Reactivities of quinone-free DsbB from Escherichia coli.
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Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence AgentsNMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbBPlasticity of the Quinone-binding Site of the Complex II Homolog Quinol:Fumarate ReductaseCritical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria.Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy.A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Disulfide bond formation system in Escherichia coli.Mechanisms of oxidative protein folding in the bacterial cell envelope.Cysteine Mutational Studies Provide Insight into a Thiol-Based Redox Switch Mechanism of Metal and DNA Binding in FurA from Anabaena sp. PCC 7120.Protein disulfide bond generation in Escherichia coli DsbB-DsbA.Unraveling the redox properties of the global regulator FurA from Anabaena sp. PCC 7120: disulfide reductase activity based on its CXXC motifs.Real-time monitoring of intermediates reveals the reaction pathway in the thiol-disulfide exchange between disulfide bond formation protein A (DsbA) and B (DsbB) on a membrane-immobilized quartz crystal microbalance (QCM) system.Menaquinone as well as ubiquinone as a bound quinone crucial for catalytic activity and intramolecular electron transfer in Escherichia coli membrane-bound glucose dehydrogenase.A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo.The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli.Kinetic characterization of the disulfide bond-forming enzyme DsbB.
P2860
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P2860
Reactivities of quinone-free DsbB from Escherichia coli.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年學術文章
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2005年學術文章
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name
Reactivities of quinone-free DsbB from Escherichia coli.
@en
Reactivities of quinone-free DsbB from Escherichia coli.
@nl
type
label
Reactivities of quinone-free DsbB from Escherichia coli.
@en
Reactivities of quinone-free DsbB from Escherichia coli.
@nl
prefLabel
Reactivities of quinone-free DsbB from Escherichia coli.
@en
Reactivities of quinone-free DsbB from Escherichia coli.
@nl
P2093
P2860
P356
P1476
Reactivities of quinone-free DsbB from Escherichia coli.
@en
P2093
Kenji Inaba
Koreaki Ito
Yoh-Hei Takahashi
P2860
P304
33035-33044
P356
10.1074/JBC.M506189200
P407
P577
2005-07-15T00:00:00Z