Association of heat shock protein 90 with the 16 kDa steroid binding core fragment of rat glucocorticoid receptors
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference33 articles.
1. Heteromeric nature of glucocorticoid receptor
2. Evidence That the 90-kDa Heat Shock Protein Is Necessary for the Steroid Binding Conformation of the L Cell Glucocorticoid Receptor
3. Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex
4. The transformed glucocorticoid receptor has a lower steroid-binding affinity than the nontransformed receptor
5. Interaction of the Mr = 90,000 heat shock protein with the steroid-binding domain of the glucocorticoid receptor.
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1. Steroid-induced conformational changes of rat glucocorticoid receptor cause altered trypsin cleavage of the putative helix 6 in the ligand binding domain1Min Xu and Kevin J. Modarress contributed equally and should each be considered as first author.1;Molecular and Cellular Endocrinology;1999-09
2. Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones;Endocrine Reviews;1997-06-01
3. Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*;Endocrine Reviews;1997-06-01
4. THE ROLE OF THEhsp90-BASED CHAPERONE SYSTEM IN SIGNAL TRANSDUCTION BY NUCLEAR RECEPTORS AND RECEPTORS SIGNALING VIA MAP KINASE;Annual Review of Pharmacology and Toxicology;1997-04
5. Use of the Thiol-specific Derivatizing Agent N-Iodoacetyl-3- I iodotyrosine to Demonstrate Conformational Differences between the Unbound and hsp90-bound Glucocorticoid Receptor Hormone Binding Domain;Journal of Biological Chemistry;1996-04
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