Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments-Reference-Cited by-同舟云学术

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Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments

Published:2008-05-18 Issue:6 Volume:15 Page:641-650
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Haslberger Tobias,Zdanowicz Agnieszka,Brand Ingo,Kirstein Janine,Turgay Kürsad,Mogk Axel,Bukau Bernd

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.1425.pdf

Reference50 articles.

1. Wickner, S., Maurizi, M.R. & Gottesman, S. Posttranslational quality control: folding, refolding, and degrading proteins. Science 286, 1888–1893 (1999).

2. Hanson, P.I. & Whiteheart, S.W. AAA+ proteins: have engine, will work. Nat. Rev. Mol. Cell Biol. 6, 519–529 (2005).

3. Baker, T.A. & Sauer, R.T. ATP-dependent proteases of bacteria: recognition logic and operating principles. Trends Biochem. Sci. 31, 647–653 (2006).

4. Maurizi, M.R. & Xia, D. Protein binding and disruption by Clp/Hsp100 chaperones. Structure 12, 175–183 (2004).

5. Squires, C.L., Pedersen, S., Ross, B.M. & Squires, C. ClpB is the Escherichia coli heat shock protein F84.1. J. Bacteriol. 173, 4254–4262 (1991).

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