Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
about
Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumMany roles of the bacterial envelope reducing pathwaysThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbBThe major catalase gene (katA) of Pseudomonas aeruginosa PA14 is under both positive and negative control of the global transactivator OxyR in response to hydrogen peroxidePeriplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsAMutational analysis of the disulfide catalysts DsbA and DsbB.Requirement of the CXXC motif of novel Francisella infectivity potentiator protein B FipB, and FipA in virulence of F. tularensis subsp. tularensis.Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae.Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditionsDsbD-catalyzed transport of electrons across the membrane of Escherichia coli.The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasmDisulfide bond formation in prokaryotes: history, diversity and designDsbC activation by the N-terminal domain of DsbD.On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamilyVitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.Oxidative protein folding in bacteria.Formation and transfer of disulphide bonds in living cells.A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelopeCritical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase.Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.Mechanism of the electron transfer catalyst DsbB from Escherichia coli.Protein folding in the bacterial periplasmKey players involved in bacterial disulfide-bond formation.Altered Escherichia coli membrane protein assembly machinery allows proper membrane assembly of eukaryotic protein vitamin K epoxide reductase.Biogenesis of respiratory cytochromes in bacteria.Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cellsStrategies for achieving high-level expression of genes in Escherichia coli.An in vivo pathway for disulfide bond isomerization in Escherichia coliRoles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC.Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.Reactivity of the two essential cysteine residues of the periplasmic mercuric ion-binding protein, MerP.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.Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors
P2860
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P2860
Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Evidence that the pathway of d ...... the cysteines of DsbB and DsbA
@ast
Evidence that the pathway of d ...... the cysteines of DsbB and DsbA
@en
type
label
Evidence that the pathway of d ...... the cysteines of DsbB and DsbA
@ast
Evidence that the pathway of d ...... the cysteines of DsbB and DsbA
@en
prefLabel
Evidence that the pathway of d ...... the cysteines of DsbB and DsbA
@ast
Evidence that the pathway of d ...... the cysteines of DsbB and DsbA
@en
P2093
P2860
P356
P1476
Evidence that the pathway of d ...... the cysteines of DsbB and DsbA
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.21.9895
P407
P577
1995-10-01T00:00:00Z