Evidence map›Paper›PMID 41217087›Full record

ReviewProteomics2026

Proteomic Profiling of Myofiber Repair Annexins and Their Role in Duchenne Muscular Dystrophy.

Paul Dowling, Dounia Bouragba, Elisa Negroni, Capucine Trollet, Margit Zweyer, Dieter Swandulla, Kay Ohlendieck

Abstract readReview
In one paragraph

Review in Proteomics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Paul DowlingDepartment of Biology, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, Ireland.
Dounia BouragbaCenter for Research in Myology U974, Sorbonne Université, INSERM, Paris, France.
Elisa NegroniCenter for Research in Myology U974, Sorbonne Université, INSERM, Paris, France.
Capucine TrolletCenter for Research in Myology U974, Sorbonne Université, INSERM, Paris, France.
Margit ZweyerGerman Centre for Neurodegenerative Diseases, Bonn, Germany.
Dieter SwandullaInstitute of Physiology, Faculty of Medicine, University of Bonn, Bonn, Germany.
Kay OhlendieckDepartment of Biology, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, Ireland.

Funding

Agence Nationale de la Recherche ANR-22-CE14-0068Agence Nationale de la Recherche #ANR-24-CE14-5209Agence Nationale de la Recherche #ANR-24-CPJ1-0122-01Association Institut de MyologyKathleen Lonsdale Institute for Human Health Research at Maynooth University, Research Ireland and Campus FranceScience Foundation Ireland Infrastructure Award SFI-12/RI/2346/3Sorbonne University
6 · The paper itself

Abstract

Myofiber regeneration and membrane repair play crucial roles in maintaining the continuous physiological functioning of the neuromuscular system. A swift and efficient repair mechanism enables the rapid restoration of sarcolemmal integrity following cellular impairment in damaged skeletal muscles. Members of the annexin family of proteins, which are characterized by the peripheral binding to acidic phospholipid membranes, are intrinsically involved in this myofiber repair process. The biochemical and proteomic profiling of dystrophinopathy, a severe and highly progressive neuromuscular disorder of early childhood, is outlined in this article with special focus on skeletal muscle-associated annexins and their role in membrane repair, myofiber regeneration and the cellular pathogenesis of Duchenne muscular dystrophy. Findings from comparative mass spectrometry-based surveys are described, and dystrophinopathy-related alterations in annexin expression patterns are discussed regarding the establishment of improved biomarker signatures of skeletal muscle wasting disorders. Mass spectrometry-based proteomic profiling is highly suitable for the systematic study of complex pathobiochemical alterations and inherent adaptations in dystrophinopathy. Disease-specific changes in annexins and related proteins of the membrane repair machinery can now be used to improve diagnosis, evaluation of disease severity, prognosis and therapeutic monitoring, and identify novel therapeutic targets to treat X-linked muscular dystrophy.

Indexed as

AnnexinsMuscle Fibers, SkeletalMuscular Dystrophy, DuchenneProteomicsAnimalsBiomarkersHumansMass SpectrometryMuscle, SkeletalRegenerationAnnexinsBiomarkersannexincaveolindysferlindystrophinmyoferlin

Identifiers

PMID41217087
PMCPMC13519369

What OpenQuestion holds

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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.