Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification.

@article{Dolgova2013CopperCA,
  title={Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification.},
  author={Nataliya V Dolgova and Sergiy M Nokhrin and Corey H. Yu and Graham N George and Oleg Y Dmitriev},
  journal={The Biochemical journal},
  year={2013},
  volume={454 1},
  pages={147-56}
}
Human copper transporters ATP7B (Wilson's disease protein) and ATP7A (Menkes' disease protein) have been implicated in tumour resistance to cisplatin, a widely used anticancer drug. Cisplatin binds to the copper-binding sites in the N-terminal domain of ATP7B, and this binding may be an essential step of cisplatin detoxification involving copper ATPases. In the present study, we demonstrate that cisplatin and a related platinum drug carboplatin produce the same adduct following reaction with… CONTINUE READING
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