Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10

Glycobiology

Volumn 21, Issue 10, 2011, Pages 1382-1388

  Tsachaki, Maria ^a   Serlidaki, Despina ^a   Fetani, Andriana ^a   Zarkou, Vasiliki ^a   Rozani, Ismini ^a   Ghiso, Jorge ^b   Efthimiopoulos, Spiros ^a  

^a UNIVERSITY OF ATHENS   (Greece)

^b NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Alzheimer's disease; BRI2; familial British dementia; familial Danish dementia; glycosylation

Indexed keywords

ADAM10 ENDOPEPTIDASE; ASPARAGINE; BRI2 PROTEIN; FURIN; MEMBRANE PROTEIN; TUNICAMYCIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BIOTINYLATION; CELL STRAIN HEK293; CELL SURFACE; CONSENSUS SEQUENCE; CONTROLLED STUDY; DEMENTIA; HUMAN; HUMAN CELL; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN TRANSPORT;

ADAM PROTEINS; AMYLOID PRECURSOR PROTEIN SECRETASES; ASPARAGINE; CELL MEMBRANE; FURIN; GLYCOSYLATION; HEK293 CELLS; HUMANS; MEMBRANE PROTEINS; PROTEIN PROCESSING, POST-TRANSLATIONAL; TRANSFECTION;

EID: 80052681746     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr097     Document Type: Article

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