Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Igaβ autotransporter pathway
- 1 January 1996
- Vol. 178 (1-2) , 107-110
- https://doi.org/10.1016/0378-1119(96)00343-5
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Common structural features of IgA1 protease‐like outer membrane protein autotransportersMolecular Microbiology, 1995
- Protein disulphide oxidoreductases in bacteriaTrends in Biochemical Sciences, 1994
- The secretion pathway of IgA protease‐type proteins in gram‐negative bacteriaBioEssays, 1993
- The complete general secretory pathway in gram-negative bacteriaMicrobiological Reviews, 1993
- Selective extracellular release of cholera toxin B subunit by Escherichia coli: dissection of Neisseria Iga beta-mediated outer membrane transport.The EMBO Journal, 1992
- Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.The EMBO Journal, 1992
- Identification of a protein required for disulfide bond formation in vivoPublished by Elsevier ,1991
- Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: conformation-dependent outer membrane translocation.The EMBO Journal, 1990
- ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purificationJournal of Bacteriology, 1988
- Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA proteaseNature, 1987