Research paperMapping of DNA topoisomerase II poisons (etoposide, clerocidin) and catalytic inhibitors (aclarubicin, ICRF-187) to four distinct steps in the topoisomerase II catalytic cycle☆
References (30)
- et al.
Mechanistic studies of amsacrine-resistant derivatives of DNA topoisomerase II—Implications in resistance to multiple antitumour drugs targeting the enzyme
J Biol Chem
(1994) - et al.
Different modes of anthracycline interaction with topoisomerase II: Separate structures critical for DNA-cleavage, and for overcoming topoisomerase II-related drug resistance
Biochem Pharmacol
(1993) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Anal Biochem
(1976)- et al.
H2O2 as a DNA fragmenting agent in the alkaline elution interstrand crosslinking and DNA-protein crosslinking assays
Analyt Biochem
(1988) - et al.
Characterization of an amsacrine-resistant line of human leukemia cells
J Biol Chem
(1989) - et al.
Mode of action of topoisomerase-II-targeting agents at a specific DNA sequence. Uncoupling the DNA binding, cleavage and religation events
J Mol Biol
(1992) - et al.
Antagonistic effect of the cardioprotector (+)-1, 2,-bis(3-5-dioxopiperazinyl-1-yl)propane (ICRF-187) on DNA breaks and cytotoxicity induced by the topoisomerase II directed drugs daunorubicin and etoposide (VP-16)
Biochem Pharmacol
(1993) - et al.
Inhibition of epipodophyllotoxin cytotoxicity by interference with topoisomerase-mediated DNA-cleavage
Biochem Pharmacol
(1985) - et al.
Role of DNA intercalation in the inhibition of purified mouse leukemia (L1210) DNA topoisomerase II by 9-aminoacridines
Biochem Pharmocol
(1987) - et al.
Radiotherapeutic enhancement by razoxane
Cancer Treat Rev
(1991)
DNA transport by a type II DNA topoisomerase: Evidence in favor of a two-gate mechanism
Cell
DNA topoisomerases—essential enzymes and lethal targets
Annu Rev Pharmacol Toxicol
Altered DNA topoisomerase II activity in Chinese hamster cells resistant to topoisomerase II inhibitors
Cancer Res
Altered catalytic activity of and DNA cleavage by DNA topoisomerase II from human leukemic cells selected for resistance to VM-26
Biochemistry
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
Cancer Res
Cited by (101)
Bacterial terpenome
2021, Natural Product ReportsDNA Topoisomerase IIα contributes to the early steps of adipogenesis in 3T3-L1 cells
2016, Cellular SignallingCitation Excerpt :In our study, we show that Topo II inhibition with the addition of ICRF-187 caused a higher percentage of cells displaying this pattern, perhaps due to the mode of action of the inhibitor. ICRF-187 is a member of the bisdioxopiperazines class of Topo II catalytic inhibitors, which are known to trap Topo II on DNA as a protein-DNA clamp [43–45]. DNA-trapped Topo IIα may indicate the sites of Topo IIα activity, which are particularly noticeable in heterochromatin, consistent with a study in human cells by Agostinho et al. [47].
Design, synthesis, topoisomerase I & II inhibitory activity, antiproliferative activity, and structure-activity relationship study of pyrazoline derivatives: An ATP-competitive human topoisomerase IIα catalytic inhibitor
2016, Bioorganic and Medicinal ChemistryCitation Excerpt :We further performed the cleavage complex assay to investigate compound 5d as a topo II catalytic inhibitor. Topo II poisons act by stabilizing transiently-formed topo II enzyme–DNA cleavage complex leading to the formation of linear DNA.74 In cleavage complex assay, initially the relaxation of the pBR322 plasmid was allowed by the addition of topo IIα and then compound 5d was treated.
Food-borne topoisomerase inhibitors: Risk or benefit
2014, Advances in Molecular ToxicologyEffects of mndpdp and icrf-187 on doxorubicin-induced cardiotoxicity and anticancer activity
2012, Translational Oncology
- ☆
The study was supported by the Danish Cancer Society, the E. Dunielsen and Wife Foundation, the Danish Cancer Research Foundation, the Georg and Ellen Bjwkner Foundation, the Soren and Helene Hempels Legacy, and the Nooo-Nordisk Foundation.