Results 231 to 240 of about 38,912 (254)

Fluoroquinolone-Gyrase-DNA Cleaved Complexes

2017
The quinolones are potent antibacterials that act by forming complexes with DNA and either gyrase or topoisomerase IV. These ternary complexes, called cleaved complexes because the DNA moiety is broken, block replication, transcription, and bacterial growth.
Gan, Luan, Karl, Drlica
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DNA Gyrase and the Supercoiling of DNA

Science, 1980
Negative supercoiling of bacterial DNA by DNA gyrase influences all metabolic processes involving DNA and is essential for replication. Gyrase supercoils DNA by a mechanism called sign inversion, whereby a positive supercoil is directly inverted to a negative one by passing a DNA segment through a transient double-strand break.
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DNA linking potential generated by gyrase

European Journal of Biochemistry, 1990
Whether or not DNA gyrase can supercoil DNA so that alternative structures will arise in it is the major question of this work. We have shown gyrase to produce in pAO3 DNA a superhelix density sufficient for cruciform formation. However, the transition does not take place because of too slow kinetics.
S A, Kozyavkin, A I, Slesarev, S R, Malkhosyan, I G, Panyutin   +3 more
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Mycoplasma pneumoniae DNA gyrase genes

Molecular Microbiology, 1990
SummaryWe have identified a clone from a λEMBL3 library containing a 19kb insert of Mycoplasma pneumoniae DNA which includes the genes that encode both subunits of DNA gyrase. The gyrB gene and the 5’end of the gyrA gene have been subcloned into M13. The gryB gene is 1953bp in length and overlaps the gryA gene by a single base.
S D, Colman, P C, Hu, K F, Bott
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Bacterial death by DNA gyrase poisoning

Trends in Microbiology, 1998
DNA gyrase is an essential topoisomerase that is found in all bacteria and is the target of potent antibiotics, such as the quinolones. By creating DNA lesions and inducing the bacterial SOS response, these drugs are not only highly cytotoxic but also mutagenic.
Couturier, Martine, Bahassi, El Mustapha, Van Melderen, Laurence   +2 more
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Triple Helix Formation Inhibits DNA Gyrase Activity

Antisense and Nucleic Acid Drug Development, 1999
The goal of this work was to examine the effect of triple helix-forming oligonucleotides on a gyrase target region and on the activity of the enzyme. Using melting temperature measurements and gel mobility shift analysis, it was found that modified oligonucleotides can form a triple helix along the 29-nucleotide region of a 32-bp duplex representing ...
H, Simon, I, Förtsch, G, Burckhardt, A, Gabrielyan, E, Birch-Hirschfeld, A, Stelzner, I, Prévot-Halter, C, Leumann, C, Zimmer   +8 more
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DNA gyrase (Topoisomerase II) from Pseudomonasaeruginosa

Biochemical and Biophysical Research Communications, 1983
DNA gyrase (Topoisomerase II) has been purified from Pseudomonas aeruginosa strain PAO. This enzyme is inhibited by novobiocin and nalidixic acid. DNA gyrase from P. aeruginosa is resistant to a much higher level of nalidixic acid than is Escherichia coli DNA gyrase. This increased level of resistance may explain, at least in part, the higher levels of
R V, Miller, T R, Scurlock
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Clinical utility of DNA gyrase inhibitors

Pharmacology & Therapeutics, 1989
Quinolone antibiotics provide potentially important therapy for many infections. These DNA gyrase inhibitors are established as excellent therapy of urinary infections and of diarrheal disease. As reviewed, the compounds have important use in respiratory, skin-structure and bone infections.
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DNA gyrase as a drug target

Trends in Microbiology, 1997
DNA gyrase is a remarkable enzyme, catalysing the seemingly complex reaction of DNA supercoiling. As gyrase is essential in prokaryotes, it is a good target for antibacterial agents. These agents have diverse chemical structures and interact with gyrase in a variety of ways.
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DNA Supercoiling Catalyzed by Bacterial Gyrase

DNA gyrase is an essential type II topoisomerase that is conserved across bacteria species and has an essential function of resolving overwound (positive supercoiled) DNA and introducing negative supercoils into relaxed DNA. The overall catalytic activity of gyrase can be determined using in vitro assays utilizing purified enzyme subunits and a DNA ...
Samika, Joshi, Neil, Osheroff
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