Hsp90: a specialized but essential protein-folding tool

被引：690

作者：

Young, JC ^{[1
]}

Moarefi, I ^{[1
]}

Hartl, FU ^{[1
]}

机构：

[1] Max Planck Inst Biochem, Dept Cellular Biochem, D-82152 Martinsried, Germany

来源：

JOURNAL OF CELL BIOLOGY | 2001年 / 154卷 / 02期

关键词：

Hsp90; molecular chaperones; protein folding; signal transduction; ansamycin;

D O I：

10.1083/jcb.200104079

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy.

引用

页码：267 / 273

页数：7

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