Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli.
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Re-examining the role of hydrogen peroxide in bacteriostatic and bactericidal activities of honeyAdaptations to submarine hydrothermal environments exemplified by the genome of Nautilia profundicolaGenome of the Epsilonproteobacterial Chemolithoautotroph Sulfurimonas denitrificansHDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulationOxidative-stress resistance mutants of Helicobacter pylori.The Escherichia coli proteome: past, present, and future prospectsGingipain-dependent interactions with the host are important for survival of Porphyromonas gingivalisComplete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaeaHydrogen peroxide scavenging is not a virulence determinant in the pathogenesis of Haemophilus influenzae type b strain Eagan.Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological RolesRegulation of oxidative stress resistance in Campylobacter jejuni, a microaerophilic foodborne pathogenStaphylococcal response to oxidative stressMany roles of the bacterial envelope reducing pathwaysReducing systems protecting the bacterial cell envelope from oxidative damageHelicobacter pylori defense against oxidative attackCrystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxinsCysteine p K a Values for the Bacterial Peroxiredoxin AhpC † ‡The Sensitive Balance between the Fully Folded and Locally Unfolded Conformations of a Model PeroxiredoxinStructure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coliThe Cell Killing Mechanisms of HydroxyureaProteomic profiling of the dioxin-degrading bacterium Sphingomonas wittichii RW1Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxinPathway for H2O2 and O2 detoxification in Clostridium acetobutylicumDesulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductasePerR acts as a switch for oxygen tolerance in the strict anaerobe Clostridium acetobutylicumThe DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureusComplete genome sequence and description of Salinispira pacifica gen. nov., sp. nov., a novel spirochaete isolated form a hypersaline microbial matDifferential expression of small RNAs from Burkholderia thailandensis in response to varying environmental and stress conditionsMetabolic changes in Klebsiella oxytoca in response to low oxidoreduction potential, as revealed by comparative proteomic profiling integrated with flux balance analysisGenome-wide analysis of putative peroxiredoxin in unicellular and filamentous cyanobacteriaCrosstalk between ROS homeostasis and secondary metabolism in S. natalensis ATCC 27448: modulation of pimaricin production by intracellular ROSBiological and Chemical Adaptation to Endogenous Hydrogen Peroxide Production in Streptococcus pneumoniae D39Hydrogen peroxide detoxification is a key mechanism for growth of ammonia-oxidizing archaeaRegulation of catalase-peroxidase KatG is OxyR dependent and Fur independent in Caulobacter crescentus.Regulation of perR expression by iron and PerR in Campylobacter jejuniohrR and ohr are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens.OxyR regulated the expression of two major catalases, KatA and KatB, along with peroxiredoxin, AhpC in Pseudomonas putida.Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin.Antisense RNA modulation of alkyl hydroperoxide reductase levels in Helicobacter pylori correlates with organic peroxide toxicity but not infectivity.Compensatory functions of two alkyl hydroperoxide reductases in the oxidative defense system of Legionella pneumophila
P2860
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P2860
Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli.
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Alkyl hydroperoxide reductase ...... peroxide in Escherichia coli.
@ast
Alkyl hydroperoxide reductase ...... peroxide in Escherichia coli.
@en
type
label
Alkyl hydroperoxide reductase ...... peroxide in Escherichia coli.
@ast
Alkyl hydroperoxide reductase ...... peroxide in Escherichia coli.
@en
prefLabel
Alkyl hydroperoxide reductase ...... peroxide in Escherichia coli.
@ast
Alkyl hydroperoxide reductase ...... peroxide in Escherichia coli.
@en
P2860
P1476
Alkyl hydroperoxide reductase ...... peroxide in Escherichia coli.
@en
P2093
P2860
P304
P356
10.1128/JB.183.24.7173-7181.2001
P407
P577
2001-12-01T00:00:00Z