Trimming and Readdition of Glucose to N-Linked Oligosaccharides Determines Calnexin Association of a Substrate Glycoprotein in Living Cells
Open Access
- 1 March 1999
- journal article
- Published by Elsevier
- Vol. 274 (11) , 7537-7544
- https://doi.org/10.1074/jbc.274.11.7537
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Lectins as chaperones in glycoprotein foldingPublished by Elsevier ,2002
- Promotion of transferrin folding by cyclic interactions with calnexin and calreticulinThe EMBO Journal, 1997
- Calnexin, calreticulin and the folding of glycoproteinsTrends in Cell Biology, 1997
- Glycan-dependent and -independent Association of Vesicular Stomatitis Virus G Protein with CalnexinJournal of Biological Chemistry, 1996
- Definition of the Lectin-like Properties of the Molecular Chaperone, Calreticulin, and Demonstration of Its Copurification with Endomannosidase from Rat Liver GolgiJournal of Biological Chemistry, 1996
- Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulumCell, 1995
- Calnexin: a molecular chaperone with a taste for carbohydrateBiochemistry and Cell Biology, 1995
- The Molecular Chaperone Calnexin Binds Glc1Man9GlcNAc2 Oligosaccharide as an Initial Step in Recognizing Unfolded GlycoproteinsJournal of Biological Chemistry, 1995
- Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulumProteins-Structure Function and Bioinformatics, 1992
- Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferaseBiochemistry, 1992