Evidence map›Paper›PMID 32629172›Full record

ReviewDrug discovery today2020

Modulating the modulators: regulation of protein arginine methyltransferases by post-translational modifications.

Antja-Voy Hartley, Tao Lu

Open access · hybridAbstract readReview
In one paragraph

Review in Drug discovery today, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer.Journal of cellular and molecular medicine · 2025
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Protein arginine methylation in transcription and epigenetic regulation.Frontiers in epigenetics and epigenomics · 2023
    Review
  12. Frontiers in microbiology · 2023
    Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
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 at 2 institutions in 1 country.

Antja-Voy HartleyDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202, USA; Department of Medicine, Dana-Farber Cancer Institute, Harvard Medical School, 450 Brookline Avenue, Boston, MA 02215, USA.
Tao LuDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202, USA; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202, USA; Department of Medical and Molecular Genetics, 975 W. Walnut Street, Indianapolis, IN 46202, USA. Electronic address: lut@iu.edu.
Harvard University · USIndiana University School of Medicine

Funding

Gene-specific responses to NF-kB through lysine and arginine methylation of p65R01GM120156 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI LU, TAO · 2017 to 2021
$1.5M
Impact of NF-kB methylation on chemoresistance and metastasis of breast cancerR03CA223906 · NCI · INDIANA UNIVERSITY INDIANAPOLIS · PI LU, TAO, NAKSHATRI, HARIKRISHNA · 2018 to 2019
$157k
NCI NIH HHS R03 CA223906NIGMS NIH HHS R01 GM120156
6 · The paper itself

Abstract

The therapeutic potential of targeting protein arginine methyltransferases (PRMTs) is inextricably linked to their key roles in various cellular functions, including splicing, proliferation, cell cycle regulation, differentiation, and DNA damage signaling. Unsurprisingly, the development of inhibitors against these enzymes has become a rapidly expanding research area. However, effective targeting of PRMTs requires a deeper understanding of the mechanistic details behind their regulation at multiple levels, involving those mechanisms that alter their activity, interactions, and localization. Recently, post-translational modifications (PTMs) of PRMTs have emerged as another crucial aspect of this regulation. Here, we review the regulatory role of PTMs in the activity and function of PRMTs, with emphasis on the contribution of these PTMs to pathological states, such as cancer.

Indexed as

Protein Processing, Post-TranslationalArginineHumansMethylationProtein-Arginine N-MethyltransferasesArginineProtein-Arginine N-Methyltransferases

Identifiers

PMID32629172
PMCPMC7572788
OpenAlexW3038498627

What OpenQuestion holds

Textmetadata
LicenceTDM
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.