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Article

Domain interactions affecting human DNA topoisomerase I catalysis and camptothecin sensitivity.

Molecular pharmacology - 1 Dec 1999

Fiorani P, Amatruda J F, Silvestri A, Butler R H, Bjornsti M A, Benedetti P

Abstract excerpt

DNA topoisomerase I (Top1p) relaxes supercoiled DNA by the formation of a covalent intermediate in which the active site tyrosine is transiently bound to the severed DNA strand. The antineoplastic agent camptothecin (Cpt) specifically targets Top1p and several mutations have been isolated that render the enzyme Cpt resistant. The mutated residues, although located in different regions of the enzyme, may...

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Source

Identifiers

PMID: 10570037
DOI: 10.1124/mol.56.6.1105

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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