Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A new class of antibacterials, the imidazopyrazinones, reveal structural transitions involved in DNA gyrase poisoning and mechanisms of resistance.

Nucleic acids research - 4 May 2018

Germe Thomas, Vörös Judit, Jeannot Frederic, Taillier Thomas, Stavenger Robert A, Bacqué Eric, Maxwell Anthony, Bax Benjamin D

Abstract excerpt

Imidazopyrazinones (IPYs) are a new class of compounds that target bacterial topoisomerases as a basis for their antibacterial activity. We have characterized the mechanism of these compounds through structural/mechanistic studies showing they bind and stabilize a cleavage complex between DNA gyrase and DNA ('poisoning') in an analogous fashion to fluoroquinolones, but without the requirement for the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Ciprofloxacin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Cleavage

Share to DNA Gyrase

Share to Fluoroquinolones

Share to Magnesium

Share to Pyrazines

Share to Topoisomerase II Inhibitors

Source

Open in PubMed Open full text

Identifiers

PMID: 29538767
DOI: 10.1093/nar/gky181
PMCID: PMC5934680

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A new class of antibacterials, the imidazopyrazinones, reveal structural transitions involved in DNA gyrase poisoning and mechanisms of resistance.PMID 29538767Read ↗

Drug Interactions with <i>Bacillus anthracis</i> Topoisomerase IV: Biochemical Basis for Quinolone Action and ResistanceSemantic proximity Read ↗

Probing the differential interactions of quinazolinedione PD 0305970 and quinolones with gyrase and topoisomerase IV.Semantic proximity Read ↗

Discovery of isoquinoline sulfonamides as allosteric gyrase inhibitors with activity against fluoroquinolone-resistant bacteriaSemantic proximity Read ↗

Overcoming target-mediated quinolone resistance in topoisomerase IV by introducing metal-ion-independent drug-enzyme interactions.Semantic proximity Read ↗

Novel N-linked aminopiperidine-based gyrase inhibitors with improved hERG and in vivo efficacy against Mycobacterium tuberculosis.Semantic proximity Read ↗

Novel Dual-Targeting Benzimidazole Urea Inhibitors of DNA Gyrase and Topoisomerase IV Possessing Potent Antibacterial Activity: Intelligent Design and Evolution through the Judicious Use of Structure-Guided Design and Stucture−Activity RelationshipsSemantic proximity Read ↗

Bacterial topoisomerase I as a target for discovery of antibacterial compounds.Semantic proximity Read ↗

Target-Mediated Fluoroquinolone Resistance in Neisseria gonorrhoeae : Actions of Ciprofloxacin against Gyrase and Topoisomerase IVSemantic proximity Read ↗

A 2.8 Å Structure of Zoliflodacin in a DNA Cleavage Complex with Staphylococcus aureus DNA GyraseSemantic proximity Read ↗

Interactions between Zoliflodacin and Neisseria gonorrhoeae Gyrase and Topoisomerase IV: Enzymological Basis for Cellular TargetingSemantic proximity Read ↗

Type II Topoisomerases as Targets for Quinolone Antibacterials Turning Dr. Jekyll into Mr. HydeSemantic proximity Read ↗

Topoisomerase IV-quinolone interactions are mediated through a water-metal ion bridge: mechanistic basis of quinolone resistance.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.