4.5 Review

Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?

期刊

FEBS LETTERS
卷 476, 期 1-2, 页码 38-41

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01666-5

关键词

endoplasmic reticulum; glycoprotein; protein folding; molecular chaperone; calnexin; ERp57

向作者/读者索取更多资源

The endoplasmic reticulum (ER) is a major site of protein synthesis and its inside, or lumen, is a major site of protein folding, The lumen of the ER contains many folding factors and molecular chaperones, which facilitate protein folding by increasing both the rate and the efficiency of this process. Amongst the many ER folding factors, there are three components that specifically modulate the folding glycoproteins bearing N-linked carbohydrate side chains. These components are calnexin, calreticulin and ERp57, and this review focuses on the molecular basis for their capacity to influence glycoprotein folding. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据