The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistance
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New agents for the treatment of drug-resistant Mycobacterium tuberculosisNew Insight into the Mechanism of Action of and Resistance to Isoniazid: Interaction of Mycobacterium tuberculosis enoyl-ACP Reductase with INH-NADPA Slow, Tight Binding Inhibitor of InhA, the Enoyl-Acyl Carrier Protein Reductase from Mycobacterium tuberculosisIsonicotinic Acid Hydrazide Conversion to Isonicotinyl-NAD by Catalase-peroxidasesTowards a new tuberculosis drug: pyridomycin - nature's isoniazidCrystal structures and kinetic properties of enoyl-acyl carrier protein reductase I fromCandidatus Liberibacter asiaticusA structural and energetic model for the slow-onset inhibition of the Mycobacterium tuberculosis enoyl-ACP reductase InhA.Time-Dependent Diaryl Ether Inhibitors of InhA: Structure-Activity Relationship Studies of Enzyme Inhibition, Antibacterial Activity, and in vivo EfficacyThe crystal structure of isoniazid-bound KatG catalase-peroxidase from Synechococcus elongatus PCC7942Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro-drug isoniazidResistance Mechanisms and the Future of Bacterial Enoyl-Acyl Carrier Protein Reductase (FabI) AntibioticsIsoniazid metabolism and hepatotoxicityDrug discovery using chemical systems biology: repositioning the safe medicine Comtan to treat multi-drug and extensively drug resistant tuberculosisMechanism and inhibition of saFabI, the enoyl reductase from Staphylococcus aureusCrystal structure of Mycobacterium tuberculosis catalase-peroxidaseMechanism and inhibition of the FabV enoyl-ACP reductase from Burkholderia malleiA Four-Point Screening Method for Assessing Molecular Mechanism of Action (MMOA) Identifies Tideglusib as a Time-Dependent Inhibitor of Trypanosoma brucei GSK3βMechanisms of action of isoniazidTuberculosis Drug Development: History and Evolution of the Mechanism-Based Paradigm.Noninvasive determination of 2-[18F]-fluoroisonicotinic acid hydrazide pharmacokinetics by positron emission tomography in Mycobacterium tuberculosis-infected miceClassic reaction kinetics can explain complex patterns of antibiotic action.Probing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis.A novel interaction linking the FAS-II and phthiocerol dimycocerosate (PDIM) biosynthetic pathways.Slow onset inhibition of bacterial beta-ketoacyl-acyl carrier protein synthases by thiolactomycin.Radiosynthesis and bioimaging of the tuberculosis chemotherapeutics isoniazid, rifampicin and pyrazinamide in baboonsNovel inhibitors of InhA efficiently kill Mycobacterium tuberculosis under aerobic and anaerobic conditions.Rational Modulation of the Induced-Fit Conformational Change for Slow-Onset Inhibition in Mycobacterium tuberculosis InhA.Drug-target residence time: critical information for lead optimization.Protein-protein interaction networks suggest different targets have different propensities for triggering drug resistance.Insights into the slow-onset tight-binding inhibition of Escherichia coli dihydrofolate reductase: detailed mechanistic characterization of pyrrolo [3,2-f] quinazoline-1,3-diamine and its derivatives as novel tight-binding inhibitors.Mechanism and inhibition of the FabI enoyl-ACP reductase from Burkholderia pseudomalleiRadiosynthesis and biological evaluation of a novel enoyl-ACP reductase inhibitor for Staphylococcus aureusPopulation genetics study of isoniazid resistance mutations and evolution of multidrug-resistant Mycobacterium tuberculosis.Enzyme Mechanism and Slow-Onset Inhibition of Plasmodium falciparum Enoyl-Acyl Carrier Protein Reductase by an Inorganic Complex.Direct inhibitors of InhA are active against Mycobacterium tuberculosis.A novel metabolite of antituberculosis therapy demonstrates host activation of isoniazid and formation of the isoniazid-NAD+ adduct.Comparative analysis of mycobacterial NADH pyrophosphatase isoforms reveals a novel mechanism for isoniazid and ethionamide inactivationVirtually Designed Triclosan-Based Inhibitors of Enoyl-Acyl Carrier Protein Reductase of Mycobacterium tuberculosis and of Plasmodium falciparum.Radiolabelling and positron emission tomography of PT70, a time-dependent inhibitor of InhA, the Mycobacterium tuberculosis enoyl-ACP reductase.Discovery of cofactor-specific, bactericidal Mycobacterium tuberculosis InhA inhibitors using DNA-encoded library technology.
P2860
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P2860
The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistance
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
@ast
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
@en
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
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label
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
@ast
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
@en
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
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prefLabel
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
@ast
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
@en
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
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P2093
P2860
P3181
P356
P1476
The isoniazid-NAD adduct is a ...... t affinity and drug resistance
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P2093
Adrian Whitty
Peter J Tonge
Richa Rawat
P2860
P304
P3181
P356
10.1073/PNAS.2235848100
P407
P577
2003-11-25T00:00:00Z