Excess of nicastrin in brain results in heterozygosity having no effect on endogenous APP processing and amyloid peptide levels in vivo

Neurobiology of Disease

Volumn 25, Issue 2, 2007, Pages 291-296

  Brijbassi, Sonya ^a,b   Amtul, Zareen ^a,b   Newbigging, Susan ^c   Westaway, David ^d   St George Hyslop, Peter ^d   Rozmahel, Richard F ^a,b  

^a UNIVERSITY OF WESTERN ONTARIO   (Canada)

^b LAWSON HEALTH RESEARCH INSTITUTE   (Canada)

^c UNIVERSITY OF GUELPH   (Canada)

^d UNIVERSITY OF TORONTO   (Canada)

Author keywords

secretase; Alzheimer's disease; Amyloid precursor protein; Nicastrin presenilin

Indexed keywords

AMYLOID PRECURSOR PROTEIN; AMYLOID PROTEIN; BRAIN PROTEIN; GAMMA SECRETASE; MEMBRANE PROTEIN; MESSENGER RNA; NICASTRIN; PEPTIDE; PRESENILIN; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SUBSTRATE COMPLEX; FIBROBLAST; FUNCTIONAL PROTEOMICS; HETEROZYGOSITY; IN VIVO STUDY; MOUSE; NERVE CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN SYNTHESIS; WILD TYPE;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; BRAIN; CELL MEMBRANE; DOWN-REGULATION; HETEROZYGOTE; MACROMOLECULAR SUBSTANCES; MEMBRANE GLYCOPROTEINS; MICE; MICE, KNOCKOUT; PRESENILIN-1; PROTEIN STRUCTURE, TERTIARY; RNA, MESSENGER;

EID: 33846283862     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2006.09.013     Document Type: Article

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