Evidence map›Paper›PMID 31226838›Full record

ReviewProteomes2019

Characterization of Contractile Proteins from Skeletal Muscle Using Gel-Based Top-Down Proteomics.

Paul Dowling, Margit Zweyer, Dieter Swandulla, Kay Ohlendieck

Erratum issuedOpen access · goldAbstract readReview
In one paragraph

Review in Proteomes, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Two-CyDye-Based 2D-DIGE Analysis of Aged Human Muscle Biopsy Specimens.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  9. Top-Down Proteomics and Comparative 2D-DIGE Analysis.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Comparative 3-Sample 2D-DIGE Analysis of Skeletal Muscles.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  11. Article
  12. Identification of Subproteomic Markers for Skeletal Muscle Profiling.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Sample Preparation and Protein Determination for 2D-DIGE Proteomics.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Bioinformatic Analysis of the Subproteomic Profile of Cardiomyopathic Tissue.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Paul DowlingDepartment of Biology, Maynooth University, Maynooth, W23F2H6 Co. Kildare, Ireland. paul.dowling@mu.ie.
Margit ZweyerInstitute of Physiology II, University of Bonn, D-53115 Bonn, Germany. margit.zweyer@ukbonn.de.
Dieter SwandullaInstitute of Physiology II, University of Bonn, D-53115 Bonn, Germany. dieter.swandulla@ukbonn.de.
Kay OhlendieckDepartment of Biology, Maynooth University, Maynooth, W23F2H6 Co. Kildare, Ireland. kay.ohlendieck@mu.ie.
National University of Ireland, Maynooth · IEUniversity of Bonn · DE

Funding

Health Research Board HRB/MRCG-2016-20
6 · The paper itself

Abstract

The mass spectrometric analysis of skeletal muscle proteins has used both peptide-centric and protein-focused approaches. The term 'top-down proteomics' is often used in relation to studying purified proteoforms and their post-translational modifications. Two-dimensional gel electrophoresis, in combination with peptide generation for the identification and characterization of intact proteoforms being present in two-dimensional spots, plays a critical role in specific applications of top-down proteomics. A decisive bioanalytical advantage of gel-based and top-down approaches is the initial bioanalytical focus on intact proteins, which usually enables the swift identification and detailed characterisation of specific proteoforms. In this review, we describe the usage of two-dimensional gel electrophoretic top-down proteomics and related approaches for the systematic analysis of key components of the contractile apparatus, with a special focus on myosin heavy and light chains and their associated regulatory proteins. The detailed biochemical analysis of proteins belonging to the thick and thin skeletal muscle filaments has decisively improved our biochemical understanding of structure-function relationships within the contractile apparatus. Gel-based and top-down proteomics has clearly established a variety of slow and fast isoforms of myosin, troponin and tropomyosin as excellent markers of fibre type specification and dynamic muscle transition processes.

Indexed as

actinmass spectrometrymuscle proteomicsmyosinskeletal muscletop-down proteomicstropomyosintroponintwo-dimensional gel electrophoresis

Identifiers

PMID31226838
PMCPMC6631179
OpenAlexW2952528243

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.