Topoisomerase I (Top1) activities are sensitive to various endogenous base modifications,
and anticancer drugs including the natural alkaloid camptothecin. Here, we show that triple …

The activity of DNA topoisomerase I (Top1), an enzyme that regulates DNA topology, is
impacted by DNA structure alterations and by the anticancer alkaloid camptothecin (CPT) …

DNA topoisomerase I (Top1) is a nuclear enzyme that plays a crucial role in the removal of
DNA supercoiling associated with replication and transcription. It is also the target of the …

Topoisomerase I (topo I) is a ubiquitous DNA-cleaving enzyme and an important therapeutic
target in cancer chemotherapy. Camptothecins (CPTs) reversibly trap topo I in covalent …

Human type II topoisomerase (Top2) isoforms, hTop2α and hTop2β, are targeted by some of
the most successful anticancer drugs. These drugs induce Top2-mediated DNA cleavage to …

Human topoisomerase I (top1) is an important target for anti-cancer drugs, which include
camptothecin (CPT) and its derivatives. To elucidate top1 inhibition in vitro, we made a …

DNA topoisomerase I (Top1p) catalyzes the relaxation of supercoiled DNA via a concerted
mechanism of DNA strand cleavage and religation. Top1p is the cellular target of the anti …

Aggressive malignancies are characterized by relatively uncontrolled cell proliferation
making them especially reliant on topoisomerase enzymes to enable high rates of DNA …

The inhibition of DNA topoisomerase I (Top1) has proven to be a successful approach in the
design of anticancer agents. However, despite the clinical successes of the camptothecin …

Type II topoisomerases (Top2s) alter DNA topology via the formation of an enzyme–DNA
adduct termed cleavage complex, which harbors a transient double-strand break in one …