Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium.
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CHIP interacts with heat shock factor 1 during heat stressThiol peroxidases ameliorate LRRK2 mutant-induced mitochondrial and dopaminergic neuronal degeneration in DrosophilaMutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal deathOxidative-stress resistance mutants of Helicobacter pylori.Protein thiol modifications visualized in vivoDistribution and Features of the Six Classes of PeroxiredoxinsMass spectrometry in studies of protein thiol chemistry and signaling: opportunities and caveatsChemical approaches to detect and analyze protein sulfenic acidsA primer on peroxiredoxin biochemistryCrystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene productCysteine p K a Values for the Bacterial Peroxiredoxin AhpC † ‡ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acidCharacterization of the Mycobacterium tuberculosis H37Rv alkyl hydroperoxidase AhpC points to the importance of ionic interactions in oligomerization and activityThe AhpC and AhpD antioxidant defense system of Mycobacterium tuberculosisSulfenic acid chemistry, detection and cellular lifetimeFormation, Reactivity, and Detection of Protein Sulfenic AcidsThe antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function.Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Exposure to cadmium elevates expression of genes in the OxyR and OhrR regulons and induces cross-resistance to peroxide killing treatment in Xanthomonas campestris.Identification of S-nitrosylation of proteins of Helicobacter pylori in response to nitric oxide stress.Crystal structure of alkyl hydroperoxidase D like protein PA0269 from Pseudomonas aeruginosa: homology of the AhpD-like structural family.Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate Anaerobe bacteroides fragilis.Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization.OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis.ohr, Encoding an organic hydroperoxide reductase, is an in vivo-induced gene in Actinobacillus pleuropneumoniaeExpression of a mitochondrial peroxiredoxin prevents programmed cell death in Leishmania donovani.Overview of peroxiredoxins in oxidant defense and redox regulation.Protein S-glutathiolation: redox-sensitive regulation of protein function.Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductaseMechanisms of group A Streptococcus resistance to reactive oxygen species.A Kinetic Platform to Determine the Fate of Hydrogen Peroxide in Escherichia coliWhy do bacteria use so many enzymes to scavenge hydrogen peroxide?The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster.AhpC is required for optimal production of enterobactin by Escherichia coliMutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activityPurification, crystallization and preliminary X-ray analysis of glutathione peroxidase Gpx3 from Saccharomyces cerevisiae.Insights into the Function of a Second, Nonclassical Ahp Peroxidase, AhpA, in Oxidative Stress Resistance in Bacillus subtilis.Quantifying changes in the thiol redox proteome upon oxidative stress in vivo.Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase system
P2860
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P2860
Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
Roles for the two cysteine res ...... e from Salmonella typhimurium.
@en
Roles for the two cysteine res ...... e from Salmonella typhimurium.
@nl
type
label
Roles for the two cysteine res ...... e from Salmonella typhimurium.
@en
Roles for the two cysteine res ...... e from Salmonella typhimurium.
@nl
prefLabel
Roles for the two cysteine res ...... e from Salmonella typhimurium.
@en
Roles for the two cysteine res ...... e from Salmonella typhimurium.
@nl
P356
P1433
P1476
Roles for the two cysteine res ...... se from Salmonella typhimurium
@en
P2093
P304
13349-13356
P356
10.1021/BI9713658
P407
P577
1997-10-01T00:00:00Z