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Article

Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4).

The Biochemical journal - 28 Feb 2020

Gunnell Emma A, Al-Noori Alaa, Muhsen Usama, Davies Clare C, Dowden James, Dreveny Ingrid

Abstract excerpt

Attenuating the function of protein arginine methyltransferases (PRMTs) is an objective for the investigation and treatment of several diseases including cardiovascular disease and cancer. Bisubstrate inhibitors that simultaneously target binding sites for arginine substrate and the cofactor (S-adenosylmethionine (SAM)) have potential utility, but structural information on their binding is required for their...

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Identifiers

PMID: 32011657
DOI: 10.1042/BCJ20190826
PMCID: PMC7054760

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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