Camptothecins as probes of the microenvironments of topoisomerase I - DNA complexes

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

By uncoupling the cleavage and ligation reactions of DNA oligonucleotides mediated by topoisomerase I, it has been possible to demonstrate modification of DNA oligonucleotide structure by the enzyme. These modifications indicate an unusual flexibility inherent in the behavior of topoisomerase I and may reflect some of the cellular roles played by the enzyme. The ability of individual camptothecin analogues to inhibit these modification processes differentially provides insight into the relative nature of the microenvironments present. To the extent that these enzyme-mediated structural modifications do constitute models of cellular roles for the enzyme, the observed differential inhibition also provides a potential strategy for assessing the function and importance of such modifications.

Original languageEnglish (US)
Pages (from-to)76-91
Number of pages16
JournalAnnals of the New York Academy of Sciences
Volume922
StatePublished - Jan 1 2000
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • History and Philosophy of Science

Cite this