Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
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Flux balance analysis of mycolic acid pathway: targets for anti-tubercular drugsPlatensimycin activity against mycobacterial beta-ketoacyl-ACP synthasesAntimycobacterial activities of isoxyl and new derivatives through the inhibition of mycolic acid synthesisThe isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistanceRedox homeostasis in mycobacteria: the key to tuberculosis control?Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrateInhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognitionNew Insight into the Mechanism of Action of and Resistance to Isoniazid: Interaction of Mycobacterium tuberculosis enoyl-ACP Reductase with INH-NADPCrystal structure of enoyl-acyl carrier protein reductase (FabK) fromStreptococcus pneumoniaereveals the binding mode of an inhibitorTriclosan Derivatives: Towards Potent Inhibitors of Drug-Sensitive and Drug-ResistantMycobacterium tuberculosisTowards a new tuberculosis drug: pyridomycin - nature's isoniazidStructure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone InhibitorsA structural and energetic model for the slow-onset inhibition of the Mycobacterium tuberculosis enoyl-ACP reductase InhA.Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanismResistance Mechanisms and the Future of Bacterial Enoyl-Acyl Carrier Protein Reductase (FabI) AntibioticsUsing modern tools to probe the structure-function relationship of fatty acid synthasesPathway 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 smegmatisIn vitro activity of a novel antimycobacterial compound, N-octanesulfonylacetamide, and its effects on lipid and mycolic acid synthesisNADH dehydrogenase defects confer isoniazid resistance and conditional lethality in Mycobacterium smegmatisAntimycobacterial action of thiolactomycin: an inhibitor of fatty acid and mycolic acid synthesisBiochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase IIPurification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosisThe missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosisOverexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosisAccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosisRevisiting the assignment of Rv0241c to fatty acid synthase type II of Mycobacterium tuberculosisMycobacterium tuberculosis genes induced during infection of human macrophagesFunction 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 cerevisiaeIsoniazid induces expression of the antigen 85 complex in Mycobacterium tuberculosisMycothiol biosynthesis is essential for ethionamide susceptibility in Mycobacterium tuberculosisSignature gene expression profiles discriminate between isoniazid-, thiolactomycin-, and triclosan-treated Mycobacterium tuberculosisThe enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilisTuberculosis Drug Development: History and Evolution of the Mechanism-Based Paradigm.MycPermCheck: the Mycobacterium tuberculosis permeability prediction tool for small molecules.Pyrrolidine carboxamides as a novel class of inhibitors of enoyl acyl carrier protein reductase from Mycobacterium tuberculosisProbing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis.Targeting fatty acid biosynthesis for the development of novel chemotherapeutics against Mycobacterium tuberculosis: evaluation of A-ring-modified diphenyl ethers as high-affinity InhA inhibitorsFunctional, thermodynamics, structural and biological studies of in silico-identified inhibitors of Mycobacterium tuberculosis enoyl-ACP(CoA) reductase enzyme.Genomic analysis of globally diverse Mycobacterium tuberculosis strains provides insights into the emergence and spread of multidrug resistance.
P2860
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P2860
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
description
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1995
@ast
im Juli 1995 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1995/07/04)
@sk
vědecký článek publikovaný v roce 1995
@cs
wetenschappelijk artikel (gepubliceerd op 1995/07/04)
@nl
наукова стаття, опублікована в липні 1995
@uk
مقالة علمية (نشرت في 4-7-1995)
@ar
name
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@ast
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@en
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@nl
type
label
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@ast
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@en
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@nl
prefLabel
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@ast
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@en
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@nl
P2093
P356
P1433
P1476
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
@en
P2093
A. Quémard
C. Vilcheze
J. C. Sacchettini
J. S. Blanchard
R. Bittman
W. R. Jacobs
P304
P356
10.1021/BI00026A004
P407
P577
1995-07-04T00:00:00Z