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- W225003906 abstract "This chapter describes steroid hormone receptors as belonging to a superfamily of ligand-activated transcription factors with structural similarities. This superfamily includes thyroid hormone, vitamin D3, and retinoic acid receptors. Sequence analysis of the receptors has revealed that they are related to the product of the v-erb-A oncogene of avian erythroblastosis virus and the c-erb-A proto-oncogene. This relationship indicates that those molecules may all be part of a superfamily of regulatory proteins that have arisen over evolutionary time. Binding sites for peptide hormones are localized almost exclusively at the surface of their target cells in the plasma membrane fraction. Polypeptide hormone receptors are integral transmembrane proteins with the specific hormone binding site at the extracellular amino terminus and an intracellular domain at the carboxyl terminus that possesses intrinsic tyrosine-kinase activity. Physiological increases in endogenous hormone positively regulate membrane receptors but major elevations in a circulating hormone often cause downregulation of luteinizing hormone receptors and desensitization in target cells." @default.
- W225003906 created "2016-06-24" @default.
- W225003906 creator A5002437874 @default.
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- W225003906 date "1991-01-01" @default.
- W225003906 modified "2023-09-25" @default.
- W225003906 title "Receptors, Mechanism of Action and Biological Responses of Hormones in the Fetal, Placental and Maternal Compartments" @default.
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