Rationally designed high-affinity 2-amino-6-halopurine heat shock protein 90 inhibitors that exhibit potent antitumor activity.

@article{Kasibhatla2007RationallyDH,
  title={Rationally designed high-affinity 2-amino-6-halopurine heat shock protein 90 inhibitors that exhibit potent antitumor activity.},
  author={Srinivas Rao Kasibhatla and Kevin C. Hong and Marco A Biamonte and David J. Busch and Patricia L Karjian and John L. Sensintaffar and Adeela Kamal and Rachel E Lough and John Brekken and Karen Lundgren and Roy Grecko and Gregg A. Timony and Yingqing Ran and Robert T Mansfield and Lawrence C. Fritz and Edgar H. Ulm and Francis J. Burrows and Marcus F. Boehm},
  journal={Journal of medicinal chemistry},
  year={2007},
  volume={50 12},
  pages={2767-78}
}
Heat shock protein 90 (Hsp90) is a molecular chaperone protein implicated in stabilizing the conformation and maintaining the function of many cell-signaling proteins. Many oncogenic proteins are more dependent on Hsp90 in maintaining their conformation, stability, and maturation than their normal counterparts. Furthermore, recent data show that Hsp90 exists in an activated form in malignant cells but in a latent inactive form in normal tissues, suggesting that inhibitors selective for the… CONTINUE READING