical
Society
2020
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| Online adgang: | 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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