Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import-Reference-Cited by-同舟云学术

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Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import

Published:2010-11-08 Issue:47 Volume:107 Page:20190-20195
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Banci L.,Bertini I.,Cefaro C.,Cenacchi L.,Ciofi-Baffoni S.,Felli I. C.,Gallo A.,Gonnelli L.,Luchinat E.,Sideris D.,Tokatlidis K.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference32 articles.

1. Protein folding and misfolding

2. Functional TIM10 Chaperone Assembly Is Redox-regulated in Vivo

3. The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier

4. Crystal Structure of the Mitochondrial Chaperone TIM9•10 Reveals a Six-Bladed α-Propeller

5. A Structural-Dynamical Characterization of Human Cox17

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