Evidence map›Paper›PMID 32349769›Full record

ReviewJournal of biomedical science2020

O-GlcNAcylation and its role in the immune system.

Yi-Hsuan Chang, Chia-Lin Weng, Kuo-I Lin

Abstract readReview
In one paragraph

Review in Journal of biomedical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing 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

110 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Metabolic Redox Modulation byMolecules (Basel, Switzerland) · 2026
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Journal for immunotherapy of cancer · 2025
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

50 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

3 authors.

Yi-Hsuan ChangGenomics Research Center, Academia Sinica, 128 Academia Road, Sec. 2, Nankang Dist., Taipei, 115, Taiwan.
Chia-Lin WengGenomics Research Center, Academia Sinica, 128 Academia Road, Sec. 2, Nankang Dist., Taipei, 115, Taiwan.
Kuo-I LinGenomics Research Center, Academia Sinica, 128 Academia Road, Sec. 2, Nankang Dist., Taipei, 115, Taiwan. kuoilin@gate.sinica.edu.tw.ORCID https://orcid.org/0000-0003-4477-0798

Funding

Academia Sinica AS-IA-107-L05Ministry of Science and Technology, Taiwan MOST 106-2320-B-001-011-MY3National Health Research Institutes NHRI-EX108-10835SI
6 · The paper itself

Abstract

O-linked-N-acetylglucosaminylation (O-GlcNAcylation) is a type of glycosylation that occurs when a monosaccharide, O-GlcNAc, is added onto serine or threonine residues of nuclear or cytoplasmic proteins by O-GlcNAc transferase (OGT) and which can be reversibly removed by O-GlcNAcase (OGA). O-GlcNAcylation couples the processes of nutrient sensing, metabolism, signal transduction and transcription, and plays important roles in development, normal physiology and physiopathology. Cumulative studies have indicated that O-GlcNAcylation affects the functions of protein substrates in a number of ways, including protein cellular localization, protein stability and protein/protein interaction. Particularly, O-GlcNAcylation has been shown to have intricate crosstalk with phosphorylation as they both modify serine or threonine residues. Aberrant O-GlcNAcylation on various protein substrates has been implicated in many diseases, including neurodegenerative diseases, diabetes and cancers. However, the role of protein O-GlcNAcylation in immune cell lineages has been less explored. This review summarizes the current understanding of the fundamental biochemistry of O-GlcNAcylation, and discusses the molecular mechanisms by which O-GlcNAcylation regulates the development, maturation and functions of immune cells. In brief, O-GlcNAcylation promotes the development, proliferation, and activation of T and B cells. O-GlcNAcylation regulates inflammatory and antiviral responses of macrophages. O-GlcNAcylation promotes the function of activated neutrophils, but inhibits the activity of nature killer cells.

Indexed as

AcylationAnimalsbeta-N-AcetylhexosaminidasesHumansImmune SystemN-Acetylglucosaminyltransferasesbeta-N-Acetylhexosaminidaseshexosaminidase CN-AcetylglucosaminyltransferasesO-GlcNAc transferaseImmune cellsOGAO-GlcNAcylationOGT

Identifiers

PMID32349769
PMCPMC7189445

What OpenQuestion holds

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Registered trials

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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.