Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress.
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Antimicrobial strategies centered around reactive oxygen species--bactericidal antibiotics, photodynamic therapy, and beyondAn Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression AnalysisStructure ofMycobacterium tuberculosisthioredoxin in complex with quinol inhibitor PMX464Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparumObserved octameric assembly of a Plasmodium yoelii peroxiredoxin can be explained by the replacement of native "ball-and-socket" interacting residues by an affinity tag.The complete genome sequence of Corynebacterium pseudotuberculosis FRC41 isolated from a 12-year-old girl with necrotizing lymphadenitis reveals insights into gene-regulatory networks contributing to virulenceThe 2-Cys peroxiredoxin alkyl hydroperoxide reductase c binds heme and participates in its intracellular availability in Streptococcus agalactiae.Regulation of the ahpC gene encoding alkyl hydroperoxide reductase in Mycobacterium smegmatis.Analysis of the peroxiredoxin family: using active-site structure and sequence information for global classification and residue analysis.Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily.Improved Catenated Structures of Bovine Peroxiredoxin III F190L Reveal Details of Ring-Ring Interactions and a Novel Conformational StateA 1-Cys Peroxiredoxin from a Thermophilic Archaeon Moonlights as a Molecular Chaperone to Protect Protein and DNA against Stress-Induced Damage.The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster.Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxinGenomic and Phenotypic Analyses Reveal the Emergence of an Atypical Salmonella enterica Serovar Senftenberg Variant in China.Functional Characterization of PknI-Rv2159c Interaction in Redox Homeostasis of Mycobacterium tuberculosis.The oligomeric conformation of peroxiredoxins links redox state to function.Virulence factors of the Mycobacterium tuberculosis complexPhosphate Limitation Induces Drastic Physiological Changes, Virulence-Related Gene Expression, and Secondary Metabolite Production in Pseudovibrio sp. Strain FO-BEG1.Development of new antituberculous agents based on new drug targets and structure-activity relationship.Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites.AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C.Molecular characterization of isoniazid resistance in Mycobacterium tuberculosis: identification of a novel mutation in inhA.Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o.Structural and electrostatic asymmetry at the active site in typical and atypical peroxiredoxin dimers.Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum.A eukaryotic-like sulfiredoxin involved in oxidative stress responses and in the reduction of the sulfinic form of 2-Cys peroxiredoxin in the cyanobacterium Anabaena PCC 7120.Alteration of molecular assembly of peroxiredoxins from hyperthermophilic archaea.A thioredoxin-dependent peroxiredoxin Q from Corynebacterium glutamicum plays an important role in defense against oxidative stress.Peroxynitrite is reduced to nitrite by AhpCUnraveling the Amycolatopsis tucumanensis copper-resistome.Computational structural analysis of proteins of Mycobacterium tuberculosis and a resource for identifying off-targetsGlutathionylation Induces the Dissociation of 1-Cys D-peroxiredoxin Non-covalent Homodimer
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P2860
Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Structure and mechanism of the ...... stem against oxidative stress.
@en
Structure and mechanism of the ...... stem against oxidative stress.
@nl
type
label
Structure and mechanism of the ...... stem against oxidative stress.
@en
Structure and mechanism of the ...... stem against oxidative stress.
@nl
prefLabel
Structure and mechanism of the ...... stem against oxidative stress.
@en
Structure and mechanism of the ...... stem against oxidative stress.
@nl
P2093
P50
P356
P1476
Structure and mechanism of the ...... stem against oxidative stress.
@en
P2093
Brigitte Saint-Joanis
Hélène Souchon
Nadine Honoré
Stewart T Cole
William Shepard
P304
25735-25742
P356
10.1074/JBC.M503076200
P407
P577
2005-05-10T00:00:00Z