Alterations in Glucocorticoid Receptor Conformation by Molybdate
- 1 April 1980
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 87 (6) , 1851-1854
- https://doi.org/10.1093/oxfordjournals.jbchem.a132930
Abstract
Glucocorticoid receptor activities in cytosol from lactating rat mammary glands were greatly stabilized by molybdate against inactivation during incubation at 25°C. The sedimentation coefficient was 9–10S in the presence of 10 mM Na2MoO4, but 6–7S in the absence of the ion. These data strongly suggest that alterations in receptor conformation induced by direct interaction with molybdate are involved in the stabilization process.This publication has 7 references indexed in Scilit:
- Inhibition of progesterone receptor activation by sodium molybdateBiochemistry, 1980
- Molybdate inhibition of glucocorticoid receptor inactivation and transformation.Journal of Biological Chemistry, 1979
- ATP-dependent activation of L cell glucocorticoid receptors to the steroid binding form.Journal of Biological Chemistry, 1979
- Activation of thymocyte glucocorticoid receptors to the steroid binding form. The roles of reduction agents, ATP, and heat-stable factors.Journal of Biological Chemistry, 1979
- Pyridoxal phosphate induced alterations in glucocorticoid receptor conformationBiochemistry, 1979
- Glucocorticoid receptor inactivation under cell-free conditions.Journal of Biological Chemistry, 1977
- Evidence that dephosphorylation inactivates glucocorticoid receptors.Proceedings of the National Academy of Sciences, 1977