Evidence map›Paper›PMID 30888583›Full record

ArticleJournal of muscle research and cell motility2019

Proteomic profiling of the mouse diaphragm and refined mass spectrometric analysis of the dystrophic phenotype.

Sandra Murphy, Margit Zweyer, Maren Raucamp, Michael Henry, Paula Meleady, Dieter Swandulla, Kay Ohlendieck

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-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, 36 citations in OpenAlex.

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  11. Identification of Subproteomic Markers for Skeletal Muscle Profiling.Methods in molecular biology (Clifton, N.J.) · 2023
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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

7 authors at 3 institutions in 3 countries.

Sandra MurphyDepartment of Biology, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, Ireland.
Margit ZweyerInstitute of Physiology II, University of Bonn, 53115, Bonn, Germany.
Maren RaucampInstitute of Physiology II, University of Bonn, 53115, Bonn, Germany.
Michael HenryNational Institute for Cellular Biotechnology, Dublin City University, Dublin 9, Ireland.
Paula MeleadyNational Institute for Cellular Biotechnology, Dublin City University, Dublin 9, Ireland.
Dieter SwandullaInstitute of Physiology II, University of Bonn, 53115, Bonn, Germany.
Kay OhlendieckDepartment of Biology, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, Ireland. kay.ohlendieck@mu.ie.ORCID 0000-0002-6266-4510
University of Bonn · DEDublin City University · IENational University of Ireland, Maynooth · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The diaphragm is a crucial muscle involved in active inspiration and whole body homeostasis. Previous biochemical, immunochemical and cell biological investigations have established the distribution and fibre type-specific expression of key diaphragm proteins. Building on these findings, it was of interest to establish the entire experimentally assessable diaphragm proteome and verify the presence of specific protein isoforms within this specialized subtype of skeletal muscle. A highly sensitive Orbitrap Fusion Tribrid mass spectrometer was used for the systematic identification of the mouse diaphragm-associated protein population. Proteomics established 2925 proteins by high confidence peptide identification. Bioinformatics was used to determine the distribution of the main protein classes, biological processes and subcellular localization within the diaphragm proteome. Following the establishment of the respiratory muscle proteome with special emphasis on protein isoform expression in the contractile apparatus, the extra-sarcomeric cytoskeleton, the extracellular matrix and the excitation-contraction coupling apparatus, the mass spectrometric analysis of the diaphragm was extended to the refined identification of proteome-wide changes in X-linked muscular dystrophy. The comparative mass spectrometric profiling of the dystrophin-deficient diaphragm from the mdx-4cv mouse model of Duchenne muscular dystrophy identified 289 decreased and 468 increased protein species. Bioinformatics was employed to analyse the clustering of changes in protein classes and potential alterations in interaction patterns of proteins involved in metabolism, the contractile apparatus, proteostasis and the extracellular matrix. The detailed pathoproteomic profiling of the mdx-4cv diaphragm suggests highly complex alterations in a variety of crucial cellular processes due to deficiency in the membrane cytoskeletal protein dystrophin.

Indexed as

Mass SpectrometryProteomicsAnimalsDiaphragmDisease Models, AnimalMiceMice, Inbred mdxMuscle ProteinsMuscular Dystrophy, DuchennePhenotypeMuscle ProteinsDiaphragmDuchenne muscular dystrophyDystrophinDystrophinopathyMdx-4cv mouseSkeletal muscle proteome

Identifiers

PMID30888583
OpenAlexW2924045225

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.