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Cancer Research|April 15, 1989
Interaction of the glucocorticoid receptor with the Mr 90,000 heat shock protein: an evolving model of ligand-mediated receptor transformation and translocationW B Pratt, E R Sanchez, E H Bresnick, et al.
The Journal of Biological Chemistry|September 1, 1995
The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptorJ K Owens-Grillo, K Hoffmann, K A Hutchison, et al.
The Journal of Biological Chemistry|August 11, 1995
The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90K A Hutchison, L F Stancato, J K Owens-Grillo, et al.
The Journal of Biological Chemistry|September 2, 1994
The native v-Raf.hsp90.p50 heterocomplex contains a novel immunophilin of the FK506 binding classL F Stancato, Y H Chow, J K Owens-Grillo, et al.
Biochemistry|November 23, 2000
hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1K C Kanelakis, P J Murphy, M D Galigniana, et al.
Molecular Endocrinology (Baltimore, Md.)|December 1, 1994
The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptorM J Czar, J K Owens-Grillo, A W Yem, et al.
Biochemistry|April 20, 1993
FK506 binding to the 56-kilodalton immunophilin (Hsp56) in the glucocorticoid receptor heterocomplex has no effect on receptor folding or functionK A Hutchison, L C Scherrer, M J Czar, et al.
The Journal of Biological Chemistry|April 15, 1994
Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplexM J Czar, J K Owens-Grillo, K D Dittmar, et al.
Biochemistry|June 4, 1991
Retinoic acid receptor belongs to a subclass of nuclear receptors that do not form "docking" complexes with hsp90F C Dalman, L J Sturzenbecker, A A Levin, et al.
The Journal of Biological Chemistry|November 25, 1990
Hormone-free mouse glucocorticoid receptors overexpressed in Chinese hamster ovary cells are localized to the nucleus and are associated with both hsp70 and hsp90E R Sanchez, M Hirst, L C Scherrer, et al.
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