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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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| 出版年: | J Biol Chem |
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| 主要な著者: | , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Biochemistry and Molecular Biology
2016
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| 主題: | |
| オンライン･アクセス: | 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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