Evidence map›Paper›PMID 31090269›Full record

ReviewJournal of Zhejiang University. Science. B2019

O-GlcNAcylation, a sweet link to the pathology of diseases.

Hao Nie, Wen Yi

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of Zhejiang University. Science. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

56 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Insights into O-GlcNAcylation and programmed cell death in cancer.Frontiers in cell and developmental biology · 2025
    Review
  10. Review
  11. Review
  12. The Role of Uridine in Health and Disease.Journal of inflammation research · 2025
    Review
  13. Article
  14. Review
  15. Glycosylation in aging and neurodegenerative diseases.Acta biochimica et biophysica Sinica · 2024
    Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. JHEP reports : innovation in hepatology · 2024
    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

2 authors at 1 institution in 1 country.

Hao NieMOE Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Wen YiMOE Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-linked N-acetylglucosamine (O-GlcNAc) is a dynamic post-translational modification occurring on myriad proteins in the cell nucleus, cytoplasm, and mitochondria. The donor sugar for O-GlcNAcylation, uridine-diphosphate N-acetylglucosamine (UDP-GlcNAc), is synthesized from glucose through the hexosamine biosynthetic pathway (HBP). The recycling of O-GlcNAc on proteins is mediated by two enzymes in cells-O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), which catalyze the addition and removal of O-GlcNAc, respectively. O-GlcNAcylation is involved in a number of important cell processes including transcription, translation, metabolism, signal transduction, and apoptosis. Deregulation of O-GlcNAcylation has been reported to be associated with various human diseases such as cancer, diabetes, neurodegenerative diseases, and cardiovascular diseases. A better understanding of the roles of O-GlcNAcylation in physiopathological processes would help to uncover novel avenues for therapeutic intervention. The aim of this review is to discuss the recent updates on the mechanisms and impacts of O-GlcNAcylation on these diseases, and its potential as a new clinical target.

Indexed as

Protein Processing, Post-TranslationalAcetylglucosamineAnimalsApoptosisbeta-N-AcetylhexosaminidasesCardiovascular DiseasesCatalysisCell NucleusCell ProliferationCytoplasmDiabetes ComplicationsDiabetes Mellitus, Type 2HexosaminesHumansInsulinMitochondriaAcetylglucosaminebeta-N-AcetylhexosaminidasesHexosamineshexosaminidase CInsulinN-AcetylglucosaminyltransferasesO-GlcNAc transferaseO-GlcNAcylation; Cancer; Diabetes; Neurodegenerative disease; Cardiovascular disease

Identifiers

PMID31090269
PMCPMC6568225
OpenAlexW2946682191

What OpenQuestion holds

Textmetadata
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.