The Hsp Organizer Protein Hop Enhances the Rate of but Is Not Essential for Glucocorticoid Receptor Folding by the Multiprotein Hsp90-based Chaperone System
Open Access
- 1 March 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (10) , 6894-6900
- https://doi.org/10.1074/jbc.275.10.6894
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- The Role of DnaJ-like Proteins in Glucocorticoid Receptor·hsp90 Heterocomplex Assembly by the Reconstituted hsp90·p60·hsp70 Foldosome ComplexJournal of Biological Chemistry, 1998
- Hop Modulates hsp70/hsp90 Interactions in Protein FoldingJournal of Biological Chemistry, 1998
- Steroid Receptor Interactions with Heat Shock Protein and Immunophilin ChaperonesEndocrine Reviews, 1997
- Folding of the Glucocorticoid Receptor by the Reconstituted hsp90-based Chaperone MachineryJournal of Biological Chemistry, 1997
- Optimal ligand binding by the recombinant human glucocorticoid receptor and assembly of the receptor complex with heat shock protein 90 correlate with high intracellular ATP levels in Spodoptera frugiperda cellsThe Journal of Steroid Biochemistry and Molecular Biology, 1997
- Molecular chaperones in cellular protein foldingNature, 1996
- Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70Molecular Endocrinology, 1996
- Cooperative Action of Hsp70, Hsp90, and DnaJ Proteins in Protein RenaturationBiochemistry, 1996
- Animal and Plant Cell Lysates Share a Conserved Chaperone System That Assembles the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90Biochemistry, 1996
- Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexesMolecular Endocrinology, 1993