ArticleACS medicinal chemistry letters2026
Structure-Guided Discovery of Novel Highly Potent and Selective MTA-Cooperative PRMT5 Inhibitors.
Article in ACS medicinal chemistry letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Methylthioadenosine (MTA) accumulation inhibits the protein arginine methyltransferase 5 (PRMT5), rendering cancers harboring methylthioadenosine phosphorylase (MTAP) deletion vulnerable; thus, PRMT5 inhibitors hold promise for treating these cancers. In this letter, a structure-guided design approach yielded many novel highly potent and selective MTA-cooperative PRMT5 inhibitors featuring a core structure of 4-amino-
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