About: Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis

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About: Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis Goto Sponge NotDistinct Permalink

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scientific journal article

Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 2004 (ast) vědecký článek publikovaný v roce 2004 (cs) 2004 թվականի մարտին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в березні 2004 (uk) 2004 թուականի Մարտին հրատարակուած գիտական յօդուած (hyw) مقالة علمية (نشرت في مارس 2004) (ar) wetenschappelijk artikel (gepubliceerd op 2004/03/01) (nl) vedecký článok (publikovaný 2004/03/01) (sk) im März 2004 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28486909-4B630110-C338-45B1-8F52-5F428FDBCFA1
publication date	2004-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28486909-B61964E5-0F4F-4E2B-9C32-C8090BE77218
language of work or name	English
author name string	wds:Q28486909-0097920A-D353-4282-A73D-2A309DB90C16 wds:Q28486909-632911EB-57DE-409E-A369-EC680C97D48A wds:Q28486909-64269775-4FBC-49A1-B082-4AA8707FBBAA wds:Q28486909-7D047942-B6AD-4379-8B96-5C213FF0DB00 wds:Q28486909-AFF290A9-8AFB-4EE1-91B0-744B0A28D4DB wds:Q28486909-C310EC10-E99A-4FB9-9BA4-892E755EB2BC wds:Q28486909-E3A1B6DA-D177-4564-B658-FADEB2045FAA
OpenCitations bibliographic resource ID	wds:Q28486909-2B71AAF1-3E43-4770-9061-9EEDEFEF8617
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1142171
author name string	Heike Budde Leopold Flohé Ulrich Menge Mahavir Singh Rafael Radi Timo Jaeger Madia Trujillo
OpenCitations bibliographic resource ID	1142171
rdfs:label	Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (en) Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (nl) Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (ast)
skos:prefLabel	Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (en) Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (nl) Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (ast)
name	Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (en) Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (nl) Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (ast)
title	wds:Q28486909-28D2B9DE-27C6-4AAA-AD65-F33A30BD52A2
title	Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis (en)
page(s)	wds:Q28486909-C3CC7141-DBB7-49FF-87A5-C3C0F3A5E61D
page(s)	182–191
instance of	wds:Q28486909-5264841C-E65C-431B-9122-AE4C7B304ED4
instance of	scholarly article
main subject	wds:Q28486909-14AE7BC4-AF6F-40D1-9E9F-8E63371D61E9 wds:Q28486909-BEDF99EF-5F9E-4CF5-912F-015F5A4FCD25
main subject	Mycobacterium tuberculosis tuberculosis
PubMed ID	wds:Q28486909-ED7B33DA-C97A-4E19-ABD5-DDD2F31405D8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14871480
PubMed ID	14871480
published in	wds:Q28486909-FB657D07-4824-47F3-8BFB-D7CCD3546FA4
published in	Archives of Biochemistry and Biophysics
issue	wds:Q28486909-24F832CF-19F8-40C4-9D74-319D0DA67640
volume	wds:Q28486909-6D1D69D4-4E15-462A-B3FE-4C04070478FD
issue	1
volume	423
DOI	wds:Q28486909-B3BCA1D3-FDC7-453C-BD35-E0F5B0015A84
DOI	http://dx.doi.org/10.1016/J.ABB.2003.11.021
DOI	10.1016/J.ABB.2003.11.021
ResearchGate publication ID	wds:Q28486909-8A253B43-CBD1-41B7-958F-688A8C87101B
ResearchGate publication ID	8779807
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28486909
is cites work of	Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin Redox homeostasis in mycobacteria: the key to tuberculosis control? Thiol peroxidase protects Salmonella enterica from hydrogen peroxide stress in vitro and facilitates intracellular growth Bacterial manipulation of innate immunity to promote infection. Pseudomonas aeruginosa thiol peroxidase protects against hydrogen peroxide toxicity and displays atypical patterns of gene regulation Functional studies of multiple thioredoxins from Mycobacterium tuberculosis Glutathione disulfide and S-nitrosoglutathione detoxification by Mycobacterium tuberculosis thioredoxin system Reducing the activity and secretion of microbial antioxidants enhances the immunogenicity of BCG. Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite Changing paradigms in thiology from antioxidant defense toward redox regulation The mycobacterial thioredoxin peroxidase can act as a one-cysteine peroxiredoxin Drug targets in mycobacterial sulfur metabolism Virulence factors of the Mycobacterium tuberculosis complex Global transcriptional profile of Mycobacterium tuberculosis during THP-1 human macrophage infection Genome sequence of Fusobacterium nucleatum subspecies polymorphum - a genetically tractable fusobacterium Measurement of peroxiredoxin activity Molecular function of WhiB4/Rv3681c of Mycobacterium tuberculosis H37Rv: a [4Fe-4S] cluster co-ordinating protein disulphide reductase Acute and persistent Mycobacterium tuberculosis infections depend on the thiol peroxidase TpX The Oxidative Stress Network of Mycobacterium tuberculosis Reveals Coordination between Radical Detoxification Systems Mycobacterium tuberculosis phosphoenolpyruvate carboxykinase is regulated by redox mechanisms and interaction with thioredoxin Kinetic studies on peroxynitrite reduction by peroxiredoxins. Mycobacterium tuberculosis expresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochlorite Perturbation of cytochrome c maturation reveals adaptability of the respiratory chain in Mycobacterium tuberculosis. Serodiagnostic markers for the prediction of the outcome of intensive phase tuberculosis therapy. Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols. Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant Defense Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis Auranofin exerts broad-spectrum bactericidal activities by targeting thiol-redox homeostasis An altered Mycobacterium tuberculosis metabolome induced by katG mutations resulting in isoniazid resistance TrxA reactivates AhpC TrxB reactivates TrxA TrxA/B1 reactivates Tpx

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