Molecular chaperones: Clamps for the Clps?

被引：17

作者：

Feng, HP ^{[1
]}

Gierasch, LM ^{[1
]}

机构：

[1] Univ Massachusetts, Dept Chem, Amherst, MA 01003 USA

来源：

CURRENT BIOLOGY | 1998年 / 8卷 / 13期

关键词：

D O I：

10.1016/S0960-9822(98)70294-5

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 Clp/Hsp100 molecular chaperones are unusual in their ability to tease apart protein aggregates and complexes. Recent results make a good case that these chaperones bind substrates via PDZ-like domains; this may reflect a general strategy for manipulating the assembly state of substrate proteins. (C) Current Biology Ltd.

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收藏

页码：R464 / R467

页数：4

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