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Exploiting bacterial DNA gyrase as a drug target: current state and perspectives.

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TLDR
Known gyrase-specific drugs and toxins are reviewed and the prospects for developing new antibacterials targeted to this enzyme are assessed.
Abstract
DNA gyrase is a type II topoisomerase that can introduce negative supercoils into DNA at the expense of ATP hydrolysis. It is essential in all bacteria but absent from higher eukaryotes, making it an attractive target for antibacterials. The fluoroquinolones are examples of very successful gyrase-targeted drugs, but the rise in bacterial resistance to these agents means that we not only need to seek new compounds, but also new modes of inhibition of this enzyme. We review known gyrase-specific drugs and toxins and assess the prospects for developing new antibacterials targeted to this enzyme.

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Journal ArticleDOI

Design, synthesis, biological evaluation of substituted benzofurans as DNA gyraseB inhibitors of Mycobacterium tuberculosis.

TL;DR: The discovery and optimization of ethyl 5-(piperazin-1-yl) benzofuran-2-carboxylate series of mycobacterial DNA gyraseB inhibitors, selected from Birla Institute of Technology and Science (BITS) database chemical library of about 3000 molecules are presented.
Journal ArticleDOI

Challenges in the development of drugs for the treatment of tuberculosis

TL;DR: The challenges for the development of novel drugs with potent bacteriostatic or bactericidal activity, which reduce the minimum time required to cure tuberculosis infection are highlighted.
Journal ArticleDOI

Allicin, a natural antimicrobial defence substance from garlic, inhibits DNA gyrase activity in bacteria.

TL;DR: Results suggest that GyrA was protected from oxidation in vivo in the allicin-tolerant Pf AR-1 background, rather than the PfAR-1 Gyr A subunit being intrinsically less susceptible to oxidation by allicIn than the Pratincole gyrase subunit.
Journal ArticleDOI

NBTI 5463 Is a Novel Bacterial Type II Topoisomerase Inhibitor with Activity against Gram-Negative Bacteria and In Vivo Efficacy

TL;DR: NBTI 5463 demonstrated promising activity against a broad range of Gram-negative pathogens, and was a potent inhibitor of both DNA gyrase and E. coli topoisomerase IV catalytic activities in studies with P. aeruginosa.
Journal ArticleDOI

Ciprofloxacin is an inhibitor of the Mcm2-7 replicative helicase.

TL;DR: The results indicate that ciprofloxacin targets Mcm2-7 in vitro, and support the feasibility of developing specific quinolone-based inhibitors of Mcm 2-7 for therapeutic and experimental applications.
References
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Journal ArticleDOI

DNA topoisomerases: structure, function, and mechanism.

TL;DR: Surprisingly, despite little or no sequence homology, both type IA and type IIA topoisomerases from prokaryotes and the typeIIA enzymes from eukaryotes share structural folds that appear to reflect functional motifs within critical regions of the enzymes.
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A Common Mechanism of Cellular Death Induced by Bactericidal Antibiotics

TL;DR: The results suggest that all three major classes of bactericidal drugs can be potentiated by targeting bacterial systems that remediate hydroxyl radical damage, including proteins involved in triggering the DNA damage response, e.g., RecA.
Journal ArticleDOI

How antibiotics kill bacteria: from targets to networks

TL;DR: The multilayered effects of drug–target interactions, including the essential cellular processes that are inhibited by bactericidal antibiotics and the associated cellular response mechanisms that contribute to killing are discussed.
Journal ArticleDOI

DNA topoisomerases and their poisoning by anticancer and antibacterial drugs.

TL;DR: This review focuses on the molecular and biochemical characteristics of topoisomerases and their inhibitors and discusses the common mechanism of action ofTopoisomerase poisons by interfacial inhibition and trapping of topisomerase cleavage complexes.
Journal ArticleDOI

Quinolone resistance from a transferable plasmid

TL;DR: Although resistance was low in wild-type strains, higher levels of quinolone resistance arose readily by mutation, suggesting that a multiresistance plasmid can speed the development and spread of resistance to these valuable antimicrobial agents.
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