Evidence map›Paper›PMID 35822169›Full record

ArticleFrontiers in aging2020

New Insights Into the Biology of Protein O-GlcNAcylation: Approaches and Observations.

Toni Mueller, Xiaosen Ouyang, Michelle S Johnson, Wei-Jun Qian, John C Chatham, Victor Darley-Usmar, Jianhua Zhang

Open access · goldAbstract readEditorial
In one paragraph

Article in Frontiers in aging, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

  1. PerturbingCells · 2026
    Article
  2. Review
  3. Review
  4. O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. O-GlcNAc regulates anti-fibrotic genes in lung fibroblasts through EZH2.Journal of cellular and molecular medicine · 2024
    Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Advances in Optical Sensors ofBioconjugate chemistry · 2022
    Review
  17. Article
  18. Review
  19. Review
  20. 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

7 authors at 2 institutions in 1 country.

Toni MuellerDepartment of Pathology and Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, United States.
Xiaosen OuyangDepartment of Pathology and Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, United States.
Michelle S JohnsonDepartment of Pathology and Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, United States.
Wei-Jun QianBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, United States.
John C ChathamDepartment of Pathology and Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, United States.
Victor Darley-UsmarDepartment of Pathology and Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, United States.
Jianhua ZhangDepartment of Pathology and Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, United States.
University of Alabama at Birmingham · USPacific Northwest National Laboratory · US

Funding

O-GlcNAc regulation of protein clearance in the context of AD and DLBR56AG060959 · NIA · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHATHAM, JOHN C, ZHANG, JIANHUA · 2019 to 2019
$371k
BLRD VA I01 BX004251NIA NIH HHS R56 AG060959
6 · The paper itself

Abstract

O-GlcNAcylation is a protein posttranslational modification that results in the addition of O-GlcNAc to Ser/Thr residues. Since its discovery in the 1980s, it has been shown to play an important role in a broad range of cellular functions by modifying nuclear, cytosolic, and mitochondrial proteins. The addition of O-GlcNAc is catalyzed by O-GlcNAc transferase (OGT), and its removal is catalyzed by O-GlcNAcase (OGA). Levels of protein O-GlcNAcylation change in response to nutrient availability and metabolic, oxidative, and proteotoxic stress. OGT and OGA levels, activity, and target engagement are also regulated. Together, this results in adaptive and, on occasions, detrimental responses that affect cellular function and survival, which impact a broad range of pathologies and aging. Over the past several decades, approaches and tools to aid the investigation of the regulation and consequences of protein O-GlcNAcylation have been developed and enhanced. This review is divided into two sections: 1) We will first focus on current standard and advanced technical approaches for assessing enzymatic activities of OGT and OGT, assessing the global and specific protein O-GlcNAcylation and 2) we will summarize

Indexed as

antibodiesclick chemistryin vivoOGAOGTThiamet G

Identifiers

PMID35822169
PMCPMC9261361
OpenAlexW3138944505

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.