ReviewCancer letters2025
Cracking PRMT5: Mechanistic insights, clinical advances, and AI-driven strategies.
Review in Cancer letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- Review
- From Laboratory to Patient Access: A Scoping Review of the Multi-Dimensional Challenges in Drug Repurposing.Pharmacy (Basel, Switzerland) · 2026Review
- Protein arginine methyltransferases in cancer: mechanisms, functions, and therapeutic opportunities.Journal of biomedical science · 2026Review
- Exploring structural diversity and dynamic stability of small-molecule PRMT5 inhibitors through machine learning-based QSAR and molecular modelling.Molecular diversity · 2026Article
- Celebrating the 40-year milestone: NF-ĸB in oncoimmunity.Cancer letters · 2026Review
- Post-translational modifications in retinoblastoma: mechanisms, immune regulation, and therapeutic opportunities.Frontiers in immunology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Protein arginine methyltransferase 5 (PRMT5) is a type II methyltransferase that catalyzes symmetric arginine dimethylation on histone and non-histone proteins, thereby modulating transcription, RNA splicing, and diverse signaling pathways. Dysregulated PRMT5 activity contributes to tumorigenesis and multiple pathological conditions, positioning it as a high-priority therapeutic target with strong translational relevance. Current inhibitor strategies encompass S-adenosylmethionine (SAM)-competitive agents, substrate-competitive and substrate-dependent modulators, dual-binding and methylthioadenosine (MTA)-cooperative inhibitors, PROTAC-based degraders, repurposed FDA-approved drugs, and rational combination regimens designed to improve efficacy or overcome resistance. These approaches differ in mechanism of action, tumor specificity, and toxicity profiles. This review highlights their mechanistic underpinnings, clinical development, and inherent limitations, while also examining the potential application of PRMT5 inhibitors in non-oncologic indications, including ocular and cardiovascular diseases. Finally, it explores the role of biomedical informatics and artificial intelligence (AI) in drug repurposing and outlines future directions for advancing PRMT5-targeted therapeutics.
Indexed as
Identifiers
What OpenQuestion holds
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.