InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II
about
The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistanceMolecular docking and structure-based drug design strategiesRational Design of Broad Spectrum Antibacterial Activity Based on a Clinically Relevant Enoyl-Acyl Carrier Protein (ACP) Reductase InhibitorPathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosisInactivation 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 smegmatisMethodological and Clinical Aspects of the Molecular Epidemiology of Mycobacterium tuberculosis and Other MycobacteriaProtein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viabilityTracking the putative biosynthetic precursors of oxygenated mycolates of Mycobacterium tuberculosis. Structural analysis of fatty acids of a mutant strain deviod of methoxy- and ketomycolatesFunction 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 cerevisiaeMycothiol biosynthesis is essential for ethionamide susceptibility in Mycobacterium tuberculosisMycolic acid biosynthesis and enzymic characterization of the beta-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosisRapid Molecular Detection of Multidrug-Resistant Tuberculosis by PCR-Nucleic Acid Lateral Flow ImmunoassayNew antimycobacterial agents in the pre-clinical phase or beyond: recent advances in patent literature (2001-2016).Tuberculosis Drug Development: History and Evolution of the Mechanism-Based Paradigm.Probing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis.Ligand specificity of group I biotin protein ligase of Mycobacterium tuberculosisA novel interaction linking the FAS-II and phthiocerol dimycocerosate (PDIM) biosynthetic pathways.Genomic analysis of globally diverse Mycobacterium tuberculosis strains provides insights into the emergence and spread of multidrug resistance.Detection of mutations associated with isoniazid resistance in Mycobacterium tuberculosis isolates from China.Phosphorylation of enoyl-acyl carrier protein reductase InhA impacts mycobacterial growth and survival.Molecular investigation of resistance to the antituberculous drug ethionamide in multidrug-resistant clinical isolates of Mycobacterium tuberculosisA postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis.Fatty acid biosynthesis as a target for novel antibacterialsAntigen 85C inhibition restricts Mycobacterium tuberculosis growth through disruption of cord factor biosynthesisInhibition of isolated Mycobacterium tuberculosis fatty acid synthase I by pyrazinamide analogs.Structural Basis for the Regulation of the MmpL Transporters of Mycobacterium tuberculosis.Molecular docking studies on InhA, MabA and PanK enzymes from Mycobacterium tuberculosis of ellagic acid derivatives from Ludwigia adscendens and Trewia nudiflora.New advances in fatty acids as antimalarial, antimycobacterial and antifungal agents.Synthesis and biological activity of alkynoic acids derivatives against mycobacteriaVersatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids.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.The Metal-Dependent Regulators FurA and FurB from Mycobacterium TuberculosisDetection and characterization of drug-resistant conferring genes in Mycobacterium tuberculosis complex strains: A prospective study in two distant regions of Ghana.Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser/Thr protein kinase.Screening and characterization of mutations in isoniazid-resistant Mycobacterium tuberculosis isolates obtained in BrazilTargeting InhA, the FASII enoyl-ACP reductase: SAR studies on novel inhibitor scaffolds.Antituberculosis drug research: a critical overview.MmpL3 a potential new target for development of novel anti-tuberculosis drugs.Fighting an old disease with modern tools: characteristics and molecular detection methods of drug-resistant Mycobacterium tuberculosis.Isoniazid: A Review of Characteristics, Properties and Analytical Methods.
P2860
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P2860
InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II
description
2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im Februar 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/02/01)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/02/01)
@nl
наукова стаття, опублікована в лютому 2000
@uk
مقالة علمية (نشرت في فبراير 2000)
@ar
name
InhA, a target of the antitube ...... acid elongation system, FAS-II
@ast
InhA, a target of the antitube ...... acid elongation system, FAS-II
@en
InhA, a target of the antitube ...... acid elongation system, FAS-II
@nl
type
label
InhA, a target of the antitube ...... acid elongation system, FAS-II
@ast
InhA, a target of the antitube ...... acid elongation system, FAS-II
@en
InhA, a target of the antitube ...... acid elongation system, FAS-II
@nl
prefLabel
InhA, a target of the antitube ...... acid elongation system, FAS-II
@ast
InhA, a target of the antitube ...... acid elongation system, FAS-II
@en
InhA, a target of the antitube ...... acid elongation system, FAS-II
@nl
P2093
P3181
P1433
P1476
InhA, a target of the antitube ...... acid elongation system, FAS-II
@en
P2093
A. Quémard
G. Lanéelle
H. Marrakchi
P304
P3181
P356
10.1099/00221287-146-2-289
P478
146 ( Pt 2)
P577
2000-02-01T00:00:00Z