Identification of a functional intermediate in receptor activation in progesterone-dependent cell-free transcription
暂无分享,去创建一个
B. O’Malley | M. Tsai | S. Tsai | M. Bagchi
[1] B. O’Malley,et al. Regulation of in vitro transcription by progesterone receptor. Characterization and kinetic studies. , 1990, The Journal of biological chemistry.
[2] B. O’Malley,et al. The progesterone receptor stimulates cell-free transcription by enhancing the formation of a stable preinitiation complex , 1990, Cell.
[3] D. Edwards,et al. Human progesterone receptor complexed with the antagonist RU 486 binds to hormone response elements in a structurally altered form. , 1989, Molecular endocrinology.
[4] W. Welch,et al. Binding of heat shock proteins to the avian progesterone receptor , 1989, Molecular and cellular biology.
[5] E. Baulieu,et al. The antiprogesterone RU486 stabilizes the heterooligomeric, non-DNA-binding, 8S-form of the rabbit uterus cytosol progesterone receptor , 1989, Steroids.
[6] M. Beato. Gene regulation by steroid hormones , 1989, Cell.
[7] M. Perricaudet,et al. Receptors bound to antiprogestin form abortive complexes with hormone responsive elements , 1988, Nature.
[8] D. Edwards,et al. Steroid hormone-dependent interaction of human progesterone receptor with its target enhancer element. , 1988, Molecular endocrinology.
[9] B. O’Malley,et al. Molecular interactions of steroid hormone receptor with its enhancer element: Evidence for receptor dimer formation , 1988, Cell.
[10] L. Poellinger,et al. Requirement of hormone for thermal conversion of the glucocorticoid receptor to a DNA-binding state , 1988, Nature.
[11] G. Chalepakis,et al. Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus , 1988, Cell.
[12] R. Evans,et al. A region in the steroid binding domain determines formation of the non-DNA-binding, 9 S glucocorticoid receptor complex. , 1988, The Journal of biological chemistry.
[13] G. Schütz,et al. A DNA sequence of 15 base pairs is sufficient to mediate both glucocorticoid and progesterone induction of gene expression. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[14] E. Baulieu. Steroid hormone antagonists at the receptor level: A role for the heat‐shock protein MW 90,000 (hsp 90) , 1987, Journal of cellular biochemistry.
[15] D. Edwards,et al. Immunologic analysis of human breast cancer progesterone receptors. 1. Immunoaffinity purification of transformed receptors and production of monoclonal antibodies. , 1987, Biochemistry.
[16] E. Baulieu,et al. Antiglucocorticosteroid effects suggest why steroid hormone is required for receptors to bind DNA in vivo but not in vitro , 1987, Nature.
[17] E. Baulieu,et al. Involvement of a non-hormone-binding 90-kilodalton protein in the nontransformed 8S form of the rabbit uterus progesterone receptor. , 1986, Biochemistry.
[18] Gerhart U. Ryffel,et al. An estrogen-responsive element derived from the 5′ flanking region of the Xenopus vitellogenin A2 gene functions in transfected human cells , 1986, Cell.
[19] M. Beato,et al. The hormone regulatory element of mouse mammary tumour virus mediates progesterone induction. , 1986, The EMBO journal.
[20] R. Harrison,et al. Molybdate-stabilized nonactivated glucocorticoid-receptor complexes contain a 90-kDa non-steroid-binding phosphoprotein that is lost on activation. , 1986, The Journal of biological chemistry.
[21] W. Pratt,et al. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. , 1985, The Journal of biological chemistry.
[22] D. Toft,et al. Inhibition of progesterone receptor activation by sodium molybdate. , 1980, Biochemistry.
[23] W. Vedeckis,et al. Transformed mouse glucocorticoid receptor: generation and interconversion of the 3.8S, monomeric and 5.2S, oligomeric species. , 1985, Biochemistry.
[24] E. Baulieu,et al. Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones , 1984, Nature.
[25] D. Philibert,et al. RU 38486: potent antiglucocorticoid activity correlated with strong binding to the cytosolic glucocorticoid receptor followed by an impaired activation. , 1984, Journal of steroid biochemistry.