Molecular chaperones in cellular protein folding

被引：3001

作者：

Hartl, FU ^{[1
]}

机构：

[1] MEM SLOAN KETTERING CANC CTR, CELLULAR BIOCHEM & BIOPHYS PROGRAM, NEW YORK, NY 10021 USA

来源：

NATURE | 1996年 / 381卷 / 6583期

关键词：

D O I：

10.1038/381571a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The folding of many newly synthesized proteins in the cell depends on a set of conserved proteins known as molecular chaperones. These prevent the formation of misfolded protein structures, both under normal conditions and when cells are exposed to stresses such as high temperature. Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.

引用

页码：571 / 580

页数：10

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