Evidence map›Paper›PMID 21798084›Full record

ArticleSkeletal muscle2011

Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques.

Kay Ohlendieck

Open access · goldAbstract read
In one paragraph

Article in Skeletal muscle, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Review
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  14. Review
  15. Two-CyDye-Based 2D-DIGE Analysis of Aged Human Muscle Biopsy Specimens.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  16. Subcellular Fractionation for DIGE-Based Proteomics.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  17. Comparative 3-Sample 2D-DIGE Analysis of Skeletal Muscles.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  18. Article
  19. Review
  20. Microproteins in skeletal muscle: hidden keys in muscle physiology.Journal of cachexia, sarcopenia and muscle · 2022
    Review

3 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

1 author at 1 institution in 1 country.

Kay OhlendieckMuscle Biology Laboratory, Department of Biology, National University of Ireland, Maynooth, County Kildare, Ireland. kay.ohlendieck@nuim.ie
National University of Ireland, Maynooth · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSkeletal muscle fibres represent one of the most abundant cell types in mammals. Their highly specialised contractile and metabolic functions depend on a large number of membrane-associated proteins with very high molecular masses, proteins with extensive posttranslational modifications and components that exist in highly complex supramolecular structures. This makes it extremely difficult to perform conventional biochemical studies of potential changes in protein clusters during physiological adaptations or pathological processes.

resultsSkeletal muscle proteomics attempts to establish the global identification and biochemical characterisation of all members of the muscle-associated protein complement. A considerable number of proteomic studies have employed large-scale separation techniques, such as high-resolution two-dimensional gel electrophoresis or liquid chromatography, and combined them with mass spectrometry as the method of choice for high-throughput protein identification. Muscle proteomics has been applied to the comprehensive biochemical profiling of developing, maturing and aging muscle, as well as the analysis of contractile tissues undergoing physiological adaptations seen in disuse atrophy, physical exercise and chronic muscle transformation. Biomedical investigations into proteome-wide alterations in skeletal muscle tissues were also used to establish novel biomarker signatures of neuromuscular disorders. Importantly, mass spectrometric studies have confirmed the enormous complexity of posttranslational modifications in skeletal muscle proteins.

conclusionsThis review critically examines the scientific impact of modern muscle proteomics and discusses its successful application for a better understanding of muscle biology, but also outlines its technical limitations and emerging techniques to establish new biomarker candidates.

Identifiers

PMID21798084
PMCPMC3143904
OpenAlexW2162625297

What OpenQuestion holds

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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.