DsbA: a protein-folding catalyst contributing to bacterial virulence.
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Moraxella osloensis gene expression in the slug host Deroceras reticulatumTargeting Bacterial Dsb Proteins for the Development of Anti-Virulence AgentsType IV pilin proteins: versatile molecular modulesGram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosisInsight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductaseStaphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative foldingAn Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression AnalysisStructural and functional characterization of Helicobacter pylori DsbGStructural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosisQuality control of disulfide bond formation in pilus subunits by the chaperone FimCComponents of the type six secretion system are substrates of Francisella tularensis Schu S4 DsbA-like FipB proteinRequirement of the CXXC motif of novel Francisella infectivity potentiator protein B FipB, and FipA in virulence of F. tularensis subsp. tularensis.Identification of an essential Francisella tularensis subsp. tularensis virulence factor.Francisella tularensis subsp. tularensis Schu S4 disulfide bond formation protein B, but not an RND-type efflux pump, is required for virulenceThe Mycobacterium avium subsp. paratuberculosis MAP3464 gene encodes an oxidoreductase involved in invasion of bovine epithelial cells through the activation of host cell Cdc42.Genome sequence of the endosymbiont Rickettsia peacockii and comparison with virulent Rickettsia rickettsii: identification of virulence factors.HtrA stress protein is involved in intramacrophagic replication of adherent and invasive Escherichia coli strain LF82 isolated from a patient with Crohn's diseaseIdentification of a disulfide isomerase protein of Leishmania major as a putative virulence factor.Structure of a DsbF homologue from Corynebacterium diphtheriae.A mutation in Flavobacterium psychrophilum tlpB inhibits gliding motility and induces biofilm formation.Oxidoreductases that act as conditional virulence suppressors in Salmonella enterica serovar TyphimuriumThe Drosophila melanogaster toll pathway participates in resistance to infection by the gram-negative human pathogen Pseudomonas aeruginosa.Survey of surface proteins from the pathogenic Mycoplasma hyopneumoniae strain 7448 using a biotin cell surface labeling approach.Identification of Differentially Abundant Proteins of Edwardsiella ictaluri during Iron Restriction.The protein disulfide isomerase 1 of Phytophthora parasitica (PpPDI1) is associated with the haustoria-like structures and contributes to plant infection.Helicobacter pylori HP0231 Influences Bacterial Virulence and Is Essential for Gastric ColonizationA comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Potential role of thiol:disulfide oxidoreductases in the pathogenesis of Helicobacter pylori.Morphological analysis of Francisella novicida epithelial cell infections in the absence of functional FipA.Identification of Actinobacillus pleuropneumoniae genes important for survival during infection in its natural hostThe oxidoreductase DsbA plays a key role in the ability of the Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 to resist macrophage killing.DsbA plays a critical and multifaceted role in the production of secreted virulence factors by the phytopathogen Erwinia carotovora subsp. atroseptica.Cooperation of both, the FKBP_N-like and the DSBA-like, domains is necessary for the correct function of FTS_1067 protein involved in Francisella tularensis virulence and pathogenesis.Extracytoplasmic-stress-responsive pathways modulate type III secretion in Yersinia pseudotuberculosis.The secretome of Campylobacter concisus.Functional analysis of the thioredoxin domain in Porphyromonas gingivalis HBP35.INHIBITION OF DIVERSE DsbA ENZYMES IN MULTI-DsbA ENCODING PATHOGENS.Bacterial periplasmic oxido-reductases are essential for the activity of oxidized human antimicrobial β-defensin 1.
P2860
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P2860
DsbA: a protein-folding catalyst contributing to bacterial virulence.
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
DsbA: a protein-folding catalyst contributing to bacterial virulence.
@ast
DsbA: a protein-folding catalyst contributing to bacterial virulence.
@en
type
label
DsbA: a protein-folding catalyst contributing to bacterial virulence.
@ast
DsbA: a protein-folding catalyst contributing to bacterial virulence.
@en
prefLabel
DsbA: a protein-folding catalyst contributing to bacterial virulence.
@ast
DsbA: a protein-folding catalyst contributing to bacterial virulence.
@en
P1476
DsbA: a protein-folding catalyst contributing to bacterial virulence.
@en
P304
P356
10.1016/S1286-4579(99)00239-7
P577
1999-12-01T00:00:00Z