Evidence map›Paper›PMID 38778254›Full record

ReviewCellular & molecular biology letters2024

SR proteins in cancer: function, regulation, and small inhibitor.

Mingrong Bei, Jianzhen Xu

Abstract readReview
In one paragraph

Review in Cellular & molecular biology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Beyond transcription: RNA-binding proteins steering angiogenesis.American journal of physiology. Heart and circulatory physiology · 2026
    Review
  9. Observational
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review
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.

Mingrong BeiSystems Biology Laboratory, Shantou University Medical College (SUMC), 22 Xinling Road, Shantou, 515041, China.
Jianzhen XuSystems Biology Laboratory, Shantou University Medical College (SUMC), 22 Xinling Road, Shantou, 515041, China. jzxu01@stu.edu.cn.ORCID http://orcid.org/0000-0002-0697-9075

Funding

Natural Science Foundation of Guangdong Province 2024A1515011328
6 · The paper itself

Abstract

Alternative splicing of pre-mRNAs is a fundamental step in RNA processing required for gene expression in most metazoans. Serine and arginine-rich proteins (SR proteins) comprise a family of multifunctional proteins that contain an RNA recognition motif (RRM) and the ultra-conserved arginine/serine-rich (RS) domain, and play an important role in precise alternative splicing. Increasing research supports SR proteins as also functioning in other RNA-processing-related mechanisms, such as polyadenylation, degradation, and translation. In addition, SR proteins interact with N

Indexed as

NeoplasmsAlternative SplicingAnimalsHumansRNA-Binding ProteinsSerine-Arginine Splicing FactorsRNA-Binding ProteinsSerine-Arginine Splicing Factorsm6A modificationRNA processingSplicingSR proteinsTumor treatment

Identifiers

PMID38778254
PMCPMC11110342

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.