Results 191 to 200 of about 28,592 (236)

Piezo1 specific deletion in endothelial cell protects the progression of pulmonary fibrosis in mice. [PDF]

Cell Commun Signal
He B, Tan Q, Xu H, Chen X, Wan R, Yao Y, Pan X, Liu S, Chen X, Jiang J, Luo S, An Y, Li J.   +12 more
europepmc   +1 more source

French National Protocol for Diagnosis and Care of Calpainopathy (LGMD R1/LGMD D4): consensus guidelines for clinical practice. [PDF]

Orphanet J Rare Dis
Severa G, Souvannanorath S, Tahiri I, Alimi C, Slioui A, Villa L, Salort-Campana E, Leturcq F, Streichenberger N, Krahn M, Solé G, Feasson L, Nadaj-Pakleza A, Tard C, Stojkovic T, Sacconi S, Malfatti E.   +16 more
europepmc   +1 more source

Multidimensional mechanism of pulsed electric field synergized L-arginine upon goose meat tenderization: Based on molecular dynamics simulation and protein interaction network. [PDF]

Food Chem X
Ma R, Chen C, Shi Z, Hu Y, Sun Y, Xia Q, Zhou C, Pan D.   +7 more
europepmc   +1 more source

GFAP degradation in TBI: linking novel modified products to astrocyte pathology and patient outcome. [PDF]

Acta Neuropathol Commun
Wanner IB, Halford J, Lopez J, Shen S, Chen Y, Zhao H, Salas C, Loo RO, Robicsek S, Ellingson BM, Gornbein J, Van Meter TE, Shaw G, Loo JA, Vespa PM.   +14 more
europepmc   +1 more source

Individual pre-slaughter muscle proteolysis levels correlated with postmortem taste-related amino acid concentrations in broiler chickens. [PDF]

Poult Sci
Katsumata S, Egawa M, Yoshino K, Katafuchi A, Shimamoto S, Ohtsuka A, Ijiri D.   +6 more
europepmc   +1 more source

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Calpain-3 mutations in Turkey

European Journal of Pediatrics, 2006
Autosomal recessive limb-girdle muscular dystrophies (LGMD2s) are a clinically and genetically heterogeneous group of disorders, characterized by progressive involvement of the proximal limb girdle muscles; the group includes at least 10 different genetic entities.
BALCI B, AURINO S, HALILOGLU G, TALIM B, ERDEM S, AKCOREN Z, TAN E, CAGLAR M, RICHARD I, NIGRO, Vincenzo, TOPALOGLU H, DINCER P.   +11 more
openaire   +3 more sources

μ-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans

American Journal of Physiology-Cell Physiology, 2006
μ-calpain and calpain-3 are Ca2+-dependent proteases found in skeletal muscle. Autolysis of calpains is observed using Western blot analysis as the cleaving of the full-length proteins to shorter products. Biochemical assays suggest that μ-calpain becomes proteolytically active in the presence of 2–200 μM Ca2+. Although calpain-3 is poorly understood,
Murphy, Robyn., Snow, Rodney., Lamb, Graham.   +2 more
openaire   +2 more sources

MEF2A regulates Calpain 3 expression in L6 myoblasts

Gene, 2018
Calpain 3 (Capn3), a skeletal muscle-specific member of the calpain family, executes some non-proteolytic functions besides its role as a Ca2+-regulated proteolytic enzyme. Previously, we found that changes in Capn3 expression were linearly correlated with the degree of muscular atrophy following reversible sciatic nerve injury and that knockdown of ...
Ronghua Wu, Jun Wang, Jian Yao, Zhangji Dong, Yan Liu, Mei Liu   +5 more
openaire   +2 more sources

Calpain 3 deficiency presenting as fibre type disproportion

Neuropathology and Applied Neurobiology, 2009
No abstract ...
VATTEMI, Gaetano Nicola, TONIN, PAOLA, Neri M., MARINI, Matteo, Gualandi F., GUGLIELMI, Valeria, Ferlini A., TOMELLERI, Giuliano   +7 more
openaire   +2 more sources