High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity.

@article{Rowlands2004HighthroughputSA,
  title={High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity.},
  author={Martin G. Rowlands and Yvette M Newbatt and Chrisostomos Prodromou and Laurence H. Pearl and Paul Workman and Wynne Aherne},
  journal={Analytical biochemistry},
  year={2004},
  volume={327 2},
  pages={176-83}
}
The molecular chaperone heat-shock protein 90 (HSP90) plays a key role in the cell by stabilizing a number of client proteins, many of which are oncogenic. The intrinsic ATPase activity of HSP90 is essential to this activity. HSP90 is a new cancer drug target as inhibition results in simultaneous disruption of several key signaling pathways, leading to a combinatorial approach to the treatment of malignancy. Inhibitors of HSP90 ATPase activity including the benzoquinone ansamycins, geldanamycin… CONTINUE READING

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