Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo
about
Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumTwo cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formationOxidative protein folding in eukaryotes: mechanisms and consequencesTargeting Bacterial Dsb Proteins for the Development of Anti-Virulence AgentsDisulfide-Bond-Forming Pathways in Gram-Positive BacteriaThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Gram-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 oxidoreductaseStructural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidisPreparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbBThe Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA EnzymesAn Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression AnalysisStructural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosisThe Escherichia coli CcmG protein fulfils a specific role in cytochrome c assemblyMutational analysis of the disulfide catalysts DsbA and DsbB.Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.FipB, an essential virulence factor of Francisella tularensis subsp. tularensis, has dual roles in disulfide bond formation.DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasmAssembly of lipopolysaccharide in Escherichia coli requires the essential LapB heat shock proteinDisulfide bond formation in prokaryotes: history, diversity and designLow ubiquinone content in Escherichia coli causes thiol hypersensitivity.Electron Transport Chain Is Biochemically Linked to Pilus Assembly Required for Polymicrobial Interactions and Biofilm Formation in the Gram-Positive Actinobacterium Actinomyces oris.Thioredoxin A Is Essential for Motility and Contributes to Host Infection of Listeria monocytogenes via Redox Interactions.XC_0531 encodes a c-type cytochrome biogenesis protein and is required for pathogenesis in Xanthomonas campestris pv. campestris.Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbAA new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coliReducing conditions are the key for efficient production of active ribonuclease inhibitor in Escherichia coli.DsbC activation by the N-terminal domain of DsbD.Oxidative protein folding in bacteria.Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells.Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.RtsA coordinately regulates DsbA and the Salmonella pathogenicity island 1 type III secretion system.Protein folding in the periplasm in the absence of primary oxidant DsbA: modulation of redox potential in periplasmic space via OmpL porin.Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.The OmpL porin does not modulate redox potential in the periplasmic space of Escherichia coli.Mechanism of the electron transfer catalyst DsbB from Escherichia coli.Protein folding in the bacterial periplasmKey players involved in bacterial disulfide-bond formation.
P2860
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P2860
Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Identification and characteriz ...... ion of disulfide bonds in vivo
@ast
Identification and characteriz ...... ion of disulfide bonds in vivo
@en
type
label
Identification and characteriz ...... ion of disulfide bonds in vivo
@ast
Identification and characteriz ...... ion of disulfide bonds in vivo
@en
prefLabel
Identification and characteriz ...... ion of disulfide bonds in vivo
@ast
Identification and characteriz ...... ion of disulfide bonds in vivo
@en
P2093
P2860
P356
P1476
Identification and characteriz ...... ion of disulfide bonds in vivo
@en
P2093
C Georgopoulos
D Missiakas
P2860
P304
P356
10.1073/PNAS.90.15.7084
P407
P577
1993-08-01T00:00:00Z