Evidence map›Paper›PMID 30836866›Full record

ReviewOpen biology2019

Post-translational modification control of RNA-binding protein hnRNPK function.

Yongjie Xu, Wei Wu, Qiu Han, Yaling Wang, Cencen Li, Pengpeng Zhang, Haixia Xu

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 2% 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

66 citing papers in PubMed, 1 synthesis or guideline pooled it, 116 citations in OpenAlex.

  1. Alternative splicing and cancer: a systematic review.Signal transduction and targeted therapy · 2021
    Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Function ofOncology letters · 2025
    Review
  11. RNA-binding proteins orchestrating immunity in plants.The Plant journal : for cell and molecular biology · 2025
    Review
  12. Article
  13. Article
  14. Recent advances on the role of G0S2.Discover oncology · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Prenatal diagnosis of aFrontiers in genetics · 2025
    Article
  20. Article

6 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

7 authors at 1 institution in 1 country.

Yongjie XuCollege of Life Science, Xinyang Normal University , Xinyang 464000 , People's Republic of China.
Wei WuCollege of Life Science, Xinyang Normal University , Xinyang 464000 , People's Republic of China.
Qiu HanCollege of Life Science, Xinyang Normal University , Xinyang 464000 , People's Republic of China.
Yaling WangCollege of Life Science, Xinyang Normal University , Xinyang 464000 , People's Republic of China.
Cencen LiCollege of Life Science, Xinyang Normal University , Xinyang 464000 , People's Republic of China.
Pengpeng ZhangCollege of Life Science, Xinyang Normal University , Xinyang 464000 , People's Republic of China.
Haixia XuCollege of Life Science, Xinyang Normal University , Xinyang 464000 , People's Republic of China.
Xinyang Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterogeneous nuclear ribonucleoprotein K (hnRNPK), a ubiquitously occurring RNA-binding protein (RBP), can interact with numerous nucleic acids and various proteins and is involved in a number of cellular functions including transcription, translation, splicing, chromatin remodelling, etc. Through its abundant biological functions, hnRNPK has been implicated in cellular events including proliferation, differentiation, apoptosis, DNA damage repair and the stress and immune responses. Thus, it is critical to understand the mechanism of hnRNPK regulation and its downstream effects on cancer and other diseases. A number of recent studies have highlighted that several post-translational modifications (PTMs) possibly play an important role in modulating hnRNPK function. Phosphorylation is the most widely occurring PTM in hnRNPK. For example, in vivo analyses of sites such as S116 and S284 illustrate the purpose of PTM of hnRNPK in altering its subcellular localization and its ability to bind target nucleic acids or proteins. Other PTMs such as methylation, ubiquitination, sumoylation, glycosylation and proteolytic cleavage are increasingly implicated in the regulation of DNA repair, cellular stresses and tumour growth. In this review, we describe the PTMs that impact upon hnRNPK function on gene expression programmes and different disease states. This knowledge is key in allowing us to better understand the mechanism of hnRNPK regulation.

Indexed as

DNA RepairProtein Processing, Post-TranslationalGlycosylationHeterogeneous-Nuclear Ribonucleoprotein KHumansMethylationPhosphorylationSerineSumoylationUbiquitinationHeterogeneous-Nuclear Ribonucleoprotein KHNRNPK protein, humanSerineglycosylationhnRNPKmethylationphosphorylationpost-translational modificationsubiquitination

Identifiers

PMID30836866
PMCPMC6451366
OpenAlexW2922469012

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.