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.

Hsp90 Chaperone Activity Requires the Full-length Protein and Interaction among Its Multiple Domains*

D. Toft, M. Catelli, A. Chadli, 2000, The Journal of Biological Chemistry.

Electrochemical behavior and surface characterization of dental materials in artificial salivary

N. Labjar, E. Lotfi, A. Dahrouch, 2020 .

Electrochemical Behavior and Surface Characterization of Two Dental Materials: Glass Ceramic and Zirconia in Artificial Saliva

N. Labjar, S. El Hajjaji, A. Dahrouch, 2020, Journal of Failure Analysis and Prevention.

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.

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.

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

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

[Functional interaction of HSP90 with steroid receptors].

F. Cadepond, M. Catelli, I. Bouhouche, 1999, Journal de la Société de Biologie.