Distance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein

Biochemical Journal

Volumn 370, Issue 1, 2003, Pages 351-355

  Walmsley, Adrian R ^a   Hooper, Nigel M ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Endoplasmic reticulum; Glycoforms; Glycosyl phosphatidylinositol; Mutagenesis; Oligosaccharyltransferase; Translocon

Indexed keywords

ADDITION REACTIONS; CELLS; COMPLEXATION; NEUROLOGY; POLYSACCHARIDES;

NEURONAL CELLS;

PROTEINS;

AMINO ACID; ASPARAGINE; GLUCOSE; ISOLEUCINE; OLIGOSACCHARYLTRANSFERASE; PHENYLALANINE; PHOSPHATIDYLINOSITOL; PRION PROTEIN; THREONINE; TRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DYNAMICS; ENZYME ACTIVE SITE; HUMAN; HUMAN CELL; NEUROBLASTOMA CELL; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN GLYCOSYLATION; PROTEIN SECRETION; WESTERN BLOTTING;

AMIDOHYDROLASES; ANIMALS; BASE SEQUENCE; BLOTTING, WESTERN; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSYLATION; HUMANS; HYDROLYSIS; MICE; PEPTIDE-N4-(N-ACETYL-BETA-GLUCOSAMINYL) ASPARAGINE AMIDASE; PHOSPHATIDYLINOSITOL DIACYLGLYCEROL-LYASE; PHOSPHOLIPASE C; PRIONS; TUMOR CELLS, CULTURED;

EID: 0037442534     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021303     Document Type: Article

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