Results 131 to 140 of about 3,769 (195)

Mechanotransduction and Skeletal Muscle Atrophy: The Interplay Between Focal Adhesions and Oxidative Stress. [PDF]

Int J Mol Sci
Kamal KY, Trombetta-Lima M.
europepmc   +1 more source

Treatabolome for finely targeting muscle pathology in LGMD. [PDF]

Acta Myol
Angelini C.
europepmc   +1 more source

Recombinant human mitsugumin 53: a potential therapeutic agent for multiple diseases. [PDF]

Front Pharmacol
Li J, Shen J, Li T, Wang L.
europepmc   +1 more source

Limb-Girdle Muscular Dystrophies (LGMD): Clinical features, diagnosis and genetic variability through next generation sequencing. [PDF]

Glob Med Genet
Mathur P, Kaur A, Vijay U, Gupta A, Agarwal K, Agrawal L.   +5 more
europepmc   +1 more source

A versatile microfluidics platform for enhanced multi-target super-resolution microscopy

Basak S, Chi-Vu K, Mougios N, Oleksiievets N, Pollack Y, Brandenburg S, Opazo F, Lehnart SE, Enderlein J, Tsukanov R.   +9 more
europepmc   +1 more source

Muscular dystrophy with marked Dysferlin deficiency is consistently caused by primary dysferlin gene mutations [PDF]

European Journal of Human Genetics, 2011
Dysferlin is a 237-kDa transmembrane protein involved in calcium-mediated sarcolemma resealing. Dysferlin gene mutations cause limb-girdle muscular dystrophy (LGMD) 2B, Miyoshi myopathy (MM) and distal myopathy of the anterior tibialis. Considering that a secondary Dysferlin reduction has also been described in other myopathies, our original goal was ...
Mafalda Cacciottolo, Marina Fanin, Carlo Minetti   +2 more
exaly   +7 more sources

Modular Dispensability of Dysferlin C2 Domains Reveals Rational Design for Mini-dysferlin Molecules [PDF]

Journal of Biological Chemistry, 2012
Dysferlin is a large transmembrane protein composed of a C-terminal transmembrane domain, two DysF domains, and seven C2 domains that mediate lipid- and protein-binding interactions. Recessive loss-of-function mutations in dysferlin lead to muscular dystrophies, for which no treatment is currently available.
Bilal A Azakir, Sabrina Di Fulvio, Christian Therrien   +2 more
exaly   +8 more sources

Characterization of zebrafish dysferlin by morpholino knockdown [PDF]

Biochemical and Biophysical Research Communications, 2011
Mutations in the gene encoding dysferlin cause two distinct muscular dystrophy phenotypes: limb-girdle muscular dystrophy type 2B (LGMD-2B) and Miyoshi myopathy (MM). Dysferlin is a large transmembrane protein involved in myoblast fusion and membrane resealing.
Genri Kawahara, Jennifer A Myers, Matthew S Alexander   +2 more
exaly   +3 more sources

Dysferlin Interacts with Affixin (β-Parvin) at the Sarcolemma [PDF]

Journal of Neuropathology and Experimental Neurology, 2005
The dysferlin gene is defective in Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B). Dysferlin is a sarcolemmal protein that is implicated in calcium-dependent membrane repair. Affixin (beta-parvin) is a novel, integrin-linked kinase-binding protein that is involved in the linkage between integrin and the cytoskeleton.
Chie Matsuda, Kimihiko Kameyama, Kazuhiko Tagawa   +2 more
exaly   +3 more sources