Three histidine residues of amyloid-β peptide control the redox activity of copper and iron

Biochemistry

Volumn 46, Issue 44, 2007, Pages 12737-12743

  Nakamura, M ^a   Shishido, N ^a   Nunomura, Akihiko ^a   Smith, Mark A ^b   Perry, George ^c   Hayashi, Y ^a   Nakayama, K ^d   Hayashi, T ^d  

^a ASAHIKAWA MEDICAL COLLEGE   (Japan)

^b CASE WESTERN RESERVE UNIVERSITY   (United States)

^c University of San Antonio   (United States)

^d HOKKAIDO INSTITUTE OF PUBLIC HEALTH   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYL RADICAL GENERATION; OXIDASE ACTIVITY;

AMINO ACIDS; CATALYST ACTIVITY; COPPER; DISEASE CONTROL; ENZYME ACTIVITY; IRON; OXIDATIVE STRESS;

PEPTIDES;

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-16]; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[25-35]; ASCORBATE OXIDASE; COPPER; FERRIC ION; GLYCYLHISTIDYLLYSINE; HISTIDINE; HYDROXYL RADICAL; IRON; SUPEROXIDE; SUPEROXIDE DISMUTASE; TRANSITION ELEMENT; UNCLASSIFIED DRUG; ZINC;

ALZHEIMER DISEASE; ARTICLE; CATALYSIS; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; FENTON REACTION; NERVE CELL; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; SENILE PLAQUE;

AMYLOID BETA-PROTEIN; ASCORBIC ACID; COPPER; HISTIDINE; HUMANS; HYDROGEN PEROXIDE; HYDROXYL RADICAL; IRON; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS;

EID: 35948936850     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701079z     Document Type: Article

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