ArticleFrontiers in chemistry2025
Discovery of novel PRMT1 inhibitors: a combined approach using AI classification model and traditional virtual screening.
Article in Frontiers in chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Targeting PRMTs with small-molecule inhibitors: a comprehensive review.RSC medicinal chemistry · 2026Review
- Negative allosteric regulation of protein arginine methyltransferase 1 (PRMT1) through half-of-sites reactivity.The Journal of biological chemistry · 2026Article
- PRMT5 is a prognostic-related biomarker associated with the tumor immune microenvironment in lung adenocarcinoma.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026Article
- Targeting the PRMT1 axis in cancer: from epigenetic plasticity to contextual therapeutic interventions.Frontiers in oncology · 2026Review
- Unveiling molecular moieties through hierarchical Grad-CAM graph explainability.BMC bioinformatics · 2025Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein arginine methyltransferases (PRMTs) play crucial roles in gene regulation, signal transduction, mRNA splicing, DNA repair, cell differentiation, and embryonic development. Due to its significant impact, PRMTs is a target for the prevention and treatment of various diseases. Among the PRMT family, PRMT1 is the most abundant and ubiquitously expressed in the human body. Although extensive research has been conducted on PRMT1, the reported inhibitors have not successfully passed clinical trials. In this study, deep learning was employed to analyze the characteristics of existing PRMTs inhibitors and to construct a classification model for PRMT1 inhibitors. Through a classification model and molecular docking, a series of potential PRMT1 inhibitors were identified. The representative compound (compound 156) demonstrates stable binding to the PRMT1 protein by molecular hybridization, molecular dynamics simulations, and binding free energy analyses. The study discovered novel scaffolds for potential PRMT1 inhibitors.
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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 Socratic graph.