ArticleProceedings of the National Academy of Sciences of the United States of America1996
Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
46 citing papers in PubMed, 121 citations in OpenAlex.
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- Proteomic insights into mycobacterial responses to elevated riboflavin reveal a role for flavin-sequestering proteins in flavin homeostasis.Frontiers in tuberculosis · 2025Article
- Drug-resistant tuberculosis: a persistent global health concern.Nature reviews. Microbiology · 2024Review
- Molecular modeling, simulation and docking of Rv1250 protein fromFrontiers in bioinformatics · 2023Article
- An autonomous portable platform for universal chemical synthesis.Nature chemistry · 2022Article
- Heterologous Expression ofAntimicrobial agents and chemotherapy · 2021Article
- Accuracy of a reverse dot blot hybridization assay for simultaneous detection of the resistance of four anti-tuberculosis drugs in Mycobacterium tuberculosis isolated from China.Infectious diseases of poverty · 2020Article
- Validation of Novel Mycobacterium tuberculosis Isoniazid Resistance Mutations Not Detectable by Common Molecular Tests.Antimicrobial agents and chemotherapy · 2018Article
- Antibiotic resistance mechanisms in M. tuberculosis: an update.Archives of toxicology · 2016Review
- Inactivation of the organic hydroperoxide stress resistance regulator OhrR enhances resistance to oxidative stress and isoniazid in Mycobacterium smegmatis.Journal of bacteriology · 2015Article
- Molecular biology of drug resistance in Mycobacterium tuberculosis.Current topics in microbiology and immunology · 2013Review
- OsmC proteins of Mycobacterium tuberculosis and Mycobacterium smegmatis protect against organic hydroperoxide stress.Tuberculosis (Edinburgh, Scotland) · 2011Article
- Performance assessment of the GenoType MTBDRplus test and DNA sequencing in detection of multidrug-resistant Mycobacterium tuberculosis.Journal of clinical microbiology · 2009Article
- Molecular and physiological effects of mycobacterial oxyR inactivation.Journal of bacteriology · 2006Article
- Drug resistance evolution of a Mycobacterium tuberculosis strain from a noncompliant patient.Journal of clinical microbiology · 2005Article
- Novel roles of ohrR-ohr in Xanthomonas sensing, metabolism, and physiological adaptive response to lipid hydroperoxide.Journal of bacteriology · 2005Article
- Multidrug resistance of a porin deletion mutant of Mycobacterium smegmatis.Antimicrobial agents and chemotherapy · 2004Article
- Requirements for nitric oxide generation from isoniazid activation in vitro and inhibition of mycobacterial respiration in vivo.Journal of bacteriology · 2004Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The exceptional sensitivity of Mycobacterium tuberculosis to isonicotinic acid hydrazide (INH) lacks satisfactory definition. M. tuberculosis is a natural mutant in oxyR, a central regulator of peroxide stress response. The ahpC gene, which encodes a critical subunit of alkyl hydroperoxide reductase, is one of the targets usually controlled by oxyR in bacteria. Unlike in mycobacterial species less susceptible to INH, the expression of ahpC was below detection limits at the protein level in INH-sensitive M. tuberculosis and Mycobacterium bovis strains. In contrast, AhpC was detected in several series of isogenic INH-resistant (INHr) derivatives. In a demonstration of the critical role of ahpC in sensitivity to INH, insertional inactivation of ahpC on the chromosome of Mycobacterium smegmatis, a species naturally insensitive to INH, dramatically increased its susceptibility to this compound. These findings suggest that AhpC counteracts the action of INH and that the levels of its expression may govern the intrinsic susceptibility of mycobacteria to this front-line antituberculosis drug.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.