ArticleAntimicrobial agents and chemotherapy2008
Mutagenesis in the alpha3alpha4 GyrA helix and in the Toprim domain of GyrB refines the contribution of Mycobacterium tuberculosis DNA gyrase to intrinsic resistance to quinolones.
Article in Antimicrobial agents and chemotherapy, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Systematic review of allelic exchange experiments aimed at identifying mutations that confer drug resistance in Mycobacterium tuberculosis.The Journal of antimicrobial chemotherapy · 2014Pooled it
- Exploring antibiotic resistance mechanisms inFrontiers in microbiology · 2024Review
- Article
- Evolution of Antibiotic Resistance in Surrogates ofFrontiers in microbiology · 2020Article
- Silver ciprofloxacin (CIPAG): a successful combination of chemically modified antibiotic in inorganic-organic hybrid.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Functional Characterization of the DNA Gyrases in Fluoroquinolone-Resistant Mutants of Francisella novicida.Antimicrobial agents and chemotherapy · 2017Article
- Crystal structure and stability of gyrase-fluoroquinolone cleaved complexes from Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Specific gyrA gene mutations predict poor treatment outcome in MDR-TB.The Journal of antimicrobial chemotherapy · 2016Article
- Evolution of drug resistance in tuberculosis: recent progress and implications for diagnosis and therapy.Drugs · 2014Review
- Structural insights into the quinolone resistance mechanism of Mycobacterium tuberculosis DNA gyrase.PloS one · 2010Article
- The pentapeptide repeat proteins MfpAMt and QnrB4 exhibit opposite effects on DNA gyrase catalytic reactions and on the ternary gyrase-DNA-quinolone complex.Journal of bacteriology · 2009Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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Abstract
The replacement of M74 in GyrA, A83 in GyrA, and R447 in GyrB of Mycobacterium tuberculosis gyrase by their Escherichia coli homologs resulted in active enzymes as quinolone susceptible as the E. coli gyrase. This demonstrates that the primary structure of gyrase determines intrinsic quinolone resistance and was supported by a three-dimensional model of N-terminal GyrA.
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