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

Effects of mutations in the F361 to R364 region of topoisomerase I (Topo I), in the presence and absence of 9-aminocamptothecin, on the Topo I-DNA interaction.

Anti-cancer drugs - 1 Aug 1999

Pond C D, Li X G, Rubin E H, Barrows L R

Abstract excerpt

Steady-state levels and rates of DNA binding and release of wild-type and mutant topoisomerase I (Topo I) proteins were quantified by surface plasmon resonance analysis. The proteins were constructed and expressed as GST fusion proteins. The Topo I mutations analyzed were F361S, R362L and R364G, all altering a highly conserved region of wild-type eukaryotic Topo I. The R362L and R364G mutations resulted in much...

Read the complete abstract on PubMed

Topics

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

Share to Antineoplastic Agents
Share to Camptothecin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to DNA Topoisomerases, Type I

Share to Mutation

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 10507314
DOI: 10.1097/00001813-199908000-00004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Effects of mutations in the F361 to R364 region of topoisomerase I (Topo I), in the presence and absence of 9-aminocamptothecin, on the Topo I-DNA interaction.PMID 10507314Read ↗

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

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

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

Cell cycle-coupled variation in topoisomerase IIalpha mRNA is regulated by the 3'-untranslated region. Possible role of redox-sensitive protein binding in mRNA accumulation.Semantic proximity Read ↗

Interdomain communication in DNA topoisomerase II. DNA binding and enzyme activation.Semantic proximity Read ↗

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

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

Quinone-induced enhancement of DNA cleavage by human topoisomerase IIalpha: adduction of cysteine residues 392 and 405.Semantic proximity Read ↗

Retroviral expression of a mutant (Gly-533) human DNA topoisomerase I cDNA confers a dominant form of camptothecin resistance.Semantic proximity Read ↗

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

Analysis of Etoposide Binding to Subdomains of Human DNA Topoisomerase II<i>α</i> in the Absence of DNASemantic proximity Read ↗

Increased camptothecin toxicity induced in mammalian cells expressing Saccharomyces cerevisiae DNA topoisomerase I.Semantic proximity Read ↗

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