About: InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II

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Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 2000 (ast) vědecký článek publikovaný v roce 2000 (cs) наукова стаття, опублікована в лютому 2000 (uk) 2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած (hyw) 2000 թվականի փետրվարին հրատարակված գիտական հոդված (hy) im Februar 2000 veröffentlichter wissenschaftlicher Artikel (de) vedecký článok (publikovaný 2000/02/01) (sk) wüsseschaftlicher Artikel, wo im Hornig 2000 veröffentlicht worden isch (gsw) مقالة علمية (نشرت في فبراير 2000) (ar) wetenschappelijk artikel (gepubliceerd op 2000/02/01) (nl) scientific journal article (en)
publication date	wds:Q28486679-22FA0A71-096B-40C4-BAD2-9EE83CFD194D
publication date	2000-02-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q28486679-7CE6DF52-30CF-4C93-B132-0F36BDB8D48F
cites work	Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
author name string	wds:Q28486679-2B67F105-655B-4ACB-9C25-0F23DC128D79 wds:Q28486679-8793A63F-81FB-4367-BF49-F1AA70DC951E wds:Q28486679-A6060A53-B88D-47AE-88B9-8BACD4F56555
OpenCitations bibliographic resource ID	wds:Q28486679-54088E6C-9D3D-4AC2-846B-3EFBA4A7D540
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1338110
author name string	A. Quémard G. Lanéelle H. Marrakchi
OpenCitations bibliographic resource ID	1338110
rdfs:label	InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (en) InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (nl) InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (ast)
skos:prefLabel	InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (en) InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (nl) InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (ast)
name	InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (en) InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (nl) InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (ast)
title	wds:Q28486679-A6E8AE20-E418-44C1-BFE1-8392B2C26FC6
title	InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II (en)
page(s)	wds:Q28486679-26B4C3BB-52AD-4284-AD2D-A5EFA1A67910
page(s)	289–296
instance of	wds:Q28486679-1EE38F45-933A-4B9B-A7F0-10C3FB86A1A6
instance of	scholarly article
main subject	wds:Q28486679-160BF664-49EE-4A9A-9E6D-DB9D12B0A4ED wds:Q28486679-99DB7CC8-8ED8-4911-9A99-096633266EF6
main subject	isoniazid fatty acid
PubMed ID	wds:Q28486679-61B2ADD2-572A-46EB-AFDE-6CC2F6980522
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10708367
PubMed ID	10708367
published in	wds:Q28486679-4532B7D2-E53C-4E5C-8941-CF1716D18C42
published in	Microbiology
volume	wds:Q28486679-17DE3FD6-CFBE-47DC-B34E-B9257670A97E
volume	146 ( Pt 2)
DOI	wds:Q28486679-C1986E2E-01AF-4F59-A72A-F4F90C6EC0A0
DOI	http://dx.doi.org/10.1099/00221287-146-2-289
DOI	10.1099/00221287-146-2-289
ResearchGate publication ID	wds:Q28486679-4DFD3ED8-9AC7-446A-9757-B980BBEBD07C
ResearchGate publication ID	12608110
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28486679
is cites work of	MmpL3 a potential new target for development of novel anti-tuberculosis drugs Detection of mutations associated with isoniazid resistance in Mycobacterium tuberculosis isolates from China Polyketide versatility in the biosynthesis of complex mycobacterial cell wall lipids Ligand-induced fit in mycobacterial MabA: the sequence-specific C-terminus locks the conformational change HemZ is essential for heme biosynthesis in Mycobacterium tuberculosis Lipid biosynthesis as a target for antibacterial agents Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability Mycolic acid biosynthesis and enzymic characterization of the beta-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosis A novel interaction linking the FAS-II and phthiocerol dimycocerosate (PDIM) biosynthetic pathways In vitro inhibition of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA by isoniazid Molecular docking and structure-based drug design strategies Principal Component Analysis of Proteome Dynamics in Iron-starved Mycobacterium Tuberculosis The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistance Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis Mn(III) pyrophosphate as an efficient tool for studying the mode of action of isoniazid on the InhA protein of Mycobacterium tuberculosis Single nucleotide polymorphisms in genes associated with isoniazid resistance in Mycobacterium tuberculosis Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis. Inhibition of InhA activity, but not KasA activity, induces formation of a KasA-containing complex in mycobacteria Detection of a point mutation associated with high-level isoniazid resistance in Mycobacterium tuberculosis by using real-time PCR technology with 3'-minor groove binder-DNA probes Mycothiol biosynthesis is essential for ethionamide susceptibility in Mycobacterium tuberculosis Molecular investigation of resistance to the antituberculous drug ethionamide in multidrug-resistant clinical isolates of Mycobacterium tuberculosis A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis Tracking the putative biosynthetic precursors of oxygenated mycolates of Mycobacterium tuberculosis. Structural analysis of fatty acids of a mutant strain deviod of methoxy- and ketomycolates The biosynthesis of mycolic acids by Mycobacteria: current and alternative hypotheses Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Screening and characterization of mutations in isoniazid-resistant Mycobacterium tuberculosis isolates obtained in Brazil Phosphorylation of enoyl-acyl carrier protein reductase InhA impacts mycobacterial growth and survival Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser/Thr protein kinase. New antimycobacterial agents in the pre-clinical phase or beyond: recent advances in patent literature (2001-2016). Fatty acid biosynthesis as a target for novel antibacterials Ligand specificity of group I biotin protein ligase of Mycobacterium tuberculosis Inhibition of Mycobacterium tuberculosis secretory serine protease blocks bacterial multiplication both in axenic culture and in human macrophages Targeting InhA, the FASII enoyl-ACP reductase: SAR studies on novel inhibitor scaffolds. Genomic analysis of globally diverse Mycobacterium tuberculosis strains provides insights into the emergence and spread of multidrug resistance Synthesis and antimycobacterial activity of a novel series of isonicotinylhydrazide derivatives Antigen 85C inhibition restricts Mycobacterium tuberculosis growth through disruption of cord factor biosynthesis New advances in fatty acids as antimalarial, antimycobacterial and antifungal agents Resistance to Isoniazid and Ethionamide in Mycobacterium tuberculosis: Genes, Mutations, and Causalities. Rational Design of Broad Spectrum Antibacterial Activity Based on a Clinically Relevant Enoyl-Acyl Carrier Protein (ACP) Reductase Inhibitor Alkylamino derivatives of N-benzylpyrazine-2-carboxamide: synthesis and antimycobacterial evaluation Elucidating drug-enzyme interactions and their structural basis for improving the affinity and potency of isoniazid and its derivatives based on computer modeling approaches

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