Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
about
Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological RolesUtilizing Natural and Engineered Peroxiredoxins As Intracellular Peroxide ReportersA primer on peroxiredoxin biochemistryCysteine p K a Values for the Bacterial Peroxiredoxin AhpC † ‡Structural Evidence that Peroxiredoxin Catalytic Power Is Based on Transition-State StabilizationThe Sensitive Balance between the Fully Folded and Locally Unfolded Conformations of a Model PeroxiredoxinModel for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational studySmall but powerful, the primary endosymbiont of moss bugs, Candidatus Evansia muelleri, holds a reduced genome with large biosynthetic capabilitiesManaging oxidative stresses in Shewanella oneidensis: intertwined roles of the OxyR and OhrR regulons.Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin.Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum.Macrophage replication screen identifies a novel Francisella hydroperoxide resistance protein involved in virulence.Characterization of the surfaceome of the metal-reducing bacterium Desulfotomaculum reducensComparative study of the roles of AhpC and KatE as respiratory antioxidants in Brucella abortus 2308Tuning of peroxiredoxin catalysis for various physiological rolesConformational studies of the robust 2-Cys peroxiredoxin Salmonella typhimurium AhpC by solution phase hydrogen/deuterium (H/D) exchange monitored by electrospray ionization mass spectrometry.Peroxiredoxins in plants and cyanobacteria.Redox regulation of protein kinases.Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin.The coenzyme A disulphide reductase of Borrelia burgdorferi is important for rapid growth throughout the enzootic cycle and essential for infection of the mammalian hostThe induction of two biosynthetic enzymes helps Escherichia coli sustain heme synthesis and activate catalase during hydrogen peroxide stress.Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpCA Kinetic Platform to Determine the Fate of Hydrogen Peroxide in Escherichia coliFumarate reductase is a major contributor to the generation of reactive oxygen species in the anaerobe Bacteroides fragilis.Peroxiredoxins in parasites.Why do bacteria use so many enzymes to scavenge hydrogen peroxide?ACHT4-driven oxidation of APS1 attenuates starch synthesis under low light intensity in Arabidopsis plants.AhpC is required for optimal production of enterobactin by Escherichia coliDistinct characteristics of two 2-Cys peroxiredoxins of Vibrio vulnificus suggesting differential roles in detoxifying oxidative stress.Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation.Francisella tularensis Catalase Restricts Immune Function by Impairing TRPM2 Channel Activity.Discovering mechanisms of signaling-mediated cysteine oxidation.Staphylococcus aureus sortase A contributes to the Trojan horse mechanism of immune defense evasion with its intrinsic resistance to Cys184 oxidation.Reactive oxygen species special feature.Measurement of peroxiredoxin activity.Enhancement of the Chaperone Activity of Alkyl Hydroperoxide Reductase C from Pseudomonas aeruginosa PAO1 Resulting from a Point-Specific Mutation Confers Heat Tolerance in Escherichia coli.Redundant hydrogen peroxide scavengers contribute to Salmonella virulence and oxidative stress resistance.NADPH oxidase-derived H2O2 subverts pathogen signaling by oxidative phosphotyrosine conversion to PB-DOPA.
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Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
@en
type
label
Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
@en
prefLabel
Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
@en
P2860
P356
P1476
Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
@en
P2093
Derek Parsonage
P2860
P304
P356
10.1073/PNAS.0708308105
P407
P577
2007-12-28T00:00:00Z