HSP100/Clp proteins: A common mechanism explains diverse functions

被引：418

作者：

Schirmer, EC ^{[1
]}

Glover, JR ^{[1
]}

Singer, MA ^{[1
]}

Lindquist, S ^{[1
]}

机构：

[1] UNIV CHICAGO, DEPT MOL GENET & CELL BIOL, CHICAGO, IL 60637 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1996年 / 21卷 / 08期

关键词：

D O I：

10.1016/0968-0004(96)10038-4

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 HSP100/Clp proteins are a newly discovered family with a great diversity of functions, such as increased tolerance to high temperatures, promotion of proteolysis of specific cellular substrates and regulation of transcription. HSP100/Clp proteins are also synthesized in a variety of specific patterns and, in eukaryotes, are localized to different subcellular compartments. Recent data suggest that a common ability to disassemble higher-order protein structures and aggregates unifies the molecular functions of this diverse family.

引用

页码：289 / 296

页数：8

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