Differential fate of glycoproteins carrying a monoglucosylated form of truncated N-glycan in a new CHO line, MadIA214, selected for a thermosensitive secretory defect

Journal of Cell Science

Volumn 110, Issue 3, 1997, Pages 323-336

  Ermonval, Myriam ^a   Cacan, René ^b   Gorgas, Karin ^c   Haas, Ingrid G ^c   Verbert, André ^b   Buttin, Gérard ^a  

^a CNRS   (France)

^b UNIVERSITÉ DES SCIENCES ET TECHNOLOGIES DE LILLE   (France)

^c UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

CHO; ER retention; Glycoprotein degradation; MHC class I; N glycosylation; Secretory alkaline phosphatase; Thermosensitive secretion

Indexed keywords

ALKALINE PHOSPHATASE PLACENTA ISOENZYME; GLYCAN; GLYCOPROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

ANIMAL CELL; ARTICLE; CELL MEMBRANE PERMEABILITY; CHO CELL; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN TRANSPORT; TEMPERATURE SENSITIVITY;

ALKALINE PHOSPHATASE; ANIMALS; BREFELDIN A; CARRIER PROTEINS; CHO CELLS; CRICETINAE; CYCLOPENTANES; ENDOPLASMIC RETICULUM; GLYCOPROTEINS; GLYCOSYLATION; GOLGI APPARATUS; H-2 ANTIGENS; HEAT-SHOCK PROTEINS; HUMANS; ISOENZYMES; MOLECULAR CHAPERONES; MUTAGENESIS; OLIGOSACCHARIDES; TEMPERATURE;

EID: 0342506459     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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