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- W137201793 abstract "As noted elsewhere in this book, the locus of action of camptothecin (CPT) (1) (Fig. 1) as an antitumor agent involves the noncovalent binding of this agent to the covalent binary complex formed between topoisomerase I (TOP-I) and DNA (Fig. 2) (1). Although the equilibrium between free enzyme and the enzyme-DNA binary complex normally lies far toward free enzyme and DNA, in the presence of CPT, the equilibrium is rapidly displaced toward ternary complex (2). At this level, the action of CPT on TOP-I function is entirely analogous to those of several agents that inhibit the function of topoisomerase II, including 4-(9-acridinylamino)-N-(methanesulfonyl)-m-anisidine (m-AMSA), etoposide, and teniposide (3)." @default.
- W137201793 created "2016-06-24" @default.
- W137201793 creator A5006249781 @default.
- W137201793 date "2005-01-01" @default.
- W137201793 modified "2023-09-23" @default.
- W137201793 title "Inhibitors of Topoisomerase I Function" @default.
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- W137201793 doi "https://doi.org/10.1385/1-59259-866-8:039" @default.
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