Quantification of copper binding to amyloid precursor protein domain 2 and its Caenorhabditis elegans ortholog. Implications for biological function

Metallomics

Volumn 6, Issue 1, 2014, Pages 105-116

  Leong, Su Ling ^a,b   Young, Tessa R ^a,b   Barnham, Kevin J ^a,b,c   Wedd, Anthony G ^a,b   Hinds, Mark G ^a,b   Xiao, Zhiguang ^a,b   Cappai, Roberto ^a,b  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

^c FLOREY INSTITUTE OF NEUROSCIENCE AND MENTAL HEALTH   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; COPPER; DISSOCIATION; GLYCOPROTEINS;

ALZHEIMER'S DISEASE; AMYLOID PRECURSOR PROTEINS; BIOLOGICAL FUNCTIONS; CAENORHABDITIS ELEGANS; COPPER HOMEOSTASIS; DISSOCIATION CONSTANT; REACTIVE OXYGEN SPECIES; SOLUTION STRUCTURES;

COPPER COMPOUNDS;

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; AMYLOID PRECURSOR PROTEIN DOMAIN 2; COPPER; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CAENORHABDITIS ELEGANS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; ANIMALS; BINDING, COMPETITIVE; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; COPPER; HYDROGEN PEROXIDE; KINETICS; MEMBRANE PROTEINS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; REACTIVE OXYGEN SPECIES; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84890923671     PISSN: 17565901     EISSN: 1756591X     Source Type: Journal    
DOI: 10.1039/c3mt00258f     Document Type: Article

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