Evidence map›Paper›PMID 41730877›Full record

ArticleNature communications2026

PRMT5 in mitochondria regulates mtDNA stability through TFAM arginine methylation.

Sangheeta Bhattacharjee, Sayan Das, Banhi Chowdhury, Benu Brata Das

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
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.

Sangheeta Bhattacharjee *Laboratory of Molecular Biology, School of Biological Sciences, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
Sayan Das *Laboratory of Molecular Biology, School of Biological Sciences, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.ORCID http://orcid.org/0009-0000-5509-8971
Banhi ChowdhuryLaboratory of Molecular Biology, School of Biological Sciences, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
Benu Brata DasLaboratory of Molecular Biology, School of Biological Sciences, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India. pcbbd@iacs.res.in.ORCID http://orcid.org/0000-0003-2519-7105

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methyltransferase 5 (PRMT5) catalyzes arginine methylation and regulates cellular functions such as proliferation, RNA splicing, and nuclear DNA damage response. This study uncovers that a fraction of nuclear-encoded PRMT5 localizes to the mitochondria, which is critical for maintaining mitochondrial DNA (mtDNA) homeostasis. PRMT5 knockout (PRMT5

Indexed as

ArginineDNA-Binding ProteinsDNA, MitochondrialMitochondriaMitochondrial ProteinsProtein-Arginine N-MethyltransferasesTranscription FactorsAnimalsHumansMethylationArginineDNA-Binding ProteinsDNA, MitochondrialMitochondrial ProteinsPRMT5 protein, humanPrmt5 protein, mouseProtein-Arginine N-MethyltransferasesTFAM protein, humanTranscription Factors

Identifiers

PMID41730877
PMCPMC13040009

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.