Translocation of a folded protein across the outer membrane in Escherichia coli.
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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 choleraeFormation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosaA periplasmic intermediate in the extracellular secretion pathway of Pseudomonas aeruginosa exotoxin AThe complete general secretory pathway in gram-negative bacteriaSubset of hybrid eukaryotic proteins is exported by the type I secretion system of Erwinia chrysanthemi.Characterization of the avian pathogenic Escherichia coli hemagglutinin Tsh, a member of the immunoglobulin A protease-type family of autotransporters.Expression and localization of HrpA1, a protein of Xanthomonas campestris pv. vesicatoria essential for pathogenicity and induction ofthe hypersensitive reaction.Secretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements.The disulfide bond in the Aeromonas hydrophila lipase/acyltransferase stabilizes the structure but is not required for secretion or activity.On the path to uncover the bacterial type II secretion system.Key players involved in bacterial disulfide-bond formation.Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein.Cell adhesion molecule DdCAD-1 is imported into contractile vacuoles by membrane invagination in a Ca2+- and conformation-dependent manner.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.The trans-envelope architecture and function of the type 2 secretion system: new insights raising new questions.Influence of deletions within domain II of exotoxin A on its extracellular secretion from Pseudomonas aeruginosa.Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase.Exchange of Xcp (Gsp) secretion machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes: species specificity unrelated to substrate recognitionDisulfide bond formation in secreton component PulK provides a possible explanation for the role of DsbA in pullulanase secretion.External loops at the C terminus of Erwinia chrysanthemi pectate lyase C are required for species-specific secretion through the out type II pathway.Metalloadsorption by Escherichia coli cells displaying yeast and mammalian metallothioneins anchored to the outer membrane protein LamB.The dsbB gene product is required for protease production by Burkholderia cepacia.Characterization of lipase-deficient mutants of Acinetobacter calcoaceticus BD413: identification of a periplasmic lipase chaperone essential for the production of extracellular lipase.Peptidoglycan as a barrier to transenvelope transport.Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation.Isolation and analysis of eight exe genes and their involvement in extracellular protein secretion and outer membrane assembly in Aeromonas hydrophila.Building bridges: disulphide bond formation in the cell.A specific targeting domain in mature exotoxin A is required for its extracellular secretion from Pseudomonas aeruginosaSignals, receptors, and cytosolic factors involved in peroxisomal protein import.Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca.Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins.Enzymatic product formation impairs both the chloroplast receptor-binding function as well as translocation competence of the NADPH: protochlorophyllide oxidoreductase, a nuclear-encoded plastid precursor protein.Maturation of Pseudomonas aeruginosa elastase. Formation of the disulfide bonds.Substrate oscillations boost recombinant protein release from Escherichia coli.The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli.Xcp-mediated protein secretion in Pseudomonas aeruginosa: identification of two additional genes and evidence for regulation of xcp gene expression.
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Translocation of a folded protein across the outer membrane in Escherichia coli.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1992
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Translocation of a folded protein across the outer membrane in Escherichia coli.
@en
Translocation of a folded protein across the outer membrane in Escherichia coli.
@nl
type
label
Translocation of a folded protein across the outer membrane in Escherichia coli.
@en
Translocation of a folded protein across the outer membrane in Escherichia coli.
@nl
prefLabel
Translocation of a folded protein across the outer membrane in Escherichia coli.
@en
Translocation of a folded protein across the outer membrane in Escherichia coli.
@nl
P2860
P356
P1476
Translocation of a folded protein across the outer membrane in Escherichia coli.
@en
P2093
Pugsley AP
P2860
P304
12058-12062
P356
10.1073/PNAS.89.24.12058
P407
P577
1992-12-01T00:00:00Z