Evidence map›Paper›PMID 38447797›Full record

ReviewThe Journal of biological chemistry2024

OGT and OGA: Sweet guardians of the genome.

Chen Wu, Jiaheng Li, Lingzi Lu, Mengyuan Li, Yanqiu Yuan, Jing Li

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.5field-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

23 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  11. Glycan-related genes and genetic disorders.Journal of human genetics · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. O-GlcNAc informatics: advances and trends.Analytical and bioanalytical chemistry · 2025
    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

6 authors at 3 institutions in 1 country.

Chen WuCollege of Life Sciences, Institute of Life Sciences and Green Development, Hebei University, Baoding, Hebei, China. Electronic address: wuchen@hbu.edu.cn.
Jiaheng LiCollege of Life Sciences, Institute of Life Sciences and Green Development, Hebei University, Baoding, Hebei, China.
Lingzi LuSchool of Pharmaceutical Sciences, Guangdong Provincial Key Laboratory of Drug Non-Clinical Evaluation and Research, Sun Yat-sen University, Guangzhou, Guangdong, China.
Mengyuan LiCollege of Life Sciences, Institute of Life Sciences and Green Development, Hebei University, Baoding, Hebei, China.
Yanqiu YuanSchool of Pharmaceutical Sciences, Guangdong Provincial Key Laboratory of Drug Non-Clinical Evaluation and Research, Sun Yat-sen University, Guangzhou, Guangdong, China. Electronic address: Yuanyq8@mail.sysu.edu.cn.
Jing LiBeijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing, China. Electronic address: jing_li@mail.cnu.edu.cn.
Sun Yat-sen University · CNBeijing Normal University · CNHebei University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The past 4 decades have witnessed tremendous efforts in deciphering the role of O-GlcNAcylation in a plethora of biological processes. Chemists and biologists have joined hand in hand in the sweet adventure to unravel this unique and universal yet uncharted post-translational modification, and the recent advent of cutting-edge chemical biology and mass spectrometry tools has greatly facilitated the process. Compared with O-GlcNAc, DNA damage response (DDR) is a relatively intensively studied area that could be traced to before the elucidation of the structure of DNA. Unexpectedly, yet somewhat expectedly, O-GlcNAc has been found to regulate various DDR pathways: homologous recombination, nonhomologous end joining, base excision repair, and translesion DNA synthesis. In this review, we first cover the recent structural studies of the O-GlcNAc transferase and O-GlcNAcase, the elegant duo that "writes" and "erases" O-GlcNAc modification. Then we delineate the intricate roles of O-GlcNAc transferase and O-GlcNAcase in DDR. We envision that this is only the beginning of our full appreciation of how O-GlcNAc regulates the blueprint of life-DNA.

Indexed as

N-AcetylglucosaminyltransferasesAnimalsbeta-N-AcetylhexosaminidasesDNADNA DamageDNA RepairGenomeHumansProtein Processing, Post-Translationalbeta-N-AcetylhexosaminidasesDNAhexosaminidase CN-AcetylglucosaminyltransferasesO-GlcNAc transferaseDNA damageOGAO-GlcNAcOGTreplication

Identifiers

PMID38447797
PMCPMC10981121
OpenAlexW4392368654

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.