SOD1 aggregation and ALS: Role of metallation states and disulfide status

Current Topics in Medicinal Chemistry

Volumn 12, Issue 22, 2012, Pages 2560-2572

  Sheng, Yuewei ^a   Chattopadhyay, Madhuri ^a   Whitelegge, Julian ^b   Valentine, Joan Selverstone ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c Ewha Womans University   (South Korea)

Author keywords

Amyotrophic lateral sclerosis; Copper zinc superoxide dismutase; Disulfide status; Metallation state; Protein aggregation

Indexed keywords

CHAPERONE; COPPER ZINC SUPEROXIDE DISMUTASE; DISULFIDE; GLUTATHIONE; SUPEROXIDE DISMUTASE;

AMYOTROPHIC LATERAL SCLEROSIS; APOPTOSIS; BINDING AFFINITY; DISEASE COURSE; GENE MUTATION; HUMAN; INFLAMMATION; MASS SPECTROMETRY; METALLATION; NONHUMAN; OLIGOMERIZATION; PATHOLOGY; PROTEIN AGGREGATION; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; DISULFIDES; HUMANS; MUTATION; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; SUPEROXIDE DISMUTASE;

EID: 84874842421     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026611212220010     Document Type: Review

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