Evidence map›Paper›PMID 34006904›Full record

ReviewExperimental & molecular medicine2021

Protein arginine methyltransferases: promising targets for cancer therapy.

Jee Won Hwang, Yena Cho, Gyu-Un Bae, Su-Nam Kim, Yong Kee Kim

Open access · goldAbstract readReview
In one paragraph

Review in Experimental & molecular medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
13.1field-weighted citation impact, top 1% 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

166 citing papers in PubMed, 244 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. KDM4A Erases the H3R17me2a Mark, Facilitating Chromosome Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  17. Article
  18. Article
  19. Article
  20. Article

106 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

5 authors at 2 institutions in 1 country.

Jee Won HwangResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Seoul, 04310, Republic of Korea.
Yena ChoResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Seoul, 04310, Republic of Korea.
Gyu-Un BaeResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Seoul, 04310, Republic of Korea.
Su-Nam KimNatural Product Research Institute, Korea Institute of Science and Technology, Gangneung, 25451, Republic of Korea.
Yong Kee KimResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Seoul, 04310, Republic of Korea. yksnbk@sookmyung.ac.kr.ORCID http://orcid.org/0000-0002-6413-7538
Sookmyung Women's University · KRKorea Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein methylation, a post-translational modification (PTM), is observed in a wide variety of cell types from prokaryotes to eukaryotes. With recent and rapid advancements in epigenetic research, the importance of protein methylation has been highlighted. The methylation of histone proteins that contributes to the epigenetic histone code is not only dynamic but is also finely controlled by histone methyltransferases and demethylases, which are essential for the transcriptional regulation of genes. In addition, many nonhistone proteins are methylated, and these modifications govern a variety of cellular functions, including RNA processing, translation, signal transduction, DNA damage response, and the cell cycle. Recently, the importance of protein arginine methylation, especially in cell cycle regulation and DNA repair processes, has been noted. Since the dysregulation of protein arginine methylation is closely associated with cancer development, protein arginine methyltransferases (PRMTs) have garnered significant interest as novel targets for anticancer drug development. Indeed, several PRMT inhibitors are in phase 1/2 clinical trials. In this review, we discuss the biological functions of PRMTs in cancer and the current development status of PRMT inhibitors in cancer therapy.

Indexed as

Biomarkers, TumorAntineoplastic AgentsArginineCell CycleDisease ManagementDisease SusceptibilityDNA DamageDrug DevelopmentEnzyme InhibitorsGene Expression Regulation, NeoplasticHumansMethylationMolecular Targeted TherapyNeoplasmsProtein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalAntineoplastic AgentsArginineBiomarkers, TumorEnzyme InhibitorsProtein-Arginine N-Methyltransferases

Identifiers

PMID34006904
PMCPMC8178397
OpenAlexW3163513997

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.