Evidence map›Paper›PMID 24921003›Full record

ReviewWorld journal of biological chemistry2014

Role of PRMTs in cancer: Could minor isoforms be leaving a mark?

R Mitchell Baldwin, Alan Morettin, Jocelyn Côté

Open access · diamondAbstract readReview
In one paragraph

Review in World journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Article
  3. Role of PRMT1 and PRMT5 in Breast Cancer.International journal of molecular sciences · 2024
    Review
  4. Article
  5. Review
  6. Protein Arginine Methyltransferase 5 (PRMT5) Mutations in Cancer Cells.International journal of molecular sciences · 2023
    Article
  7. Targeting epigenetic regulators to overcome drug resistance in cancers.Signal transduction and targeted therapy · 2023
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
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  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

3 authors at 1 institution in 1 country.

R Mitchell BaldwinR Mitchell Baldwin, Alan Morettin, Jocelyn Côté, Department of Cellular and Molecular Medicine, Rm. 3111a, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
Alan MorettinR Mitchell Baldwin, Alan Morettin, Jocelyn Côté, Department of Cellular and Molecular Medicine, Rm. 3111a, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
Jocelyn CôtéR Mitchell Baldwin, Alan Morettin, Jocelyn Côté, Department of Cellular and Molecular Medicine, Rm. 3111a, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
University of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methyltransferases (PRMTs) catalyze the methylation of a variety of protein substrates, many of which have been linked to the development, progression and aggressiveness of different types of cancer. Moreover, aberrant expression of PRMTs has been observed in several cancer types. While the link between PRMTs and cancer is a relatively new area of interest, the functional implications documented thus far warrant further investigations into its therapeutic potential. However, the expression of these enzymes and the regulation of their activity in cancer are still significantly understudied. Currently there are nine main members of the PRMT family. Further, the existence of alternatively spliced isoforms for several of these family members provides an additional layer of complexity. Specifically, PRMT1, PRMT2, CARM1 and PRMT7 have been shown to have alternative isoforms and others may be currently unrealized. Our knowledge with respect to the relative expression and the specific functions of these isoforms is largely lacking and needs attention. Here we present a review of the current knowledge of the known alternative PRMT isoforms and provide a rationale for how they may impact on cancer and represent potentially useful targets for the development of novel therapeutic strategies.

Indexed as

Arginine methylationCancer, Alternative splicingIsoformsProtein arginine methyltransferase

Identifiers

PMID24921003
PMCPMC4050107
OpenAlexW1603391166

What OpenQuestion holds

Textmetadata
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.