The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease

Journal of Alzheimer's Disease

Volumn 43, Issue 4, 2014, Pages 1163-1168

  Gough, Mallory ^a   Blanthorn Hazell, Sophee ^a   Parkin, Edward T ^a  

^a LANCASTER UNIVERSITY   (United Kingdom)

Author keywords

Amyloid protein precursor; amyloidogenic processing; histidine 14; secretase

Indexed keywords

ALANINE; AMYLOID BETA PROTEIN; BETA SECRETASE; COPPER; HISTIDINE; AMYLOID PRECURSOR PROTEIN; APP PROTEIN, HUMAN; SECRETASE;

ALZHEIMER DISEASE; ARTICLE; BINDING AFFINITY; DOWN REGULATION; HUMAN; PROTEIN DEGRADATION; CHEMISTRY; GENETIC TRANSFECTION; GENETICS; HEK293 CELL LINE; METABOLISM; MUTATION; PROTEIN TERTIARY STRUCTURE; TUMOR CELL LINE;

ALANINE; ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; CELL LINE, TUMOR; COPPER; HEK293 CELLS; HISTIDINE; HUMANS; MUTATION; PROTEIN STRUCTURE, TERTIARY; TRANSFECTION;

EID: 84919932303     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-141650     Document Type: Article

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