The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter.

@article{Kang1999TheMC,
  title={The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter.},
  author={Kwang Il Kang and Xiangjun Meng and Jocelyne Devin-Leclerc and I Bouhouche and Ahmed Chadli and Françoise Cadepond and Etienne Emile Baulieu and Maria Grazia Catelli},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 4},
  pages={1439-44}
}
Hsp90, a molecular chaperone required for the functioning of glucocorticosteroid receptor (GR), ensures, by direct interaction, the conformational competence of the steroid-binding pocket. In addition to having this positive function, Hsp90 maintains steroid receptors in an inactive form in the absence of hormone. However, neither the participation of Hsp90 once the pathway has been activated by the ligand nor the importance of increased Hsp90 levels in determining the amplitude of the response… CONTINUE READING
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Kang et al

  • N. C. Collier, Schlessinger, M. J. J. Cell Biol. 103, 1495–1507. 1444 Cell Biology
  • Proc. Natl. Acad. Sci. USA 96
  • 1999

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