Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
about
Tuberculosis and trimethoprim-sulfamethoxazoleStrategies for potentiation of ethionamide and folate antagonists against Mycobacterium tuberculosisNew Insight into the Mechanism of Action of and Resistance to Isoniazid: Interaction of Mycobacterium tuberculosis enoyl-ACP Reductase with INH-NADPX-ray structure of the ternary MTX.NADPH complex of the anthrax dihydrofolate reductase: a pharmacophore for dual-site inhibitor designHigh-throughput screening and sensitized bacteria identify an M. tuberculosis dihydrofolate reductase inhibitor with whole cell activityMechanisms of action of isoniazidProbing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis.PocketMatch: a new algorithm to compare binding sites in protein structures.Kinetic and chemical mechanism of the dihydrofolate reductase from Mycobacterium tuberculosisAn upstream truncation of the furA-katG operon confers high-level isoniazid resistance in a Mycobacterium tuberculosis clinical isolate with no known resistance-associated mutations.Molecular investigation of resistance to the antituberculous drug ethionamide in multidrug-resistant clinical isolates of Mycobacterium tuberculosisBioactivation of antituberculosis thioamide and thiourea prodrugs by bacterial and mammalian flavin monooxygenases.Depletion of antibiotic targets has widely varying effects on growthBacterial conversion of folinic acid is required for antifolate resistance.A novel metabolite of antituberculosis therapy demonstrates host activation of isoniazid and formation of the isoniazid-NAD+ adduct.In silico-based high-throughput screen for discovery of novel combinations for tuberculosis treatmentAntimicrobial susceptibility testing, drug resistance mechanisms, and therapy of infections with nontuberculous mycobacteria.Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis.Antibiotic resistance in Mycobacterium tuberculosis: peroxidase intermediate bypass causes poor isoniazid activation by the S315G mutant of M. tuberculosis catalase-peroxidase (KatG)Contribution of dfrA and inhA mutations to the detection of isoniazid-resistant Mycobacterium tuberculosis isolatesMycobacterium tuberculosis: drug resistance and future perspectives.Characterizing the pocketome of Mycobacterium tuberculosis and application in rationalizing polypharmacological target selection.Targeting InhA, the FASII enoyl-ACP reductase: SAR studies on novel inhibitor scaffolds.Inhibitors of fatty acid synthesis in prokaryotes and eukaryotes as anti-infective, anticancer and anti-obesity drugs.Is repositioning of drugs a viable alternative in the treatment of tuberculosis?Drug Resistance Mechanisms in Mycobacterium tuberculosis.The potential role of trimethoprim-sulfamethoxazole in the treatment of drug-resistant tuberculosis.Examining the basis of isoniazid tolerance in nonreplicating Mycobacterium tuberculosis using transcriptional profiling.Structural analysis of dihydrofolate reductases enables rationalization of antifolate binding affinities and suggests repurposing possibilities.Development of new antituberculous agents based on new drug targets and structure-activity relationship.Mycobacterium tuberculosis dihydrofolate reductase is not a target relevant to the antitubercular activity of isoniazid.Role of mutations in dihydrofolate reductase DfrA (Rv2763c) and thymidylate synthase ThyA (Rv2764c) in Mycobacterium tuberculosis drug resistance.Two parallel pathways in the kinetic sequence of the dihydrofolate reductase from Mycobacterium tuberculosisSynthesis of Novel Fluorene Bisamide Derivatives via Ugi Reaction and Evaluation their Biological Activity against Mycobacterium species.Mechanism of inhibition of wt-dihydrofolate reductase from E. coli by tea epigallocatechin-gallate.Structure based drug discovery for designing leads for the non-toxic metabolic targets in multi drug resistant Mycobacterium tuberculosis.Update of Antitubercular Prodrugs from a Molecular Perspective: Mechanisms of Action, Bioactivation Pathways, and Associated Resistance.Probing the binding mechanism of mercaptoguanine derivatives as inhibitors of HPPK by docking and molecular dynamics simulations.Transfer of a point mutation in Mycobacterium tuberculosis inhA resolves the target of isoniazid.
P2860
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P2860
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
description
2006 nî lūn-bûn
@nan
2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
@ast
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
@en
type
label
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
@ast
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
@en
prefLabel
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
@ast
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
@en
P2093
P356
P1476
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
@en
P2093
Argyrides Argyrou
Bola Aladegbami
John S Blanchard
Matthew W Vetting
P2888
P304
P356
10.1038/NSMB1089
P577
2006-04-30T00:00:00Z
P6179
1050639406