Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae.
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The Crystal Structure of a Binary Complex of two Pseudopilins: EpsI and EpsJ from the Type 2 Secretion System of Vibrio vulnificusNanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificusCrystal Structure of the N-Terminal Domain of the Secretin GspD from ETEC Determined with the Assistance of a NanobodyThe three-dimensional structure of the cytoplasmic domains of EpsF from the type 2 secretion system of Vibrio choleraeThe dimer formed by the periplasmic domain of EpsL from the Type 2 Secretion System of Vibrio parahaemolyticusStructural and Functional Studies on the Interaction of GspC and GspD in the Type II Secretion SystemStructure and secretion of CofJ, a putative colonization factor of enterotoxigenic Escherichia coliStructure-function analysis of XcpP, a component involved in general secretory pathway-dependent protein secretion in Pseudomonas aeruginosaThe complete general secretory pathway in gram-negative bacteriaCoordinated assembly of multisubunit proteins: oligomerization of bacterial enterotoxins in vivo and in vitro.Testing the efficacy and toxicity of adenylyl cyclase inhibitors against enteric pathogens using in vitro and in vivo models of infection.Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway.Subset of hybrid eukaryotic proteins is exported by the type I secretion system of Erwinia chrysanthemi.Identification of a gene within a pathogenicity island of enterotoxigenic Escherichia coli H10407 required for maximal secretion of the heat-labile enterotoxin.Type II secretion and pathogenesisHeteropentameric cholera toxin B subunit chimeric molecules genetically fused to a vaccine antigen induce systemic and mucosal immune responses: a potential new strategy to target recombinant vaccine antigens to mucosal immune systems.Structure of the cholera toxin secretion channel in its closed stateThe extracellular transport signal of the Vibrio cholerae endochitinase (ChiA) is a structural motif located between amino acids 75 and 555Temporal expression of pertussis toxin and Ptl secretion proteins by Bordetella pertussis.Immune response induced by recombinant Mycobacterium bovis BCG producing the cholera toxin B subunit.Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins, including three related serine proteasesEnterotoxigenic Escherichia coli secretes active heat-labile enterotoxin via outer membrane vesicles.Initial studies of the structural signal for extracellular transport of cholera toxin and other proteins recognized by Vibrio cholerae.The binding of cholera toxin to the periplasmic vestibule of the type II secretion channel.The disulfide bond in the Aeromonas hydrophila lipase/acyltransferase stabilizes the structure but is not required for secretion or activity.General secretion pathway (eps) genes required for toxin secretion and outer membrane biogenesis in Vibrio cholerae.Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxinProteolytic activation of bacterial toxins: role of bacterial and host cell proteases.On the path to uncover the bacterial type II secretion system.A Conformational Shift in the Dissociated Cholera Toxin A1 Subunit Prevents Reassembly of the Cholera Holotoxin.Extracellular secretion of cloned aerolysin and phospholipase by Aeromonas salmonicida.Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein.Characterization of hybrid toxins produced in Escherichia coli by assembly of A and B polypeptides from type I and type II heat-labile enterotoxinsThe type II secretion system: biogenesis, molecular architecture and mechanism.A quinazoline-2,4-diamino analog suppresses Vibrio cholerae flagellar motility by interacting with motor protein PomB and induces envelope stress.Cell envelope perturbation induces oxidative stress and changes in iron homeostasis in Vibrio cholerae.Translocation of a folded protein across the outer membrane in Escherichia coli.Bacterial toxins deliver the goods.Different assay conditions for detecting the production and release of heat-labile and heat-stable toxins in enterotoxigenic Escherichia coli isolates.Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins.
P2860
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P2860
Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae.
description
1987 nî lūn-bûn
@nan
1987 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Conformation of protein secret ...... location from Vibrio cholerae.
@ast
Conformation of protein secret ...... location from Vibrio cholerae.
@en
Conformation of protein secret ...... location from Vibrio cholerae.
@nl
type
label
Conformation of protein secret ...... location from Vibrio cholerae.
@ast
Conformation of protein secret ...... location from Vibrio cholerae.
@en
Conformation of protein secret ...... location from Vibrio cholerae.
@nl
prefLabel
Conformation of protein secret ...... location from Vibrio cholerae.
@ast
Conformation of protein secret ...... location from Vibrio cholerae.
@en
Conformation of protein secret ...... location from Vibrio cholerae.
@nl
P2860
P356
P1476
Conformation of protein secret ...... location from Vibrio cholerae.
@en
P2093
P2860
P304
P356
10.1073/PNAS.84.21.7418
P407
P50
P577
1987-11-01T00:00:00Z