Evidence map›Paper›PMID 29456783›Full record

ReviewOxidative medicine and cellular longevity2017

The Role of Stress-Induced O-GlcNAc Protein Modification in the Regulation of Membrane Transport.

Viktória Fisi, Attila Miseta, Tamás Nagy

Open access · hybridAbstract readReview
In one paragraph

Review in Oxidative medicine and cellular longevity, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Genome ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The Role of Glycosyltransferases in Colorectal Cancer.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Article
  14. Frontiers in cell and developmental biology · 2020
    Article
  15. Glucose Metabolism in Cardiac Hypertrophy and Heart Failure.Journal of the American Heart Association · 2019
    Review
  16. Article
  17. 'Molecules (Basel, Switzerland) · 2018
    Review
  18. Molecules (Basel, Switzerland) · 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.

Viktória FisiDepartment of Laboratory Medicine, School of Medicine, University of Pécs, Ifjúság str. 13, Pécs 7624, Hungary.
Attila MisetaDepartment of Laboratory Medicine, School of Medicine, University of Pécs, Ifjúság str. 13, Pécs 7624, Hungary.
Tamás NagyDepartment of Laboratory Medicine, School of Medicine, University of Pécs, Ifjúság str. 13, Pécs 7624, Hungary.ORCID 0000-0001-5437-1411
University of Pecs · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-linked N-acetylglucosamine (O-GlcNAc) is a posttranslational modification that is increasingly recognized as a signal transduction mechanism. Unlike other glycans, O-GlcNAc is a highly dynamic and reversible process that involves the addition and removal of a single N-acetylglucosamine molecule to Ser/Thr residues of proteins. UDP-GlcNAc-the direct substrate for O-GlcNAc modification-is controlled by the rate of cellular metabolism, and thus O-GlcNAc is dependent on substrate availability. Serving as a feedback mechanism, O-GlcNAc influences the regulation of insulin signaling and glucose transport. Besides nutrient sensing, O-GlcNAc was also implicated in the regulation of various physiological and pathophysiological processes. Due to improvements of mass spectrometry techniques, more than one thousand proteins were detected to carry the O-GlcNAc moiety; many of them are known to participate in the regulation of metabolites, ions, or protein transport across biological membranes. Recent studies also indicated that O-GlcNAc is involved in stress adaptation; overwhelming evidences suggest that O-GlcNAc levels increase upon stress. O-GlcNAc elevation is generally considered to be beneficial during stress, although the exact nature of its protective effect is not understood. In this review, we summarize the current data regarding the oxidative stress-related changes of O-GlcNAc levels and discuss the implications related to membrane trafficking.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionAnimalsBiological TransportGlycosylationHumansMembrane Transport ProteinsN-AcetylglucosaminyltransferasesOxidative StressMembrane Transport ProteinsN-AcetylglucosaminyltransferasesO-GlcNAc transferase

Identifiers

PMID29456783
PMCPMC5804373
OpenAlexW2777796134

What Socratic 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 Socratic graph.