Evidence map›Paper›PMID 42908009›Full record

ReviewEpigenetics & chromatin2026

Protein arginine methyltransferase crosstalk: decoding the synergistic-antagonistic axis in cancer therapy.

Yu Han, Lie Ma, Xiangyu Ma, Baiqu Huang

Abstract readReview
In one paragraph

Review in Epigenetics & chromatin, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Yu HanCollege of Medicine, Xi'an International University, Xi'an, 710077, China. hyml1994@163.com.ORCID http://orcid.org/0009-0003-5691-8742
Lie MaThe Key Laboratory of Molecular Epigenetics of Ministry of Education (MOE), Northeast Normal University, Changchun, 130024, China.ORCID http://orcid.org/0000-0001-5239-9330
Xiangyu MaShandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, 250021, Shandong, China.
Baiqu HuangThe Key Laboratory of Molecular Epigenetics of Ministry of Education (MOE), Northeast Normal University, Changchun, 130024, China.

Funding

Initiation Funds for High-level Talents Program of Xi'an International University XAIU202588
6 · The paper itself

Abstract

backgroundProtein arginine methyltransferases (PRMTs) are abnormally expressed in various tumors and participate in multiple tumorigenic processes, including proliferation, metastasis, drug resistance, and metabolic reprogramming. However, in recent years, with the in-depth exploration of the functions of PRMTs and their associated tumorigenic mechanisms, the complex crosstalk relationships among different PRMTs have been increasingly highlighted. Different PRMTs may not only exhibit synergistic tumor-promoting effects but also demonstrate antagonistic effects in certain tumor biological functions. This makes the scientific and rational use of PRMT inhibitors a key factor for effective tumor suppression. MAIN BODY: The review aims to provide a comprehensive overview of the functional roles of different PRMTs in tumors, with a particular focus on their cross-functional regulatory mechanisms within the complex regulatory networks of tumors. Meanwhile, it summarizes the current research progress on PRMT inhibitors and elaborates on some limitations associated with PRMT-targeted therapy. Through the integration and analysis of existing research findings, this review offers a novel perspective on the complex regulatory roles of different PRMTs jointly participating in biological functions.

conclusionsAccumulating evidence suggests that implementing a multi-targeted intervention strategy for PRMTs and conducting stage-specific inhibition of PRMTs according to the progression stage of tumor development hold the potential to exert more significant therapeutic effects in the field of tumor treatment.

Indexed as

NeoplasmsProtein-Arginine N-MethyltransferasesAnimalsAntineoplastic AgentsEnzyme InhibitorsHumansAntineoplastic AgentsEnzyme InhibitorsProtein-Arginine N-MethyltransferasesAntagonistic effectPRMT inhibitorsProtein arginine methyltransferasesSynergistic effect

Identifiers

PMID42908009
PMCPMC13688906

What OpenQuestion holds

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Registered trials

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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.