An examination of αb-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis

Journal of Neurochemistry

Volumn 113, Issue 5, 2010, Pages 1092-1100

  Karch, Celeste M ^a,b   Borchelt, David R ^a  

^a UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

B crystallin; Amyotrophic lateral sclerosis; Cu Zn superoxide dismutase; Heat shock proteins; Protein misfolding

Indexed keywords

ALPHA CRYSTALLIN; COPPER ZINC SUPEROXIDE DISMUTASE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL CELL; ANIMAL CELL CULTURE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CENTRIFUGATION; CONTROLLED STUDY; HOMEOSTASIS; MOUSE; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; SPINAL CORD; TISSUE DISTRIBUTION; TRANSGENIC MOUSE;

ALPHA-CRYSTALLIN B CHAIN; AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; CENTRIFUGATION; DETERGENTS; DISEASE MODELS, ANIMAL; DISEASE PROGRESSION; HUMANS; KAPLAN-MEIERS ESTIMATE; MICE; MICE, KNOCKOUT; MICE, TRANSGENIC; MUSCLE, SKELETAL; MUTATION; SUPEROXIDE DISMUTASE; SURVIVAL ANALYSIS;

MUS; MUS MUSCULUS;

EID: 77951889547     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.06572.x     Document Type: Article

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