Elucidating the Mechanism of Substrate Recognition by the Bacterial Hsp90 Molecular Chaperone-Reference-Cited by-同舟云学术

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Elucidating the Mechanism of Substrate Recognition by the Bacterial Hsp90 Molecular Chaperone

Published:2014-06 Issue:12 Volume:426 Page:2393-2404
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Street Timothy O.,Zeng Xiaohui,Pellarin Riccardo,Bonomi Massimiliano,Sali Andrej,Kelly Mark J.S.,Chu Feixia,Agard David A.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference36 articles.

1. Some like it hot: the structure and function of small heat-shock proteins;Haslbeck;Nat Struct Mol Biol,2005

2. Bleach activates a redox-regulated chaperone by oxidative protein unfolding;Winter;Cell,2008

3. Protein refolding by pH-triggered chaperone binding and release;Tapley;Proc Natl Acad Sci U S A,2010

4. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements;Shiau;Cell,2006

5. Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide;Krukenberg;Protein Sci,2009

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