Evidence map›Paper›PMID 23620203›Full record

ArticleCell stress & chaperones2013

Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis.

Jennifer A Groves, Albert Lee, Gokben Yildirir, Natasha E Zachara

Open access · bronzeAbstract read
In one paragraph

Article in Cell stress & chaperones, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

83 citing papers in PubMed, 136 citations in OpenAlex.

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  9. Identification of a Polypeptide Inhibitor ofJournal of the American Chemical Society · 2024
    Article
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  12. Article
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  14. Review
  15. The O-GlcNAc dichotomy: when does adaptation become pathological?Clinical science (London, England : 1979) · 2023
    Review
  16. Article
  17. Article
  18. Article
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  20. Article

23 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

4 authors at 2 institutions in 1 country.

Jennifer A GrovesThe Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 N. Wolfe St, Baltimore, MD 21205-2185, USA.
Albert Lee
Gokben Yildirir
Natasha E Zachara
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
JHU-UMD Diabetes Research CenterP30DK079637 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI AHIMA, REXFORD S. · 2013 to 2017
$9.7M
Defining the Molecular Mechanisms by Which O-GlcNAc Mediates CardioprotectionR21HL108003 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI ZACHARA, NATASHA ELIZABETH · 2011 to 2012
$454k
NHLBI NIH HHS 1P01-HL-107153NHLBI NIH HHS P01 HL107153NHLBI NIH HHS P01-HL-107153NHLBI NIH HHS R21 HL108003NHLBI NIH HHS R21-HL-108003NIDDK NIH HHS P30 DK079637
6 · The paper itself

Abstract

O-linked N-acetyl-β-D-glucosamine (O-GlcNAc) is a ubiquitous and dynamic post-translational modification known to modify over 3,000 nuclear, cytoplasmic, and mitochondrial eukaryotic proteins. Addition of O-GlcNAc to proteins is catalyzed by the O-GlcNAc transferase and is removed by a neutral-N-acetyl-β-glucosaminidase (O-GlcNAcase). O-GlcNAc is thought to regulate proteins in a manner analogous to protein phosphorylation, and the cycling of this carbohydrate modification regulates many cellular functions such as the cellular stress response. Diverse forms of cellular stress and tissue injury result in enhanced O-GlcNAc modification, or O-GlcNAcylation, of numerous intracellular proteins. Stress-induced O-GlcNAcylation appears to promote cell/tissue survival by regulating a multitude of biological processes including: the phosphoinositide 3-kinase/Akt pathway, heat shock protein expression, calcium homeostasis, levels of reactive oxygen species, ER stress, protein stability, mitochondrial dynamics, and inflammation. Here, we will discuss the regulation of these processes by O-GlcNAc and the impact of such regulation on survival in models of ischemia reperfusion injury and trauma hemorrhage. We will also discuss the misregulation of O-GlcNAc in diseases commonly associated with the stress response, namely Alzheimer's and Parkinson's diseases. Finally, we will highlight recent advancements in the tools and technologies used to study the O-GlcNAc modification.

Indexed as

AcetylglucosamineAlzheimer DiseaseAnimalsbeta-N-AcetylhexosaminidasesCalciumHeat-Shock ProteinsHumansMitochondriaN-AcetylglucosaminyltransferasesParkinson DiseasePhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktReactive Oxygen SpeciesSignal TransductionAcetylglucosaminebeta-N-AcetylhexosaminidasesCalciumHeat-Shock Proteinshexosaminidase CN-AcetylglucosaminyltransferasesO-GlcNAc transferasePhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktReactive Oxygen Species

Identifiers

PMID23620203
PMCPMC3745259
OpenAlexW2088852871

What OpenQuestion holds

Textmetadata
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.