Preparation of a highly translocation-competent proOmpA/SecB complex
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Reference35 articles.
1. Three pure chaperone proteins of Escherichia coli-SecB, trigger factor and GroEL-form soluble complexes with precursor proteins in vitro;Lecker;EMBO J,1989
2. ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein;Lecker;EMBO J,1990
3. Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein;Liu;Proc Natl Acad Sci USA,1989
4. ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes;Crooke;EMBO J,1988
5. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane;Hartl;Cell,1990
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2. Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase;EMBO reports;2020-04-19
3. CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo;Scientific Reports;2019-02-04
4. Navigating the structure–function–evolutionary relationship of CsaA chaperone in archaea;Critical Reviews in Microbiology;2017-09-18
5. Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation;Proceedings of the National Academy of Sciences;2013-05-28
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