Evidence map›Paper›PMID 31101937›Full record

ReviewCellular and molecular life sciences : CMLS2019

Cellular consequences of arginine methylation.

Benjamin M Lorton, David Shechter

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing 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

88 citing papers in PubMed.

  1. Article
  2. Article
  3. The GNMT N-terminus Couples Folate Feedback to Methyl-donor Homeostasis.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. The MethyltransferaseJournal of fungi (Basel, Switzerland) · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

28 more citing papers are in PubMed but not listed here.

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

2 authors.

Benjamin M LortonDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, 10461, USA.
David ShechterDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. david.shechter@einstein.yu.edu.ORCID http://orcid.org/0000-0001-9388-6004

Funding

PRMT5-MEP50 Histone Arginine Methylation in Early DevelopmentR01GM108646 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SHECHTER, DAVID · 2014 to 2022
$3.2M
American Lung Association LCD-564723NIGMS NIH HHS R01 GM108646NIH HHS R01GM108646The SAS Foundation for Cancer Research HHS-0007-16SF
6 · The paper itself

Abstract

Arginine methylation is a ubiquitous post-translational modification. Three predominant types of arginine-guanidino methylation occur in Eukarya: mono (Rme1/MMA), symmetric (Rme2s/SDMA), and asymmetric (Rme2a/ADMA). Arginine methylation frequently occurs at sites of protein-protein and protein-nucleic acid interactions, providing specificity for binding partners and stabilization of important biological interactions in diverse cellular processes. Each methylarginine isoform-catalyzed by members of the protein arginine methyltransferase family, Type I (PRMT1-4,6,8) and Type II (PRMT5,9)-has unique downstream consequences. Methylarginines are found in ordered domains, domains of low complexity, and in intrinsically disordered regions of proteins-the latter two of which are intimately connected with biological liquid-liquid phase separation. This review highlights discoveries illuminating how arginine methylation affects genome integrity, gene transcription, mRNA splicing and mRNP biology, protein translation and stability, and phase separation. As more proteins and processes are found to be regulated by arginine methylation, its importance for understanding cellular physiology will continue to grow.

Indexed as

ActinsArginineChromatinDNA RepairHistonesHumansMethylationProtein-Arginine N-MethyltransferasesRibonucleoproteinsRNA SplicingActinsArginineChromatinHistonesProtein-Arginine N-MethyltransferasesRibonucleoproteinsCrosstalkHistonesLiquid–liquid phase separationProtein arginine methyltransferaseRibonucleoprotein

Identifiers

PMID31101937
PMCPMC6642692

What OpenQuestion holds

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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.