The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.
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Disulfide-Bond-Forming Pathways in Gram-Positive BacteriaDisulfide bond formation in the bacterial periplasm: major achievements and challenges aheadMany roles of the bacterial envelope reducing pathwaysFuranose-specific Sugar Transport: CHARACTERIZATION OF A BACTERIAL GALACTOFURANOSE-BINDING PROTEINX-Ray Structure and Site-Directed Mutagenesis Analysis of the Escherichia coli Colicin M Immunity ProteinCrystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbCDissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosaDissecting the Escherichia coli periplasmic chaperone network using differential proteomics.The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics.Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activityDetection and function of an intramolecular disulfide bond in the pH-responsive CadC of Escherichia coli.Protein determinants of phage T4 lysis inhibition.Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.Genetic analysis of 15 protein folding factors and proteases of the Escherichia coli cell envelope.Thermal-induced dissociation and unfolding of homodimeric DsbC revealed by temperature-jump time-resolved infrared spectra.Mechanisms of oxidative protein folding in the bacterial cell envelope.Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.A new role for Escherichia coli DsbC protein in protection against oxidative stressSpanin function requires subunit homodimerization through intermolecular disulfide bonds.Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.DsbA plays a critical and multifaceted role in the production of secreted virulence factors by the phytopathogen Erwinia carotovora subsp. atroseptica.Engineered pathways for correct disulfide bond oxidation.A secretory system for bacterial production of high-profile protein targets.Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons.Wheat germ in vitro translation to produce one of the most toxic sodium channel specific toxins.Changes in the phosphoproteome of brown adipose tissue during hibernation in the ground squirrel, Ictidomys tridecemlineatus.Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Bacterial periplasmic oxido-reductases are essential for the activity of oxidized human antimicrobial β-defensin 1.
P2860
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P2860
The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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name
The disulphide isomerase DsbC ...... in a DsbD-independent manner.
@en
The disulphide isomerase DsbC ...... in a DsbD-independent manner.
@nl
type
label
The disulphide isomerase DsbC ...... in a DsbD-independent manner.
@en
The disulphide isomerase DsbC ...... in a DsbD-independent manner.
@nl
prefLabel
The disulphide isomerase DsbC ...... in a DsbD-independent manner.
@en
The disulphide isomerase DsbC ...... in a DsbD-independent manner.
@nl
P2093
P2860
P50
P1476
The disulphide isomerase DsbC ...... in a DsbD-independent manner.
@en
P2093
James C A Bardwell
Jean-Pierre Szikora
Jonathan Pan
Laurent Knoops
Matthieu Depuydt
P2860
P304
P356
10.1111/J.1365-2958.2007.06030.X
P407
P577
2007-11-25T00:00:00Z