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) …

Hairpin pyrrole− imidazole polyamides are synthetic ligands that bind in the minor groove of
DNA with affinities and specificities comparable to those of DNA binding proteins. Three …

Revised Manuscript Received March 8, 1995® abstract: Camptothecins belong to a group of
anticancer agents with a specific mechanism of action: stabilization and trapping of …

The mechanism of cytotoxicity of the camptothecin family of antitumor drugs is thought to be
the consequence of a collision between moving replication forks and camptothecin …

DNA topoisomerase I (top1) is a ubiquitous nuclear enzyme. It is specifically inhibited by
camptothecin, a natural product derived from the bark of the tree Camptotheca acuminata …

We investigated the mode of action of the antitumor drug, camptothecin, by use of a partly
double-stranded suicide DNA substrate which enables uncoupling of the cleavage and …

We and others have clearly demonstrated that a topoisomerase I (Top1) inhibitor, such as
camptothecin (CPT), coupled to a triplex-forming oligonucleotide (TFO) through a suitable …

The interaction of DNA topoisomerase I (topo I) with a set of single-and double-stranded
oligonucleotides containing 5–27 mononucleotides was investigated. All single-and double …

Using the X-ray crystal structure of the human topoisomerase I (TOP1)− DNA cleavable
complex, we have developed a general model for the ternary drug− DNA− TOP1 cleavable …

A recent X-ray crystallographic analysis of the binding of a water soluble camptothecin
analogue to the human topoisomerase I–DNA covalent binary complex has suggested the …