Evidence map›Paper›PMID 32379587›Full record

ReviewCurrent protein & peptide science2020

Non-Histone Arginine Methylation by Protein Arginine Methyltransferases.

Ayad A Al-Hamashi, Krystal Diaz, Rong Huang

Open access · greenAbstract readReview
In one paragraph

Review in Current protein & peptide science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

38 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
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  15. Targeting PRMT7-mediated monomethylation of MAVS enhances antiviral innate immune responses and inhibits RNA virus replication.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Onametostat, a PfPRMT5 inhibitor, exhibits antimalarial activity toAntimicrobial agents and chemotherapy · 2024
    Article
  17. Review
  18. Epigenetic Regulation of Fungal Secondary Metabolism.Journal of fungi (Basel, Switzerland) · 2024
    Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Ayad A Al-HamashiDepartment of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907, United States.
Krystal DiazDepartment of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907, United States.
Rong HuangDepartment of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907, United States.
Purdue University West Lafayette · US

Funding

Protein N-terminal Methylation Mechanisms and InhibitionR01GM117275 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI HUANG, RONG · 2016 to 2025
$3.2M
Discovery of small molecule inhibitors for protein N-terminal methyltransferaseU01CA214649 · NCI · PURDUE UNIVERSITY · PI HUANG, RONG · 2017 to 2019
$1.1M
NCI NIH HHS U01 CA214649NIGMS NIH HHS R01 GM117275
6 · The paper itself

Abstract

Protein arginine methyltransferase (PRMT) enzymes play a crucial role in RNA splicing, DNA damage repair, cell signaling, and differentiation. Arginine methylation is a prominent posttransitional modification of histones and various non-histone proteins that can either activate or repress gene expression. The aberrant expression of PRMTs has been linked to multiple abnormalities, notably cancer. Herein, we review a number of non-histone protein substrates for all nine members of human PRMTs and how PRMT-mediated non-histone arginine methylation modulates various diseases. Additionally, we highlight the most recent clinical studies for several PRMT inhibitors.

Indexed as

Protein Processing, Post-TranslationalAntineoplastic AgentsArginineCardiovascular DiseasesEnzyme InhibitorsEpigenesis, GeneticHistonesHumansMetabolic DiseasesMethylationNeoplasmsProtein-Arginine N-MethyltransferasesRNA SplicingSignal TransductionTranscription FactorsAntineoplastic AgentsArginineEnzyme InhibitorsHistonesProtein-Arginine N-MethyltransferasesTranscription Factorsarginine methylationcancerepigenetic modificationsnon-histone proteinPRMTPRMT inhibitor

Identifiers

PMID32379587
PMCPMC7529871
OpenAlexW3023426671

What OpenQuestion holds

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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.