Interactions of apurinic/apyrimidinic endonuclease with a redox inhibitor: evidence for an alternate conformation of the enzyme.

@article{Su2011InteractionsOA,
  title={Interactions of apurinic/apyrimidinic endonuclease with a redox inhibitor: evidence for an alternate conformation of the enzyme.},
  author={Dian Su and Sarah Delaplane and Meihua Luo and Don L. Rempel and Bich Vu and Mark R Kelley and Michael L Gross and Millie M Georgiadis},
  journal={Biochemistry},
  year={2011},
  volume={50 1},
  pages={82-92}
}
Apurinic/apyrimidinic endonuclease (APE1) is an essential base excision repair protein that also functions as a reduction and oxidation (redox) factor in mammals. Through a thiol-based mechanism, APE1 reduces a number of important transcription factors, including AP-1, p53, NF-κB, and HIF-1α. What is known about the mechanism to date is that the buried residues Cys 65 and Cys 93 are critical for APE1's redox activity. To further detail the redox mechanism, we developed a chemical footprinting… CONTINUE READING
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