Evidence map›Paper›PMID 28488246›Full record

ReviewProtein & cell2017

Potential coordination role between O-GlcNAcylation and epigenetics.

Donglu Wu, Yong Cai, Jingji Jin

Open access · diamondAbstract readReview
In one paragraph

Review in Protein & cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

30 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. International journal of molecular sciences · 2025
    Review
  4. Article
  5. O-GlcNAcylation mediates HActa pharmacologica Sinica · 2024
    Article
  6. Review
  7. Article
  8. H3K4me3 remodeling induced acquired resistance through O-GlcNAc transferase.Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Cells · 2022
    Review
  13. Article
  14. Writing and erasing O-GlcNAc from target proteins in cells.Biochemical Society transactions · 2021
    Article
  15. Review
  16. Article
  17. Review
  18. Feedback Regulation ofInternational journal of molecular sciences · 2021
    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

3 authors at 1 institution in 2 countries.

Donglu WuSchool of Life Sciences, Jilin University, Changchun, 130012, China.
Yong CaiSchool of Life Sciences, Jilin University, Changchun, 130012, China.
Jingji JinSchool of Life Sciences, Jilin University, Changchun, 130012, China. jjjin@jlu.edu.cn.ORCID http://orcid.org/0000-0001-9432-5954
Jilin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamic changes of the post-translational O-GlcNAc modification (O-GlcNAcylation) are controlled by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and the glycoside hydrolase O-GlcNAcase (OGA) in cells. O-GlcNAcylation often occurs on serine (Ser) and threonine (Thr) residues of the specific substrate proteins via the addition of O-GlcNAc group by OGT. It has been known that O-GlcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GlcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GlcNAcylation as 'protein code' or 'histone code' may provide recognition platforms or executive instructions for subsequent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GlcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O-GlcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GlcNAcylation with epigenetic changes in intracellular biological processes.

Indexed as

Epigenesis, GeneticProtein Processing, Post-TranslationalAcetylglucosamineAnimalsGlycoside HydrolasesHumansN-AcetylglucosaminyltransferasesNeoplasmsAcetylglucosamineGlycoside HydrolasesN-AcetylglucosaminyltransferasesO-GlcNAc transferaseepigeneticshistone modificationO-GlcNAcylationpost-translational modification

Identifiers

PMID28488246
PMCPMC5636747
OpenAlexW2613861803

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.