Evidence map›Paper›PMID 24524620›Full record

ReviewCritical reviews in biochemistry and molecular biology

Functional O-GlcNAc modifications: implications in molecular regulation and pathophysiology.

Krithika Vaidyanathan, Sean Durning, Lance Wells

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Heliyon · 2024
    Article
  5. Review
  6. Article
  7. Development of a Novel [ACS chemical neuroscience · 2023
    Article
  8. Article
  9. O-Linked β-Frontiers in immunology · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. PET ligands [Science translational medicine · 2020
    Article
  18. Article
  19. Article
  20. Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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 1 country.

Krithika Vaidyanathan *Complex Carbohydrate Research Center, University of Georgia, Athens, USA.
Sean Durning *Complex Carbohydrate Research Center, University of Georgia, Athens, USA.
Lance WellsComplex Carbohydrate Research Center, University of Georgia, Athens, USA.
University of Georgia · US

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR018502 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI AZADI, PARASTOO · 2003 to 2011
$13.1M
Tumor Glycomics Laboratory for Discovery of Pancreatic Cancer MarkersU01CA128454 · NCI · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2007 to 2017
$5.7M
NCI NIH HHS U01 CA128454NCI NIH HHS U01CA128454NCRR NIH HHS P41 RR018502NCRR NIH HHS P41RR018502NIGMS NIH HHS P41 GM103490
6 · The paper itself

Abstract

O-linked β-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification of intracellular proteins. The dynamic and inducible cycling of the modification is governed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) in response to UDP-GlcNAc levels in the hexosamine biosynthetic pathway (HBP). Due to its reliance on glucose flux and substrate availability, a major focus in the field has been on how O-GlcNAc contributes to metabolic disease. For years this post-translational modification has been known to modify thousands of proteins implicated in various disorders, but direct functional connections have until recently remained elusive. New research is beginning to reveal the specific mechanisms through which O-GlcNAc influences cell dynamics and disease pathology including clear examples of O-GlcNAc modification at a specific site on a given protein altering its biological functions. The following review intends to focus primarily on studies in the last half decade linking O-GlcNAc modification of proteins with chromatin-directed gene regulation, developmental processes, and several metabolically related disorders including Alzheimer's, heart disease and cancer. These studies illustrate the emerging importance of this post-translational modification in biological processes and multiple pathophysiologies.

Indexed as

Protein Processing, Post-TranslationalAcetylglucosamineAlzheimer DiseaseAnimalsbeta-N-AcetylhexosaminidasesChromatinGene Expression RegulationHeart DiseasesHumansMetabolic DiseasesN-AcetylglucosaminyltransferasesNeoplasmsProteinsAcetylglucosaminebeta-N-AcetylhexosaminidasesChromatinhexosaminidase CN-AcetylglucosaminyltransferasesO-GlcNAc transferaseProteins

Identifiers

PMID24524620
PMCPMC4912837
OpenAlexW2074437836

What OpenQuestion holds

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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.