Evidence map›Paper›PMID 32937226›Full record

ReviewCurrent opinion in pharmacology2021

Role of O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins in diabetic cardiovascular complications.

John C Chatham, Martin E Young, Jianhua Zhang

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in pharmacology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
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  8. Immunohistochemical Study onActa histochemica et cytochemica · 2025
    Review
  9. Review
  10. International journal of molecular sciences · 2025
    Review
  11. Mechanistic underpinnings of AGEs-RAGE via DIAPH1 in ischemic, diabetic, and failing hearts.American journal of physiology. Heart and circulatory physiology · 2025
    Article
  12. Review
  13. Review
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  16. O-GlcNAc modification of GSDMD attenuates LPS-induced endothelial cells pyroptosis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024
    Article
  17. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

John C ChathamDivision of Molecular and Cellular Pathology, Department of Pathology, University of Alabama at Birmingham, Birmingham, AL, United States. Electronic address: jchatham@uabmc.edu.
Martin E YoungDivision of Cardiovascular Diseases, Department of Medicine, University of Alabama at Birmingham, Birmingham, AL, United States.
Jianhua ZhangDivision of Molecular and Cellular Pathology, Department of Pathology, University of Alabama at Birmingham, Birmingham, AL, United States; Birmingham VA Medical Center, Birmingham, AL, United States.
University of Alabama at Birmingham · USBirmingham VA Medical Center · US

Funding

Aberrant Circadian Regulation of Autophagy in the Heart During DiabetesR01HL142216 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHATHAM, JOHN C, YOUNG, MARTIN E · 2018 to 2021
$2.3M
Mechanisms of Impaired Lysosomal Biogenesis and Autophagy in Alcohol-Associated Alzheimer's DiseaseR01AG072895 · NIA · UNIVERSITY OF KANSAS MEDICAL CENTER · PI DING, WEN-XING · 2020 to 2024
$1.9M
The role of protein O-linked N-Acetylglucosamine in regulating cardiac physiologyR21HL152354 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHATHAM, JOHN C, WENDE, ADAM RAYMOND · 2020 to 2021
$408k
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
O-GlcNAc in protein homeostasis in the context of PD, AD and DLBI01BX004251 · VA · BIRMINGHAM VA MEDICAL CENTER · PI ZHANG, JIANHUA · 2019 to 2023
–
BLRD VA I01 BX004251NHLBI NIH HHS R01 HL142216NHLBI NIH HHS R21 HL152354NIA NIH HHS R01 AG072895NIA NIH HHS R56 AG060959
6 · The paper itself

Abstract

The post-translational modification of serine and threonine residues of proteins by O-linked N-acetylglucosamine (O-GlcNAc) regulates diverse cellular processes in the cardiovascular system. UDP-GlcNAc is a substrate for O-GlcNAc transferase, which catalyzes the attachment of O-GlcNAc to proteins. O-GlcNAcase catalyzes the removal of O-GlcNAc from proteins. UDP-GlcNAc is the end product of the hexosamine biosynthesis pathway, which is regulated primarily by glucose-6-phosphate-Glutamine:fructose-6-phosphate amidotransferase (GFAT). GFAT catalyzes the formation of glucosamine-6-phosphate from fructose-6-phosphate and glutamine. Whereas O-GlcNAc is essential for cell viability, sustained increases in O-GlcNAc levels have been implicated in the etiology of many chronic diseases and is associated with glucose toxicity and diabetic complications in various organs including the cardiovascular system. This review provides an overview of the regulation of protein O-GlcNAcylation followed by a discussion of potential mechanisms by which dysregulation in O-GlcNAc cycling contributes to the adverse effects of diabetes on the cardiovascular system.

Indexed as

Cardiovascular SystemDiabetes ComplicationsDiabetes MellitusAcetylglucosamineHexosaminesHumansProtein Processing, Post-TranslationalAcetylglucosamineHexosamines

Identifiers

PMID32937226
PMCPMC9027139
OpenAlexW3087372344

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.