Cargando…
Suppression of gyrase-mediated resistance by C7 aryl fluoroquinolones
Fluoroquinolones form drug-topoisomerase-DNA complexes that rapidly block transcription and replication. Crystallographic and biochemical studies show that quinolone binding involves a water/metal-ion bridge between the quinolone C3-C4 keto-acid and amino acids in helix-4 of the target proteins, Gyr...
Autores principales: | Malik, Muhammad, Mustaev, Arkady, Schwanz, Heidi A., Luan, Gan, Shah, Nirali, Oppegard, Lisa M., de Souza, Ernane C., Hiasa, Hiroshi, Zhao, Xilin, Kerns, Robert J., Drlica, Karl |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4838383/ https://www.ncbi.nlm.nih.gov/pubmed/26984528 http://dx.doi.org/10.1093/nar/gkw161 |
Ejemplares similares
-
Bypassing Fluoroquinolone Resistance with Quinazolinediones:
Studies of Drug–Gyrase–DNA Complexes Having Implications
for Drug Design
por: Drlica, Karl, et al.
Publicado: (2014) -
Activities of gyrase and topoisomerase IV on positively supercoiled DNA
por: Ashley, Rachel E., et al.
Publicado: (2017) -
Insights into RNA polymerase catalysis and adaptive evolution gained from mutational analysis of a locus conferring rifampicin resistance
por: Yurieva, Olga, et al.
Publicado: (2017) -
Mutations compensating for the fitness cost of rifampicin resistance in Escherichia coli exert pleiotropic effect on RNA polymerase catalysis
por: Kurepina, Natalia, et al.
Publicado: (2022) -
The role of Ca(2+) in the activity of Mycobacterium tuberculosis DNA gyrase
por: Karkare, Shantanu, et al.
Publicado: (2012)