Molecular chaperones and protein quality control

被引：1262

作者：

Bukau, Bernd

Weissman, Jonathan

Horwich, Arthur

机构：

[1] Heidelberg Univ, Zentrum Mol Biol, D-69120 Heidelberg, Germany

[2] Univ Calif San Francisco, Dept Cellular & Mol Pharmacol, San Francisco, CA 94143 USA

[3] Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94143 USA

[4] Scripps Res Inst, La Jolla, CA 92037 USA

[5] Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA

[6] Yale Univ, Sch Med, Dept Genet, New Haven, CT 06510 USA

来源：

CELL | 2006年 / 125卷 / 03期

关键词：

D O I：

10.1016/j.cell.2006.04.014

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：

In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for protein quality control in the endoplasmic reticulum; and provide new insight into two classes of molecular chaperones, the Hsp70 system and the AAA+ (Hsp100) unfoldases. © 2006 Elsevier Inc. All rights reserved.

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收藏

页码：443 / 451

页数：9

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