Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: Parallels to precursors in amyloid disease

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 27, 2006, Pages 10218-10223

  Nordlund, Anna ^a   Oliveberg, Mikael ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Neurodegenerative disease; Protein folding; Transition state

Indexed keywords

COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; ENZYME; PROTEIN PRECURSOR; PROTEIN SUBUNIT; SUPEROXIDE DISMUTASE; ZINC;

AMYLOID NEUROPATHY; AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; CONTROLLED STUDY; CYTOTOXICITY; DISEASE ASSOCIATION; DISEASE MODEL; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME MODIFICATION; ENZYME STRUCTURE; ENZYME SUBUNIT; NERVE DEGENERATION; NEUROPATHOLOGY; NEUROTOXICITY; PHYSIOLOGY; PRECURSOR; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; STRUCTURAL PROTEOMICS;

AMYLOIDOSIS; AMYOTROPHIC LATERAL SCLEROSIS; HUMANS; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SUPEROXIDE DISMUTASE; THERMODYNAMICS;

EID: 33745889333     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0601696103     Document Type: Article

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