Evidence map›Paper›PMID 23642195›Full record

ReviewAnnual review of nutrition2013

O-GlcNAc cycling: a link between metabolism and chronic disease.

Michelle R Bond, John A Hanover

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of nutrition, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 199 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
199citing papers in PubMed, 1 pooled it
10.5field-weighted citation impact, top 1% 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

199 citing papers in PubMed, 1 synthesis or guideline pooled it, 312 citations in OpenAlex.

  1. Pooled it
  2. Observational
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. O-GlcNAc informatics: advances and trends.Analytical and bioanalytical chemistry · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Ultradeep O-GlcNAc proteomics reveals widespread O-GlcNAcylation on tyrosine residues of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Article
  20. Article

139 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

2 authors at 2 institutions in 1 country.

Michelle R BondNational Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. bondmr@mail.nih.gov
John A Hanover
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Targeted disruption the enzymes of O-GlcNAc cycling: Animal models of DiseaseZIADK060101 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HANOVER, JOHN A. · 2009 to 2025
$25.7M
Enzymes of O-GlcNAc cycling linked to type-2 diabetes and neurodegenerationZIADK060103 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HANOVER, JOHN A. · 2009 to 2025
$20.8M
Targeted disruption the enzymes of O-GlcNAc cycling: Animal models of DiseaseZ01DK060101 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HANOVER, JOHN A. · 2007 to 2008
$744k
Intramural NIH HHS Z01 DK060101Intramural NIH HHS ZIA DK060103
6 · The paper itself

Abstract

To maintain homeostasis under variable nutrient conditions, cells rapidly and robustly respond to fluctuations through adaptable signaling networks. Evidence suggests that the O-linked N-acetylglucosamine (O-GlcNAc) posttranslational modification of serine and threonine residues functions as a critical regulator of intracellular signaling cascades in response to nutrient changes. O-GlcNAc is a highly regulated, reversible modification poised to integrate metabolic signals and acts to influence many cellular processes, including cellular signaling, protein stability, and transcription. This review describes the role O-GlcNAc plays in governing both integrated cellular processes and the activity of individual proteins in response to nutrient levels. Moreover, we discuss the ways in which cellular changes in O-GlcNAc status may be linked to chronic diseases such as type 2 diabetes, neurodegeneration, and cancers, providing a unique window through which to identify and treat disease conditions.

Indexed as

Energy MetabolismHealth StatusAcetylglucosamineAnimalsbeta-N-AcetylhexosaminidasesDiabetes Mellitus, Type 2DietGene Expression RegulationHumansN-AcetylglucosaminyltransferasesNeoplasmsNeurodegenerative DiseasesProtein Processing, Post-TranslationalProtein StabilityUridine Diphosphate N-AcetylglucosamineAcetylglucosaminebeta-N-Acetylhexosaminidaseshexosaminidase CN-AcetylglucosaminyltransferasesO-GlcNAc transferaseUridine Diphosphate N-Acetylglucosamine

Identifiers

PMID23642195
PMCPMC10483992
OpenAlexW2096443403

What OpenQuestion holds

Textmetadata
LicenceTDM
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.