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 single mutation in the 729 residue modulates human DNA topoisomerase IB DNA binding and drug resistance.

Nucleic acids research - 1 Oct 2008

Losasso Carmen, Cretaio Erica, Fiorani Paola, D'Annessa Ilda, Chillemi Giovanni, Benedetti Piero

Abstract excerpt

Human DNA topoisomerase I (hTop1p) catalyzes the relaxation of supercoiled DNA and constitutes the cellular target of the antitumor drug camptothecin (CPT). The X-ray crystal structure of the enzyme covalently joined to DNA and bound to the CPT analog Topotecan suggests that there are two classes of mutations that can produce a CPT-resistant enzyme. The first class includes changes in residues that directly...

Read the complete abstract on PubMed

Topics

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

Share to Antineoplastic Agents, Phytogenic
Share to Camptothecin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to DNA Topoisomerases, Type I

Share to Drug Resistance, Neoplasm

Share to Enzyme Inhibitors

Share to Threonine

Share to Topoisomerase I Inhibitors

Source

Open in PubMed Open full text

Identifiers

PMID: 18772225
DOI: 10.1093/nar/gkn557
PMCID: PMC2553582

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A single mutation in the 729 residue modulates human DNA topoisomerase IB DNA binding and drug resistance.PMID 18772225Read ↗

Mechanisms of camptothecin resistance by human topoisomerase I mutations.Semantic proximity Read ↗

Thr729 in human topoisomerase I modulates anti-cancer drug resistance by altering protein domain communications as suggested by molecular dynamics simulations.Semantic proximity Read ↗

Domain interactions affecting human DNA topoisomerase I catalysis and camptothecin sensitivity.Semantic proximity Read ↗

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

Computational Study of Anticancer Drug Resistance Caused by 10 Topisomerase I Mutations, Including 7 Camptothecin Analogs and Lucanthone.Semantic proximity Read ↗

Structural and Dynamical Effects Induced by the Anticancer Drug Topotecan on the Human Topoisomerase I – DNA ComplexSemantic proximity Read ↗

Intragenic suppressors of mutant DNA topoisomerase I-induced lethality diminish enzyme binding of DNA.Semantic proximity Read ↗

Camptothecin resistance from a single mutation changing glycine 363 of human DNA topoisomerase I to cysteine.Semantic proximity Read ↗

New Topoisomerase I mutations are associated with resistance to camptothecin.Semantic proximity Read ↗

CDC45 and DPB11 are required for processive DNA replication and resistance to DNA topoisomerase I-mediated DNA damage.Semantic proximity Read ↗

Involvement of amino acids 361 to 364 of human topoisomerase I in camptothecin resistance and enzyme catalysis.Semantic proximity Read ↗

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

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