ArticleFrontiers in neurology2025
Proteomic analysis of nemaline myopathy in infants reveals distinct common dysregulated proteins and cellular pathways.
Article in Frontiers in neurology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- A novel myopathy with autophagic vacuoles associated with biallelic variants in CLN8.Brain pathology (Zurich, Switzerland) · 2026Article
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5 authors.
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Abstract
Background: Nemaline myopathy is a rare congenital muscle disorder characterized by the presence of nemaline rods, protein aggregates, in muscle fibers. Pathogenic variants in several genes, most commonly Methods: In this study, we employed quantitative nanoscale liquid chromatography-tandem mass spectrometry (LC-MS Results: We identified and quantified 4,846 proteins across all samples, with 183 proteins showing significant dysregulation. Protein-protein interaction analysis revealed nine upregulated, muscle-specific proteins: NRAP, FBXO40, TRIM63, TRIM54, ALPK3, XIRP1, ANKRD2, LMOD2, and CSRP3. Further pathway analysis indicated upregulation of protein synthesis and proteasomal degradation processes, alongside downregulation of glycolysis. Notably, the dysregulated proteins and pathways were consistent across both genetic subtypes, suggesting shared molecular mechanisms underlying the disease. Conclusion: This proteomic profiling study has identified key dysregulated proteins and pathways in infantile nemaline myopathy. These findings advance our understanding of the disease's molecular basis and highlight candidate targets for future therapeutic intervention.
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