메뉴 건너뛰기




Volumn 23, Issue SUPPL., 1996, Pages

Mechanisms of action of sex steroid hormones: Basic concepts and clinical correlations

Author keywords

Cell membrane; Nuclear; Steroid receptor; Transcription

Indexed keywords

PROGESTERONE RECEPTOR; SEX HORMONE; STEROID RECEPTOR; TRANSCRIPTION FACTOR;

EID: 0343807219     PISSN: 03785122     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-5122(96)01004-3     Document Type: Article
Times cited : (16)

References (75)
  • 1
    • 0028935426 scopus 로고
    • Emerging diversities in the mechanism of action of steroid hormones
    • Brann DW, Hendry LB, Mahesh VB. Emerging diversities in the mechanism of action of steroid hormones. J Steroid Biochem Molec Biol 1995; 52: 113-133.
    • (1995) J Steroid Biochem Molec Biol , vol.52 , pp. 113-133
    • Brann, D.W.1    Hendry, L.B.2    Mahesh, V.B.3
  • 3
    • 0024312377 scopus 로고
    • Glucocorticoidspecific and progesteronespecific effects are determined by differential expression of the respective hormone receptors
    • Strahle U, Boshart M, Klock G, Stewart F, Schutz G. Glucocorticoidspecific and Progesteronespecific Effects Are Determined by Differential Expression of the Respective Hormone Receptors. Nature 1989; 339: 629-632.
    • (1989) Nature , vol.339 , pp. 629-632
    • Strahle, U.1    Boshart, M.2    Klock, G.3    Stewart, F.4    Schutz, G.5
  • 4
    • 0017100992 scopus 로고
    • Binding of steroids to uteroglobin
    • Beato M. Binding of steroids to uteroglobin. J Steroid Biochem 1976; 7: 327-334.
    • (1976) J Steroid Biochem , vol.7 , pp. 327-334
    • Beato, M.1
  • 6
    • 0021320840 scopus 로고
    • Progesterone receptor characterized by photoaffinity labelling in the plasma membrane of Xenopus laevis oocytes
    • Blondeau J.-P.BE-E. Progesterone receptor characterized by photoaffinity labelling in the plasma membrane of Xenopus laevis oocytes. Biochem J 1984; 219: 785-792.
    • (1984) Biochem J , vol.219 , pp. 785-792
    • Blondeau, J.-P.B.E.-E.1
  • 7
    • 0028925081 scopus 로고
    • Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding
    • Pappas TC, Gametchu B, Watson CS. Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding. Faseb Journal 1995; 9: 404-410.
    • (1995) Faseb Journal , vol.9 , pp. 404-410
    • Pappas, T.C.1    Gametchu, B.2    Watson, C.S.3
  • 8
    • 0020695007 scopus 로고
    • Steroid binding of synaptic plasma membrane: Differential binding of glucocorticoids and gonadal steroids
    • Towle AC, Sze PY. Steroid binding of synaptic plasma membrane: differential binding of glucocorticoids and gonadal steroids. Journal of Steroid Biochemistry 1983; 18: 135-143.
    • (1983) Journal of Steroid Biochemistry , vol.18 , pp. 135-143
    • Towle, A.C.1    Sze, P.Y.2
  • 9
    • 0025697567 scopus 로고
    • Regulation of progesterone receptor-mediated transcription by phosphorylation
    • Denner LA, Wiegel NL, Maxwell BL, Schrader WT, O'Malley BW. Regulation of progesterone receptor-mediated transcription by phosphorylation. Science 1990; 250: 1740-1748.
    • (1990) Science , vol.250 , pp. 1740-1748
    • Denner, L.A.1    Wiegel, N.L.2    Maxwell, B.L.3    Schrader, W.T.4    O'Malley, B.W.5
  • 11
    • 0025806284 scopus 로고
    • Superfamily of steroid nuclear receptors-positive and negative regulators of gene expression
    • Wahli W, Martinez E. Superfamily of Steroid Nuclear Receptors-Positive and Negative Regulators of Gene Expression. FASEB Journal 1991; 5: 2243-2249.
    • (1991) FASEB Journal , vol.5 , pp. 2243-2249
    • Wahli, W.1    Martinez, E.2
  • 13
    • 0024724575 scopus 로고
    • Did eucaryotic steroid receptors evolve from intracrine gene regulators
    • Omalley BW. Did Eucaryotic Steroid Receptors Evolve from Intracrine Gene Regulators. Endocrinology 1989; 125: 1119-1120.
    • (1989) Endocrinology , vol.125 , pp. 1119-1120
    • Omalley, B.W.1
  • 14
    • 0025302559 scopus 로고
    • Diversity and unity in the nuclear hormone receptors: A terpenoid receptor superfamily
    • Moore DD. Diversity and unity in the nuclear hormone receptors: a terpenoid receptor superfamily. New Biol 1990; 2: 100-105.
    • (1990) New Biol , vol.2 , pp. 100-105
    • Moore, D.D.1
  • 17
    • 0024365823 scopus 로고
    • The chicken progesterone receptor-A and receptor-B isoforms are products of an alternate translation initiation event
    • Conneely OM, Kettelberger DM, Tsai MJ, Schrader WT, O'Malley BW. The Chicken Progesterone Receptor-A and Receptor-B Isoforms Are Products of an Alternate Translation Initiation Event. Journal of Biological Chemistry 1989; 264: 14062-14064.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 14062-14064
    • Conneely, O.M.1    Kettelberger, D.M.2    Tsai, M.J.3    Schrader, W.T.4    O'Malley, B.W.5
  • 18
    • 0025323132 scopus 로고
    • Transient expression of humanand chicken progesterone receptors does not support alternative translational initiation from a single mRNA as the mechanism generating two receptor isoforms
    • Kastner P, Boquel MT, Turcotte B, Garnier JM, Horwitz KB, Chambon P et al. Transient expression of humanand chicken progesterone receptors does not support alternative translational initiation from a single mRNA as the mechanism generating two receptor isoforms. J Biol Chem 1990; 265: 12163-12167.
    • (1990) J Biol Chem , vol.265 , pp. 12163-12167
    • Kastner, P.1    Boquel, M.T.2    Turcotte, B.3    Garnier, J.M.4    Horwitz, K.B.5    Chambon, P.6
  • 19
    • 0023935721 scopus 로고
    • The N-terminal region of the chicken progesterone receptor specifies target gene activation
    • Tora L, Gronemeyer H, Turcotte B, Gaub P, Chambon P. The N-terminal Region of the Chicken Progesterone Receptor Specifies Target Gene Activation. Nature 1988; 333: 185-188.
    • (1988) Nature , vol.333 , pp. 185-188
    • Tora, L.1    Gronemeyer, H.2    Turcotte, B.3    Gaub, P.4    Chambon, P.5
  • 20
    • 0028597916 scopus 로고
    • Gene expression of progesterone receptor isoforms in the rat brain
    • Kato J, Hirata S, Nozawa A, Yamadamoun N. Gene expression of progesterone receptor isoforms in the rat brain. Hormones and Behavior 1994; 28: 454-463.
    • (1994) Hormones and Behavior , vol.28 , pp. 454-463
    • Kato, J.1    Hirata, S.2    Nozawa, A.3    Yamadamoun, N.4
  • 22
    • 0028137227 scopus 로고
    • How do breast cancers become hormone resistant?
    • Horwitz KB. How do breast cancers become hormone resistant? J Steroid Biochem Molec Biol 1994; 49: 295-302.
    • (1994) J Steroid Biochem Molec Biol , vol.49 , pp. 295-302
    • Horwitz, K.B.1
  • 24
    • 0028693807 scopus 로고
    • Autoregulation of corticosteroid receptors
    • Schmidt TJ, Meyer AS. Autoregulation of corticosteroid receptors. Receptor 1994; 4: 229-257.
    • (1994) Receptor , vol.4 , pp. 229-257
    • Schmidt, T.J.1    Meyer, A.S.2
  • 25
    • 0025850532 scopus 로고
    • Control of transcription of chicken progesterone receptor gene: In vitro and vivo studies
    • Turcotte B, Meyer ME, Bellard M, Dretzen G, Gronemeyer H, Chambon P. Control of transcription of chicken progesterone receptor gene: in vitro and vivo studies. J Biol Chem 1991; 266: 2582-2589.
    • (1991) J Biol Chem , vol.266 , pp. 2582-2589
    • Turcotte, B.1    Meyer, M.E.2    Bellard, M.3    Dretzen, G.4    Gronemeyer, H.5    Chambon, P.6
  • 26
    • 0021352569 scopus 로고
    • Augementation of progesterone receptor concentration by progesterone and estrogen treatment in the chick oviduct
    • Ylikomi TIJ, Ratia T, Vähä-Tahlo T, Tuohimaa P. Augementation of progesterone receptor concentration by progesterone and estrogen treatment in the chick oviduct. J Steroid Biochem 1984; 20: 445-447.
    • (1984) J Steroid Biochem , vol.20 , pp. 445-447
    • Ylikomi, T.I.J.1    Ratia, T.2    Vähä-Tahlo, T.3    Tuohimaa, P.4
  • 27
    • 0023878411 scopus 로고
    • Progesterone receptor regulation in T47D human breast cancer cells: Analysis by density labeling of progesterone receptor synthesis and degradation and their modulation by progestin
    • Nardulli AM, Katzenellenbogen BS. Progesterone receptor regulation in T47D human breast cancer cells: analysis by density labeling of progesterone receptor synthesis and degradation and their modulation by progestin. Endocrinology 1988; 122(4): 1532-1540.
    • (1988) Endocrinology , vol.122 , Issue.4 , pp. 1532-1540
    • Nardulli, A.M.1    Katzenellenbogen, B.S.2
  • 28
    • 0025196785 scopus 로고
    • H-1 NMR studies of the glucocorticoid receptor DNA-binding domain-sequential assignments and identification of secondary structure elements
    • Hard T, Kellenbach E, Boelens R, Kaptein R, Dahlman K, Carlstedtduke J et al. H-1 NMR Studies of the Glucocorticoid Receptor DNA-Binding Domain-Sequential Assignments and Identification of Secondary Structure Elements. Biochemistry 1990; 29: 9015-9023.
    • (1990) Biochemistry , vol.29 , pp. 9015-9023
    • Hard, T.1    Kellenbach, E.2    Boelens, R.3    Kaptein, R.4    Dahlman, K.5    Carlstedtduke, J.6
  • 30
    • 0025828493 scopus 로고
    • Transcriptional control by nuclear receptors
    • Beato M. Transcriptional Control by Nuclear Receptors. FASEB Journal 1991; 5: 2044-2051.
    • (1991) FASEB Journal , vol.5 , pp. 2044-2051
    • Beato, M.1
  • 31
    • 0002488167 scopus 로고
    • The steroid hormone receptor superfamily
    • Weintraub BD, ed. Molecular Endocrinology: Basic concepts and clinical correlations Raven Press, New York.
    • Ing NH, O'Malley BW. The steroid hormone receptor superfamily: In: Weintraub BD, ed. Molecular mechanisms of action. Molecular Endocrinology: Basic concepts and clinical correlations Raven Press, New York. 1995; 195-215.
    • (1995) Molecular Mechanisms of Action , pp. 195-215
    • Ing, N.H.1    O'Malley, B.W.2
  • 32
    • 0021261383 scopus 로고
    • Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones
    • Joab I, Radanyi C, Renoir M, Bouchou T, Catelli MG, Binart N et al. Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones. Nature 1984; 308: 850-853.
    • (1984) Nature , vol.308 , pp. 850-853
    • Joab, I.1    Radanyi, C.2    Renoir, M.3    Bouchou, T.4    Catelli, M.G.5    Binart, N.6
  • 33
    • 0024519049 scopus 로고
    • The cDNA-derived amino acid sequence of chick heat shock protein M 90 000 (HSP 90) reveals a DNA like structure - Potential site of interaction with steroid receptors
    • Binart N, Chambraud B, Dumas B, Rowlands DA, Bigogne C, Levin JM et al. The cDNA-Derived Amino Acid Sequence of Chick Heat Shock Protein M 90 000 (HSP 90) Reveals a DNA Like Structure - Potential Site of Interaction with Steroid Receptors. Biochemical and Biophysical Research Communications 1989; 159 (1): 140-147.
    • (1989) Biochemical and Biophysical Research Communications , vol.159 , Issue.1 , pp. 140-147
    • Binart, N.1    Chambraud, B.2    Dumas, B.3    Rowlands, D.A.4    Bigogne, C.5    Levin, J.M.6
  • 34
    • 0024434439 scopus 로고
    • Antibodies to chicken progesterone receptor peptide-523-536 recognize a site exposed in receptor-deoxyribonucleic acid complexes but not in receptor-heat shock protein-90 complexes
    • Weigel NL, Schrader WT, O'Malley BW. Antibodies to Chicken Progesterone Receptor Peptide-523-536 Recognize a Site Exposed in Receptor-Deoxyribonucleic Acid Complexes But Not in Receptor-Heat Shock Protein-90 Complexes. Endocrinology 1989; 125: 2494-2501.
    • (1989) Endocrinology , vol.125 , pp. 2494-2501
    • Weigel, N.L.1    Schrader, W.T.2    O'Malley, B.W.3
  • 35
    • 0027106265 scopus 로고
    • Control of steroid receptor function and cytoplasmic-nuclear transport by heat shock proteins
    • Pratt WB. Control of steroid receptor function and cytoplasmic-nuclear transport by heat shock proteins. Bioessays 1992; 14: 841-848.
    • (1992) Bioessays , vol.14 , pp. 841-848
    • Pratt, W.B.1
  • 36
    • 0023432622 scopus 로고
    • Steroid hormone antagonists at the receptor level: A role for the heat-shock protein MW 90 000 (hsp 90)
    • Baulieu EE. Steroid hormone antagonists at the receptor level: a role for the heat-shock protein MW 90 000 (hsp 90). J Cell Biochem 1987; 35 (2): 161-174.
    • (1987) J Cell Biochem , vol.35 , Issue.2 , pp. 161-174
    • Baulieu, E.E.1
  • 38
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones, and proteotoxicity
    • Hightower LE. Heat shock, stress proteins, chaperones, and proteotoxicity. Cell 1991; 66: 191-197.
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 39
    • 0024524385 scopus 로고
    • The contribution of the N-terminal and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific
    • Bocquel MT, Kumar V, Stricker C, Chambon P, Gronemeyer H. The Contribution of the N-Terminal and C-Terminal Regions of Steroid Receptors to Activation of Transcription Is Both Receptor and Cell-Specific. Nucleic Acids Research 1989; 17(7): 2581-2595.
    • (1989) Nucleic Acids Research , vol.17 , Issue.7 , pp. 2581-2595
    • Bocquel, M.T.1    Kumar, V.2    Stricker, C.3    Chambon, P.4    Gronemeyer, H.5
  • 40
    • 0343179939 scopus 로고
    • Specific association of androgen receptors and estrogen receptors with the nuclear matrix: Summary and perspectives
    • Moudgil VK, ed. Berlin
    • Barrack ER. Specific association of androgen receptors and estrogen receptors with the nuclear matrix: summary and perspectives. In: Moudgil VK, ed. Recent advances in steroid hormone action Walter de Gruijter, Berlin 1987; 85-107.
    • (1987) Recent Advances in Steroid Hormone Action Walter de Gruijter , pp. 85-107
    • Barrack, E.R.1
  • 41
    • 0028914933 scopus 로고
    • Domains of the human androgen receptor and glucocorticoid receptor involved in binding to the nuclear matrix
    • Steensel Bv, Jenster G, Damm K, Brinkmann AO, Driel RV. Domains of the human androgen receptor and glucocorticoid receptor involved in binding to the nuclear matrix. Journal of Cellular Biochemistry 1995; 57: 465-478.
    • (1995) Journal of Cellular Biochemistry , vol.57 , pp. 465-478
    • Steensel, Bv.1    Jenster, G.2    Damm, K.3    Brinkmann, A.O.4    Driel, R.V.5
  • 43
    • 0021711644 scopus 로고
    • Progesterone receptor in the chick oviduct: An immunohistochemical study with antibodies to distinct receptor components
    • Gasc JM, Renoir JM, Radanyi C, Joab I, Tuohimaa P, Baulieu EE. Progesterone receptor in the chick oviduct: an immunohistochemical study with antibodies to distinct receptor components. J Cell Biol 1984; 99: 1193-1201.
    • (1984) J Cell Biol , vol.99 , pp. 1193-1201
    • Gasc, J.M.1    Renoir, J.M.2    Radanyi, C.3    Joab, I.4    Tuohimaa, P.5    Baulieu, E.E.6
  • 44
    • 0022895160 scopus 로고
    • YTaTP. Nuclear origin of progesterone receptor of the chick oviduct cytosol: An immunoelectron microscopic study
    • Isola J. YTaTP. Nuclear origin of progesterone receptor of the chick oviduct cytosol: an immunoelectron microscopic study. Histochemistry 1986; 86: 53-58.
    • (1986) Histochemistry , vol.86 , pp. 53-58
    • Isola, J.1
  • 45
    • 0023131671 scopus 로고
    • PM, YTaTP. Immunoelectron microscopic localization of progesterone receptor in the chick oviduct
    • Isola J. PM,YTaTP. Immunoelectron microscopic localization of progesterone receptor in the chick oviduct. J Steroid Biochem 1987; 26: 19-23.
    • (1987) J Steroid Biochem , vol.26 , pp. 19-23
    • Isola, J.1
  • 46
    • 0025915087 scopus 로고
    • Different immunoelectron microscopic locations of progesterone receptor and hsp90 in chick oviduct epithelial cells
    • Pekki AK. Different immunoelectron microscopic locations of progesterone receptor and hsp90 in chick oviduct epithelial cells. J Histochem Cytochem 1991; 39: 1095-1101.
    • (1991) J Histochem Cytochem , vol.39 , pp. 1095-1101
    • Pekki, A.K.1
  • 47
    • 0026713869 scopus 로고
    • Cooperation of protosignals for nuclear accumulation of estrogen and progesterone receptors
    • Ylikomi T, Bocquel MT, Berry M, Gronemeyer H, Chambon P. Cooperation of protosignals for nuclear accumulation of estrogen and progesterone receptors. EMBO J 1992; 11: 3681-3694.
    • (1992) EMBO J , vol.11 , pp. 3681-3694
    • Ylikomi, T.1    Bocquel, M.T.2    Berry, M.3    Gronemeyer, H.4    Chambon, P.5
  • 48
    • 0024372113 scopus 로고
    • Mechanism of nuclear localization of the progesterone receptor: Evidence for interaction between monomers
    • Guichon-Mantel A, Loosfelt H, Llescop P, Star S, Atger M, Perrot-Applanat M et al. Mechanism of Nuclear Localization of the Progesterone Receptor: Evidence for Interaction Between Monomers. Cell 1989; 57: 1147-1154.
    • (1989) Cell , vol.57 , pp. 1147-1154
    • Guichon-Mantel, A.1    Loosfelt, H.2    Llescop, P.3    Star, S.4    Atger, M.5    Perrot-Applanat, M.6
  • 51
    • 0023585164 scopus 로고
    • Chick oviduct progesterone receptor phosphorylation: Characterization of a copurified kinase and phosphorylation in primary cultures
    • Garcia T, Buchou T, Jung-testas I, Renoir J, Baulieu EE. Chick oviduct progesterone receptor phosphorylation: Characterization of a copurified kinase and phosphorylation in primary cultures. J Steroid Biochem 1987; 27: 227-234.
    • (1987) J Steroid Biochem , vol.27 , pp. 227-234
    • Garcia, T.1    Buchou, T.2    Jung-Testas, I.3    Renoir, J.4    Baulieu, E.E.5
  • 52
  • 53
    • 0024308856 scopus 로고
    • Hormone-dependent regulation of chicken progesterone receptor deoxyribonucleic acid binding and phosphorylation
    • Denner LA, Weigel NL, Schrader WT, Omalley BW. Hormone-Dependent Regulation of Chicken Progesterone Receptor Deoxyribonucleic Acid Binding and Phosphorylation. Endocrinology 1989; 125: 3051-3058.
    • (1989) Endocrinology , vol.125 , pp. 3051-3058
    • Denner, L.A.1    Weigel, N.L.2    Schrader, W.T.3    Omalley, B.W.4
  • 54
    • 0026608982 scopus 로고
    • Chicken progesterone receptor is phosphorylated by a DNA-dependent protein kinase during invitro transcription assays
    • Weigel NL, Carter TH, Schrader WT, Omalley BW. Chicken Progesterone Receptor Is Phosphorylated by a DNA-Dependent Protein Kinase During Invitro Transcription Assays. Molecular Endocrinology 1992; 6: 8-14.
    • (1992) Molecular Endocrinology , vol.6 , pp. 8-14
    • Weigel, N.L.1    Carter, T.H.2    Schrader, W.T.3    Omalley, B.W.4
  • 55
    • 0027509780 scopus 로고
    • Identification of a hormone-dependent phosphorylation site adjacent to the DNA-binding domain of the chicken progesterone receptor
    • Poletti A, Weigel NL. Identification of a Hormone-dependent Phosphorylation Site Adjacent to the DNA-binding Domain of the Chicken Progesterone Receptor. Molecular Endocrinology 1993; 7: 241-246.
    • (1993) Molecular Endocrinology , vol.7 , pp. 241-246
    • Poletti, A.1    Weigel, N.L.2
  • 57
    • 0029041681 scopus 로고
    • Identification of three proline-directed phosphorylation sites in the human androgen receptor
    • Zhou ZX, Kemppainen JA, Wilson EM. Identification of three proline-directed phosphorylation sites in the human androgen receptor. Molecular Endocrinology 1995; 9: 605-615.
    • (1995) Molecular Endocrinology , vol.9 , pp. 605-615
    • Zhou, Z.X.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 59
    • 0025864888 scopus 로고
    • Development and evaluation of an immunoenzymometric assay for the chicken progesterone receptor
    • Blauer MK, Tuohimaa PJ, Vilja PJ. Development and Evaluation of an Immunoenzymometric Assay for the Chicken Progesterone Receptor. Journal of Endocrinology 1991; 129: 189-196.
    • (1991) Journal of Endocrinology , vol.129 , pp. 189-196
    • Blauer, M.K.1    Tuohimaa, P.J.2    Vilja, P.J.3
  • 60
    • 0017325605 scopus 로고
    • Progesterone receptors in the chick oviduct. Determination of the total concentration of binding sites in the cytosol and nuclear fraction and effect of progesterone on their distribution
    • Mester J, Baulieu EE. Progesterone receptors in the chick oviduct. Determination of the total concentration of binding sites in the cytosol and nuclear fraction and effect of progesterone on their distribution. Eur J Biochem 1977; 72: 405-414.
    • (1977) Eur J Biochem , vol.72 , pp. 405-414
    • Mester, J.1    Baulieu, E.E.2
  • 61
    • 0020484080 scopus 로고
    • Protease substrates inhibit binding of 3H-R5020 to the G-fragment in chick oviduct cytosol
    • Baker ME, Kimlinger WR. Protease substrates inhibit binding of 3H-R5020 to the G-fragment in chick oviduct cytosol. Biochem Biophys Res Commun 1982; 108 (3): 1067-1073.
    • (1982) Biochem Biophys Res Commun , vol.108 , Issue.3 , pp. 1067-1073
    • Baker, M.E.1    Kimlinger, W.R.2
  • 62
    • 0020385424 scopus 로고
    • Interaction of serine protease inhibitors and substrates with human uterine estrogen receptor
    • Lukola A, Punnonen R. Interaction of serine protease inhibitors and substrates with human uterine estrogen receptor. Biochem Biophys Res Communic 1982; 108: 822-.
    • (1982) Biochem Biophys Res Communic , vol.108 , pp. 822
    • Lukola, A.1    Punnonen, R.2
  • 64
    • 0026625044 scopus 로고
    • Induction of avidin messenger ribonucleic acid in the chick oviduct by progesterone and other steroids
    • Kunnas TA, Joensuu TK, Viitala KK, Sopanen P, Tuohimaa P, Kulomaa MS. Induction of Avidin Messenger Ribonucleic Acid in the Chick Oviduct by Progesterone and Other Steroids. Endocrinology 1992; 130: 3421-3426.
    • (1992) Endocrinology , vol.130 , pp. 3421-3426
    • Kunnas, T.A.1    Joensuu, T.K.2    Viitala, K.K.3    Sopanen, P.4    Tuohimaa, P.5    Kulomaa, M.S.6
  • 65
    • 0025155251 scopus 로고
    • The human estrogen receptor has transcriptional activator and repressor functions in the absence of ligand
    • Tzuckerman M, Zhang XK, Hermann T, Wills KN, Graupner K, Pfahl M. The Human Estrogen Receptor Has Transcriptional Activator And Repressor Functions In The Absence Of Ligand. New-Biol 1990; 2: 613-620.
    • (1990) New-biol , vol.2 , pp. 613-620
    • Tzuckerman, M.1    Zhang, X.K.2    Hermann, T.3    Wills, K.N.4    Graupner, K.5    Pfahl, M.6
  • 68
    • 0025297904 scopus 로고
    • Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate
    • Bresnick EH, John S, Berard DS, LeFebvre P, Hager GL. Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate. Proc Natl Acad Sci 1990; 87: 3977-3981.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 3977-3981
    • Bresnick, E.H.1    John, S.2    Berard, D.S.3    LeFebvre, P.4    Hager, G.L.5
  • 69
    • 0023000008 scopus 로고
    • Steroid-free glucorticoid reseptor binds specifically to mouse mammary tumor virus DNA
    • Willmann T, Beato M. Steroid-free glucorticoid reseptor binds specifically to mouse mammary tumor virus DNA. Nature 1986; 324: 688-691.
    • (1986) Nature , vol.324 , pp. 688-691
    • Willmann, T.1    Beato, M.2
  • 71
  • 73
    • 0027383287 scopus 로고
    • Plasma concentrations of phyto-oestrogens in japanese men
    • Adlercreutz H, Markkanen H, Watanabe S. Plasma concentrations of phyto-oestrogens in japanese men. Lancet 1993; 342: 1209-1210.
    • (1993) Lancet , vol.342 , pp. 1209-1210
    • Adlercreutz, H.1    Markkanen, H.2    Watanabe, S.3
  • 74
    • 0027994209 scopus 로고
    • Stimulation of androgen-regulated transactivation by modulators of protein phosphorylation
    • Ikonen T, Palvimo JJ, Kallio PJ, Reinikainen P, Janne OA. Stimulation of androgen-regulated transactivation by modulators of protein phosphorylation. Endocrinology 1994; 135: 1359-1366.
    • (1994) Endocrinology , vol.135 , pp. 1359-1366
    • Ikonen, T.1    Palvimo, J.J.2    Kallio, P.J.3    Reinikainen, P.4    Janne, O.A.5
  • 75
    • 0029038986 scopus 로고
    • Analysis of estrogen receptor function in Vitro reveals three distinct classes of antiestrogens
    • McDonnell DP, Clemm DL, Hermann T, Goldman ME, Pike JW. Analysis of estrogen receptor function in Vitro reveals three distinct classes of antiestrogens. Molecular Endocrinology 1995; 9: 659-669.
    • (1995) Molecular Endocrinology , vol.9 , pp. 659-669
    • McDonnell, D.P.1    Clemm, D.L.2    Hermann, T.3    Goldman, M.E.4    Pike, J.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.