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Trends in Plant Science|February 15, 2001
Hsp90-binding immunophilins in plants: the protein moversW B Pratt, P Krishna, L J OlsenBiochemistry|January 16, 1996
Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90L F Stancato, K A Hutchison, P Krishna, et al.Biochemistry|December 3, 1996
Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plantsJ K Owens-Grillo, L F Stancato, K Hoffmann, et al.The Journal of Biological Chemistry|August 22, 1997
Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70K D Dittmar, D R Demady, L F Stancato, et al.Annual Review of Pharmacology and Toxicology|January 1, 1997
The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinaseW B PrattJournal of Cellular Biochemistry|September 1, 1987
Transformation of glucocorticoid and progesterone receptors to the DNA-binding stateW B PrattProceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)|April 1, 1998
The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptorsW B PrattBioessays : News and Reviews in Molecular, Cellular and Developmental Biology|December 1, 1992
Control of steroid receptor function and cytoplasmic-nuclear transport by heat shock proteinsW B PrattJournal of Steroid Biochemistry|January 1, 1989
Evidence that removal of an endogenous metal that stabilizes the untransformed glucocorticoid receptor in cytosol allows ligand-independent receptor transformationS Meshinchi, W B PrattOrthopaedic Review|October 1, 1989
Laboratory testing of bolts and screws in cancellous boneW B Pratt, S YazdaniPageof 28