Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.
Open Access
- 1 October 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (23) , 12398-12401
- https://doi.org/10.1016/s0021-9258(17)38886-5
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Structure of Mammalian Steroid Receptors: Evolving Concepts and Methodological DevelopmentsAnnual Review of Physiology, 1984
- Effects of Molybdate and Endogenous Inhibitors on Steroid-Receptor Inactivation, Transformation, and TranslocationAnnual Review of Physiology, 1984
- Polypeptide components of two 8 S forms of chicken oviduct progesterone receptor.Journal of Biological Chemistry, 1984
- Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormonesNature, 1984
- Purification by affinity chromatography and immunological characterization of a 110kDa component of the chick oviduct progesterone receptorBiochemical Journal, 1984
- Subunit dissociation as a possible mechanism of glucocorticoid receptor activationBiochemistry, 1983
- Direct demonstration of glucocorticoid receptor phosphorylation by intact L-cells.Journal of Biological Chemistry, 1983
- The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteinsCell, 1981
- A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein.Proceedings of the National Academy of Sciences, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970