Periplasmic Chaperones—New Structural and Functional Insights
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference10 articles.
1. Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
2. Semin;Sauer;Cell Dev. Biol,2000
3. A Temperature-Dependent Switch from Chaperone to Protease in a Widely Conserved Heat Shock Protein
4. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
5. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.
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1. The crystal structure of the leptospiral hypothetical protein LIC12922 reveals homology with the periplasmic chaperone SurA;Journal of Structural Biology;2011-02
2. The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity;Protein Science;2009-10-28
3. Protein secretion and outer membrane assembly inAlphaproteobacteria;FEMS Microbiology Reviews;2008-11
4. The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities;FEBS Journal;2008-06-28
5. Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space;Biochemical Journal;2007-12-21
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