A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance-Reference-Cited by-同舟云学术

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A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance

Published:2011-09-04 Issue:10 Volume:7 Page:671-677
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Zhang Meng,Lin Shixian,Song Xinwen,Liu Jun,Fu Ye,Ge Xi,Fu Xinmiao,Chang Zengyi,Chen Peng R

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/nchembio.644.pdf

Reference30 articles.

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

2. Hartl, F.U. & Hayer-Hartl, M. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16, 574–581 (2009).

3. Clausen, T., Southan, C. & Ehrmann, M. The HtrA family of proteases: Implications for protein composition and cell fate. Mol. Cell 10, 443–455 (2002).

4. Sklar, J.G., Wu, T., Kahne, D. & Silhavy, T.J. Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev. 21, 2473–2484 (2007).

5. Hagan, C.L., Kim, S. & Kahne, D. Reconstitution of outer membrane protein assembly from purified components. Science 328, 890–892 (2010).

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