Protein folding in vivo:: the importance of molecular chaperones

被引：155

作者：

Feldman, DE ^{[1
]}

Frydman, J ^{[1
]}

机构：

[1] Stanford Univ, Dept Biol Sci, Stanford, CA 94305 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2000年 / 10卷 / 01期

关键词：

D O I：

10.1016/S0959-440X(99)00044-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The contribution of the two major cytosolic chaperone systems. Hsp70 and the cylindrical chaperonins, to cellular protein folding has been clarified by a number of recent papers. These studies found that, in vivo, a significant fraction of newly synthesized polypeptides transit through these chaperone systems in both prokaryotic and eukaryotic cells. The identification and characterization of the cellular substrates of chaperones will be instrumental in understanding how proteins fold in vivo.

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页码：26 / 33

页数：8

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