Catalase abrogates β-lapachone-induced PARP1 hyperactivation-directed programmed necrosis in NQO1-positive breast cancers.

@article{Bey2013CatalaseA,
  title={Catalase abrogates β-lapachone-induced PARP1 hyperactivation-directed programmed necrosis in NQO1-positive breast cancers.},
  author={Erik A. Bey and Kathryn E. Reinicke and Melissa C. Srougi and Marie Varnes and Vernon E. Anderson and John J. Pink and Long Shan Li and Malina Patel and Lifen Cao and Zachary Moore and Amy Rommel and Michael A Boatman and Cheryl Lewis and David Michael Euhus and William G. Bornmann and Donald J Buchsbaum and Douglas R. Spitz and Jinming Gao and David A. Boothman},
  journal={Molecular cancer therapeutics},
  year={2013},
  volume={12 10},
  pages={2110-20}
}
Improving patient outcome by personalized therapy involves a thorough understanding of an agent's mechanism of action. β-Lapachone (clinical forms, Arq501/Arq761) has been developed to exploit dramatic cancer-specific elevations in the phase II detoxifying enzyme NAD(P)H:quinone oxidoreductase (NQO1). NQO1 is dramatically elevated in solid cancers, including primary and metastatic [e.g., triple-negative (ER-, PR-, Her2/Neu-)] breast cancers. To define cellular factors that influence the… CONTINUE READING
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