ReviewBrain pathology (Zurich, Switzerland)2009
Extralysosomal protein degradation in myofibrillar myopathies.
Review in Brain pathology (Zurich, Switzerland), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Differential proteomic analysis of abnormal intramyoplasmic aggregates in desminopathy.Journal of proteomics · 2013Trial
- MYH7 mutation associated with two phenotypes of myopathy.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2018Article
- New insights into the protein aggregation pathology in myotilinopathy by combined proteomic and immunolocalization analyses.Acta neuropathologica communications · 2016Article
- Chemical chaperone ameliorates pathological protein aggregation in plectin-deficient muscle.The Journal of clinical investigation · 2014Article
- A combined laser microdissection and mass spectrometry approach reveals new disease relevant proteins accumulating in aggregates of filaminopathy patients.Molecular & cellular proteomics : MCP · 2013Article
- Clinical, morphological and genetic studies in a cohort of 21 patients with myofibrillar myopathy.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2011Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
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Abstract
Myofibrillar myopathies (MFMs) are a group of heterogeneous muscle disorders morphologically defined by the presence of foci of dissolution of the myofibrils, accumulation of the products of myofibrillar degradation and ectopic expression of multiple proteins. MFMs represent the paradigm of conformational protein diseases of skeletal and cardiac muscles. Protein aggregation in MFMs is now considered to be the result of a failure of the extralysosomal proteolytic degradation system. Several factors including mutant proteins, aggresome formation and oxidative stress may compromise the ubiquitin-proteasome system, promoting the accumulation of potentially toxic protein aggregates within muscle cells.
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Registered trials
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.