N-linked oligosaccharide chains of Sendai virus fusion protein determine the interaction with endoplasmic reticulum molecular chaperones
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(02)02229-9/fullpdf
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1. Calnexin, calreticulin and the folding of glycoproteins
2. Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
3. Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57
4. BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum
5. The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation
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1. Viral Evolution Shaped by Host Proteostasis Networks;Annual Review of Virology;2023-09-29
2. Nitazoxanide inhibits paramyxovirus replication by targeting the Fusion protein folding: role of glycoprotein-specific thiol oxidoreductase ERp57;Scientific Reports;2018-07-11
3. Stepwise Assembly of Fibrinogen Is Assisted by the Endoplasmic Reticulum Lectin-Chaperone System in HepG2 Cells;PLoS ONE;2013-09-10
4. Sendai Virus Biology and Engineering Leading up to the Development of a Novel Class of Expression Vector;Sendai Virus Vector;2013
5. Membrane Receptors for Vitamin D Metabolites and the Role of Reactive Oxygen Species;Oxidative Stress and Disease;2012-11-21
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