DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
about
Disulfide-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.Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulenceThe dithiol:disulfide oxidoreductases DsbA and DsbB of Rhodobacter capsulatus are not directly involved in cytochrome c biogenesis, but their inactivation restores the cytochrome c biogenesis defect of CcdA-null mutantsDsbC activation by the N-terminal domain of DsbD.Oxidative protein folding in bacteria.Formation and transfer of disulphide bonds in living cells.Thioredoxin 1 promotes intracellular replication and virulence of Salmonella enterica serovar Typhimurium.Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD.Key players involved in bacterial disulfide-bond formation.The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis.Comprehensive analysis of transport proteins encoded within the genome of Bdellovibrio bacteriovorus.A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm.Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells.Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.Reconstitution of a disulfide isomerization system.Metabolic shift at the class level sheds light on adaptation of methanogens to oxidative environments.Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.Overproduction of CcmABCDEFGH restores cytochrome c maturation in a DsbD deletion strain of E. coli: another route for reductant?The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases.
P2860
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P2860
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
description
2000 nî lūn-bûn
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2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
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name
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
@ast
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
@en
type
label
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
@ast
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
@en
prefLabel
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
@ast
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
@en
P2093
P2860
P356
P1476
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
@en
P2093
P2860
P304
P356
10.1074/JBC.M009500200
P407
P577
2000-11-20T00:00:00Z