About: Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability

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About: Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability Goto Sponge NotDistinct Permalink

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scientific journal article

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rdf:type	Item
description	article scientifique publié en 2004 (fr) artículu científicu espublizáu en 2004 (ast) vědecký článek publikovaný v roce 2004 (cs) مقالة علمية (نشرت في ديسمبر 2004) (ar) 2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в грудні 2004 (uk) 2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 2004/12/01) (sk) wetenschappelijk artikel (gepubliceerd op 2004/12/01) (nl) im Dezember 2004 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28486363-CF9CAED7-7ED7-470A-A789-5A43126765CF
publication date	2004-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28486363-43F5A09A-EAF1-4253-9A19-728A65E4EC86
language of work or name	English
cites work	wds:Q28486363-459787FA-E152-422D-80BF-6789BA3C37F1 wds:Q28486363-85B47DFB-ED29-46C5-968D-DF727DB79DCB wds:Q28486363-CB9389DD-5D1A-417A-A282-6522D3C393A1 wds:Q28486363-D19D10EF-B063-44C0-B756-87B3D06870CE
cites work	Fatty acid synthetase activity in Mycobacterium smegmatis Characterization of the acyl carrier protein-dependent elongating system MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II Biochemical and genetic data suggest that InhA is not the primary target for activated isoniazid in Mycobacterium tuberculosis
author name string	wds:Q28486363-1121DB28-4BF4-4ECD-944A-F6F659C59FFA wds:Q28486363-C7494146-9FF9-4E4A-9898-888B8A58F0B1
author name string	Lionel Mourey Olivier Guerrini
rdfs:label	Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (en) Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (nl) Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (ast)
skos:prefLabel	Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (en) Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (nl) Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (ast)
name	Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (en) Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (nl) Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (ast)
author	wds:Q28486363-1CA2B8C7-2184-49B5-A41F-9C577B97BB80 wds:Q28486363-79F16460-9E66-43B8-9A23-E19E6E56C8A0 wds:Q28486363-FF04E88A-D58B-4C9E-866C-C6E21A23232C
author	Romain Veyron-Churlet Didier Zerbib Mamadou Daffé
title	wds:Q28486363-03C0857F-AF20-4D77-81C2-F6F9AFA1CFE5
title	Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability (en)
page(s)	wds:Q28486363-F0E4CB6C-E683-461B-A0ED-094E58E77D83
page(s)	1161–1172
instance of	wds:Q28486363-916F6E37-8C5E-459D-B7E5-79CE1E4A2CD6
instance of	scholarly article
main subject	wds:Q28486363-1898DDDE-2C28-498D-8CAF-74B10B95EA1A wds:Q28486363-6A673A3C-B69E-4D9E-8678-7D96CFC8CCAE wds:Q28486363-C3B73FE8-811B-443B-AEBC-86424D23FD2C wds:Q28486363-C99BD61E-ED0B-4084-A1A9-F4A940D51DAD
main subject	protein-protein interaction Mycobacterium tuberculosis tuberculosis fatty acid
PubMed ID	wds:Q28486363-015571E0-F3DF-4442-822D-1DEF128D1C75
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15554959
PubMed ID	15554959
published in	wds:Q28486363-A141E607-743A-46B4-91ED-48FEB0595B45
published in	Molecular Microbiology
issue	wds:Q28486363-5DF5CBB4-8891-444D-B64F-E35C21FE2800
volume	wds:Q28486363-C3D549DA-9004-4051-ACA7-F07317CCB330
issue	5
volume	54
DOI	wds:Q28486363-099031F1-ADA6-4CB0-8F20-6347DBBDE46C
DOI	http://dx.doi.org/10.1111/J.1365-2958.2004.04334.X
DOI	10.1111/J.1365-2958.2004.04334.X
ResearchGate publication ID	wds:Q28486363-4F67D0D9-EE98-4709-8B6C-01B008ACCEF2
ResearchGate publication ID	8172234
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28486363
is cites work of	The Mycobacterium tuberculosis FAS-II dehydratases and methyltransferases define the specificity of the mycolic acid elongation complexes A common mechanism of inhibition of the Mycobacterium tuberculosis mycolic acid biosynthetic pathway by isoxyl and thiacetazone Point mutations within the fatty acid synthase type II dehydratase components HadA or HadC contribute to isoxyl resistance in Mycobacterium tuberculosis Antibacterial targets in fatty acid biosynthesis The essential mycobacterial genes, fabG1 and fabG4, encode 3-oxoacyl-thioester reductases that are functional in yeast mitochondrial fatty acid synthase type 2 Mycobacterium tuberculosis maltosyltransferase GlgE, a genetically validated antituberculosis target, is negatively regulated by Ser/Thr phosphorylation AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation A novel interaction linking the FAS-II and phthiocerol dimycocerosate (PDIM) biosynthetic pathways Functional complementation of the essential gene fabG1 of Mycobacterium tuberculosis by Mycobacterium smegmatis fabG but not Escherichia coli fabG Identification of the Mycobacterium tuberculosis SUF machinery as the exclusive mycobacterial system of [Fe-S] cluster assembly: evidence for its implication in the pathogen's survival Crystal Structures of Mycobacterium tuberculosis KasA Show Mode of Action within Cell Wall Biosynthesis and its Inhibition by Thiolactomycin Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis Mycobacterium tuberculosis proteins involved in mycolic acid synthesis and transport localize dynamically to the old growing pole and septum Probing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis Synthesis, antitubercular activity and mechanism of resistance of highly effective thiacetazone analogues The Non-Essential Mycolic Acid Biosynthesis Genes hadA and hadC Contribute to the Physiology and Fitness of Mycobacterium smegmatis Evolution of Mycolic Acid Biosynthesis Genes and Their Regulation during Starvation in Mycobacterium tuberculosis Mycolic acids: deciphering and targeting the Achilles' heel of the tubercle bacillus Novel intermolecular iterative mechanism for biosynthesis of mycoketide catalyzed by a bimodular polyketide synthase. Function of heterologous Mycobacterium tuberculosis InhA, a type 2 fatty acid synthase enzyme involved in extending C20 fatty acids to C60-to-C90 mycolic acids, during de novo lipoic acid synthesis in Saccharomyces cerevisiae Examining the role of protein structural dynamics in drug resistance in Mycobacterium tuberculosis. Phosphorylation of KasB regulates virulence and acid-fastness in Mycobacterium tuberculosis In Vivo Methods to Study Protein-Protein Interactions as Key Players in Mycobacterium Tuberculosis Virulence The MmpL3 interactome reveals a complex crosstalk between cell envelope biosynthesis and cell elongation and division in mycobacteria Covalent modification of the Mycobacterium tuberculosis FAS-II dehydratase by Isoxyl and Thiacetazone

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