Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC.
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Sulfur metabolism in the extreme acidophile acidithiobacillus caldusNitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaeaPlasmids pMOL28 and pMOL30 of Cupriavidus metallidurans are specialized in the maximal viable response to heavy metalsDisulfide-Bond-Forming Pathways in Gram-Positive BacteriaResistance mechanisms of Mycobacterium tuberculosis against phagosomal copper overloadThe structure of BVU2987 from Bacteroides vulgatus reveals a superfamily of bacterial periplasmic proteins with possible inhibitory functionThe oxidase DsbA folds a protein with a nonconsecutive disulfideProperties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid ResidueQuality control of disulfide bond formation in pilus subunits by the chaperone FimCStructure of the periplasmic copper-binding protein CueP from Salmonella enterica serovar TyphimuriumThe multiple antibiotic resistance regulator MarR is a copper sensor in Escherichia coliA novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 proteinLaboratory evolution of one disulfide isomerase to resemble anotherFipB, an essential virulence factor of Francisella tularensis subsp. tularensis, has dual roles in disulfide bond formation.Pathogenicity of Salmonella enterica in Caenorhabditis elegans relies on disseminated oxidative stress in the infected hostBacterial thiol oxidoreductases - from basic research to new antibacterial strategiesThe multi-copper-ion oxidase CueO of Salmonella enterica serovar Typhimurium is required for systemic virulence.Thioredoxin A Is Essential for Motility and Contributes to Host Infection of Listeria monocytogenes via Redox Interactions.Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.Chemical shift assignments of a reduced N-terminal truncation mutant of the disulfide bond isomerase TrbB from plasmid F, TrbBΔ29.Oxidoreductases that act as conditional virulence suppressors in Salmonella enterica serovar TyphimuriumCharacterization of DsbD in Neisseria meningitidis.Survival and growth in the presence of elevated copper: transcriptional profiling of copper-stressed Pseudomonas aeruginosa.TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.Modulation of biofilm-formation in Salmonella enterica serovar Typhimurium by the periplasmic DsbA/DsbB oxidoreductase system requires the GGDEF-EAL domain protein STM3615Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231.Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli.Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coliCrystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive BacteriaFunctional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domainGenomic island genes in a coastal marine Synechococcus strain confer enhanced tolerance to copper and oxidative stress.The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Thioredoxin-like proteins in F and other plasmid systemsEngineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231)A multicopper oxidase is required for copper resistance in Mycobacterium tuberculosisActivation of Cu,Zn-superoxide dismutase in the absence of oxygen and the copper chaperone CCS.Mechanisms of oxidative protein folding in the bacterial cell envelope.Proteomic methods unravel the protein quality control in Escherichia coli.Copper tolerance and virulence in bacteria.Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues.
P2860
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P2860
Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC.
description
2005 nî lūn-bûn
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2005年の論文
@ja
2005年学术文章
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2005年学术文章
@zh
2005年学术文章
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2005年学术文章
@zh-hans
2005年学术文章
@zh-my
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name
Copper stress causes an in viv ...... coli disulfide isomerase DsbC.
@en
Copper stress causes an in viv ...... coli disulfide isomerase DsbC.
@nl
type
label
Copper stress causes an in viv ...... coli disulfide isomerase DsbC.
@en
Copper stress causes an in viv ...... coli disulfide isomerase DsbC.
@nl
prefLabel
Copper stress causes an in viv ...... coli disulfide isomerase DsbC.
@en
Copper stress causes an in viv ...... coli disulfide isomerase DsbC.
@nl
P2860
P356
P1476
Copper stress causes an in viv ...... coli disulfide isomerase DsbC.
@en
P2093
Annie Hiniker
James C A Bardwell
P2860
P304
33785-33791
P356
10.1074/JBC.M505742200
P407
P577
2005-08-08T00:00:00Z