Converging concepts of protein folding in vitro and in vivo

被引：855

作者：

Hartl, F. Ulrich ^{[1
]}

Hayer-Hartl, Manajit ^{[1
]}

机构：

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

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2009年 / 16卷 / 06期

关键词：

MOLECULAR CHAPERONE DNAK; NUCLEOTIDE EXCHANGE FACTOR; NEWLY SYNTHESIZED PROTEINS; TRIGGER FACTOR; CRYSTAL-STRUCTURE; CYTOSOLIC CHAPERONIN; INTERACTION NETWORK; SUBSTRATE-BINDING; ESCHERICHIA-COLI; POLYPEPTIDE FLUX;

D O I：

10.1038/nsmb.1591

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：

Most proteins must fold into precise three-dimensional conformations to fulfill their biological functions. Here we review recent concepts emerging from studies of protein folding in vitro and in vivo, with a focus on how proteins navigate the complex folding energy landscape inside cells with the aid of molecular chaperones. Understanding these reactions is also of considerable medical relevance, as the aggregation of misfolding proteins that escape the cellular quality-control machinery underlies a range of debilitating diseases, including many age-onset neurodegenerative disorders.

引用

页码：574 / 581

页数：8

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