ArticleJournal of medicinal chemistry2013
Exploiting an allosteric binding site of PRMT3 yields potent and selective inhibitors.
Article in Journal of medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 72 citations in OpenAlex.
- Targeting PRMTs with small-molecule inhibitors: a comprehensive review.RSC medicinal chemistry · 2026Review
- Discovery of a potent and orally bioavailable type Ⅰ PRMTs inhibitor for triple-negative breast cancer treatment.Acta pharmacologica Sinica · 2026Article
- PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer.Journal of cellular and molecular medicine · 2025Review
- PRMT3 at the crossroads of inflammation: dual roles in metabolic reprogramming and immune dysregulation in chronic diseases.Frontiers in immunology · 2025Review
- Chemical probes and methods for the study of protein arginine methylation.RSC chemical biology · 2023Review
- Naturally occurring cancer-associated mutations disrupt oligomerization and activity of protein arginine methyltransferase 1 (PRMT1).The Journal of biological chemistry · 2021Article
- Broad Scope and High-Yield Access to Unsymmetrical Acyclic [Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- A Pan-Inhibitor for Protein Arginine Methyltransferase Family Enzymes.Biomolecules · 2021Article
- A First-in-Class, Highly Selective and Cell-Active Allosteric Inhibitor of Protein Arginine Methyltransferase 6.Journal of medicinal chemistry · 2021Article
- Allosteric Modulation of Protein Arginine Methyltransferase 5 (PRMT5).ACS medicinal chemistry letters · 2020Article
- Discovery of a First-in-Class Protein Arginine Methyltransferase 6 (PRMT6) Covalent Inhibitor.Journal of medicinal chemistry · 2020Article
- Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level.Cellular and molecular life sciences : CMLS · 2019Review
- Article
- Inhibitors of Protein Methyltransferases and Demethylases.Chemical reviews · 2018Review
- Discovery of Potent and Selective Allosteric Inhibitors of Protein Arginine Methyltransferase 3 (PRMT3).Journal of medicinal chemistry · 2018Article
- Allosteric regulation of epigenetic modifying enzymes.Current opinion in chemical biology · 2017Review
- The winding path of protein methylation research: milestones and new frontiers.Nature reviews. Molecular cell biology · 2017Review
- Targeting human SET1/MLL family of proteins.Protein science : a publication of the Protein Society · 2017Review
- Discovery of a Potent, Selective, and Cell-Active Dual Inhibitor of Protein Arginine Methyltransferase 4 and Protein Arginine Methyltransferase 6.Journal of medicinal chemistry · 2016Article
- Epigenetic modifiers in immunotherapy: a focus on checkpoint inhibitors.Immunotherapy · 2016Review
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein arginine methyltransferases (PRMTs) play an important role in diverse biological processes. Among the nine known human PRMTs, PRMT3 has been implicated in ribosomal biosynthesis via asymmetric dimethylation of the 40S ribosomal protein S2 and in cancer via interaction with the DAL-1 tumor suppressor protein. However, few selective inhibitors of PRMTs have been discovered. We recently disclosed the first selective PRMT3 inhibitor, which occupies a novel allosteric binding site and is noncompetitive with both the peptide substrate and cofactor. Here we report comprehensive structure-activity relationship studies of this series, which resulted in the discovery of multiple PRMT3 inhibitors with submicromolar potencies. An X-ray crystal structure of compound 14u in complex with PRMT3 confirmed that this inhibitor occupied the same allosteric binding site as our initial lead compound. These studies provide the first experimental evidence that potent and selective inhibitors can be created by exploiting the allosteric binding site of PRMT3.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.