I. Bouhouche

The Heat Shock Protein 90 Antagonist Novobiocin Interacts with a Previously Unrecognized ATP-binding Domain in the Carboxyl Terminus of the Chaperone*

L. Neckers, M. Marcu, M. Catelli, 2000, The Journal of Biological Chemistry.

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

E. Baulieu, F. Cadepond, M. Catelli, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90.

D. Toft, M. Catelli, A. Chadli, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Luciferase activity and synthesis of Hsp70 and Hsp90 are insensitive to 50Hz electromagnetic fields.

E. Baulieu, M. Catelli, D. Fortin, 1998, Life sciences.