Periplasmic Chaperones and Peptidyl-Prolyl Isomerases
Author:
Affiliation:
1. Unité de Repliement et Modelisation des Proteines; Institut Pasteur-CNRS URA2185; 75724 Paris cedex 15 France
Publisher
ASM Press
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1128/9781555815806.ch8/fullpdf
Reference65 articles.
1. Regulation of the Escherichia coli σE-dependent envelope stress response;Alba;Mol. Microbiol.,2004
2. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli;Arie;Mol. Microbiol,2001
3. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity;Behrens;EMBO J.,2001
4. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins;Bitto;Structure,2002
5. The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins;Bitto;J. Biol. Chem.,2003
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