PROTEIN-CATALYZED PROTEIN FOLDING

被引：40

作者：

HORWICH, AL

NEUPERT, W

HARTL, FU

机构：

[1] UNIV MUNICH,INST PHYSIOL CHEM,W-8000 MUNICH 2,GERMANY

[2] UNIV CALIF LOS ANGELES,INST MOLEC BIOL,LOS ANGELES,CA 90024

来源：

TRENDS IN BIOTECHNOLOGY | 1990年 / 8卷 / 05期

关键词：

D O I：

10.1016/0167-7799(90)90153-O

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A number of proteins, termed chaperonins, have been identified as part of the mechanism of folding other proteins into their biologically active forms. The role of chaperonins appears to be twofold - to prevent illegitimate interactions with other proteins and to facilitate folding, possibly through an energy-dependent, catalytic function. Controlled overexpression of chaperonins may be of therapeutic value in manipulating human immune response and rescuing certain inherited human mutations. © 1990.

引用

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页码：126 / 131

页数：6

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