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

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

Nucleic acids research - 1 Oct 2008

Chillemi Giovanni, D'Annessa Ilda, Fiorani Paola, Losasso Carmen, Benedetti Piero, Desideri Alessandro

Abstract excerpt

The role of Thr729 in modulating the enzymatic function of human topoisomerase I has been characterized by molecular dynamics (MD) simulation. In detail, the structural-dynamical behaviour of the Thr729Lys and the Thr729Pro mutants have been characterized because of their in vivo and in vitro functional properties evidenced in the accompanying paper. Both mutants can bind to the DNA substrate and are...

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 DNA Topoisomerases, Type I

Share to Enzyme Inhibitors

Share to Lysine

Share to Proline

Share to Threonine

Share to Topoisomerase I Inhibitors

Source

Open in PubMed Open full text

Identifiers

PMID: 18765473
DOI: 10.1093/nar/gkn558
PMCID: PMC2553568

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

Thr729 in human topoisomerase I modulates anti-cancer drug resistance by altering protein domain communications as suggested by molecular dynamics simulations.PMID 18765473Read ↗

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

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

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

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

Computational analysis of Amsacrine resistance in human topoisomerase II alpha mutants (R487K and E571K) using homology modeling, docking and all-atom molecular dynamics simulation in explicit solvent.Semantic proximity Read ↗

Investigating Conformational Dynamics and Allostery in the p53 DNA-Binding Domain Using Molecular Simulations.Semantic proximity Read ↗

Effect on DNA relaxation of the single Thr718Ala mutation in human topoisomerase I: a functional and molecular dynamics study.Semantic proximity Read ↗

Evidence of the crucial role of the linker domain on the catalytic activity of human topoisomerase I by experimental and simulative characterization of the Lys681Ala mutant.Semantic proximity Read ↗

Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I.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 ↗

Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA.Semantic proximity Read ↗

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