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Volumn 2, Issue , 2004, Pages 1082-1092

Estrogen, Signal Transduction, and Systemic Lupus Erythematosus: Molecular Mechanisms

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EID: 79953292166     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012440905-7/50375-3     Document Type: Chapter
Times cited : (1)

References (154)
  • 2
    • 84873764137 scopus 로고
    • Systemic lupus erythematosus: review of the literature and clinical analysis of 138 cases
    • Harvey AM, Shulman LE, Tumulty PA Systemic lupus erythematosus: review of the literature and clinical analysis of 138 cases. Medicine 1954, 33:291-437.
    • (1954) Medicine , vol.33 , pp. 291-437
    • Harvey, A.M.1    Shulman, L.E.2    Tumulty, P.A.3
  • 3
    • 0004949839 scopus 로고
    • Epidemiology of systemic lupus erythematosus
    • Churchill Livingstone, New York, R.G. Lahita (Ed.)
    • Hochberg MC Epidemiology of systemic lupus erythematosus. Systemic Lupus Erythematosus 1992, 103-117. Churchill Livingstone, New York. R.G. Lahita (Ed.).
    • (1992) Systemic Lupus Erythematosus , pp. 103-117
    • Hochberg, M.C.1
  • 4
    • 0030007880 scopus 로고    scopus 로고
    • The connective tissue diseases and the overall influence of gender
    • Lahita RG The connective tissue diseases and the overall influence of gender. Int J Fertil Menopausal Stud. 1996, 41:156-165.
    • (1996) Int J Fertil Menopausal Stud. , vol.41 , pp. 156-165
    • Lahita, R.G.1
  • 5
    • 0026571946 scopus 로고
    • The importance of estrogens in systemic lupus erythematosus
    • Lahita RG The importance of estrogens in systemic lupus erythematosus. Clin Immunol Immunopathol 1992, 63:17-18.
    • (1992) Clin Immunol Immunopathol , vol.63 , pp. 17-18
    • Lahita, R.G.1
  • 6
    • 0035654219 scopus 로고    scopus 로고
    • Sex hormones in the pathogenesis of systemic lupus erythematosus
    • McMurray RW Sex hormones in the pathogenesis of systemic lupus erythematosus. Frontiers Biosci 2001, 6:193-206.
    • (2001) Frontiers Biosci , vol.6 , pp. 193-206
    • McMurray, R.W.1
  • 7
    • 0035022926 scopus 로고    scopus 로고
    • Membrane estrogen and glucocorticoid receptors-implications for hormonal control of immune function and autoimmunity
    • Watson CS, Gametchu B Membrane estrogen and glucocorticoid receptors-implications for hormonal control of immune function and autoimmunity. Int Immunopharmacol 2001, 1:1049-1063.
    • (2001) Int Immunopharmacol , vol.1 , pp. 1049-1063
    • Watson, C.S.1    Gametchu, B.2
  • 8
    • 0035962678 scopus 로고    scopus 로고
    • Evidence for estradiol-induced apoptosis and dysregulated T cell maturation in the thymus
    • Okasha SA, Ryu S, Do Y, et al. Evidence for estradiol-induced apoptosis and dysregulated T cell maturation in the thymus. Toxicology 2001, 163:49-62.
    • (2001) Toxicology , vol.163 , pp. 49-62
    • Okasha, S.A.1    Ryu, S.2    Do, Y.3
  • 9
    • 0034844610 scopus 로고    scopus 로고
    • 17-β-Estradiol alters Jurkat lymphocyte cell cycling and induces apoptosis through suppression of Bcl-2 and cyclin A
    • Jenkins JK, Suwannaroj S, Elbourne KB, et al. 17-β-Estradiol alters Jurkat lymphocyte cell cycling and induces apoptosis through suppression of Bcl-2 and cyclin A. Int Immunopharmacol 2001, 1:1897-1911.
    • (2001) Int Immunopharmacol , vol.1 , pp. 1897-1911
    • Jenkins, J.K.1    Suwannaroj, S.2    Elbourne, K.B.3
  • 10
    • 0035036345 scopus 로고    scopus 로고
    • Gender differences in autoimmunity: molecular basis for estrogen effects in systemic lupus erythematosus
    • Rider V, Abdou NI Gender differences in autoimmunity: molecular basis for estrogen effects in systemic lupus erythematosus. Int Immunopharmacol 2001, 1:1009-1024.
    • (2001) Int Immunopharmacol , vol.1 , pp. 1009-1024
    • Rider, V.1    Abdou, N.I.2
  • 11
    • 0034646432 scopus 로고    scopus 로고
    • Estrogen up-regulates Bcl-2 and blocks tolerance induction of naïve B cells
    • Bynoe MS, Grimaldi CM, Diamond B Estrogen up-regulates Bcl-2 and blocks tolerance induction of naïve B cells. Proc Natl Acad Sci USA 2000, 97:2703-2708.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2703-2708
    • Bynoe, M.S.1    Grimaldi, C.M.2    Diamond, B.3
  • 12
    • 0002895241 scopus 로고    scopus 로고
    • Overview of cellular immune function in systemic lupus erythematosus
    • Academic Press, New York, R.G. Lahita (Ed.)
    • Tsokos GC Overview of cellular immune function in systemic lupus erythematosus. Systemic Lupus Erythematosus 1999, 17-54. Academic Press, New York. R.G. Lahita (Ed.).
    • (1999) Systemic Lupus Erythematosus , pp. 17-54
    • Tsokos, G.C.1
  • 14
    • 0033755567 scopus 로고    scopus 로고
    • Molecular aberrations in human systemic lupus erythematosus
    • Tsokos GC, Kammer GM Molecular aberrations in human systemic lupus erythematosus. Mol Med Today 2000, 6:418-424.
    • (2000) Mol Med Today , vol.6 , pp. 418-424
    • Tsokos, G.C.1    Kammer, G.M.2
  • 15
    • 0028288510 scopus 로고
    • Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes
    • Casciola-Rosen LA, Anhalt G, Rosen A Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes. J Exp Med. 1994, 179:1317-1330.
    • (1994) J Exp Med. , vol.179 , pp. 1317-1330
    • Casciola-Rosen, L.A.1    Anhalt, G.2    Rosen, A.3
  • 16
    • 0036560022 scopus 로고    scopus 로고
    • Abnormal T cell signal transduction in systemic lupus erythematosus
    • Kammer GM, Perl A, Richardson BC, et al. Abnormal T cell signal transduction in systemic lupus erythematosus. Arthritis Rheum. 2002, 46:1139-1154.
    • (2002) Arthritis Rheum. , vol.46 , pp. 1139-1154
    • Kammer, G.M.1    Perl, A.2    Richardson, B.C.3
  • 18
    • 0029862164 scopus 로고    scopus 로고
    • Increased expression of CD40 ligand on systemic lupus erythematosus lymphocytes
    • Koshy M, Berger D, Crow MK Increased expression of CD40 ligand on systemic lupus erythematosus lymphocytes. J Clin Invest 1996, 98:826-837.
    • (1996) J Clin Invest , vol.98 , pp. 826-837
    • Koshy, M.1    Berger, D.2    Crow, M.K.3
  • 19
    • 0015972362 scopus 로고
    • A depression of cell-mediated immunity to measles antigen in patients with systemic lupus etythematosus
    • Utermohlen V, Winfield JB, Zabriskie JB, et al. A depression of cell-mediated immunity to measles antigen in patients with systemic lupus etythematosus. J Exp Med. 1974, 139:1019-1024.
    • (1974) J Exp Med. , vol.139 , pp. 1019-1024
    • Utermohlen, V.1    Winfield, J.B.2    Zabriskie, J.B.3
  • 20
    • 0026741293 scopus 로고
    • Phenotypic and functional similarities between 5-azacytidine-treated T cells and a T cell subset in patients with active systemic lupus erythematosus
    • Richardson BC, Strahler JR, Pivirotto TS, et al. Phenotypic and functional similarities between 5-azacytidine-treated T cells and a T cell subset in patients with active systemic lupus erythematosus. Arthritis Rheum. 1992, 35:647-662.
    • (1992) Arthritis Rheum. , vol.35 , pp. 647-662
    • Richardson, B.C.1    Strahler, J.R.2    Pivirotto, T.S.3
  • 21
    • 0028063746 scopus 로고
    • Lymphocyte function-associated antigen 1 overexpression and T cell autoreactivity
    • Richardson BC, Powers D, Hooper F, et al. Lymphocyte function-associated antigen 1 overexpression and T cell autoreactivity. Arthritis Rheum. 1994, 37:1363-1372.
    • (1994) Arthritis Rheum. , vol.37 , pp. 1363-1372
    • Richardson, B.C.1    Powers, D.2    Hooper, F.3
  • 22
    • 0023743861 scopus 로고
    • Activated T lymphocytes in the peripheral blood of patients with systemic lupus erythematosus induce B cells to produce immunoglobulin
    • Inghirami G, Simon J, Balow JE, et al. Activated T lymphocytes in the peripheral blood of patients with systemic lupus erythematosus induce B cells to produce immunoglobulin. Clin Exp Rheumatol. 1988, 6:269-276.
    • (1988) Clin Exp Rheumatol. , vol.6 , pp. 269-276
    • Inghirami, G.1    Simon, J.2    Balow, J.E.3
  • 23
    • 0033509782 scopus 로고    scopus 로고
    • High prevalence of T cell type I protein kinase A deficiency in systemic lupus erythematosus
    • Kammer GM High prevalence of T cell type I protein kinase A deficiency in systemic lupus erythematosus. Arthritis Rheum. 1999, 42:1458-1465.
    • (1999) Arthritis Rheum. , vol.42 , pp. 1458-1465
    • Kammer, G.M.1
  • 24
    • 0009484670 scopus 로고    scopus 로고
    • Cytokines in the pathogenesis of systemic lupus erythematosus
    • Lippincott Williams & Wilkins, Philadelphia, D.J. Wallace, B.H. Hahn (Eds.)
    • Froncek MJ, Horwitz DA Cytokines in the pathogenesis of systemic lupus erythematosus. Dubois' Lupus Erythematosus 2002, 187-204. Lippincott Williams & Wilkins, Philadelphia. D.J. Wallace, B.H. Hahn (Eds.).
    • (2002) Dubois' Lupus Erythematosus , pp. 187-204
    • Froncek, M.J.1    Horwitz, D.A.2
  • 25
    • 0033053103 scopus 로고    scopus 로고
    • Circulating levels of β-chemokines in systemic lupus erythematosus
    • Kaneko H, Ogasawara H, Naito T, et al. Circulating levels of β-chemokines in systemic lupus erythematosus. J Rheumatol. 1999, 26:568-573.
    • (1999) J Rheumatol. , vol.26 , pp. 568-573
    • Kaneko, H.1    Ogasawara, H.2    Naito, T.3
  • 26
    • 0029913381 scopus 로고    scopus 로고
    • Hyperexpression of CD40 ligand by B and T cells in human lupus and its role in pathogenic autoantibody production
    • Desai-Mehta A, Lu LJ, Ramsey-Goldmarr R, et al. Hyperexpression of CD40 ligand by B and T cells in human lupus and its role in pathogenic autoantibody production. J Clin Invest. 1996, 97:2063-2073.
    • (1996) J Clin Invest. , vol.97 , pp. 2063-2073
    • Desai-Mehta, A.1    Lu, L.J.2    Ramsey-Goldmarr, R.3
  • 27
    • 0005702987 scopus 로고    scopus 로고
    • Immune complexes
    • Human Press, Totowa, NJ, G.C. Tsokos (Ed.)
    • Wener MH Immune complexes. Principles of Molecular Rheumatology 2000, 127-144. Human Press, Totowa, NJ. G.C. Tsokos (Ed.).
    • (2000) Principles of Molecular Rheumatology , pp. 127-144
    • Wener, M.H.1
  • 28
    • 0032493059 scopus 로고    scopus 로고
    • Antibodies to DNA
    • Hahn BH Antibodies to DNA. N Engl J Med. 1998, 338:1359-1368.
    • (1998) N Engl J Med. , vol.338 , pp. 1359-1368
    • Hahn, B.H.1
  • 29
    • 0025248398 scopus 로고
    • T lymphocyte immune dysfunctions in systemic lupus erythematosus
    • Kammer GM, Stein RL T lymphocyte immune dysfunctions in systemic lupus erythematosus. J Lab Clin Med. 1990, 115:273-282.
    • (1990) J Lab Clin Med. , vol.115 , pp. 273-282
    • Kammer, G.M.1    Stein, R.L.2
  • 30
    • 0020444252 scopus 로고
    • Abnormal adenosine-induced immunosuppression and caMP metabolism in T lymphocytes of patients with systemic lupus erythematosus
    • Mandler R, Birch RE, Polmar S, et al. Abnormal adenosine-induced immunosuppression and caMP metabolism in T lymphocytes of patients with systemic lupus erythematosus. Proc Natl Acad Sci USA 1982, 79:7542-7546.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7542-7546
    • Mandler, R.1    Birch, R.E.2    Polmar, S.3
  • 31
    • 0032036481 scopus 로고    scopus 로고
    • Altered pattern of TCR/CD3-mediated protein-tyrosyl phosphorylation in T cells from patients with systemic lupus erythematosus-Deficient expression of the T cell receptor zeta chain
    • Liossis SNC, Ding XZ, Dennis GJ, et al. Altered pattern of TCR/CD3-mediated protein-tyrosyl phosphorylation in T cells from patients with systemic lupus erythematosus-Deficient expression of the T cell receptor zeta chain. J Clin Invest. 1998, 101:1448-1457.
    • (1998) J Clin Invest. , vol.101 , pp. 1448-1457
    • Liossis, S.N.C.1    Ding, X.Z.2    Dennis, G.J.3
  • 32
    • 0031840785 scopus 로고    scopus 로고
    • TCRβ chain lacking exon 7 in two patients with systemic lupus erythematosus
    • Takeuchi T, Tsuzaka K, Pang M, et al. TCRβ chain lacking exon 7 in two patients with systemic lupus erythematosus. Int Immunol. 1998, 10:911-921.
    • (1998) Int Immunol. , vol.10 , pp. 911-921
    • Takeuchi, T.1    Tsuzaka, K.2    Pang, M.3
  • 33
    • 0033494977 scopus 로고    scopus 로고
    • Diminished levels of T cell receptor zeta chains in peripheral blood T lymphocytes from patients with systemic lupus erythematosus
    • Brundula V, Rivas LJ, Blasini AM, et al. Diminished levels of T cell receptor zeta chains in peripheral blood T lymphocytes from patients with systemic lupus erythematosus. Arthritis Rheum. 1999, 42:1908-1916.
    • (1999) Arthritis Rheum. , vol.42 , pp. 1908-1916
    • Brundula, V.1    Rivas, L.J.2    Blasini, A.M.3
  • 34
    • 0033136320 scopus 로고    scopus 로고
    • Diminished levels of protein kinase A RIα and RIβ transcripts and proteins in systemic lupus erythematosus T lymphocytes
    • Laxminarayana D, Khan IU, Mishra N, et al. Diminished levels of protein kinase A RIα and RIβ transcripts and proteins in systemic lupus erythematosus T lymphocytes. J Immunol. 1999, 162:5639-5648.
    • (1999) J Immunol. , vol.162 , pp. 5639-5648
    • Laxminarayana, D.1    Khan, I.U.2    Mishra, N.3
  • 35
    • 0034519709 scopus 로고    scopus 로고
    • Impaired translational response and increased protein kinase PKR expression in T cells from lupus patients
    • Grolleau A, Kaplan MJ, Hanash SM, et al. Impaired translational response and increased protein kinase PKR expression in T cells from lupus patients. J Clin Invest. 2000, 106:1561-1568.
    • (2000) J Clin Invest. , vol.106 , pp. 1561-1568
    • Grolleau, A.1    Kaplan, M.J.2    Hanash, S.M.3
  • 36
    • 0029164734 scopus 로고
    • TCR/CD3 complex-mediated signal transduction pathway in T cells and T cell lines from patients with systemic lupus erythematosus
    • Vassilopoulos D, Kovacs B, Tsokos GC TCR/CD3 complex-mediated signal transduction pathway in T cells and T cell lines from patients with systemic lupus erythematosus. J Immunol. 1995, 155:2269-2281.
    • (1995) J Immunol. , vol.155 , pp. 2269-2281
    • Vassilopoulos, D.1    Kovacs, B.2    Tsokos, G.C.3
  • 37
    • 0036161789 scopus 로고    scopus 로고
    • Mitochondrial hyper-polarization and ATP depletion in patients with systemic lupus erythematosus
    • Gergely P, Grossman C, Niland B, et al. Mitochondrial hyper-polarization and ATP depletion in patients with systemic lupus erythematosus. Arthritis Rheum. 2002, 46:175-190.
    • (2002) Arthritis Rheum. , vol.46 , pp. 175-190
    • Gergely, P.1    Grossman, C.2    Niland, B.3
  • 38
    • 0035096761 scopus 로고    scopus 로고
    • Decreased ras-mitogen-activated protein kinase signaling may cause DNA hypomethylation in T lymphocytes from lupus patients
    • Deng C, Kaplan MJ, Yang J, et al. Decreased ras-mitogen-activated protein kinase signaling may cause DNA hypomethylation in T lymphocytes from lupus patients. Arthritis Rheum 2001, 44:397-407.
    • (2001) Arthritis Rheum , vol.44 , pp. 397-407
    • Deng, C.1    Kaplan, M.J.2    Yang, J.3
  • 39
    • 0001464486 scopus 로고
    • Basic guides to the mechanism of estrogen action
    • Jensen EV, Jacobson HI Basic guides to the mechanism of estrogen action. Recent Prog Horm Res. 1962, 18:387-414.
    • (1962) Recent Prog Horm Res. , vol.18 , pp. 387-414
    • Jensen, E.V.1    Jacobson, H.I.2
  • 40
    • 0001063332 scopus 로고
    • Cloning of the human estrogen receptor cDNA
    • Walter P, Green S, Greene G, et al. Cloning of the human estrogen receptor cDNA. Proc Natl Acad Sci USA 1985, 82:7889-7893.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7889-7893
    • Walter, P.1    Green, S.2    Greene, G.3
  • 41
    • 0022653964 scopus 로고
    • Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A
    • Green S, Walter P, Kumar V, et al. Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature 1986, 320:134-139.
    • (1986) Nature , vol.320 , pp. 134-139
    • Green, S.1    Walter, P.2    Kumar, V.3
  • 42
    • 0022473069 scopus 로고
    • Sequence and expression of human estrogen receptor complementary DNA
    • Greene GL, Gilna P, Waterfield M, et al. Sequence and expression of human estrogen receptor complementary DNA. Science. 1986, 231:1150-1154.
    • (1986) Science. , vol.231 , pp. 1150-1154
    • Greene, G.L.1    Gilna, P.2    Waterfield, M.3
  • 43
    • 0030579801 scopus 로고    scopus 로고
    • Cloning of a novel estrogen receptor expressed in rat prostate and ovary
    • Kuiper GGJM, Enmark E, Pelto-Huikko M, et al. Cloning of a novel estrogen receptor expressed in rat prostate and ovary. Proc Natl Acad Sci USA 1996, 93:5925-5930.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5925-5930
    • Kuiper, G.G.J.M.1    Enmark, E.2    Pelto-Huikko, M.3
  • 44
    • 0033386954 scopus 로고    scopus 로고
    • Estrogen receptor β-a new dimension in estrogen mechanism of action
    • Gustafsson JA Estrogen receptor β-a new dimension in estrogen mechanism of action. J Endocrinol. 1999, 163:379-383.
    • (1999) J Endocrinol. , vol.163 , pp. 379-383
    • Gustafsson, J.A.1
  • 45
    • 0030593681 scopus 로고    scopus 로고
    • ER beta: identification and characterization of a novel human estrogen receptor
    • Mosselman S, Polman J, Dijkema R ER beta: identification and characterization of a novel human estrogen receptor. FEBS Lett. 1996, 392:49-53.
    • (1996) FEBS Lett. , vol.392 , pp. 49-53
    • Mosselman, S.1    Polman, J.2    Dijkema, R.3
  • 46
    • 0031838044 scopus 로고    scopus 로고
    • Peripheral blood T cells and monocytes and B cell lines derived from patients with lupus express estrogen receptor transcripts similar to those of normal cells
    • Suenaga R, Evans MJ, Mitamura K, et al. Peripheral blood T cells and monocytes and B cell lines derived from patients with lupus express estrogen receptor transcripts similar to those of normal cells. J Rheumatol. 1998, 25:1305-1312.
    • (1998) J Rheumatol. , vol.25 , pp. 1305-1312
    • Suenaga, R.1    Evans, M.J.2    Mitamura, K.3
  • 48
    • 0021017421 scopus 로고
    • Sex steroid receptors in peripheral T cells: absence of androgen receptors and restriction of estrogen receptors to OKT8-positive cells
    • Cohen JHM, Danel L, Cordier G, et al. Sex steroid receptors in peripheral T cells: absence of androgen receptors and restriction of estrogen receptors to OKT8-positive cells. J Immunol. 1983, 131:2767-2771.
    • (1983) J Immunol. , vol.131 , pp. 2767-2771
    • Cohen, J.H.M.1    Danel, L.2    Cordier, G.3
  • 49
    • 0023774948 scopus 로고
    • Oestrogen and human T lymphocytes: Presence of specific receptors in the T-suppressor/cytotoxic subset
    • Stimson WH Oestrogen and human T lymphocytes: Presence of specific receptors in the T-suppressor/cytotoxic subset. Scand J Immunol. 1988, 28:345-350.
    • (1988) Scand J Immunol. , vol.28 , pp. 345-350
    • Stimson, W.H.1
  • 50
    • 0033188163 scopus 로고    scopus 로고
    • Estrogen in autoimmunity: expression of estrogen receptors in thymic and autoimmune T cells
    • Tornwall J, Carey AB, Fox RI, et al. Estrogen in autoimmunity: expression of estrogen receptors in thymic and autoimmune T cells. J Gend Specif Med. 1999, 2:33-40.
    • (1999) J Gend Specif Med. , vol.2 , pp. 33-40
    • Tornwall, J.1    Carey, A.B.2    Fox, R.I.3
  • 51
    • 0034815173 scopus 로고    scopus 로고
    • The role of the Fas/Fas ligand system in estrogen-induced thymic alteration
    • Mor G, Munoz A, Redlinger R, et al. The role of the Fas/Fas ligand system in estrogen-induced thymic alteration. Am J Reprod Immunol. 2001, 46:298-307.
    • (2001) Am J Reprod Immunol. , vol.46 , pp. 298-307
    • Mor, G.1    Munoz, A.2    Redlinger, R.3
  • 52
    • 0035043327 scopus 로고    scopus 로고
    • In vitro-activated human lupus T cells express normal estrogen receptor proteins which bind to the estrogen response element
    • Suenaga R, Rider V, Evans MJ, et al. In vitro-activated human lupus T cells express normal estrogen receptor proteins which bind to the estrogen response element. Lupus. 2001, 10:116-122.
    • (2001) Lupus. , vol.10 , pp. 116-122
    • Suenaga, R.1    Rider, V.2    Evans, M.J.3
  • 53
    • 0032481256 scopus 로고    scopus 로고
    • The complete primary structure of human estrogen receptor beta (hERbeta) and its heterodimerization with ER alpha in vivo and in vitro
    • Ogawa S, Inoue S, Watanabe T, et al. The complete primary structure of human estrogen receptor beta (hERbeta) and its heterodimerization with ER alpha in vivo and in vitro. Biochem Biophys Res Commun. 1998, 243:122-126.
    • (1998) Biochem Biophys Res Commun. , vol.243 , pp. 122-126
    • Ogawa, S.1    Inoue, S.2    Watanabe, T.3
  • 54
    • 0032499611 scopus 로고    scopus 로고
    • Cloning and characterization of humna estrogen receptor beta isoforms
    • Moore JT, McKee DD, Slentz-Kesler K, et al. Cloning and characterization of humna estrogen receptor beta isoforms. Biochem Biophys Res Commun. 1998, 247:75-78.
    • (1998) Biochem Biophys Res Commun. , vol.247 , pp. 75-78
    • Moore, J.T.1    McKee, D.D.2    Slentz-Kesler, K.3
  • 55
    • 0031790490 scopus 로고    scopus 로고
    • A novel human estrogen receptor beta: identification and functional analysis of additional N-terminal amino acids
    • Bhat RA, Harnish DC, Stevis PE, et al. A novel human estrogen receptor beta: identification and functional analysis of additional N-terminal amino acids. J Steroid Biochem Mol Biol. 1998, 67:233-240.
    • (1998) J Steroid Biochem Mol Biol. , vol.67 , pp. 233-240
    • Bhat, R.A.1    Harnish, D.C.2    Stevis, P.E.3
  • 56
    • 0032495993 scopus 로고    scopus 로고
    • A novel isoform of rat estrogen receptor beta with 18 amino acid insertion in the ligand binding domain as a putative dominant negative regulation of estrogen action
    • Maruyama K, Endoh H, Sasaki-Iwaoka H, et al. A novel isoform of rat estrogen receptor beta with 18 amino acid insertion in the ligand binding domain as a putative dominant negative regulation of estrogen action. Biochem Biophys Res Commun. 1998, 246:142-147.
    • (1998) Biochem Biophys Res Commun. , vol.246 , pp. 142-147
    • Maruyama, K.1    Endoh, H.2    Sasaki-Iwaoka, H.3
  • 57
    • 0031791153 scopus 로고    scopus 로고
    • Identification of estrogen receptor beta2, a functional variant of estrogen receptor beta expressed in normal rat tissues
    • Petersen DN, Tkalcevic GT, Koza-Taylor PH, et al. Identification of estrogen receptor beta2, a functional variant of estrogen receptor beta expressed in normal rat tissues. Endocrinology. 1998, 139:1082-1092.
    • (1998) Endocrinology. , vol.139 , pp. 1082-1092
    • Petersen, D.N.1    Tkalcevic, G.T.2    Koza-Taylor, P.H.3
  • 58
    • 0029197511 scopus 로고
    • Structure and function of estrogen receptors
    • Parker MG Structure and function of estrogen receptors. Vitam Horm. 1995, 51:267-287.
    • (1995) Vitam Horm. , vol.51 , pp. 267-287
    • Parker, M.G.1
  • 59
    • 0032813510 scopus 로고    scopus 로고
    • Oestrogen receptors-an overview
    • Enmark E, Gustafsson JA Oestrogen receptors-an overview. J Int Med. 1999, 246:133-138.
    • (1999) J Int Med. , vol.246 , pp. 133-138
    • Enmark, E.1    Gustafsson, J.A.2
  • 60
    • 0027154780 scopus 로고
    • RARs and RXRs: evidence for two autonomous transactivation functions (AF-1 and AF-2) and heterodimerization in vivo
    • Nagpal S, Friant S, Nakshatri H, et al. RARs and RXRs: evidence for two autonomous transactivation functions (AF-1 and AF-2) and heterodimerization in vivo. EMBO J. 1993, 12:2349-2360.
    • (1993) EMBO J. , vol.12 , pp. 2349-2360
    • Nagpal, S.1    Friant, S.2    Nakshatri, H.3
  • 61
    • 0024814733 scopus 로고
    • Cooperative binding of estrogen receptor in imperfect estrogen-responsive DNA elements correlates with their synergistic hormone-dependent enhancer activity
    • Martinez E, Wahli W Cooperative binding of estrogen receptor in imperfect estrogen-responsive DNA elements correlates with their synergistic hormone-dependent enhancer activity. EMBO J. 1989, 8:3781-3791.
    • (1989) EMBO J. , vol.8 , pp. 3781-3791
    • Martinez, E.1    Wahli, W.2
  • 62
    • 0033053616 scopus 로고    scopus 로고
    • Dominant activity of activation function 1 (AF-1) and differential stoichiometric requirements for AF-1 and -2 in the estrogen receptor alpha-beta heterodimeric complex
    • Tremblay GB, Tremblay A, Labrie F, et al. Dominant activity of activation function 1 (AF-1) and differential stoichiometric requirements for AF-1 and -2 in the estrogen receptor alpha-beta heterodimeric complex. Mol Cell Biol. 1999, 19:1919-1927.
    • (1999) Mol Cell Biol. , vol.19 , pp. 1919-1927
    • Tremblay, G.B.1    Tremblay, A.2    Labrie, F.3
  • 63
    • 0032548797 scopus 로고    scopus 로고
    • Cross-inhibition of both estrogen receptor alpha and beta pathways by each dominant-negative mutant
    • Ogawa S, Inoue S, Orimo A, et al. Cross-inhibition of both estrogen receptor alpha and beta pathways by each dominant-negative mutant. FEBS Lett. 1998, 423:129-132.
    • (1998) FEBS Lett. , vol.423 , pp. 129-132
    • Ogawa, S.1    Inoue, S.2    Orimo, A.3
  • 64
    • 0026504910 scopus 로고
    • A far upstream estrogen response element of the ovalbumin gene contains several half-palindromic 5'-TGACC-3' motifs acting synergistically
    • Kato S, Tora L, Yamauchi J, et al. A far upstream estrogen response element of the ovalbumin gene contains several half-palindromic 5'-TGACC-3' motifs acting synergistically. Cell. 1992, 68:731-742.
    • (1992) Cell. , vol.68 , pp. 731-742
    • Kato, S.1    Tora, L.2    Yamauchi, J.3
  • 65
    • 0033559831 scopus 로고    scopus 로고
    • Interaction of human estrogen receptors α and β with the same naturally occurring estrogen response elements
    • Hyder SM, Chiappetta C, Stancel GM Interaction of human estrogen receptors α and β with the same naturally occurring estrogen response elements. Biochem Pharmacol. 1999, 57:597-601.
    • (1999) Biochem Pharmacol. , vol.57 , pp. 597-601
    • Hyder, S.M.1    Chiappetta, C.2    Stancel, G.M.3
  • 66
    • 0031043390 scopus 로고    scopus 로고
    • Cloning, chromosomal localization, and functional analysis of the murne estrogen receptor beta
    • Tremblay GB, Tremblay A, Copeland NG, et al. Cloning, chromosomal localization, and functional analysis of the murne estrogen receptor beta. Mol Endocrinol. 1997, 11:353-365.
    • (1997) Mol Endocrinol. , vol.11 , pp. 353-365
    • Tremblay, G.B.1    Tremblay, A.2    Copeland, N.G.3
  • 67
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • Tora L, White J, Brou C, et al. The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell. 1989, 59:477-487.
    • (1989) Cell. , vol.59 , pp. 477-487
    • Tora, L.1    White, J.2    Brou, C.3
  • 68
    • 0034717277 scopus 로고    scopus 로고
    • P300 mediates functional synergism between AF-1 and AF-2 of estrogen receptor α and β by interacting directly with the N-terminal A/B domains
    • Kobayashi Y, Kitamoto T, Masuhiro Y, et al. p300 mediates functional synergism between AF-1 and AF-2 of estrogen receptor α and β by interacting directly with the N-terminal A/B domains. J Biol Chem. 2000, 275:15645-15651.
    • (2000) J Biol Chem. , vol.275 , pp. 15645-15651
    • Kobayashi, Y.1    Kitamoto, T.2    Masuhiro, Y.3
  • 69
    • 0025223160 scopus 로고
    • Solution structure of the DNA-binding domain of the oestrogen receptor
    • Schwabe JW, Neuhaus D, Rhodes D Solution structure of the DNA-binding domain of the oestrogen receptor. Nature. 1990, 348:458-461.
    • (1990) Nature. , vol.348 , pp. 458-461
    • Schwabe, J.W.1    Neuhaus, D.2    Rhodes, D.3
  • 70
    • 0027365669 scopus 로고
    • The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements
    • Schwabe JW, Chapman L, Finch JT, et al. The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell. 1993, 75:567-578.
    • (1993) Cell. , vol.75 , pp. 567-578
    • Schwabe, J.W.1    Chapman, L.2    Finch, J.T.3
  • 71
    • 0030822421 scopus 로고    scopus 로고
    • Dimerizing the estrogen receptor DNA binding domain enhances binding to estrogen response elements
    • Kuntz MA, Shapiro DJ Dimerizing the estrogen receptor DNA binding domain enhances binding to estrogen response elements. J Biol Chem. 1997, 272:27949-27956.
    • (1997) J Biol Chem. , vol.272 , pp. 27949-27956
    • Kuntz, M.A.1    Shapiro, D.J.2
  • 72
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers
    • Glass CK Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers. Endocr Rev. 1994, 15:391-407.
    • (1994) Endocr Rev. , vol.15 , pp. 391-407
    • Glass, C.K.1
  • 73
    • 0030667676 scopus 로고    scopus 로고
    • Molecular basis of agonism and antagonism in the oestrogen receptor
    • Brzozowski AM, Pike AC, Dauter Z, et al. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 1997, 389:753-758.
    • (1997) Nature. , vol.389 , pp. 753-758
    • Brzozowski, A.M.1    Pike, A.C.2    Dauter, Z.3
  • 74
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau AK, Barstad D, Loria PM, et al. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 1998, 95:927-937.
    • (1998) Cell. , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3
  • 75
    • 0342616837 scopus 로고    scopus 로고
    • A canonical structure for the ligand-binding domain of nuclear receptors
    • Wurtz JM, Bourguet W, Renaud JP, et al. A canonical structure for the ligand-binding domain of nuclear receptors. Nat Struc Biol. 1996, 3:206.
    • (1996) Nat Struc Biol. , vol.3 , pp. 206
    • Wurtz, J.M.1    Bourguet, W.2    Renaud, J.P.3
  • 76
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery M, Kalkhoven E, Hoare S, et al. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature. 1997, 387:733-736.
    • (1997) Nature. , vol.387 , pp. 733-736
    • Heery, M.1    Kalkhoven, E.2    Hoare, S.3
  • 77
    • 0031561119 scopus 로고    scopus 로고
    • Agonistic effect of tamoxifen is dependent on the cell type, ERE-promoter context and estrogen subtype: Functional difference between estrogen receptors α and β
    • Watanabe T, Inoue S, Ogawa S, et al. Agonistic effect of tamoxifen is dependent on the cell type, ERE-promoter context and estrogen subtype: Functional difference between estrogen receptors α and β. Biochem Biophys Res Commun. 1997, 236:140-145.
    • (1997) Biochem Biophys Res Commun. , vol.236 , pp. 140-145
    • Watanabe, T.1    Inoue, S.2    Ogawa, S.3
  • 78
    • 0031816540 scopus 로고    scopus 로고
    • Differential response of estrogen receptor alpha and estrogen receptor beta to partial estrogen agonists/antagonists
    • Barkhem T, Carlsson B, Nilsson Y, et al. Differential response of estrogen receptor alpha and estrogen receptor beta to partial estrogen agonists/antagonists. Mol Pharmacol. 1998, 54:105-112.
    • (1998) Mol Pharmacol. , vol.54 , pp. 105-112
    • Barkhem, T.1    Carlsson, B.2    Nilsson, Y.3
  • 79
    • 0035347192 scopus 로고    scopus 로고
    • Rapid actions of plasma membrane estrogen receptors
    • Kelly MJ, Levin ER Rapid actions of plasma membrane estrogen receptors. Trends Endocrinol Metab. 2001, 12:152-156.
    • (2001) Trends Endocrinol Metab. , vol.12 , pp. 152-156
    • Kelly, M.J.1    Levin, E.R.2
  • 80
    • 0033214424 scopus 로고    scopus 로고
    • Estradiol coupling to human monocyte nitric oxide release is dependent on intracellular calcium transients: evidence for an estrogen surface receptor
    • Stefano GB, Prevot V, Beauvillain JC, et al. Estradiol coupling to human monocyte nitric oxide release is dependent on intracellular calcium transients: evidence for an estrogen surface receptor. J Immunol. 1999, 163:3758-3763.
    • (1999) J Immunol. , vol.163 , pp. 3758-3763
    • Stefano, G.B.1    Prevot, V.2    Beauvillain, J.C.3
  • 81
    • 0034624062 scopus 로고    scopus 로고
    • Estrogen signals to the preservation of endothelial cell form and function
    • Razandi M, Pedram A, Levin ER Estrogen signals to the preservation of endothelial cell form and function. J Biol Chem 2000, 275:38540-38546.
    • (2000) J Biol Chem , vol.275 , pp. 38540-38546
    • Razandi, M.1    Pedram, A.2    Levin, E.R.3
  • 82
    • 0032589745 scopus 로고    scopus 로고
    • Estrogen receptor α mediates the nongenomic activation of endothelial nitric oxide synthase by estrogen
    • Chen Z, Yuhanna IS, Galcheva-Gargova Z, et al. Estrogen receptor α mediates the nongenomic activation of endothelial nitric oxide synthase by estrogen. J Clin Invest 1999, 103:401-406.
    • (1999) J Clin Invest , vol.103 , pp. 401-406
    • Chen, Z.1    Yuhanna, I.S.2    Galcheva-Gargova, Z.3
  • 83
    • 0032488877 scopus 로고    scopus 로고
    • Estradiol binding to cell surface raises cytosolic free calcium in T cells
    • Benten WP, Lieberherr M, Giese G, et al. Estradiol binding to cell surface raises cytosolic free calcium in T cells. FEBS Lett 1998, 422:349-353.
    • (1998) FEBS Lett , vol.422 , pp. 349-353
    • Benten, W.P.1    Lieberherr, M.2    Giese, G.3
  • 84
    • 0033304691 scopus 로고    scopus 로고
    • Estrogen receptor-alpha detected on the plasma membrane of aldehyde-fixed GH3/B6/F10 rat pituitary tumor cells by enzyme linked immunocytochemistry
    • Norfleet AM, Thomas ML, Gametchu B, et al. Estrogen receptor-alpha detected on the plasma membrane of aldehyde-fixed GH3/B6/F10 rat pituitary tumor cells by enzyme linked immunocytochemistry. Endocrinology 1999, 140:3805-3814.
    • (1999) Endocrinology , vol.140 , pp. 3805-3814
    • Norfleet, A.M.1    Thomas, M.L.2    Gametchu, B.3
  • 85
    • 0033985036 scopus 로고    scopus 로고
    • Antibodies to the estrogen receptor-alpha modulate rapid prolactin release from rat pituitary tumor cells through plasma membrane estrogen receptors
    • Norfleet AM, Clarke CH, Gametchu B, et al. Antibodies to the estrogen receptor-alpha modulate rapid prolactin release from rat pituitary tumor cells through plasma membrane estrogen receptors. FASEB J 2000, 14:157-165.
    • (2000) FASEB J , vol.14 , pp. 157-165
    • Norfleet, A.M.1    Clarke, C.H.2    Gametchu, B.3
  • 86
    • 0030978296 scopus 로고    scopus 로고
    • Modulation of G proteincoupled receptors by an estrogen receptor that activates protein kinase A
    • Lagrange AH, Ronnekleiv OK, Kelly MJ Modulation of G proteincoupled receptors by an estrogen receptor that activates protein kinase A. Mol Pharmacol 1997, 51:605-612.
    • (1997) Mol Pharmacol , vol.51 , pp. 605-612
    • Lagrange, A.H.1    Ronnekleiv, O.K.2    Kelly, M.J.3
  • 87
    • 0001548401 scopus 로고    scopus 로고
    • Cell membrane and nuclear estrogen receptors derive from a single transcript: studies of ERα and ERβ expressed in CHO cells
    • Razandi M, Pedram A, Greene GL, et al. Cell membrane and nuclear estrogen receptors derive from a single transcript: studies of ERα and ERβ expressed in CHO cells. Mol Endocrinol 1999, 13:307-319.
    • (1999) Mol Endocrinol , vol.13 , pp. 307-319
    • Razandi, M.1    Pedram, A.2    Greene, G.L.3
  • 88
    • 0030978912 scopus 로고    scopus 로고
    • Phospholipase C beta and membrane action of calcitriol and estradiol
    • Le Mellay V, Grosse B, Lieberherr M Phospholipase C beta and membrane action of calcitriol and estradiol. J Biol Chem 1997, 272:11902-11907.
    • (1997) J Biol Chem , vol.272 , pp. 11902-11907
    • Le Mellay, V.1    Grosse, B.2    Lieberherr, M.3
  • 91
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna NJ, O'Malley BW Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 2002, 108:465-474.
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 93
    • 0028233383 scopus 로고
    • Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription
    • Halachmi S, Marden E, Martin G, et al. Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science 1994, 264:1455-1458.
    • (1994) Science , vol.264 , pp. 1455-1458
    • Halachmi, S.1    Marden, E.2    Martin, G.3
  • 94
    • 0028846193 scopus 로고    scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate SA, Tsai SY, Tsai MJ, et al. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 1996, 270:1354-1357.
    • (1996) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3
  • 95
    • 0032489555 scopus 로고    scopus 로고
    • The receptor-associated coactivator 3 activates transcription through CREB-binding protein recruitment and autoregulation
    • Li H, Chen JD The receptor-associated coactivator 3 activates transcription through CREB-binding protein recruitment and autoregulation. J Biol Chem 1998, 273:5948-5954.
    • (1998) J Biol Chem , vol.273 , pp. 5948-5954
    • Li, H.1    Chen, J.D.2
  • 96
    • 0032479304 scopus 로고    scopus 로고
    • Steroid receptor coactivator-1 coactivates activating protein-1-mediated transactivations through interaction with the c-Jun and c-Fos subunits
    • Lee SK, Kim HJ, Na SY, et al. Steroid receptor coactivator-1 coactivates activating protein-1-mediated transactivations through interaction with the c-Jun and c-Fos subunits. J Biol Chem 1998, 273:16651-16654.
    • (1998) J Biol Chem , vol.273 , pp. 16651-16654
    • Lee, S.K.1    Kim, H.J.2    Na, S.Y.3
  • 97
    • 0032080237 scopus 로고    scopus 로고
    • Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates NF-kB-mediated transactivation
    • Na SY, Lee SK, Han SJ, et al. Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates NF-kB-mediated transactivation. J Biol Chem 1998, 273:10831-10834.
    • (1998) J Biol Chem , vol.273 , pp. 10831-10834
    • Na, S.Y.1    Lee, S.K.2    Han, S.J.3
  • 98
    • 0032524634 scopus 로고    scopus 로고
    • The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF-1) and AF-2 domains of steroid receptors
    • Onate SA, Boonyaratanakornkit V, Spencer TE, et al. The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF-1) and AF-2 domains of steroid receptors. J Biol Chem 1998, 273:12101-12108.
    • (1998) J Biol Chem , vol.273 , pp. 12101-12108
    • Onate, S.A.1    Boonyaratanakornkit, V.2    Spencer, T.E.3
  • 99
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T. Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev 1999, 9:40-48.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 100
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang XJ, Ogryzko VV, Nishikawa J, et al. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 1996, 382:319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3
  • 101
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 160-kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel JJ, Heine MJ, Zechel C, et al. TIF2, a 160-kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J 1996, 15:3667-3675.
    • (1996) EMBO J , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.2    Zechel, C.3
  • 102
    • 0029978605 scopus 로고    scopus 로고
    • GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors
    • Hong H, Kohli K, Trivedi A, et al. GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc Natl Acad Sci U S A 1996, 93:4948-4952.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4948-4952
    • Hong, H.1    Kohli, K.2    Trivedi, A.3
  • 103
    • 0030949836 scopus 로고    scopus 로고
    • GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors
    • Hong H, Kohli K, Garabedian MJ, et al. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol Cell Biol 1997, 17:2735-2744.
    • (1997) Mol Cell Biol , vol.17 , pp. 2735-2744
    • Hong, H.1    Kohli, K.2    Garabedian, M.J.3
  • 104
    • 0035502975 scopus 로고    scopus 로고
    • Factor recruitment and TIF2/GRIP1 corepressor activity at a collagenase-3 response element that mediates regulation by phorbol esters and hormones
    • Rogatsky I, Zarember KA, Yamamoto KR Factor recruitment and TIF2/GRIP1 corepressor activity at a collagenase-3 response element that mediates regulation by phorbol esters and hormones. EMBO J 2001, 20:6071-6083.
    • (2001) EMBO J , vol.20 , pp. 6071-6083
    • Rogatsky, I.1    Zarember, K.A.2    Yamamoto, K.R.3
  • 105
    • 0030797902 scopus 로고    scopus 로고
    • AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer
    • Anzick SL, Kononen J, Walker RL, et al. AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science 1997, 277:965-968.
    • (1997) Science , vol.277 , pp. 965-968
    • Anzick, S.L.1    Kononen, J.2    Walker, R.L.3
  • 106
    • 0032538434 scopus 로고    scopus 로고
    • A transcriptional coactivator, steroid receptor coactivqator-3, selectively augments steroid receptor transcriptional activity
    • Suen CS, Berrodin TJ, Mastroeni R, et al. A transcriptional coactivator, steroid receptor coactivqator-3, selectively augments steroid receptor transcriptional activity. J Biol Chem 1998, 273:27645-27653.
    • (1998) J Biol Chem , vol.273 , pp. 27645-27653
    • Suen, C.S.1    Berrodin, T.J.2    Mastroeni, R.3
  • 107
    • 0036242554 scopus 로고    scopus 로고
    • Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by IkB kinase
    • Wu RC, Qin J, Hashimoto Y, et al. Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by IkB kinase. Mol Cell Biol 2002, 22:3549-3561.
    • (2002) Mol Cell Biol , vol.22 , pp. 3549-3561
    • Wu, R.C.1    Qin, J.2    Hashimoto, Y.3
  • 108
    • 0028987872 scopus 로고
    • The aryl hydrocarbon receptor complex
    • Hankinson O The aryl hydrocarbon receptor complex. Ann Rev Pharmacol Toxicol 1995, 35:307-340.
    • (1995) Ann Rev Pharmacol Toxicol , vol.35 , pp. 307-340
    • Hankinson, O.1
  • 109
    • 0032578450 scopus 로고    scopus 로고
    • Distinct steady-state nuclear receptor coregulator complexes exist in vivo
    • McKenna NJ, Nawaz Z, Tsai SY, et al. Distinct steady-state nuclear receptor coregulator complexes exist in vivo. Proc Natl Acad Sci U S A 1998, 95:11697-11702.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 11697-11702
    • McKenna, N.J.1    Nawaz, Z.2    Tsai, S.Y.3
  • 110
    • 0027433708 scopus 로고
    • Phosphorylated CREB binds specifically to the nuclear protein CBP
    • Chrivia JC, Kwok RSP, Lamb N, et al. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 1993, 365:855-859.
    • (1993) Nature , vol.365 , pp. 855-859
    • Chrivia, J.C.1    Kwok, R.S.P.2    Lamb, N.3
  • 111
    • 0028060029 scopus 로고
    • Nuclear protein CBP is a coactivator for the transcription factor CREB
    • Kwok RSP, Lundblad JR, Chrivia JC, et al. Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 1994, 370:223-226.
    • (1994) Nature , vol.370 , pp. 223-226
    • Kwok, R.S.P.1    Lundblad, J.R.2    Chrivia, J.C.3
  • 112
    • 0242587820 scopus 로고    scopus 로고
    • A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors
    • Kamei Y, Xu L, Heinzel T, et al. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 1996, 85:403-414.
    • (1996) Cell , vol.85 , pp. 403-414
    • Kamei, Y.1    Xu, L.2    Heinzel, T.3
  • 113
    • 0029817669 scopus 로고    scopus 로고
    • Role of CBP/p300 in nuclear receptor signalling
    • Chakravarti D, LaMorte VJ, Nelson MC, et al. Role of CBP/p300 in nuclear receptor signalling. Nature 1996, 383:99-103.
    • (1996) Nature , vol.383 , pp. 99-103
    • Chakravarti, D.1    LaMorte, V.J.2    Nelson, M.C.3
  • 114
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
    • Torchia J, Rose DW, Inostroza J, et al. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 1997, 387:677-684.
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1    Rose, D.W.2    Inostroza, J.3
  • 115
    • 0029773871 scopus 로고    scopus 로고
    • The nuclear hormone receptor coactivator SRC-1 is a specific target of p300
    • Yao TP, Ku G, Zhou N, et al. The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc Natl Acad Sci U S A 1996, 93:10626-10631.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10626-10631
    • Yao, T.P.1    Ku, G.2    Zhou, N.3
  • 116
    • 0029858911 scopus 로고    scopus 로고
    • P300 is a component of an estrogen receptor coactivator complex
    • Hanstein B, Eckner R, DiRenzo J, et al. p300 is a component of an estrogen receptor coactivator complex. Proc Natl Acad Sci U S A 1996, 93:11540-11545.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 11540-11545
    • Hanstein, B.1    Eckner, R.2    DiRenzo, J.3
  • 117
    • 0032006563 scopus 로고    scopus 로고
    • P300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation
    • Kraus WL, Kadonaga JT p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation. Genes Dev 1998, 12:331-342.
    • (1998) Genes Dev , vol.12 , pp. 331-342
    • Kraus, W.L.1    Kadonaga, J.T.2
  • 118
    • 0025176042 scopus 로고
    • Ligand-activated thyroid hormone and retinoic acid receptors inhibit growth factor receptor promoter expression
    • Hudson LG, Santon JB, Glass CK, et al. Ligand-activated thyroid hormone and retinoic acid receptors inhibit growth factor receptor promoter expression. Cell 1990, 62:1165-1175.
    • (1990) Cell , vol.62 , pp. 1165-1175
    • Hudson, L.G.1    Santon, J.B.2    Glass, C.K.3
  • 119
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 2000, 14:121-141.
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 120
    • 0025043711 scopus 로고
    • Dimerization among nuclear hormone receptors
    • Forman BM, Samuels HH Dimerization among nuclear hormone receptors. New Biol 1990, 2:587-594.
    • (1990) New Biol , vol.2 , pp. 587-594
    • Forman, B.M.1    Samuels, H.H.2
  • 121
    • 0027435514 scopus 로고
    • Interaction of human thyroid hormone receptor beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone
    • Baniahmad A, Ha I, Reinberg D, et al. Interaction of human thyroid hormone receptor beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone. Proc Natl Acad Sci U S A 1993, 90:8832-8836.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8832-8836
    • Baniahmad, A.1    Ha, I.2    Reinberg, D.3
  • 122
    • 0025015647 scopus 로고
    • Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone
    • Jonat C, Rahmsdorf HJ, Park KK, et al. Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone. Cell 1990, 62:1189-1204.
    • (1990) Cell , vol.62 , pp. 1189-1204
    • Jonat, C.1    Rahmsdorf, H.J.2    Park, K.K.3
  • 123
    • 0030946198 scopus 로고    scopus 로고
    • Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen
    • Smith CL, Nawaz Z, O'Malley BW Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol Endocrinol 1998, 11:657-666.
    • (1998) Mol Endocrinol , vol.11 , pp. 657-666
    • Smith, C.L.1    Nawaz, Z.2    O'Malley, B.W.3
  • 124
    • 0033536054 scopus 로고    scopus 로고
    • An estrogen receptorselective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens
    • Montano MM, Ekena K, Delage-Mourroux R, et al. An estrogen receptorselective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens. Proc Natl Acad Sci U S A 1999, 96:6947-6952.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6947-6952
    • Montano, M.M.1    Ekena, K.2    Delage-Mourroux, R.3
  • 125
    • 0030001371 scopus 로고    scopus 로고
    • An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors
    • Seol W, Choi HS, Moore DD An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors. Science 1996, 272:1336-1339.
    • (1996) Science , vol.272 , pp. 1336-1339
    • Seol, W.1    Choi, H.S.2    Moore, D.D.3
  • 126
    • 0032230250 scopus 로고    scopus 로고
    • Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner)
    • Seol W, Hanstein B, Brown M, et al. Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner). Mol Endocrinol 1998, 12:1551-1557.
    • (1998) Mol Endocrinol , vol.12 , pp. 1551-1557
    • Seol, W.1    Hanstein, B.2    Brown, M.3
  • 127
    • 0032951135 scopus 로고    scopus 로고
    • The orphan nuclear receptor SHP inhibits agonist-dependent transcriptional activity of estrogen receptors ERα and ERβ
    • Johansson L, Thomsen JS, Damdimopoulos AE, et al. The orphan nuclear receptor SHP inhibits agonist-dependent transcriptional activity of estrogen receptors ERα and ERβ. J Biol Chem 2002, 274:345-353.
    • (2002) J Biol Chem , vol.274 , pp. 345-353
    • Johansson, L.1    Thomsen, J.S.2    Damdimopoulos, A.E.3
  • 128
    • 0342980409 scopus 로고    scopus 로고
    • The orphan nuclear receptor SHP utilizes conserved LXXLL-related motifs for interactions with ligand-activated estrogen receptors
    • Johansson L, Bavner A, Thomsen JS, et al. The orphan nuclear receptor SHP utilizes conserved LXXLL-related motifs for interactions with ligand-activated estrogen receptors. Mol Cell Bioll 2000, 20:1124-1133.
    • (2000) Mol Cell Bioll , vol.20 , pp. 1124-1133
    • Johansson, L.1    Bavner, A.2    Thomsen, J.S.3
  • 129
    • 0032579292 scopus 로고    scopus 로고
    • Transcription factor-specific requirements for coactivators and their acetyltransferase functions
    • Korzus E, Torchia J, Rose DW, et al. Transcription factor-specific requirements for coactivators and their acetyltransferase functions. Science 1998, 279:703-707.
    • (1998) Science , vol.279 , pp. 703-707
    • Korzus, E.1    Torchia, J.2    Rose, D.W.3
  • 130
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • Nagy L, Kao HY, Chakravarti D, et al. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 1997, 89:373-380.
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.Y.2    Chakravarti, D.3
  • 131
    • 0033601106 scopus 로고    scopus 로고
    • Sin meets NuRD and other tails of repression
    • Knoepfler PS, Eisenman RN Sin meets NuRD and other tails of repression. Cell 1999, 99:447-450.
    • (1999) Cell , vol.99 , pp. 447-450
    • Knoepfler, P.S.1    Eisenman, R.N.2
  • 132
    • 0029563173 scopus 로고
    • Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element
    • Arnold SF, Vorojeikina DP, Notides AC Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element. J Biol Chem 1995, 270:30205-30212.
    • (1995) J Biol Chem , vol.270 , pp. 30205-30212
    • Arnold, S.F.1    Vorojeikina, D.P.2    Notides, A.C.3
  • 133
    • 0030940071 scopus 로고    scopus 로고
    • An estrogen receptor mutant with strong hormone-independent activity from a metastatic breast cancer
    • Zhang QX, Borg A, Wolf DM, et al. An estrogen receptor mutant with strong hormone-independent activity from a metastatic breast cancer. Cancer Res 1997, 57:1244-1249.
    • (1997) Cancer Res , vol.57 , pp. 1244-1249
    • Zhang, Q.X.1    Borg, A.2    Wolf, D.M.3
  • 134
    • 0027405070 scopus 로고
    • Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region
    • Ali S, Metzger D, Bornert JM, et al. Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region. EMBO J 1993, 12:1153-1160.
    • (1993) EMBO J , vol.12 , pp. 1153-1160
    • Ali, S.1    Metzger, D.2    Bornert, J.M.3
  • 135
    • 0028850007 scopus 로고
    • Phosphorylation of the human estrogen receptor by nitogen-activated protein kinase and casein kinase II: Consequence on DNA binding
    • Arnold SF, Obourn JD, Jaffe H, et al. Phosphorylation of the human estrogen receptor by nitogen-activated protein kinase and casein kinase II: Consequence on DNA binding. J Steroid Biochem Mol Biol 1995, 55:163-172.
    • (1995) J Steroid Biochem Mol Biol , vol.55 , pp. 163-172
    • Arnold, S.F.1    Obourn, J.D.2    Jaffe, H.3
  • 136
    • 0028886694 scopus 로고
    • Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase
    • Kato S, Endoh H, Masuhiro Y, et al. Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase. Science 1995, 270:1491-1494.
    • (1995) Science , vol.270 , pp. 1491-1494
    • Kato, S.1    Endoh, H.2    Masuhiro, Y.3
  • 137
    • 0029877913 scopus 로고    scopus 로고
    • Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation
    • Bunone G, Briand PA, Miksicek RJ, et al. Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. EMBO J 1996, 15:2174-2183.
    • (1996) EMBO J , vol.15 , pp. 2174-2183
    • Bunone, G.1    Briand, P.A.2    Miksicek, R.J.3
  • 138
    • 0027302009 scopus 로고
    • Stimulation of estrogen receptor-mediated transcription and alteration in the phosphorylation state of the rat uterine estrogen receptor by estrogen, cyclic adenosine monophosphate, and insulin-like growth factor-1
    • Aronica SM, Katzenellenbogen BS Stimulation of estrogen receptor-mediated transcription and alteration in the phosphorylation state of the rat uterine estrogen receptor by estrogen, cyclic adenosine monophosphate, and insulin-like growth factor-1. Mol Endocrinol 1993, 7:743-752.
    • (1993) Mol Endocrinol , vol.7 , pp. 743-752
    • Aronica, S.M.1    Katzenellenbogen, B.S.2
  • 139
    • 0032557452 scopus 로고    scopus 로고
    • Estradiol-induced phosphorylation of serine 118 in the estrogen receptor is independent of p42/p44 mitogenactivated protein kinase
    • Joel PB, Traish AM, Lannigan DA Estradiol-induced phosphorylation of serine 118 in the estrogen receptor is independent of p42/p44 mitogenactivated protein kinase. J Biol Chem 1998, 273:13317-13323.
    • (1998) J Biol Chem , vol.273 , pp. 13317-13323
    • Joel, P.B.1    Traish, A.M.2    Lannigan, D.A.3
  • 140
    • 0032906876 scopus 로고    scopus 로고
    • Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization
    • Chen DS, Pace PE, Coombes RC, et al. Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization. Mol Cell Biol 1999, 19:1002-1015.
    • (1999) Mol Cell Biol , vol.19 , pp. 1002-1015
    • Chen, D.S.1    Pace, P.E.2    Coombes, R.C.3
  • 141
    • 0027978187 scopus 로고
    • Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor
    • Amold SF, Obourn JD, Jaffe H, et al. Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. Mol Endocrinol 1994, 8:1208-1214.
    • (1994) Mol Endocrinol , vol.8 , pp. 1208-1214
    • Amold, S.F.1    Obourn, J.D.2    Jaffe, H.3
  • 142
    • 0031594574 scopus 로고    scopus 로고
    • Pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167
    • Joel PB, Smith J, Sturgill TW, et al. pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167. Mol Cell Biol 1998, 18:1978-1984.
    • (1998) Mol Cell Biol , vol.18 , pp. 1978-1984
    • Joel, P.B.1    Smith, J.2    Sturgill, T.W.3
  • 143
    • 0033120030 scopus 로고    scopus 로고
    • Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1
    • Tremblay A, Tremblay GB, Labrie F, et al. Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1. Mol Cell 1999, 3:513-519.
    • (1999) Mol Cell , vol.3 , pp. 513-519
    • Tremblay, A.1    Tremblay, G.B.2    Labrie, F.3
  • 144
    • 0036138806 scopus 로고    scopus 로고
    • Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs
    • Ko L, Cardona GR, Iwasaki T, et al. Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs. Mol Endocrinol 2002, 16:128-140.
    • (2002) Mol Endocrinol , vol.16 , pp. 128-140
    • Ko, L.1    Cardona, G.R.2    Iwasaki, T.3
  • 145
    • 0031840580 scopus 로고    scopus 로고
    • Ligand-independent activation of steroid hormone receptors
    • Weigel NL, Zhang Y Ligand-independent activation of steroid hormone receptors. J Mol Med 1998, 76:469-479.
    • (1998) J Mol Med , vol.76 , pp. 469-479
    • Weigel, N.L.1    Zhang, Y.2
  • 146
    • 0038776380 scopus 로고    scopus 로고
    • Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARγ
    • Hu E, Kim JB, Sarrf P, et al. Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARγ. Science 1996, 274:2100-2103.
    • (1996) Science , vol.274 , pp. 2100-2103
    • Hu, E.1    Kim, J.B.2    Sarrf, P.3
  • 147
    • 0030775347 scopus 로고    scopus 로고
    • Phosphorylation of activation functions AF-1 and AF-2 of RARα and RARγ is indispensable for differentiation of F9 cells upon retinoic acid and cAMP treatment
    • Taneja R, Rochette-Egly C, Plassat JL, et al. Phosphorylation of activation functions AF-1 and AF-2 of RARα and RARγ is indispensable for differentiation of F9 cells upon retinoic acid and cAMP treatment. EMBO J 1997, 16:6452-6465.
    • (1997) EMBO J , vol.16 , pp. 6452-6465
    • Taneja, R.1    Rochette-Egly, C.2    Plassat, J.L.3
  • 148
    • 0032569902 scopus 로고    scopus 로고
    • Interdomain communication regulation ligand binding by PPAR-α
    • Shao D, Rangwata SM, Bailey ST, et al. Interdomain communication regulation ligand binding by PPAR-α. Nature 1998, 396:377-380.
    • (1998) Nature , vol.396 , pp. 377-380
    • Shao, D.1    Rangwata, S.M.2    Bailey, S.T.3
  • 150
    • 0035034215 scopus 로고    scopus 로고
    • Estrogen and progesterone receptors in murine models of systemic lupus erythematosus
    • Greenstein B, Roa R, Dhaher Y, et al. Estrogen and progesterone receptors in murine models of systemic lupus erythematosus. Int Immunopharmacol 2001, 1:1025-1035.
    • (2001) Int Immunopharmacol , vol.1 , pp. 1025-1035
    • Greenstein, B.1    Roa, R.2    Dhaher, Y.3
  • 151
    • 0030271604 scopus 로고    scopus 로고
    • Presence of a variant form of the estrogen receptor in peripheral blood mononuclear cells from normal individuals and lupus patients
    • Wilson KB, Evans M, Abdou NI Presence of a variant form of the estrogen receptor in peripheral blood mononuclear cells from normal individuals and lupus patients. J Reprod Immunol 1996, 31:199-208.
    • (1996) J Reprod Immunol , vol.31 , pp. 199-208
    • Wilson, K.B.1    Evans, M.2    Abdou, N.I.3
  • 152
    • 0030872716 scopus 로고    scopus 로고
    • RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2
    • Li H, Gomes PJ, Chen JD RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci U S A 1997, 94:8479-8484.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8479-8484
    • Li, H.1    Gomes, P.J.2    Chen, J.D.3
  • 153
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H, Lin RJ, Schiltz RL, et al. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 1997, 90:569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3
  • 154
    • 0030786270 scopus 로고    scopus 로고
    • TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule exhibits distinct properties from steroid receptor coactivator-1
    • Takeshita A, Cardona GR, Koibuchi N, et al. TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule exhibits distinct properties from steroid receptor coactivator-1. J Biol Chem 1997, 272:27629-27634.
    • (1997) J Biol Chem , vol.272 , pp. 27629-27634
    • Takeshita, A.1    Cardona, G.R.2    Koibuchi, N.3


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