A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae.
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A pathway for disulfide bond formation in vivoTwo cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formationEfficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasmTargeting Bacterial Dsb Proteins for the Development of Anti-Virulence AgentsCrystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITEThe complete general secretory pathway in gram-negative bacteriaProteomic analysis of enterotoxigenic Escherichia coli (ETEC) in neutral and alkaline conditions.Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae.Potent immunogenicity of the B subunits of Escherichia coli heat-labile enterotoxin: receptor binding is essential and induces differential modulation of lymphocyte subsets.Secretion and assembly of regular surface structures in Gram-negative bacteria.Type II secretion and pathogenesisBradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like protein involved in the biogenesis of cytochrome aa3 and development of symbiosisIdentification of a disulfide isomerase protein of Leishmania major as a putative virulence factor.Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells.Targeting of cholera toxin and Escherichia coli heat labile toxin in polarized epithelia: role of COOH-terminal KDELRtsA coordinately regulates DsbA and the Salmonella pathogenicity island 1 type III secretion system.Mutant Escherichia coli heat-labile toxin B subunit that separates toxoid-mediated signaling and immunomodulatory action from trafficking and delivery functionsAlkaline pH Is a signal for optimal production and secretion of the heat labile toxin, LT in enterotoxigenic Escherichia coli (ETEC).Heat-labile enterotoxin: beyond G(m1) bindingSecretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements.Protein folding in the bacterial periplasmPapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbAKey players involved in bacterial disulfide-bond formation.Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.Deletion mutations in N-terminal alpha1 helix render heat labile enterotoxin B subunit susceptible to degradation.Disulfide bond formation and ToxR activity in Vibrio cholerae.Role of the two-component regulator CpxAR in the virulence of Salmonella enterica serotype Typhimurium.Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivoA comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Formation of an Intramolecular Periplasmic Disulfide Bond in TcpP Protects TcpP and TcpH from Degradation in Vibrio cholerae.The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis.Potential role of thiol:disulfide oxidoreductases in the pathogenesis of Helicobacter pylori.The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis.Translocation of a folded protein across the outer membrane in Escherichia coli.Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus.Proteus mirabilis genes that contribute to pathogenesis of urinary tract infection: identification of 25 signature-tagged mutants attenuated at least 100-fold.Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli.Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.Comparison of serum humoral responses induced by oral immunization with the hepatitis B virus core antigen and the cholera toxin B subunit
P2860
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P2860
A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
A homologue of the Escherichia ...... biogenesis in Vibrio cholerae.
@en
A homologue of the Escherichia ...... biogenesis in Vibrio cholerae.
@nl
type
label
A homologue of the Escherichia ...... biogenesis in Vibrio cholerae.
@en
A homologue of the Escherichia ...... biogenesis in Vibrio cholerae.
@nl
prefLabel
A homologue of the Escherichia ...... biogenesis in Vibrio cholerae.
@en
A homologue of the Escherichia ...... biogenesis in Vibrio cholerae.
@nl
P2093
P2860
P1476
A homologue of the Escherichia ...... biogenesis in Vibrio cholerae.
@en
P2093
P2860
P304
P356
10.1111/J.1365-2958.1992.TB01368.X
P407
P577
1992-07-01T00:00:00Z