In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product.
about
Active cytotoxic necrotizing factor 1 associated with outer membrane vesicles from uropathogenic Escherichia coli.The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar TyphimuriumIntimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation.Folding machineries displayed on a cation-exchanger for the concerted refolding of cysteine- or proline-rich proteins.Low ubiquinone content in Escherichia coli causes thiol hypersensitivity.Expression and crystallization of SeDsbA, SeDsbL and SeSrgA from Salmonella enterica serovar Typhimurium.Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membraneEvidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbADsbC activation by the N-terminal domain of DsbD.Bradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like protein involved in the biogenesis of cytochrome aa3 and development of symbiosisDisulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells.Enhanced biofilm formation by Escherichia coli LPS mutants defective in Hep biosynthesisTransduction of envelope stress in Escherichia coli by the Cpx two-component system.PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbARole of disulfide bonds in maintaining the structural integrity of the sheath of Leptothrix discophora SP-6Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA.A novel method for increasing production of mature proteins in the periplasm of Escherichia coliIdentification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivoRespiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cellsCharacterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073.The Tobacco mosaic virus movement protein associates with but does not integrate into biological membranes.Protein abundances can distinguish between naturally-occurring and laboratory strains of Yersinia pestis, the causative agent of plague.Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.A novel Escherichia coli lipid A mutant that produces an antiinflammatory lipopolysaccharide.A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli.Disruption of a gene encoding a novel thioredoxin-like protein alters the cyanobacterial photosynthetic apparatusDisulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.Dsb-insensitive expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA.Characterization of dominantly negative mutant ClyA cytotoxin proteins in Escherichia coli.Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation.Multicopy suppressors of the cold-sensitive phenotype of the pcsA68 (dinD68) mutation in Escherichia coliStructural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm.Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.Differences between the electronic environments of reduced and oxidized Escherichia coli DsbA inferred from heteronuclear magnetic resonance spectroscopyFerredoxin is involved in secretion of cytotoxic necrotizing factor 1 across the cytoplasmic membrane in Escherichia coli K1.Methanosarcina acetivorans utilizes a single NADPH-dependent thioredoxin system and contains additional thioredoxin homologues with distinct functions.
P2860
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P2860
In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product.
description
1992 nî lūn-bûn
@nan
1992 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
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
name
In vitro catalysis of oxidativ ...... coli dsbA (ppfA) gene product.
@ast
In vitro catalysis of oxidativ ...... coli dsbA (ppfA) gene product.
@en
type
label
In vitro catalysis of oxidativ ...... coli dsbA (ppfA) gene product.
@ast
In vitro catalysis of oxidativ ...... coli dsbA (ppfA) gene product.
@en
prefLabel
In vitro catalysis of oxidativ ...... coli dsbA (ppfA) gene product.
@ast
In vitro catalysis of oxidativ ...... coli dsbA (ppfA) gene product.
@en
P2093
P1476
In vitro catalysis of oxidativ ...... coli dsbA (ppfA) gene product.
@en
P2093
P304
22440-22445
P407
P577
1992-11-01T00:00:00Z