Evidence map›Paper›PMID 25173736›Full record

ReviewAmino acids2014

O-GlcNAc transferase and O-GlcNAcase: achieving target substrate specificity.

Alexis K Nagel, Lauren E Ball

Abstract readReview
In one paragraph

Review in Amino acids, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Discovery of Sennoside A as a NaturalResearch (Washington, D.C.) · 2026
    Article
  6. Article
  7. O-GlcNAcase Inhibitor Improves Denervation-Induced Muscle Atrophy in Mice.Journal of cachexia, sarcopenia and muscle · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Radiosynthesis and evaluation of a carbon-11 labeled PET ligand for imaging of O-GlcNAcase.American journal of nuclear medicine and molecular imaging · 2025
    Article
  13. Article
  14. Heliyon · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

2 authors.

Alexis K NagelDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, 173 Ashley Avenue, BSB 358 MSC 509, Charleston, SC, 29425, USA.
Lauren E Ball

Funding

Regulation of IGF-1 and Insulin Signaling by O-GlcNAc GlycosylationR01DE020925 · NIDCR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI BALL, LAUREN ELIZABETH · 2010 to 2014
$1.8M
Orbitrap Mass SpectrometerS10OD010731 · OD · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI BALL, LAUREN ELIZABETH · 2012 to 2012
$600k
NIDCR NIH HHS R01 DE020925NIH HHS S10 OD010731
6 · The paper itself

Abstract

O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) catalyze the dynamic cycling of intracellular, post-translational O-GlcNAc modification on thousands of Ser/Thr residues of cytosolic, nuclear, and mitochondrial signaling proteins. The identification of O-GlcNAc modified substrates has revealed a functionally diverse set of proteins, and the extent of O-GlcNAcylation fluctuates in response to nutrients and cellular stress. As a result, OGT and OGA are implicated in widespread, nutrient-responsive regulation of numerous signaling pathways and transcriptional programs. These enzymes are required for normal embryonic development and are dysregulated in metabolic and age-related disease states. While a recent surge of interest in the field has contributed to understanding the functional impacts of protein O-GlcNAcylation, little is known about the upstream mechanisms which modulate OGT and OGA substrate targeting. This review focuses on elements of enzyme structure among splice variants, post-translational modification, localization, and regulatory protein interactions which drive the specificity of OGT and OGA toward different subsets of the cellular proteome. Ongoing efforts in this rapidly advancing field are aimed at revealing mechanisms of OGT and OGA regulation to harness the potential therapeutic benefit of manipulating these enzymes' activities.

Indexed as

Models, BiologicalModels, MolecularAnimalsbeta-N-AcetylhexosaminidasesBiocatalysisEpigenesis, GeneticGene Expression Regulation, EnzymologicHumansIsoenzymesN-AcetylglucosaminyltransferasesProtein ConformationProtein MultimerizationProtein Processing, Post-TranslationalProtein StabilityProtein TransportSubstrate Specificitybeta-N-Acetylhexosaminidaseshexosaminidase CIsoenzymesN-AcetylglucosaminyltransferasesO-GlcNAc transferase

Identifiers

PMID25173736
PMCPMC4584397

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.