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The role of heat-shock proteins as molecular chaperones.

作者信息

Welch W J

机构信息

University of California, San Francisco.

出版信息

Curr Opin Cell Biol. 1991 Dec;3(6):1033-8. doi: 10.1016/0955-0674(91)90125-i.

DOI:10.1016/0955-0674(91)90125-i
PMID:1687649
Abstract

Recent studies have revealed that protein folding and assembly events in vivo require the participation of accessory components, now being referred to as 'molecular chaperones'. A number of chaperones have been identified as members of the heat-shock (or stress) protein family. This review discusses the roles of two classes of chaperones, the heat-shock protein 70 and groEL/ES families, in facilitating protein maturation, and describes how such events are perturbed in the cell subjected to metabolic stress.

摘要

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The role of heat-shock proteins as molecular chaperones.
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ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells.ClpB和HtpG有助于应激条件下的大肠杆菌细胞中的新生蛋白质折叠。
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Curr Top Cell Regul. 1992;33:127-43. doi: 10.1016/b978-0-12-152833-1.50013-7.

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