Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
about
Drug targets and mechanisms of resistance in the anaerobic protozoaNitric oxide generated from isoniazid activation by KatG: source of nitric oxide and activity against Mycobacterium tuberculosisThe crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug designThe mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kineticsAnalysis of ahpC gene mutations in isoniazid-resistant clinical isolates of Mycobacterium tuberculosisNADH dehydrogenase defects confer isoniazid resistance and conditional lethality in Mycobacterium smegmatisThe AhpC and AhpD antioxidant defense system of Mycobacterium tuberculosisThe alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosisRole of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpFMechanisms of action of isoniazidNovel selection for isoniazid (INH) resistance genes supports a role for NAD+-binding proteins in mycobacterial INH resistanceNovel roles of ohrR-ohr in Xanthomonas sensing, metabolism, and physiological adaptive response to lipid hydroperoxideMolecular evidence for heterogeneity of the multiple-drug-resistant Mycobacterium tuberculosis population in Scotland (1990 to 1997).Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivationInactivation of the organic hydroperoxide stress resistance regulator OhrR enhances resistance to oxidative stress and isoniazid in Mycobacterium smegmatis.Rapid detection of pyrazinamide-resistant Mycobacterium tuberculosis by a PCR-based in vitro systemInhibition of Mycobacterium tuberculosis AhpD, an element of the peroxiredoxin defense against oxidative stress.Interactions of OxyR with the promoter region of the oxyR and ahpC genes from Mycobacterium leprae and Mycobacterium tuberculosis.Disruption of gene mg218 of Mycoplasma genitalium through homologous recombination leads to an adherence-deficient phenotype.A novel antioxidant gene from Mycobacterium tuberculosisMolecular biology of drug resistance in Mycobacterium tuberculosisAntibiotic resistance mechanisms in M. tuberculosis: an update.Requirements for nitric oxide generation from isoniazid activation in vitro and inhibition of mycobacterial respiration in vivo.Mapping of Mycobacterium tuberculosis katG promoters and their differential expression in infected macrophages.Transcriptional regulation of furA and katG upon oxidative stress in Mycobacterium smegmatis.Role of superoxide in catalase-peroxidase-mediated isoniazid action against mycobacteria.Isoniazid-induced transient high-level resistance in Mycobacterium tuberculosis.Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoliConstruction and physiological analysis of a Xanthomonas mutant to examine the role of the oxyR gene in oxidant-induced protection against peroxide killing.Oxidative stress response and characterization of the oxyR-ahpC and furA-katG loci in Mycobacterium marinum.A Xanthomonas alkyl hydroperoxide reductase subunit C (ahpC) mutant showed an altered peroxide stress response and complex regulation of the compensatory response of peroxide detoxification enzymes.Oxidative stress increases susceptibility of Mycobacterium tuberculosis to isoniazid.Analysis of the oxyR-ahpC region in isoniazid-resistant and -susceptible Mycobacterium tuberculosis complex organisms recovered from diseased humans and animals in diverse localities.OsmC proteins of Mycobacterium tuberculosis and Mycobacterium smegmatis protect against organic hydroperoxide stress.Multidrug resistance of a porin deletion mutant of Mycobacterium smegmatis.Molecular and physiological effects of mycobacterial oxyR inactivation.Docking studies and network analyses reveal capacity of compounds from Kandelia rheedii to strengthen cellular immunity by interacting with host proteins during tuberculosis infection.Drug resistance evolution of a Mycobacterium tuberculosis strain from a noncompliant patient.Performance assessment of the GenoType MTBDRplus test and DNA sequencing in detection of multidrug-resistant Mycobacterium tuberculosis.Mutation of katG in a clinical isolate of Mycobacterium tuberculosis: effects on catalase-peroxidase for isoniazid activation.
P2860
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P2860
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
@ast
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
@en
type
label
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
@ast
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
@en
prefLabel
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
@ast
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
@en
P2860
P356
P1476
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
@en
P2093
S Dhandayuthapani
P2860
P304
13212-13216
P356
10.1073/PNAS.93.23.13212
P407
P50
P577
1996-11-01T00:00:00Z