Glycan-dependent and -independent Association of Vesicular Stomatitis Virus G Protein with Calnexin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference42 articles.
1. Association of folding intermediates of glycoproteins with calnexin during protein maturation
2. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.
3. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.
4. Persistence of glucose residues on core oligosaccharides prevents association of TCR alpha and TCR beta proteins with calnexin and results specifically in accelerated degradation of nascent TCR alpha proteins within the endoplasmic reticulum.
5. The Molecular Chaperone Calnexin Binds Glc1Man9GlcNAc2 Oligosaccharide as an Initial Step in Recognizing Unfolded Glycoproteins
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1. Calnexin mediates the maturation of GPI-anchors through ER retention;Journal of Biological Chemistry;2020-11
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3. Protein Quality Control in the Endoplasmic Reticulum;The Protein Journal;2019-04-19
4. Endoplasmic reticulum–retained podocin mutants are massively degraded by the proteasome;Journal of Biological Chemistry;2018-03
5. N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle;Traffic;2016-01-10
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