I. Segard-Maurel

Interaction of glucocorticosteroid receptor and wild-type or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells.

E. Baulieu, G. Schweizer-Groyer, F. Cadepond, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Heat shock protein 90 as a critical factor in maintaining glucocorticosteroid receptor in a nonfunctional state.

R. Evans, E. Baulieu, V. Giguère, 1991, The Journal of biological chemistry.

Stimulation of transcription in vitro from a liver-specific promoter by human glucocorticoid receptor (hGRalpha).

E. Baulieu, G. Schweizer-Groyer, F. Cadepond, 1997, The Biochemical journal.

Selective deletions in the 90 kDa heat shock protein (hsp90) impede hetero-oligomeric complex formation with the glucocorticosteroid receptor (GR) or hormone binding by GR

E. Baulieu, G. Schweizer-Groyer, F. Cadepond, 1994, The Journal of Steroid Biochemistry and Molecular Biology.

Hormonal regulation of the nuclear localization signals of the human glucocorticosteroid receptor.

R. Evans, E. Baulieu, G. Schweizer-Groyer, 1992, Experimental cell research.

Mutations in the “zinc fingers” or in the n-terminal region of the DNA binding domain of the human glucocorticosteroid receptor facilitate its salt-induced transformation, but do not modify hormone binding

E. Baulieu, G. Schweizer-Groyer, F. Cadepond, 1992, The Journal of Steroid Biochemistry and Molecular Biology.

Glucocorticosteroid receptor dimerization investigated by analysis of receptor binding to glucocorticosteroid responsive elements using a monomer-dimer equilibrium model.

E. Baulieu, G. Schweizer-Groyer, F. Cadepond, 1996, Biochemistry.