Protein folding and unfolding by Escherichia coli chaperones and chaperonins

被引：33

作者：

Gottesman, ME ^{[1
]}

Hendrickson, WA

机构：

[1] Columbia Univ, Inst Canc Res, New York, NY 10032 USA

[2] Columbia Univ, Dept Microbiol, New York, NY 10032 USA

[3] Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10032 USA

[4] Columbia Univ, Howard Hughes Med Inst, Dept Mol Biophys & Biochem, New York, NY 10032 USA

来源：

CURRENT OPINION IN MICROBIOLOGY | 2000年 / 3卷 / 02期

关键词：

D O I：

10.1016/S1369-5274(00)00075-8

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The folding of proteins from their initial unstructured state to their mature form has long been known to be promoted by other proteins known as chaperones and chaperonins. Recent biochemical and structural discoveries have provided dramatic insight into how these folding proteins work. This review will discuss these findings and suggest future experimental directions.

引用

页码：197 / 202

页数：6

共 48 条

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