Evidence map›Paper›PMID 25400587›Full record

ReviewFrontiers in physiology2014

O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle.

Caroline Cieniewski-Bernard, Matthias Lambert, Erwan Dupont, Valérie Montel, Laurence Stevens, Bruno Bastide

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Posttranslational modifications in diabetes: Mechanisms and functions.Reviews in endocrine & metabolic disorders · 2022
    Review
  3. ProteinMetabolites · 2022
    Review
  4. Article
  5. Cells · 2022
    Review
  6. Role ofPhysiological reviews · 2021
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. 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

6 authors at 1 institution in 1 country.

Caroline Cieniewski-BernardUniversité Lille Lille, France ; EA4488, APMS, URePsss, Université de Lille 1 Villeneuve d'Ascq, France.
Matthias LambertUniversité Lille Lille, France ; EA4488, APMS, URePsss, Université de Lille 1 Villeneuve d'Ascq, France.
Erwan DupontUniversité Lille Lille, France ; EA4488, APMS, URePsss, Université de Lille 1 Villeneuve d'Ascq, France.
Valérie MontelUniversité Lille Lille, France ; EA4488, APMS, URePsss, Université de Lille 1 Villeneuve d'Ascq, France.
Laurence StevensUniversité Lille Lille, France ; EA4488, APMS, URePsss, Université de Lille 1 Villeneuve d'Ascq, France.
Bruno BastideUniversité Lille Lille, France ; EA4488, APMS, URePsss, Université de Lille 1 Villeneuve d'Ascq, France.
Université de Lille · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-GlcNAcylation, a generally undermined atypical protein glycosylation process, is involved in a dynamic and highly regulated interplay with phosphorylation. Akin to phosphorylation, O-GlcNAcylation is also involved in the physiopathology of several acquired diseases, such as muscle insulin resistance or muscle atrophy. Recent data underline that the interplay between phosphorylation and O-GlcNAcylation acts as a modulator of skeletal muscle contractile activity. In particular, the O-GlcNAcylation level of the phosphoprotein myosin light chain 2 seems to be crucial in the modulation of the calcium activation properties, and should be responsible for changes in calcium properties observed in functional atrophy. Moreover, since several key structural proteins are O-GlcNAc-modified, and because of the localization of the enzymes involved in the O-GlcNAcylation/de-O-GlcNAcylation process to the nodal Z disk, a role of O-GlcNAcylation in the modulation of the sarcomeric structure should be considered.

Indexed as

contractile propertiescontractile proteinsMLC2O-GlcNAcylationO-GlcNAcylation/phosphorylation interplayphosphorylationsarcomeric structure

Identifiers

PMID25400587
PMCPMC4214218
OpenAlexW1992114876

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.