Protein misfolding, mitochondrial dysfunction and muscle loss are not directly dependent on soluble and aggregation state of mSOD1 protein in skeletal muscle of ALS

Biochemical and Biophysical Research Communications

Volumn 417, Issue 4, 2012, Pages 1275-1279

  Wei, Rochelle ^a   Bhattacharya, Arunabh ^a,b   Chintalaramulu, Naveen ^a   Jernigan, Amanda L ^b   Liu, Yuhong ^a   Van Remmen, Holly ^a,b,c   Chaudhuri, Asish R ^a,c  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^b Mays Cancer Center at UT Health San Antonio   (United States)

^c SOUTH TEXAS VETERANS HEALTH CARE SYSTEM   (United States)

Author keywords

ALS; G93A; Mitochondria; Protein misfolding; Reactive oxygen species

Indexed keywords

CHYMOTRYPSIN; COPPER ZINC SUPEROXIDE DISMUTASE; MUTANT SUPEROXIDE DISMUTASE 1; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CELL FUNCTION; CONTROLLED STUDY; DISEASE SEVERITY; ENZYME ACTIVITY; HUMAN; HUMAN TISSUE; MITOCHONDRION; MOTONEURON; MOUSE; MUSCLE MASS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SKELETAL MUSCLE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; FEMALE; MICE; MICE, INBRED C57BL; MITOCHONDRIAL DISEASES; MUSCLE, SKELETAL; PROTEIN FOLDING; SOLUBILITY; SUPEROXIDE DISMUTASE;

EID: 84863035837     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.12.126     Document Type: Article

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