Folding mechanisms of periplasmic proteins
- 1 August 2014
- journal article
- review article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 1843 (8) , 1517-1528
Abstract
No abstract availableKeywords
This publication has 142 references indexed in Scilit:
- The Bam machine: A molecular cooperBiochimica et Biophysica Acta (BBA) - Biomembranes, 2012
- Making a beta-barrel: assembly of outer membrane proteins in Gram-negative bacteriaCurrent Opinion in Microbiology, 2012
- Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in HdeB and May Have a Role in Periplasmic Chaperone FunctionJournal of Molecular Biology, 2012
- Genetic selection designed to stabilize proteins uncovers a chaperone called SpyNature Structural & Molecular Biology, 2011
- The crystal structure Escherichia coli SpyProtein Science, 2010
- The prolyl isomerase domain of PpiD fromEscherichia colishows a parvulin fold but is devoid of catalytic activityProtein Science, 2009
- Detecting Folding Intermediates of a Protein as It Passes through the Bacterial Translocation ChannelCell, 2009
- Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergenceCellular and Molecular Life Sciences, 2009
- Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteinsProceedings of the National Academy of Sciences, 2008
- The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic ResiduesJournal of Molecular Biology, 2007