Binding of hsp90 to the Glucocorticoid Receptor Requires a Specific 7-Amino Acid Sequence at the Amino Terminus of the Hormone-binding Domain
Open Access
- 1 May 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (22) , 13918-13924
- https://doi.org/10.1074/jbc.273.22.13918
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Identification of a Third Autonomous Activation Domain within the Human Estrogen ReceptorMolecular Endocrinology, 1997
- Steroid Receptor Interactions with Heat Shock Protein and Immunophilin ChaperonesEndocrine Reviews, 1997
- Modular Structure of Glucocorticoid Receptor Domains Is Not Equivalent to Functional IndependencePublished by Elsevier ,1996
- Molecular chaperones in cellular protein foldingNature, 1996
- Animal and Plant Cell Lysates Share a Conserved Chaperone System That Assembles the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90Biochemistry, 1996
- Genetic analysis of the N-terminal end of the glucocorticoid receptor hormone binding domainThe Journal of Steroid Biochemistry and Molecular Biology, 1994
- A highly conserved region in the hormone-binding domain of the human estrogen receptor functions as an efficient transactivation domain in yeastGene, 1994
- A new cis-acting element involved in tissue-selective glucocorticoid inducibility of tyrosine aminotransferase gene expressionMolecular Endocrinology, 1993
- Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat-shock protein 90Biochemistry, 1993
- Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNABiochemical and Biophysical Research Communications, 1987