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

Altered Formation of Topotecan-Stabilized Topoisomerase I-DNA Adducts in Human Leukemia Cells

15 Mar 1997

Abstract excerpt

Topotecan (TPT) is a topoisomerase I (topo I) poison that has shown promising antineoplastic activity in solid tumors and acute leukemia. In the present study, a band depletion assay was used to evaluate the ability of TPT to stabilize topo I-DNA adducts in human leukemia cell lines and in clinical leukemia samples ex vivo. This assay showed that 50% of the cellular topo I in HL-60 human myelomonocytic leukemia...

Read the complete abstract on PubMed

Topics

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

Share to Cancer therapeutics and mechanisms
Share to Lung Cancer Research Studies
Share to Neutropenia and Cancer Infections

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 9058732
DOI: 10.1182/blood.v89.6.2098

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Altered Formation of Topotecan-Stabilized Topoisomerase I-DNA Adducts in Human Leukemia CellsPMID 9058732Read ↗

The Current Status of Camptothecin Analogues as Antitumor AgentsSemantic proximity Read ↗

Activity of Topotecan, a New Topoisomerase I Inhibitor, Against Human Tumor Colony-Forming Units In VitroSemantic proximity Read ↗

Sequential topoisomerase targeting and analysis of mechanisms of resistance to topotecan in patients with acute myelogenous leukemia.Semantic proximity Read ↗

Topotecan-triggered degradation of topoisomerase I is p53-dependent and impacts cell survival.Semantic proximity Read ↗

The mechanism of topoisomerase I poisoning by a camptothecin analog.Semantic proximity Read ↗

The Efficacy of Topoisomerase II-Targeted Anticancer Agents Reflects the Persistence of Drug-Induced Cleavage Complexes in CellsSemantic proximity Read ↗

DNA Damage and Cell Killing by Camptothecin and Its Derivative in Human Leukemia HL‐60 CellsSemantic proximity Read ↗

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

Teniposide-resistant CEM cells, which express mutant DNA topoisomerase II alpha, when treated with non-complex-stabilizing inhibitors of the enzyme, display no cross-resistance and reveal aberrant functions of the mutant enzyme.Semantic proximity Read ↗

Altered stability of etoposide-induced topoisomerase II-DNA complexes in resistant human leukaemia K562 cellsSemantic proximity Read ↗

Attenuation of drug-stimulated topoisomerase II-DNA cleavable complex formation in wild-type HL-60 cells treated with an intracellular calcium buffer is correlated with decreased cytotoxicity and site-specific hypophosphorylation of topoisomerase IIalpha.Semantic proximity Read ↗

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

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