Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions-Reference-Cited by-同舟云学术

Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions

Published:2003-12-15 Issue:3 Volume:51 Page:849-859
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:

Author:

Mujacic Mirna,Bader Martin W.,Baneyx François

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1365-2958.2003.03871.x/fullpdf

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3. Trigger factor and DnaK possess overlapping substrate pools and binding specificities;Deuerling;Mol Microbiol,2003

4. Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question;Dougan;Cell Mol Life Sci,2002

5. Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution;Du;Proc Natl Acad Sci USA,2000

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