Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: Implications for ALS

Biochemistry

Volumn 43, Issue 51, 2004, Pages 16525-16531

  Lynch, Sandra M ^a   Boswell, Sarah A ^a,b   Colón, Wilfredo ^a  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^b ORDWAY RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; DISEASES; ENZYMES; PROTEINS; STABILITY; THERMODYNAMIC STABILITY; ZINC;

FAMILIAN AMYOTROPHIC LATERAL SCLEROSIS (FALS); NEURODEGENERATIVE DISEASES; SOD MUTATIONS; SUPEROXIDE DISMUTASE (SOD);

COPPER;

ALANINE; ARGININE; ASPARTIC ACID; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; GLYCINE; HISTIDINE; LEUCINE; METAL; PHENYLALANINE; ZINC;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DEGENERATIVE DISEASE; ENZYME KINETICS; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; THERMODYNAMICS;

AMYOTROPHIC LATERAL SCLEROSIS; COPPER; ENZYME STABILITY; HUMANS; KINETICS; LIGANDS; MUTATION; PROTEIN DENATURATION; SUPEROXIDE DISMUTASE; THERMODYNAMICS; ZINC;

EID: 11144256229     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048831v     Document Type: Article

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