Publications by authors named "MaryJean Pendleton"
Article Synopsis
- Coordination between the N-terminal gate and the catalytic core of topoisomerase II is essential for effectively manipulating DNA during its catalytic cycle.
- Research on human topoisomerase IIα showed that the catalytic core can differentiate between negatively and positively supercoiled DNA, but struggles with substrates lacking transport segments.
- Distinctions between interfacial and covalent poisons like etoposide quinone highlight how these components work together, with the catalytic core sensing DNA's supercoil handedness and the N-terminal gate essential for transport and the activity of covalent drugs.
Type II topoisomerases are essential enzymes that modulate DNA under- and overwinding, knotting, and tangling. Beyond their critical physiological functions, these enzymes are the targets for some of the most widely prescribed anticancer drugs (topoisomerase II poisons) in clinical use. Topoisomerase II poisons kill cells by increasing levels of covalent enzyme-cleaved DNA complexes that are normal reaction intermediates.
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