Calnexin can interact withN-linked glycans located close to the endoplasmic reticulum membrane
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(96)01207-0/fullpdf
Reference19 articles.
1. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum
2. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
3. C. Hammond I. Braakman A. Helenius Proc. Nad. Acad. Sci. USA 91 1994 913 917
4. Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis.
5. Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90).
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1. In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases;Physiological Reviews;2007-10
2. Comparative glycoproteomics based on lectins affinity capture ofN-linked glycoproteins from human Chang liver cells and MHCC97-H cells;PROTEOMICS;2007-07
3. Mechanisms of Pharmacological Rescue of Trafficking-defective hERG Mutant Channels in Human Long QT Syndrome;Journal of Biological Chemistry;2006-02
4. More Than One Glycan Is Needed for ER Glucosidase II to Allow Entry of Glycoproteins into the Calnexin/Calreticulin Cycle;Molecular Cell;2005-07
5. Glycosidase Inhibitors as Potential HIV Entry Inhibitors?;Current Drug Metabolism;2004-08-01
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