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Contributions of the Lectin and Polypeptide Binding Sites of Calreticulin to Its Chaperone Functions in Vitro and in Cells

Calreticulin is a lectin chaperone of the endoplasmic reticulum that interacts with newly synthesized glycoproteins by binding to Glc(1)Man(9)GlcNAc(2) oligosaccharides as well as to the polypeptide chain. In vitro, the latter interaction potently suppresses the aggregation of various non-glycosylat...

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Detalhes bibliográficos
Publicado no:J Biol Chem
Main Authors: Lum, Ronnie, Ahmad, Samar, Hong, Seo Jung, Chapman, Daniel C., Kozlov, Guennadi, Williams, David B.
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2016
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC5016696/
https://ncbi.nlm.nih.gov/pubmed/27413183
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M116.746321
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