The Noncatalytic Portion of Human UDP-glucose:Glycoprotein Glucosyltransferase I Confers UDP-glucose Binding and Transferase Function to the Catalytic Domain
Open Access
- 1 October 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (44) , 43320-43328
- https://doi.org/10.1074/jbc.m305800200
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzymeGlycobiology, 2000
- Conformational Requirements for Glycoprotein Reglucosylation in the Endoplasmic ReticulumThe Journal of cell biology, 2000
- Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57Journal of Biological Chemistry, 1998
- Interaction of the Thiol-Dependent Reductase ERp57 with Nascent GlycoproteinsScience, 1997
- 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
- Chaperone Function of Calreticulin When Expressed in the Endoplasmic Reticulum as the Membrane-anchored and Soluble FormsJournal of Biological Chemistry, 1995
- The Molecular Chaperone Calnexin Binds Glc1Man9GlcNAc2 Oligosaccharide as an Initial Step in Recognizing Unfolded GlycoproteinsJournal of Biological Chemistry, 1995
- Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.Proceedings of the National Academy of Sciences, 1994
- Protein folding in the cellNature, 1992
- ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDESAnnual Review of Biochemistry, 1985