Selective deletions in the 90 kDa heat shock protein (hsp90) impede hetero-oligomeric complex formation with the glucocorticosteroid receptor (GR) or hormone binding by GR
- 1 March 1994
- journal article
- Published by Elsevier in The Journal of Steroid Biochemistry and Molecular Biology
- Vol. 48 (4) , 361-367
- https://doi.org/10.1016/0960-0760(94)90076-0
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- 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
- Cloning of Chicken hsp90β: The Only Vertebrate hsp90 Insensitive to Heat ShockBiochemical and Biophysical Research Communications, 1993
- Steroid receptor folding by heat-shock proteins and composition of the receptor heterocomplexTrends in Endocrinology & Metabolism, 1992
- Hormonal regulation of the nuclear localization signals of the human glucocorticosteroid receptorExperimental Cell Research, 1992
- Protein folding in the cellNature, 1992
- Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complexBiochemistry, 1990
- A highly charged sequence of chick hsp90: A good candidate for interaction with steroid receptorsJournal of Steroid Biochemistry, 1989
- The cDNA-derived amino acid sequence of chick heat shock protein Mr 90,000 (HSP 90) reveals A “DNA like” structure: Potential site of interaction with steroid receptorsBiochemical and Biophysical Research Communications, 1989
- Relationship between glucocorticoid receptor steroid-binding capacity and association of the Mr 90,000 heat shock protein with the unliganded receptorJournal of Steroid Biochemistry, 1988
- 402 Immunological studies of chick oviduct progesterone receptorJournal of Steroid Biochemistry, 1983