Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
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Redox homeostasis in mycobacteria: the key to tuberculosis control?Structural Changes Common to Catalysis in the Tpx Peroxiredoxin SubfamilyStructure ofMycobacterium tuberculosisthioredoxin in complex with quinol inhibitor PMX464Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingFunctional studies of multiple thioredoxins from Mycobacterium tuberculosisMolecular function of WhiB4/Rv3681c of Mycobacterium tuberculosis H37Rv: a [4Fe-4S] cluster co-ordinating protein disulphide reductaseAcute and persistent Mycobacterium tuberculosis infections depend on the thiol peroxidase TpXGlutathione disulfide and S-nitrosoglutathione detoxification by Mycobacterium tuberculosis thioredoxin systemMycobacterium tuberculosis expresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochloriteThe mycobacterial thioredoxin peroxidase can act as a one-cysteine peroxiredoxinPseudomonas aeruginosa thiol peroxidase protects against hydrogen peroxide toxicity and displays atypical patterns of gene regulationMycobacterium tuberculosis Thioredoxin Reductase Is Essential for Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant DefenseAuranofin exerts broad-spectrum bactericidal activities by targeting thiol-redox homeostasisGenome sequence of Fusobacterium nucleatum subspecies polymorphum - a genetically tractable fusobacteriumReducing the activity and secretion of microbial antioxidants enhances the immunogenicity of BCG.Thiol peroxidase protects Salmonella enterica from hydrogen peroxide stress in vitro and facilitates intracellular growth.Regulation of the ahpC gene encoding alkyl hydroperoxide reductase in Mycobacterium smegmatis.Drug targets in mycobacterial sulfur metabolism.New targets and inhibitors of mycobacterial sulfur metabolism.Transcriptional profiling of Mycobacterium tuberculosis replicating ex vivo in blood from HIV- and HIV+ subjectsThe Oxidative Stress Network of Mycobacterium tuberculosis Reveals Coordination between Radical Detoxification SystemsInsights into the Function of a Second, Nonclassical Ahp Peroxidase, AhpA, in Oxidative Stress Resistance in Bacillus subtilis.Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxinMeasurement of peroxiredoxin activity.Perturbation of cytochrome c maturation reveals adaptability of the respiratory chain in Mycobacterium tuberculosis.Transcriptional characterization of the antioxidant response of Mycobacterium tuberculosis in vivo and during adaptation to hypoxia in vitro.Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite.Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis.Superoxide Generation and Its Involvement in the Growth of Mycobacterium smegmatis.Virulence factors of the Mycobacterium tuberculosis complexOne- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates.Nitrosative stress defences of the enterohepatic pathogenic bacterium Helicobacter pullorumAn altered Mycobacterium tuberculosis metabolome induced by katG mutations resulting in isoniazid resistance.Mycobacterium tuberculosis phosphoenolpyruvate carboxykinase is regulated by redox mechanisms and interaction with thioredoxin.Global transcriptional profile of Mycobacterium tuberculosis during THP-1 human macrophage infection.AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C.Quantitative analysis of cellular proteome alterations of Pseudomonas putida to naphthalene-induced stress.Mass Spectrometric Analysis of Mycothiol levels in Wild-Type and Mycothiol Disulfide Reductase Mutant Mycobacterium smegmatis.Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols.Protein tyrosine kinase, PtkA, is required for Mycobacterium tuberculosis growth in macrophages.
P2860
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P2860
Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
description
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2004
@ast
im März 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/03/01)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/03/01)
@nl
наукова стаття, опублікована в березні 2004
@uk
مقالة علمية (نشرت في مارس 2004)
@ar
name
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@ast
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@en
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@nl
type
label
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@ast
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@en
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@nl
prefLabel
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@ast
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@en
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@nl
P2093
P3181
P1476
Multiple thioredoxin-mediated ...... in Mycobacterium tuberculosis
@en
P2093
Heike Budde
Leopold Flohé
Madia Trujillo
Mahavir Singh
Rafael Radi
Timo Jaeger
Ulrich Menge
P304
P3181
P356
10.1016/J.ABB.2003.11.021
P407
P577
2004-03-01T00:00:00Z