Results 61 to 70 of about 31,110 (115)

Role of Exercise Therapy in Prevention of Decline in Aging Muscle Function: Glucocorticoid Myopathy and Unloading

Journal of Aging Research, 2012
Changes in skeletal muscle quantity and quality lead to disability in the aging population. Physiological changes in aging skeletal muscle are associated with a decline in mass, strength, and inability to maintain balance.
Teet Seene, Priit Kaasik
doaj   +1 more source

Polymorphic myopathological findings in a 77‐year‐old woman with oculo‐bulbo‐facial and distal weakness

Brain Pathology, EarlyView.
Michele Tosi, Angela Puma, Elena Faedo, Gianmarco Severa, Luisa Villa, Sabrina Sacconi, Edoardo Malfatti   +6 more
wiley   +1 more source

Piperine disrupts the OFF state of the resting thick filament of rat skeletal muscle, enhancing dynamic contractility in a fibre‐type‐dependent manner

The Journal of Physiology, Volume 604, Issue 18, Page 7739-7771, 15 September 2026.
Abstract figure legend We investigated the effects of piperine on (1) the structure of the resting thick filament and (2) dynamic contractility in fibres and intact slow (soleus) and fast (extensor digitorum longus, EDL) rat muscles, respectively. The structure of the resting thick filament was assessed pre‐ and post‐piperine incubation using small ...
Daniel Z. Kruse, Jon Herskind, Michel N. Kuehn, Annika J. Klotz, Anthony L. Hessel, Kristian Overgaard   +5 more
wiley   +1 more source

Unveiling New Insights: Reinterpreting DES Mutation, p.Arg383His, Through a Study of an Iranian Family With Isolated Hypertrophic Cardiomyopathy, Implication for Phenotype–Genotype Correlation Analysis

Clinical Case Reports, Volume 14, Issue 8, August 2026.
ABSTRACT Desmin, a crucial intermediate filament in muscle cells, maintains structural integrity in cardiac muscle and provides stability to striated muscle cells. Mutations in the DES gene lead to desminopathies, causing diverse cardiac and skeletal myopathies.
Saeideh Kavousi, Farzad Kamali, Bahareh Rabbani, Mehrdad Behmanesh, Nejat Mahdieh, Mehrdad Noruzinia   +5 more
wiley   +1 more source

Phenotype standardization for statin-induced myotoxicity. [PDF]

, 2014
Statins are widely used lipid-lowering drugs that are effective in reducing cardiovascular disease risk. Although they are generally well tolerated, they can cause muscle toxicity, which can lead to severe rhabdomyolysis.
Fahy, J., Neely, D, Fahy, J, Wadelius, M, Palmer, CN, Carr, D. F., Maitland-van Der Zee, AH, Laaksonen, R, Maitland-van Der Zee, A. H., Wadelius, M., Yue, QY, Chinoy, H.; id_orcid, Psaty, BM, Bloch, K. M., Cooper, R. G., Neely, D., Psaty, B. M., Chinoy, H., Pirmohamed, M., Chinoy, H, Palmer, C. N. A., Voora, D, Palmer, C. N. A.; id_orcid, Voora, D., Armitage, J., Wadelius, Mia,, Yue, Q. Y., Alfirevic, A., Alfirevic, A, Armitage, J, Palmer, C. N A, Pirmohamed, M, Palmer, PN, Hanson, A., Bloch, KM, Laaksonen, R., Cooper, RG, Yue, Q-Y, Wadelius, Mia, Carr, DF, Hanson, A   +40 more
core   +1 more source

A Mutation in the Dimerization Domain of Filamin C Causes a Novel Type of Autosomal Dominant Myofibrillar Myopathy [PDF]

, 2005
Myofibrillar myopathy (MFM) is a human disease that is characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations. In an extended German pedigree with a novel form of MFM characterized by clinical features of a limb-
Schröder, Rolf, Kley, Rudolf A., Fürst, Dieter O., Löwe, Thomas, Huebner, Angela, Himmel, Mirko, Vorgerd, Matthias, Lochmüller, Hanns, van der Ven, Peter F.M., Bruchertseifer, Vera, Koehler, Katrin   +10 more
core   +2 more sources

Myosin Post‐Translational Modifications Associated With Critical Illness Myopathy

Acta Physiologica, Volume 242, Issue 7, July 2026.
ABSTRACT Background Critical illness myopathy is a common and devastating consequence of critical care, causing dramatic loss of muscle mass and function in intensive care unit patients. Functional deficits often exceed the loss in muscle mass and myosin content.
Fernando Ribeiro, Bruno Di Geronimo, Nicola Cacciani, Anna Widgren, Yvette Hedström, Anselmo S. Moriscot, Peter M. Kasson, Shina C. L. Kamerlin, Jonas Bergquist, Lars Larsson   +9 more
wiley   +1 more source

Metformin rescues muscle function in BAG3 myofibrillar myopathy models

, 2020
Dominant de novo mutations in the co-chaperone BAG3 cause a severe form of myofibrillar myopathy, exhibiting progressive muscle weakness, muscle structural failure, and protein aggregation. To elucidate the mechanism of disease in, and identify therapies
Emmanuelle Lacene (6177269), Emily C. Baxter (9491444), Tanya Stojkovic (445701), Keyne Monro (2924136), Viola Oorschot (113700), Yvan Torrente (54046), Clara Lee (2557852), Caitlin Williams (2069830), Mirella Meregalli (141757), Keith E. Schulze (6895205), Robert J. Bryson-Richardson (7907198), Rita J. Serrano (9491441), Avnika A. Ruparelia (4839585), Margit Fuchs (817677), Georg Ramm (173555), Josée N. Lavoie (9491447), Emily A. McKaige (4839582)   +16 more
core   +1 more source

UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) binds to alpha-actinin 1: novel pathways in skeletal muscle? [PDF]

, 2008
Hereditary inclusion body myopathy (HIBM) is a rare neuromuscular disorder caused by mutations in GNE, the key enzyme in the biosynthetic pathway of sialic acid.
North Kathryn N., Mitrani-Rosenbaum, S, Shira Amsili, Stephan Hinderlich, Krause, S, Hinderlich Stephan, Hagit Zer, MacArthur, DG, Mitrani-Rosenbaum Stella, Mitrani-Rosenbaum, Stella, Zer, Hagit, Amsili Shira, Becker-Cohen, M, Hinderlich, S, Amsili, S, Becker-Cohen Michal, Krause, Sabine, Krause Sabine, Kathryn N North, North, Kathryn N., Zer Hagit, Sabine Krause, Daniel G MacArthur, Hinderlich, Stephan, Michal Becker-Cohen, MacArthur Daniel G., Zer, H, MacArthur, Daniel G., Stella Mitrani-Rosenbaum, Becker-Cohen, Michal, Amsili, Shira, North, KN   +31 more
core   +2 more sources

A muscular dystrophy associated with bi‐allelic LEMD2 variants: Expanding the genotype of nuclear envelopathies

Brain Pathology, Volume 36, Issue 4, July 2026.
Proteomics‐guided exome re‐analysis identifies bi‐allelic variants in the nuclear envelope LEMD2 gene, expanding its phenotypic spectrum. Created in BioRender. Pauper, M. (2026) https://BioRender.com/xamvo92.
Marc Pauper, Heike Kölbel, Iakowos Karakesisoglou, Anne Schänzer, Johann Böhm, Rachel Thompson, Nicolai Kohlschmidt, Bernd Ringel, Gisèle Bonne, Katja Neuhoff, Andrea Gangfuß, Ozge Aksel Kilicarslan, Sergi Beltran Agullo, Andreas Hentschel, Ulrike Schara‐Schmidt, Hanns Lochmüller, Kiran Polavarapu, Andreas Roos   +17 more
wiley   +1 more source