N-linked glycosylation of β-amyloid precursor protein

Biochemical and Biophysical Research Communications

Volumn 189, Issue 3, 1992, Pages 1667-1673

  Påhlsson, Peter ^a   Shakin Eshleman, Susan H ^a   Spitalnik, Steven L ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; PROTEIN PRECURSOR;

ANIMAL CELL; ARTICLE; CHO CELL; DNA TRANSFECTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; PROTEIN PROCESSING;

ALTERNATIVE SPLICING; AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; ANIMAL; ASPARAGINE; CELL-FREE SYSTEM; CHO CELLS; GLYCOSIDE HYDROLASES; GLYCOSYLATION; HAMSTERS; HUMAN; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RESTRICTION MAPPING; SUPPORT, U.S. GOV'T, P.H.S.; TRANSCRIPTION, GENETIC; TRANSFECTION; TRANSLATION, GENETIC;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS;

EID: 0027053399     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/0006-291X(92)90269-Q     Document Type: Article

References (31)

1. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
2. Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments
3. Glycosylation at specific sites of erythropoietin is essential for biosynthesis, secretion, and biological function.