Evidence map›Paper›PMID 34575100›Full record

ReviewLife (Basel, Switzerland)2021

Structure, Activity and Function of the Protein Arginine Methyltransferase 6.

Somlee Gupta, Rajashekar Varma Kadumuri, Anjali Kumari Singh, Sreenivas Chavali, Arunkumar Dhayalan

Open access · goldAbstract readReview
In one paragraph

Review in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-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

27 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  5. Article
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  13. Review
  14. PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer.Journal of cellular and molecular medicine · 2025
    Review
  15. Review
  16. Article
  17. Circadian rhythm disruption and endocrine-related tumors.World journal of clinical oncology · 2024
    Review
  18. Article
  19. Review
  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

5 authors at 2 institutions in 1 country.

Somlee GuptaDepartment of Biotechnology, Pondicherry University, Puducherry 605014, India.
Rajashekar Varma KadumuriDepartment of Biology, Indian Institute of Science Education and Research (IISER) Tirupati, Tirupati 517507, India.
Anjali Kumari SinghDepartment of Biology, Indian Institute of Science Education and Research (IISER) Tirupati, Tirupati 517507, India.ORCID 0000-0002-0444-7913
Sreenivas ChavaliDepartment of Biology, Indian Institute of Science Education and Research (IISER) Tirupati, Tirupati 517507, India.ORCID 0000-0001-8307-1645
Arunkumar DhayalanDepartment of Biotechnology, Pondicherry University, Puducherry 605014, India.
Indian Institute of Science Education and Research, Tirupati · INPondicherry University · IN

Funding

Board of Research in Nuclear Sciences 37(1)/14/17/2017-BRNS/37019Department of Biotechnology, Ministry of Science and Technology, India BT/RLF/Re-entry/05/2018Indian Council of Medical Research Senior Research FellowshipMinistry of Education: Prime Minister's Research Fellowship Research FellowshipScience and Engineering Research Board National Post-Doctoral FellowshipScience and Engineering Research Board SRG/2019/001785
6 · The paper itself

Abstract

Members of the protein arginine methyltransferase (PRMT) family methylate the arginine residue(s) of several proteins and regulate a broad spectrum of cellular functions. Protein arginine methyltransferase 6 (PRMT6) is a type I PRMT that asymmetrically dimethylates the arginine residues of numerous substrate proteins. PRMT6 introduces asymmetric dimethylation modification in the histone 3 at arginine 2 (H3R2me2a) and facilitates epigenetic regulation of global gene expression. In addition to histones, PRMT6 methylates a wide range of cellular proteins and regulates their functions. Here, we discuss (i) the biochemical aspects of enzyme kinetics, (ii) the structural features of PRMT6 and (iii) the diverse functional outcomes of PRMT6 mediated arginine methylation. Finally, we highlight how dysregulation of PRMT6 is implicated in various types of cancers and response to viral infections.

Indexed as

cancerepigeneticsH3R2me2apost-translational modificationPRMT6protein arginine methylation

Identifiers

PMID34575100
PMCPMC8470942
OpenAlexW3201648510

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.