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

Substitutions in Spodoptera exigua topoisomerase I modulate its relaxation activity and camptothecin sensitivity.

Pest management science - 1 Jun 2017

Zhang Pei, Zhang Lan, Zhang Yanning, Mao Liangang, Jiang Hongyun

Abstract excerpt

BACKGROUND: Topoisomerase I (Top I) is referred as the cellular target of the camptothecins (CPTs) which are now being explored as potential pesticides for insect control. Three amino acid substitutions, including L530P, A653T and S729T, in Top Is of insects were found in our previous studies. In order to investigate the effect of these three substitutions, a comparative analysis was conducted between the...

Read the complete abstract on PubMed

Topics

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

Share to Camptothecin
Share to DNA Topoisomerases, Type I

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Insect Proteins

Share to Insecticides

Share to Mutation

Share to Polymorphism, Genetic

Share to Spodoptera

Source

Identifiers

PMID: 27643798
DOI: 10.1002/ps.4440

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

Substitutions in Spodoptera exigua topoisomerase I modulate its relaxation activity and camptothecin sensitivity.PMID 27643798Read ↗

Structural insight of DNA topoisomerases I from camptothecin-producing plants revealed by molecular dynamics simulations.Semantic proximity Read ↗

Analysis of a core domain in Drosophila DNA topoisomerase II. Targeting of an antitumor agent ICRF-159.Semantic proximity Read ↗

Directed evolution to increase camptothecin sensitivity of human DNA topoisomerase I.Semantic proximity Read ↗

Binding Mode and Molecular Mechanism of the Two-Component Histidine Kinase Bos1 of Botrytis cinerea to Fludioxonil and Iprodione.Semantic proximity Read ↗

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

Mutation of Gly721 alters DNA topoisomerase I active site architecture and sensitivity to camptothecin.Semantic proximity Read ↗

[The structure and mechanism of the action of type-IB DNA topoisomerases].Semantic proximity Read ↗

Targeting DNA Topoisomerase II in Antifungal ChemotherapySemantic proximity Read ↗

A single mutation in the 729 residue modulates human DNA topoisomerase IB DNA binding and drug resistance.Semantic proximity Read ↗

Mutation adjacent to the active site tyrosine can enhance DNA cleavage and cell killing by the TOPRIM Gly to Ser mutant of bacterial topoisomerase I.Semantic proximity Read ↗

Mutations in topoisomerase I as a self-resistance mechanism coevolved with the production of the anticancer alkaloid camptothecin in plants.Semantic proximity Read ↗

Molecular principle of topotecan resistance by topoisomerase I mutations through molecular modeling approaches.Semantic proximity Read ↗

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