Mutant desmin substantially perturbs mitochondrial morphology, function and maintenance in skeletal muscle tissue

Secondary mitochondrial dysfunction is a feature in a wide variety of human protein aggregate diseases caused by mutations in different proteins, both in the central nervous system and in striated muscle. The functional relationship between the expression of a mutated protein and mitochondrial dysfu...

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Bibliographic Details
Published in:	Acta neuropathologica Vol. 132; no. 3; pp. 453 - 473
Main Authors:	Winter, Lilli, Wittig, Ilka, Peeva, Viktoriya, Eggers, Britta, Heidler, Juliana, Chevessier, Frederic, Kley, Rudolf A., Barkovits, Katalin, Strecker, Valentina, Berwanger, Carolin, Herrmann, Harald, Marcus, Katrin, Kornblum, Cornelia, Kunz, Wolfram S., Schröder, Rolf, Clemen, Christoph S.
Format:	Journal Article
Language:	English
Published:	Berlin/Heidelberg Springer Berlin Heidelberg 01-09-2016 Springer Springer Nature B.V
Subjects:	Analysis Animals Biochemistry Cardiomyopathy Cytoskeleton Cytoskeleton - metabolism Cytoskeleton - pathology Desmin - genetics Desmin - metabolism Disease Genetic aspects Hospitals Humans Informatics Intermediate filament proteins Intermediate Filaments - genetics Intermediate Filaments - pathology Medicine Medicine & Public Health Mice, Transgenic Mitochondria Mitochondria - metabolism Mitochondria - pathology Mitochondrial DNA Morphology Muscle, Skeletal - pathology Muscular Diseases - genetics Muscular Diseases - pathology Musculoskeletal system Mutation Mutation - genetics Neurosciences Original Paper Pathology Proteins Skeletal muscle Germany Desmin knock-out Mitochondria Desminopathy R350P desmin R349P desmin knock-in mtDNA Proteome Myofibrillar myopathy Intermediate filament Protein aggregate myopathy
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