A periplasmic reducing system protects single cysteine residues from oxidation. - Wikidata - awgldk - TriplyDB

A periplasmic reducing system protects single cysteine residues from oxidation.

A periplasmic reducing system protects single cysteine residues from oxidation.

http://www.wikidata.org/entity/Q43228884

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Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead Many roles of the bacterial envelope reducing pathways Reducing systems protecting the bacterial cell envelope from oxidative damage Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC Structural and functional characterization of Helicobacter pylori DsbG Structural and Functional Characterization of ScsC, a Periplasmic Thioredoxin-Like Protein from Salmonella enterica Serovar Typhimurium The Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide Isomerase An Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter pylori Protein Oxidative Modifications: Beneficial Roles in Disease and Health A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein Sulfenic acid chemistry, detection and cellular lifetime The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.Components of the type six secretion system are substrates of Francisella tularensis Schu S4 DsbA-like FipB protein Legionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activity DsbA2 (27 kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system Plant thioredoxin CDSP32 regenerates 1-cys methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid.Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies Disulfide bond formation in prokaryotes: history, diversity and design Detection and function of an intramolecular disulfide bond in the pH-responsive CadC of Escherichia coli.Site-specific mapping and quantification of protein S-sulphenylation in 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 envelope Vital dye reaction and granule localization in periplasm of Escherichia coli In and out: an analysis of epibiotic vs periplasmic bacterial predators.New method for effectively and quantitatively labeling cysteine residues on chicken eggshell membrane.Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-α or mFIZZ1) in a wheat germ cell-free extract.Characterization of DsbD in Neisseria meningitidis.Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Mechanism-based proteomic screening identifies targets of thioredoxin-like proteins TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.Identification of a redox-modulatory interaction between uncoupling protein 3 and thioredoxin 2 in the mitochondrial intermembrane space Peptidoglycan hydrolases of Escherichia coli.Profiling the Reactivity of Cyclic C-Nucleophiles towards Electrophilic Sulfur in Cysteine Sulfenic Acid Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain Global, in situ, site-specific analysis of protein S-sulfenylation

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P2860

A periplasmic reducing system protects single cysteine residues from oxidation.

http://www.wikidata.org/entity/Q43228884

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

@zh-cn

2009年学术文章

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2009年学术文章

@zh-my

2009年学术文章

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2009年學術文章

@yue

2009年學術文章

@zh-hant

name

A periplasmic reducing system protects single cysteine residues from oxidation.

@en

A periplasmic reducing system protects single cysteine residues from oxidation.

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type

label

A periplasmic reducing system protects single cysteine residues from oxidation.

@en

A periplasmic reducing system protects single cysteine residues from oxidation.

@nl

prefLabel

A periplasmic reducing system protects single cysteine residues from oxidation.

@en

A periplasmic reducing system protects single cysteine residues from oxidation.

@nl

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A periplasmic reducing system protects single cysteine residues from oxidation.

@en

P2093

Katleen Denoncin

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Khadija Wahni

http://www.w3.org/2001/XMLSchema#string

Matthieu Depuydt

http://www.w3.org/2001/XMLSchema#string

Stephen E Leonard

http://www.w3.org/2001/XMLSchema#string

P2860

How thioredoxin can reduce a buried disulphide bond.

Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli.

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.

A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR.

Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.

Identification of the L,D-transpeptidases responsible for attachment of the Braun lipoprotein to Escherichia coli peptidoglycan.

Pathways of disulfide bond formation in Escherichia coli.

Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria.

Discovering mechanisms of signaling-mediated cysteine oxidation.

Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation.

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1109-1111

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scholarly article

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10.1126/SCIENCE.1179557

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5956

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326

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Didier Vertommen

Jean-francois Collet

Pierre Morsomme

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2009-11-01T00:00:00Z

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40452403

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19965429

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