Inhibition of apurinic/apyrimidinic endonuclease I's redox activity revisited.

  title={Inhibition of apurinic/apyrimidinic endonuclease I's redox activity revisited.},
  author={Jun Zhang and Meihua Luo and Daniela Marasco and Derek P Logsdon and Kaice A LaFavers and Qiujia Chen and April Reed and Mark R Kelley and Michael L Gross and Millie M Georgiadis},
  volume={52 17},
The essential base excision repair protein, apurinic/apyrimidinic endonuclease 1 (APE1), plays an important role in redox regulation in cells and is currently targeted for the development of cancer therapeutics. One compound that binds APE1 directly is (E)-3-[2-(5,6-dimethoxy-3-methyl-1,4-benzoquinonyl)]-2-nonylpropenoic acid (E3330). Here, we revisit the mechanism by which this negatively charged compound interacts with APE1 and inhibits its redox activity. At high concentrations (millimolar… CONTINUE READING
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