Animal and Plant Cell Lysates Share a Conserved Chaperone System That Assembles the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90

The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor.

1993 • 652 citations

Evidence That the 90-kDa Heat Shock Protein Is Necessary for the Steroid Binding Conformation of the L Cell Glucocorticoid Receptor

1989 • 394 citations

Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system.

1993 • 302 citations

Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex.

1990 • 190 citations

Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000.

1991 • 177 citations

ATP-dependent chaperoning activity of reticulocyte lysate

1994 • 143 citations

Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro

1989 • 140 citations

In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90.

1990 • 112 citations

A 50-kDa cytosolic protein complexed with the 90-kDa heat shock protein (hsp90) is the same protein complexed with pp60v-src hsp90 in cells transformed by the Rous sarcoma virus.

1991 • 101 citations