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Titlebook: Gene Regulation by Steroid Hormones III; Arun K. Roy,James H. Clark Conference proceedings 1987 Springer-Verlag New York Inc. 1987 Activat

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书目名称Gene Regulation by Steroid Hormones III
编辑Arun K. Roy,James H. Clark
视频video
图书封面Titlebook: Gene Regulation by Steroid Hormones III;  Arun K. Roy,James H. Clark Conference proceedings 1987 Springer-Verlag New York Inc. 1987 Activat
描述The field of steroid hormone action has continued to expand into the realm of molecular biology at a pace even faster than most of us ever imagined. techniques of molecular biology have made it possible to clone The hormone-regulated genes and to examine steroid-receptor interactions with these genes. Nucleotide sequences of these genes, which show preferential binding of steroid receptors, have been identified. These results are complemented by the identification of chromatin acceptor proteins, which also show preferential binding for steroid-receptor complexes. Thus, one can envision the day when cloned genes, purified acceptor proteins, and receptor-steroid complexes will be recombined in vitro to form a functional unit. Cellular localization of steroid receptors has undergone recent revision, and it now appears that receptors are localized primarily in the nuclear compartment. These findings, although controversial, will lead to a reassessment of many of the previous concepts of steroid-receptor interactions and regulation. The way in which these observations at the of physiology, molecular and cellular levels fit into the overall scheme development, and evolution are continuin
出版日期Conference proceedings 1987
关键词Activation; G proteins; Nucleotide; Vitamin D; estrogen receptor; gene expression; glucocorticoid; proteins
版次1
doihttps://doi.org/10.1007/978-1-4612-4686-2
isbn_softcover978-1-4612-9114-5
isbn_ebook978-1-4612-4686-2
copyrightSpringer-Verlag New York Inc. 1987
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Structure, Dynamics, and Cloning of the Estrogen Receptor,t the majority of functional estrogen receptor may reside in the nucleus, regardless of hormone status, and that binding of hormone to receptor leads to a tighter association of steroid-receptor complex with nuclear components. The nature of this association is not known, although a number of nuclea
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Type II Binding Sites: Cellular Origin and an Endogenous Ligand,Markaverich and Clark, 1979; Watson and Clark, 1980) and malignanttissues. Type I sites represent the classical estrogen receptor, which has a high affinity for estradiol (.. = 0.1 − 1.0 n.) and is present in target tissues in relatively low quantities. Nuclear type II sites appear to be a specific
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Human Progesterone Receptors Have Two Intracellular Hormone Binding Proteins That Are Covalently Morganization nor the nuclear sites of action of these proteins is resolved. The questions that persist include the size and number of hormone-binding subunits of the holoreceptors and the means by which receptors are transformed* to tight chromatin-binding proteins in response to hormone treatment. W
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The Two Phosphorylation Reactions of the Progesterone Receptor,mone interacts with a specific receptor. The second step is the tight binding of the steroid-receptor complex to chromatin, where it modulates the transcription of specific genes. We have recently observed, in the case of the progesterone receptor, the existence of a third step involving a hormone-d
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Receptor-Mediated Action of the Vitamin D Hormone, Fig. 1, 1,25(OH).D. is formed in the kidney according to the calcium and phosphorus needs of the organism (Haussler and McCain, 1977). Its main functions are the stimulation of intestinal calcium and phosphate absorption as well as bone remodeling. In addition to its mineral conservation effects in
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Characterization of the Nuclear Binding Sites (Acceptor Sites) for a Steroid Receptor,n of gene transcription (Thrall et al., 1978; Spelsberg et al., 1983). Although steroids can affect the rate of processing and stability of mRNAs (Moore et al., 1984) as well as membrane transport, one of the major sites of action appears to be directed at the transcription of the genes. For steroid
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Antibodies to Estrogen, Progesterone, Glucocorticoid, Vitamin D Receptors and Autoantibodies to Andeans, 1974; Liao, 1975; Muldoon, 1980; Schrader, et al., 1981; Schmidt and Litwack, 1982; Jensen et al., 1982; Ringold, 1985). Specific receptors for a number of steroid hormones have been purified (O’Malley and Schrader, 1976; Govindan, 1979; Kuhn et al., 1975; Pike et al., 1982; Jensen et al., 198
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