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Volumn 34, Issue 4, 2000, Pages 203-218

Intracellular estrogen receptors, their characterization and function (Review)

Author keywords

Estrogen receptors; Hormone responsive element; Ligand inducible transcription factors; Nuclear receptors; Review; Steroid thyroid receptor superfamily

Indexed keywords

CELL RECEPTOR; ESRRB PROTEIN, HUMAN; ESRRG PROTEIN, HUMAN; ESTROGEN RECEPTOR; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; ESTROGEN RECEPTOR GAMMA; ESTROGEN RECEPTOR RELATED RECEPTOR BETA; ESTROGEN RECEPTOR-RELATED RECEPTOR BETA; LIGAND;

EID: 0034573961     PISSN: 12100668     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (64)

References (141)
  • 1
    • 0031036099 scopus 로고    scopus 로고
    • Estradiol-binding mechanism and binding capacity of the human estrogen receptor is regulated by tyrosine phosphorylation
    • ARNOLD SF, MELAMED M, VOROJEIKINA DP et al.: Estradiol-binding mechanism and binding capacity of the human estrogen receptor is regulated by tyrosine phosphorylation. Mol. Endocrinol. 11, 48-53, 1997
    • (1997) Mol. Endocrinol. , vol.11 , pp. 48-53
    • Arnold, S.F.1    Melamed, M.2    Vorojeikina, D.P.3
  • 2
    • 0030729211 scopus 로고    scopus 로고
    • Differential expression of estrogen receptors α and β m RNA during differentiation of human osteoblast SV-HFO cells
    • ARTS J, KUIPER GGJM, JANSSEN JMMF et al.: Differential expression of estrogen receptors α and β m RNA during differentiation of human osteoblast SV-HFO cells. Endocrinology. 138, 5067-5070, 1997
    • (1997) Endocrinology , vol.138 , pp. 5067-5070
    • Arts, J.1    Kuiper, G.G.J.M.2    Janssen, J.M.M.F.3
  • 4
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • BEATO M: Gene regulation by steroid hormones. Cell 56, 335-344, 1989
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 5
    • 0027521287 scopus 로고
    • Transcriptional activation by the estrogen receptor requires a conformational change in the ligand binding domain
    • BEEKMAN JM, ALLAN GF, TSAI SY et al.: Transcriptional activation by the estrogen receptor requires a conformational change in the ligand binding domain. Mol. Endocrinol. 1, 1266-1274, 1993
    • (1993) Mol. Endocrinol. , vol.1 , pp. 1266-1274
    • Beekman, J.M.1    Allan, G.F.2    Tsai, S.Y.3
  • 6
    • 0029812470 scopus 로고    scopus 로고
    • II68, novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II
    • II68, novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II. EMBO J. 15, 5022-5031, 1996
    • (1996) EMBO J. , vol.15 , pp. 5022-5031
    • Bertolotti, A.1    Lutz, Y.2    Heard, D.J.3
  • 7
    • 0031790490 scopus 로고    scopus 로고
    • A novel human estrogen receptor β: Identification and functional analysis of additional N-terminal amino acids
    • BHAT R A, HARNISH DC, STEVIS PE et al.: A novel human estrogen receptor β: Identification and functional analysis of additional N-terminal amino acids. J. Steroid. Biochem. Molec. Biol. 67, 233-240, 1998
    • (1998) J. Steroid. Biochem. Molec. Biol. , vol.67 , pp. 233-240
    • Bhat, R.A.1    Harnish, D.C.2    Stevis, P.E.3
  • 8
    • 0027941067 scopus 로고
    • 3,5,3′- Triiodothyronine nuclear receptors and their role in the thyroid hormone action
    • BRTKO J,.PASCUAL A, ARANDA A: 3,5,3′- Triiodothyronine nuclear receptors and their role in the thyroid hormone action. Endocr. Regul. 28, 107-115, 1994a
    • (1994) Endocr. Regul. , vol.28 , pp. 107-115
    • Brtko, J.1    Pascual, A.2    Aranda, A.3
  • 9
    • 0028114824 scopus 로고
    • Accurate determination and physicochemical properties of rat liver nuclear retinoic acid (RA) receptors
    • BRTKO J: Accurate determination and physicochemical properties of rat liver nuclear retinoic acid (RA) receptors. Biochem. Biophys. Res. Commun. 204, 439-445, 1994b
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 439-445
    • Brtko, J.1
  • 10
    • 0028291252 scopus 로고
    • The basics of basal transcription by RNA polymerase II
    • BURATOWSKI S: The basics of basal transcription by RNA polymerase II. Cell 77, 1-3, 1994
    • (1994) Cell , vol.77 , pp. 1-3
    • Buratowski, S.1
  • 11
    • 0031032212 scopus 로고    scopus 로고
    • Estrogen receptor-β mRNA expression in rat ovary: Down-regulation by gonadotropins
    • BYERS M, KUIPER GGJM., GUSTAFSSON JA et al.: Estrogen receptor-β mRNA expression in rat ovary: down-regulation by gonadotropins. Mol. Endocrinol. 11, 172-182, 1997
    • (1997) Mol. Endocrinol. , vol.11 , pp. 172-182
    • Byers, M.1    Kuiper, G.G.J.M.2    Gustafsson, J.A.3
  • 12
    • 0034007998 scopus 로고    scopus 로고
    • Cloning and characterization of RAP250, a novel nuclear receptor coactivator
    • CAIRA F, ANTONSON P, PELTO-HUIKKO M et al.: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J. Biol. Chem. 275, 5308-5317, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 5308-5317
    • Caira, F.1    Antonson, P.2    Pelto-Huikko, M.3
  • 13
    • 0032906876 scopus 로고    scopus 로고
    • Phosphorylation of human estrogen receptor alpha by protein ki-nase A regulates dimerization
    • CHEN DS, PACE PE, COOMBES RC et al.: Phosphorylation of human estrogen receptor alpha by protein ki-nase A regulates dimerization. Mol. Cell. Biol. 19, 1002-1015, 1999
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1002-1015
    • Chen, D.S.1    Pace, P.E.2    Coombes, R.C.3
  • 14
    • 0030995945 scopus 로고    scopus 로고
    • Estrogen receptor ligands modulates its interaction with DNA
    • CHESKIS BJ, KARATHANASIS S, LYTTLE CR: Estrogen receptor ligands modulates its interaction with DNA. J. Biol. Chem. 272, 11384-11391, 1997
    • (1997) J. Biol. Chem. , vol.272 , pp. 11384-11391
    • Cheskis, B.J.1    Karathanasis, S.2    Lyttle, C.R.3
  • 15
    • 9944234986 scopus 로고
    • The biology and pharmacology of estrogen receptor binding: Relationship to uterine growth
    • (Eds. O'Malley BW and Birnbaumer L) Academic Press, Inc., New York
    • CLARK JH, PECK Jr. EJ, HARDIN JW et al.: The biology and pharmacology of estrogen receptor binding: Relationship to uterine growth. In: Receptors and hormone action I (Eds. O'Malley BW and Birnbaumer L)pp. 1-31, Academic Press, Inc., New York 1978
    • (1978) Receptors and Hormone Action I , pp. 1-31
    • Clark, J.H.1    Peck Jr., E.J.2    Hardin, J.W.3
  • 16
    • 0028866648 scopus 로고
    • Analysis of transcription and estrogen insensitivity in the female mouse after targeted disruption of the estrogen receptor gene
    • COUSE JF, CURTIS SW, WASHBURN TF et al.: Analysis of transcription and estrogen insensitivity in the female mouse after targeted disruption of the estrogen receptor gene. Mol. Endocrinol. 9, 1441-1454, 1995
    • (1995) Mol. Endocrinol. , vol.9 , pp. 1441-1454
    • Couse, J.F.1    Curtis, S.W.2    Washburn, T.F.3
  • 17
    • 0030728930 scopus 로고    scopus 로고
    • Tissue distribution and quantitative analysis of estrogen receptor-α (ERα) and estrogen receptor-β (ERβ) messenger ribonucleic acid in the wild-type and ERα-knockout mouse
    • COUSE JF, LINDZEY J, GRANDIEN K et al.: Tissue distribution and quantitative analysis of estrogen receptor-α (ERα) and estrogen receptor-β (ERβ) messenger ribonucleic acid in the wild-type and ERα-knockout mouse. Endocrinology. 138, 4613-4621, 1997
    • (1997) Endocrinology , vol.138 , pp. 4613-4621
    • Couse, J.F.1    Lindzey, J.2    Grandien, K.3
  • 18
    • 0024356431 scopus 로고
    • Two amino acids within the knuckle of the first zinc finger specify DNA response element activation by the glucocorticoid receptor
    • DANIELSEN M, HINCK L, RINGOLD GM: Two amino acids within the knuckle of the first zinc finger specify DNA response element activation by the glucocorticoid receptor. Cell. 57, 1131-1138, 1989
    • (1989) Cell , vol.57 , pp. 1131-1138
    • Danielsen, M.1    Hinck, L.2    Ringold, G.M.3
  • 19
    • 0027768899 scopus 로고
    • The antiestrogen ICI 182780 disrupts estrogen receptor nucleocytoplasmic shuttling
    • DAUVOIS S, WHITE R, PARKER MG: The antiestrogen ICI 182780 disrupts estrogen receptor nucleocytoplasmic shuttling. J. Cell Sci. 106, 1377-1388, 1993
    • (1993) J. Cell Sci. , vol.106 , pp. 1377-1388
    • Dauvois, S.1    White, R.2    Parker, M.G.3
  • 20
    • 0034098360 scopus 로고    scopus 로고
    • Estrogen receptors alpha and beta: Two receptors of a kind?
    • DECHERING K, BOERSMA C, MOSSELMAN S: Estrogen receptors alpha and beta: Two receptors of a kind? Current Med. Chem. 7, 561-576, 2000
    • (2000) Current Med. Chem. , vol.7 , pp. 561-576
    • Dechering, K.1    Boersma, C.2    Mosselman, S.3
  • 21
    • 0026406078 scopus 로고
    • Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors
    • DE FRANCO DB, QI M, BORROR KC et al.: Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors. Mol. Endocrinol. 5, 1215-1228, 1991
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1215-1228
    • De Franco, D.B.1    Qi, M.2    Borror, K.C.3
  • 22
    • 0033630453 scopus 로고    scopus 로고
    • Steroid/nuclear receptor coactivators
    • DON CHEN J: Steroid/nuclear receptor coactivators. Vitamins and Hormones. 58, 391-448, 2000
    • (2000) Vitamins and Hormones , vol.58 , pp. 391-448
    • Don Chen, J.1
  • 23
    • 0030744629 scopus 로고    scopus 로고
    • Expression of estrogen receptor-Beta in human breast tumors
    • DOTZLAW H, LEYGUE E, WATSON PH et al.: Expression of estrogen receptor-Beta in human breast tumors. J. Clin. Endocrinol. Metab. 82, 2371-2374, 1996
    • (1996) J. Clin. Endocrinol. Metab. , vol.82 , pp. 2371-2374
    • Dotzlaw, H.1    Leygue, E.2    Watson, P.H.3
  • 24
    • 0029969771 scopus 로고    scopus 로고
    • Target disruption of the estrogen receptor gene in male mice causes alteration of spermatogenesis and infertility
    • EDDY EM, WASHBURN TF, BUNCH DO et al.: Target disruption of the estrogen receptor gene in male mice causes alteration of spermatogenesis and infertility. Endocrinology 137, 4796-4805, 1996
    • (1996) Endocrinology , vol.137 , pp. 4796-4805
    • Eddy, E.M.1    Washburn, T.F.2    Bunch, D.O.3
  • 25
    • 0031040614 scopus 로고    scopus 로고
    • Different residues of the human estrogen receptor are involved in the recognition of structurally diverse estrogens and antiestrogens
    • EKENA K, WEIS KE, KATZENELLENDOGEN JA et al.: Different residues of the human estrogen receptor are involved in the recognition of structurally diverse estrogens and antiestrogens. J. Biol. Chem. 272, 5069-5075, 1997
    • (1997) J. Biol. Chem. , vol.272 , pp. 5069-5075
    • Ekena, K.1    Weis, K.E.2    Katzenellendogen, J.A.3
  • 26
    • 0018136531 scopus 로고
    • Heterogeneity of estrogen receptors in the cytosol and nuclear fraction of the rat uterus
    • ERIKSSON H, UPCHURCH S, HARDIN JW et al.: Heterogeneity of estrogen receptors in the cytosol and nuclear fraction of the rat uterus. Biochem. Biophys. Res. Commun. 81, 1-7, 1978
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 1-7
    • Eriksson, H.1    Upchurch, S.2    Hardin, J.W.3
  • 27
    • 0032568663 scopus 로고    scopus 로고
    • The putative cofactor TIFIα is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors
    • FRASER RA, HEARD DJ, ADAM S et al.: The putative cofactor TIFIα is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors. J. Biol. Chem. 273, 16199-16204, 1998
    • (1998) J. Biol. Chem. , vol.273 , pp. 16199-16204
    • Fraser, R.A.1    Heard, D.J.2    Adam, S.3
  • 28
    • 0033485326 scopus 로고    scopus 로고
    • Multimeric coactivator complexes for steroid/nuclear receptors
    • FREEDMAN LP: Multimeric coactivator complexes for steroid/nuclear receptors. Trends Endocrinol. Metab. 10, 403-407, 1999
    • (1999) Trends Endocrinol. Metab. , vol.10 , pp. 403-407
    • Freedman, L.P.1
  • 29
    • 0033152586 scopus 로고    scopus 로고
    • Identification of a unique liganded estrogen receptor complex released from the nucleus by decavanadate
    • FRITSCH M, ALUKER M, MURDOCH FE: Identification of a unique liganded estrogen receptor complex released from the nucleus by decavanadate. Bichemistry 38, 6987-6996, 1999
    • (1999) Bichemistry , vol.38 , pp. 6987-6996
    • Fritsch, M.1    Aluker, M.2    Murdoch, F.E.3
  • 30
    • 0025043711 scopus 로고
    • Dimerization among nuclear hormone receptors
    • FORMAN BN, SAMUELS HH: Dimerization among nuclear hormone receptors. New. Biol. 2, 587-594, 1990
    • (1990) New. Biol. , vol.2 , pp. 587-594
    • Forman, B.N.1    Samuels, H.H.2
  • 31
    • 0023857147 scopus 로고
    • Identification of a new class of steroid hormone receptors
    • GIGUERE V, YANG N, SEGUI P et al.: Identification of a new class of steroid hormone receptors. Nature 331, 91-94, 1988
    • (1988) Nature , vol.331 , pp. 91-94
    • Giguere, V.1    Yang, N.2    Segui, P.3
  • 32
    • 0010320958 scopus 로고
    • Selective accumulation of tritium-labelled hexoestrol by the reproductive organs of immature female goats and sheep
    • GLASCOCK RF, HOEKSTRA WG: Selective accumulation of tritium-labelled hexoestrol by the reproductive organs of immature female goats and sheep. Biochem. J. 72, 673-682, 1959
    • (1959) Biochem. J. , vol.72 , pp. 673-682
    • Glascock, R.F.1    Hoekstra, W.G.2
  • 34
    • 9944234483 scopus 로고
    • A low-affinity estrogen binding site in pregnant rat uteri: Analysis and partial purification
    • GRAY WGN, BISWAS EE, BASHIRELAHI N et al.: A low-affinity estrogen binding site in pregnant rat uteri: analysis and partial purification. Proc. Natl. Acad. Sci. USA. 88, 8606-8610, 1994
    • (1994) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8606-8610
    • Gray, W.G.N.1    Biswas, E.E.2    Bashirelahi, N.3
  • 35
    • 0022653964 scopus 로고
    • Human estrogen receptor cDNA: Sequence, expression and homology to v-erb-A
    • GREEN S, WALTER P, KUMAR V et al.: Human estrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature (Lond.) 320, 134-139, 1986
    • (1986) Nature (Lond.) , vol.320 , pp. 134-139
    • Green, S.1    Walter, P.2    Kumar, V.3
  • 36
    • 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. 163, 379-383, 1999
    • (1999) J. Endocrinol. , vol.163 , pp. 379-383
    • Gustafsson, J.A.1
  • 37
    • 0033304993 scopus 로고    scopus 로고
    • The estrogen receptor beta-isoform (ER beta) of the human estrogen receptor modulates ER alpha transcriptional activity and is a key regulator of the cellular response to estrogens and antiestrogens
    • HALL JM and MCDONNELL DP: The estrogen receptor beta-isoform (ER beta) of the human estrogen receptor modulates ER alpha transcriptional activity and is a key regulator of the cellular response to estrogens and antiestrogens. Endocrinology 140, 5566-5578, 1999
    • (1999) Endocrinology , vol.140 , pp. 5566-5578
    • Hall, J.M.1    Mcdonnell, D.P.2
  • 38
    • 0032947720 scopus 로고    scopus 로고
    • Functional analysis of novel estrogen receptor-beta isoform
    • HANSTEIN B, Liu H, YANCISIN MC et al.: Functional analysis of novel estrogen receptor-beta isoform. Mol. Endocrinol. 13, 129-137, 1999
    • (1999) Mol. Endocrinol. , vol.13 , pp. 129-137
    • Hanstein, B.1    Liu, H.2    Yancisin, M.C.3
  • 39
    • 0034335415 scopus 로고    scopus 로고
    • Human ERR gamma, a third member of the estrogen receptor-related receptor (ERR) subfamily of orphan nuclear receptors: Tissue-specific isoforms are expressed during development and in the adult
    • HEARD DJ, NORBY PL, HOLLOWAY J et al.: Human ERR gamma, a third member of the estrogen receptor-related receptor (ERR) subfamily of orphan nuclear receptors: Tissue-specific isoforms are expressed during development and in the adult. Mol. Endocrinol. 14, 382-392, 2000
    • (2000) Mol. Endocrinol. , vol.14 , pp. 382-392
    • Heard, D.J.1    Norby, P.L.2    Holloway, J.3
  • 40
    • 0028964168 scopus 로고
    • The requirement for the basal transcription factor HE is determined by the helical stability of promoter DNA
    • HOLSTEGE F.C., TANTIN D., CAREY M et al.: The requirement for the basal transcription factor HE is determined by the helical stability of promoter DNA. EMBO J. 14, 810-819, 1995
    • (1995) EMBO J. , vol.14 , pp. 810-819
    • Holstege, F.C.1    Tantin, D.2    Carey, M.3
  • 41
    • 0030949836 scopus 로고    scopus 로고
    • GRIPI, a transcriptional coactivator for AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors
    • HONG H, KOHLI K, GARABEDIAN MJ et al.: GRIPI, a transcriptional coactivator for AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell. Biol. 17, 2735-2744, 1997
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2735-2744
    • Hong, H.1    Kohli, K.2    Garabedian, M.J.3
  • 43
    • 0032919564 scopus 로고    scopus 로고
    • Direct visualisation of the human estrogen receptor alpha reveals a role for ligand in the nuclear distribution of the receptor
    • HTUN H, HOLTH LT, WALKER D et al.: Direct visualisation of the human estrogen receptor alpha reveals a role for ligand in the nuclear distribution of the receptor. Mol. Biol. Cell 10, 471-486, 1999
    • (1999) Mol. Biol. Cell , vol.10 , pp. 471-486
    • Htun, H.1    Holth, L.T.2    Walker, D.3
  • 44
    • 0033559831 scopus 로고    scopus 로고
    • Interaction of human estrogen receptors alpha and beta with the same naturally occurring estrogen response elements
    • HYDER SM, CHIAPPETTA C , STANCEL GM: Interaction of human estrogen receptors alpha and beta with the same naturally occurring estrogen response elements. Biochem. Pharm. 57, 597-601, 1999
    • (1999) Biochem. Pharm. , vol.57 , pp. 597-601
    • Hyder, S.M.1    Chiappetta, C.2    Stancel, G.M.3
  • 45
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcriptional factors by histone acetyltransferases
    • IMHOF A, YANG X, OGRYZKO VV et al.: Acetylation of general transcriptional factors by histone acetyltransferases. Curr. Biol. 7, 689-692, 1997.
    • (1997) Curr. Biol. , vol.7 , pp. 689-692
    • Imhof, A.1    Yang, X.2    Ogryzko, V.V.3
  • 46
    • 0030998328 scopus 로고    scopus 로고
    • The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and corepressors N-CoR or SMRT
    • JACKSON TW, RICHTER JK, BAIN DL et al.: The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and corepressors N-CoR or SMRT. Mol. Endocrinol. 11, 693-705, 1997
    • (1997) Mol. Endocrinol. , vol.11 , pp. 693-705
    • Jackson, T.W.1    Richter, J.K.2    Bain, D.L.3
  • 49
    • 0015476151 scopus 로고
    • Mechanism of action of the female sex hormones
    • JENSEN EV, DESOMBRE ER: Mechanism of action of the female sex hormones. Ann. Rev. Biochem. 41, 203-230, 1972
    • (1972) Ann. Rev. Biochem. , vol.41 , pp. 203-230
    • Jensen, E.V.1    Desombre, E.R.2
  • 50
    • 0030878878 scopus 로고    scopus 로고
    • Steroid receptor induction of gene transcription: A two step model
    • JENSTER G, SPENCER TE, BURCIN MM et al.: Steroid receptor induction of gene transcription: A two step model. Proc. Natl. Acad. Sci. USA 94, 7879-7889, 1997
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7879-7889
    • Jenster, G.1    Spencer, T.E.2    Burcin, M.M.3
  • 51
    • 0032566365 scopus 로고    scopus 로고
    • At the cutting edge. Coactivators and corepressors as mediators of nuclear receptor function: An update
    • JENSTER G: At the cutting edge. Coactivators and corepressors as mediators of nuclear receptor function: An update. Mol. Cell. Endocrinol. 143, 1-7, 1998
    • (1998) Mol. Cell. Endocrinol. , vol.143 , pp. 1-7
    • Jenster, G.1
  • 52
    • 0030851847 scopus 로고    scopus 로고
    • Proposed mechanism for the stabilization of nuclear receptor DNA binding via protein dimerization
    • JIANG G, LEE U, SLADEK FM: Proposed mechanism for the stabilization of nuclear receptor DNA binding via protein dimerization. Mol. Cell. Biol. 17, 6546-6554, 1997
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6546-6554
    • Jiang, G.1    Lee, U.2    Sladek, F.M.3
  • 53
    • 0031044228 scopus 로고    scopus 로고
    • Estrogen-related receptor á-functionally binds as a monomer to extended half-site sequences including ones contained within estrogen-response elements
    • JOHNSTON SD, LIU X, ZUO F et al.: Estrogen-related receptor á-functionally binds as a monomer to extended half-site sequences including ones contained within estrogen-response elements. Mol. Endocrinol. 11, 342-352, 1997
    • (1997) Mol. Endocrinol. , vol.11 , pp. 342-352
    • Johnston, S.D.1    Liu, X.2    Zuo, F.3
  • 54
    • 0032436976 scopus 로고    scopus 로고
    • Molecular mechanism of a cross-talk between estrogen and growth-factor signalling pathways
    • KATO S, KITAMOTO T, MASUHIRO Y et al.: Molecular mechanism of a cross-talk between estrogen and growth-factor signalling pathways. Oncology 55, Suppl. 1, 5-10, 1998
    • (1998) Oncology , vol.55 , Issue.1 SUPPL. , pp. 5-10
    • Kato, S.1    Kitamoto, T.2    Masuhiro, Y.3
  • 55
    • 0030199294 scopus 로고    scopus 로고
    • Nuclear hormone receptors: Ligand-activated regulators of transcription and diverse cell responses
    • KATZENELLENBOGEN JA and KATZENELLENBOGEN BS: Nuclear hormone receptors: ligand-activated regulators of transcription and diverse cell responses. Chemistry and Biology 3, 529-536, 1996
    • (1996) Chemistry and Biology , vol.3 , pp. 529-536
    • Katzenellenbogen, J.A.1    Katzenellenbogen, B.S.2
  • 56
    • 0032915424 scopus 로고    scopus 로고
    • Role of Hsp90-associated cochaperone p23 in estrogen receptor signal transduction
    • KNOBLAUCH R and GARABEDIAN MJ: Role of Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. Mol. Cell. Biol. 19, 3748-3759, 1999
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3748-3759
    • Knoblauch, R.1    Garabedian, M.J.2
  • 57
    • 0034717277 scopus 로고    scopus 로고
    • p300 mediates functional synergism between AF-1 and AF-2 estrogen receptor α and β by interacting directly with the N-terminal A/B domains
    • KOBAYASHI Y, KITAMOTO T, MASUHIRO Y: p300 mediates functional synergism between AF-1 and AF-2 estrogen receptor α and β by interacting directly with the N-terminal A/B domains. J. Biol. Chem. 275, 15645-15651, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 15645-15651
    • Kobayashi, Y.1    Kitamoto, T.2    Masuhiro, Y.3
  • 58
    • 0029616211 scopus 로고
    • Ligand-independent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor
    • KRAUS WL, MCINERNEY EM, KATZENELLENBOGEN BS: Ligand-independent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor. Proc. Natl. Acad. Sci. USA. 92, 12314-12318, 1995
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12314-12318
    • Kraus, W.L.1    Mcinerney, E.M.2    Katzenellenbogen, B.S.3
  • 59
    • 0028331871 scopus 로고
    • Steroid hormone receptor phosphorylation: Is there a physiological role?
    • KUIPER GGJM, BRINKMAN AO: Steroid hormone receptor phosphorylation: Is there a physiological role? Mol. Cell Endocrinol. 100, 103-107, 1994
    • (1994) Mol. Cell Endocrinol. , vol.100 , pp. 103-107
    • Kuiper, G.1    Brinkman, A.O.2
  • 60
    • 0030579801 scopus 로고    scopus 로고
    • Cloning of novel estrogen receptor expressed in rat prostate and ovary
    • KUIPER GGJM, ENMARK E, PELTO-HUIKKO M et al.: Cloning of novel estrogen receptor expressed in rat prostate and ovary. Proc. Natl. Acad. Sci. USA. 93, 5925-5930, 1996
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5925-5930
    • Kuiper, G.G.J.M.1    Enmark, E.2    Pelto-Huikko, M.3
  • 61
    • 0030738318 scopus 로고    scopus 로고
    • The novel receptor-β subtype: Potential role in the cell- and promoter-specific actions of estrogens and antiestrogens
    • KUIPER GGJM and GUSTAFSSON JA: The novel receptor-β subtype: potential role in the cell- and promoter-specific actions of estrogens and antiestrogens. FEBS Letters. 410, 87-90, 1997
    • (1997) FEBS Letters , vol.410 , pp. 87-90
    • Kuiper, G.G.J.M.1    Gustafsson, J.A.2
  • 62
    • 9944248578 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • LANDSCHULTZ WH, JOHNSON PF, MCKNIGTH SL: The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Cell 60, 953-962, 1990
    • (1990) Cell , vol.60 , pp. 953-962
    • Landschultz, W.H.1    Johnson, P.F.2    Mcknigth, S.L.3
  • 63
    • 0033589797 scopus 로고    scopus 로고
    • Low oestrogen receptor alpha expression in normal breast tissue underlies low breast cancer incidence in Japan
    • LAWSON JS, FIELD AS, CHAMPION S et al.: Low oestrogen receptor alpha expression in normal breast tissue underlies low breast cancer incidence in Japan. Lancet 354, 1787-1788, 1999
    • (1999) Lancet , vol.354 , pp. 1787-1788
    • Lawson, J.S.1    Field, A.S.2    Champion, S.3
  • 64
    • 0033607672 scopus 로고    scopus 로고
    • A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo
    • LEE SK, ANZICK SL, CHOI JE et al.: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J. Biol. Chem. 274, 34283-34293, 1999
    • (1999) J. Biol. Chem. , vol.274 , pp. 34283-34293
    • Lee, S.K.1    Anzick, S.L.2    Choi, J.E.3
  • 65
    • 0033230631 scopus 로고    scopus 로고
    • Cellular functions of the plasma membrane estrogen receptor
    • LEVIN ER: Cellular functions of the plasma membrane estrogen receptor. TEM 10, 374-377, 1999
    • (1999) TEM , vol.10 , pp. 374-377
    • Levin, E.R.1
  • 66
    • 0030869565 scopus 로고    scopus 로고
    • Placental abnormalities on mouse embryos lacking the orphan nuclear receptor ERR-β
    • LUO J, SLADEK R, BADER JA et al.: Placental abnormalities on mouse embryos lacking the orphan nuclear receptor ERR-β. Nature (Lond.) 388, 778-782, 1997
    • (1997) Nature (Lond.) , vol.388 , pp. 778-782
    • Luo, J.1    Sladek, R.2    Bader, J.A.3
  • 67
    • 0031778177 scopus 로고    scopus 로고
    • Basic guide to the mechanisms of antiestrogen action
    • MACGREGOR JI, and JORDAN VC: Basic guide to the mechanisms of antiestrogen action. Pharmacol. Rew. 50, 151-196, 1998
    • (1998) Pharmacol. Rew. , vol.50 , pp. 151-196
    • Macgregor, J.I.1    Jordan, V.C.2
  • 68
    • 0024600621 scopus 로고
    • Three amino acids of the estrogen receptor are essential to its ability to distinguish an oestrogen from glucocorticoid-responsive element
    • MADER S, KUMAR V, DE VERNEUIL H et al.: Three amino acids of the estrogen receptor are essential to its ability to distinguish an oestrogen from glucocorticoid-responsive element. Nature. 338, 271-274, 1989
    • (1989) Nature , vol.338 , pp. 271-274
    • Mader, S.1    Kumar, V.2    De Verneuil, H.3
  • 70
    • 0017195989 scopus 로고
    • Endometrial content of nuclear estrogen receptor and receptivity for ovoimplantation in the rat
    • MARTEL D and PSYCHOYOS A: Endometrial content of nuclear estrogen receptor and receptivity for ovoimplantation in the rat. Endocrinology 99, 470-475, 1976
    • (1976) Endocrinology , vol.99 , pp. 470-475
    • Martel, D.1    Psychoyos, A.2
  • 71
    • 0024814733 scopus 로고
    • Cooperative binding of estrogen receptor to imperfect estrogen-responsive DNA.elements correlates with their synergistic hormone-dependent enhancer activity
    • MARTINEZ E and WAHLI W: Cooperative binding of estrogen receptor to imperfect estrogen-responsive DNA.elements correlates with their synergistic hormone-dependent enhancer activity. EMBO J. 8, 3781-3791, 1989
    • (1989) EMBO J. , vol.8 , pp. 3781-3791
    • Martinez, E.1    Wahli, W.2
  • 72
    • 0026472371 scopus 로고
    • Identification of a negative regulatory function for steroid receptors
    • MCDONNELL DP, VEGETO E, O'MALLEY BW: Identification of a negative regulatory function for steroid receptors. Proc Natl Acad Sci USA 89, 10563-10567, 1987, 1992
    • (1987) Proc Natl Acad Sci USA , vol.89 , pp. 10563-10567
    • Mcdonnell, D.P.1    Vegeto, E.2    O'Malley, B.W.3
  • 73
    • 0029038986 scopus 로고
    • Analysis of estrogen receptor function in vitro reveals three distinct classes of antiestrogens
    • MCDONNELL DP, CLEMM DL, HERMANN T et al.: Analysis of estrogen receptor function in vitro reveals three distinct classes of antiestrogens. Mol Endocrinol 9, 659-669, 1995
    • (1995) Mol Endocrinol , vol.9 , pp. 659-669
    • Mcdonnell, D.P.1    Clemm, D.L.2    Hermann, T.3
  • 74
    • 0033051731 scopus 로고    scopus 로고
    • Nuclear receptor coactivators: Multiple enzymes, multiple complexes, multiple functions
    • MCKENNA NJ, Xu JM, NAWAZ Z et al.: Nuclear receptor coactivators: multiple enzymes, multiple complexes, multiple functions. J. Steroid Biochem. Mol. Biol. 69, 1-6 Sp. Iss., 3-12, 1999
    • (1999) J. Steroid Biochem. Mol. Biol. , vol.69 , Issue.3-12 SPEC. ISSUE , pp. 1-6
    • Mckenna, N.J.1    Xu, J.M.2    Nawaz, Z.3
  • 75
    • 0033545929 scopus 로고    scopus 로고
    • PCAF associates with cyclin D1 and potentiates its activation of the estrogen receptor
    • MCMAHON C, SUTHIPHONGCHAI T, DIRENZO J et al.: PCAF associates with cyclin D1 and potentiates its activation of the estrogen receptor. Proc. Nat. Acad. Sci. USA, 96, 5382-5387, 1999
    • (1999) Proc. Nat. Acad. Sci. USA , vol.96 , pp. 5382-5387
    • Mcmahon, C.1    Suthiphongchai, T.2    Direnzo, J.3
  • 76
    • 0027259169 scopus 로고
    • Localization of the estrogen receptor locus (ESR) to chromosome 6q25.1 by FISH and a simple post-FISH banding technique
    • MENASCE LP, WHITE GR, HARRISON CJ et al.: Localization of the estrogen receptor locus (ESR) to chromosome 6q25.1 by FISH and a simple post-FISH banding technique. Genomics 17, 263-265, 1993
    • (1993) Genomics , vol.17 , pp. 263-265
    • Menasce, L.P.1    White, G.R.2    Harrison, C.J.3
  • 77
    • 0029058152 scopus 로고
    • The carboxy-terminal F domain of the human estrogen receptor: Role in the transcriptional activity of the receptor and the effectiveness of antiestrogens as estrogen antagonists
    • MONTANO MM., MULLER V, TROBAUGH A et al.: The carboxy-terminal F domain of the human estrogen receptor: Role in the transcriptional activity of the receptor and the effectiveness of antiestrogens as estrogen antagonists. Mol. Endocrinol. 9, 814-825, 1995
    • (1995) Mol. Endocrinol. , vol.9 , pp. 814-825
    • Montano, M.M.1    Muller, V.2    Trobaugh, A.3
  • 78
    • 0033536054 scopus 로고    scopus 로고
    • An estrogen receptor-selective coregulator that potentiates the effectivness of antiestrogens and represses the activity of estrogens
    • MONTANO MM, EKENA K, DELAGE-MOURROUX R et al.: An estrogen receptor-selective coregulator that potentiates the effectivness of antiestrogens and represses the activity of estrogens. Proc. Natl. Acad. Sci. USA 96, 6947-6952, 1999
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6947-6952
    • Montano, M.M.1    Ekena, K.2    Delage-Mourroux, R.3
  • 79
    • 0032898045 scopus 로고    scopus 로고
    • Estrogen: Mechanisms for a rapid action in CA1 hippocampal neurons
    • Moss RL and Gu Q: Estrogen: mechanisms for a rapid action in CA1 hippocampal neurons. Steroids 64, 1-2, 1999
    • (1999) Steroids , vol.64 , pp. 1-2
    • Moss, R.L.1    Gu, Q.2
  • 80
    • 0030593681 scopus 로고    scopus 로고
    • ERβ - Identification and characterisation of a novel human estrogen receptor
    • MOSSELMAN S, POLMAN J, DIJKEMA R: ERβ - identification and characterisation of a novel human estrogen receptor. FEBS Letters. 392, 49-53, 1996
    • (1996) FEBS Letters , vol.392 , pp. 49-53
    • Mosselman, S.1    Polman, J.2    Dijkema, R.3
  • 81
  • 82
    • 0034595096 scopus 로고    scopus 로고
    • Estrogen receptors: How do they control reproductive and nonreproductive functions?
    • MURAMATSU M and INOUE S: Estrogen receptors: How do they control reproductive and nonreproductive functions? Biochem. Biophys. Res. Commun. 270, 1-10, 2000
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 1-10
    • Muramatsu, M.1    Inoue, S.2
  • 83
    • 0025860708 scopus 로고
    • The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptors
    • NAAR AM, BOUTIN JM, LIPKINS SM et al.: The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptors. Cell 65, 1267-1279, 1991
    • (1991) Cell , vol.65 , pp. 1267-1279
    • Naar, A.M.1    Boutin, J.M.2    Lipkins, S.M.3
  • 84
    • 0022455431 scopus 로고
    • Mechanism of the rapid effect of 17β-estradiol on medial amygdala neurones
    • NABEKURA J, OOMURA Y, MINAMI T et al.: Mechanism of the rapid effect of 17β-estradiol on medial amygdala neurones. Science 233, 226-228, 1986
    • (1986) Science , vol.233 , pp. 226-228
    • Nabekura, J.1    Oomura, Y.2    Minami, T.3
  • 85
    • 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 89, 373-380, 1997
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.Y.2    Chakravarti, D.3
  • 86
    • 0022998095 scopus 로고
    • Dynamics of estrogen receptor turnover in uterine cells in vitro and in uteri in vivo
    • NARDULLI AM and KATZENELLENBOGEN BS: Dynamics of estrogen receptor turnover in uterine cells in vitro and in uteri in vivo. Endocrinology 119, 2038-2046, 1986
    • (1986) Endocrinology , vol.119 , pp. 2038-2046
    • Nardulli, A.M.1    Katzenellenbogen, B.S.2
  • 87
    • 0030818340 scopus 로고    scopus 로고
    • Vulnerability of the endocrine system to xenobiotic influence
    • NEUBERT D: Vulnerability of the endocrine system to xenobiotic influence. Regul. Toxicol. Pharmacol. 26, 9-29, 1997
    • (1997) Regul. Toxicol. Pharmacol. , vol.26 , pp. 9-29
    • Neubert, D.1
  • 88
    • 0030910962 scopus 로고    scopus 로고
    • Identification of a third autonomous activation domain within human estrogen receptor
    • NORRIS JD, FAN D, KERNER SA et al.: Identification of a third autonomous activation domain within human estrogen receptor. Mol. Endocrinol. 11, 747-754, 1997
    • (1997) Mol. Endocrinol. , vol.11 , pp. 747-754
    • Norris, J.D.1    Fan, D.2    Kerner, S.A.3
  • 90
    • 13044267130 scopus 로고    scopus 로고
    • Underdeveloped uterus and reduced estrogen responsiveness in mice with disruption of the estrogen-responsive finger protein gene, which is a direct target of estrogen receptor α
    • ORIMO A, INOUE S, MINOWA O et al.: Underdeveloped uterus and reduced estrogen responsiveness in mice with disruption of the estrogen-responsive finger protein gene, which is a direct target of estrogen receptor α. P.N.A.S., 96, 12027-12032, 1999
    • (1999) P.N.A.S. , vol.96 , pp. 12027-12032
    • Orimo, A.1    Inoue, S.2    Minowa, O.3
  • 91
    • 2642544810 scopus 로고    scopus 로고
    • Estrogen receptor (ER) modulators each induce distinct conformational changes in ERα and ERβ
    • PAIGE LA, CHRISTENSEN DJ, GRON H et al: Estrogen receptor (ER) modulators each induce distinct conformational changes in ERα and ERβ. Proc. Natl. Acad. Sci. USA 96, 3999-4004, 1999
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3999-4004
    • Paige, L.A.1    Christensen, D.J.2    Gron, H.3
  • 92
    • 0029197511 scopus 로고
    • Structure and function of estrogen receptors
    • Academic Press, London
    • PARKER MG: Structure and function of estrogen receptors. In: Vitamins and Hormones, vol. 15, pp. 267- 287, Academic Press, London 1995
    • (1995) Vitamins and Hormones , vol.15 , pp. 267-287
    • Parker, M.G.1
  • 93
    • 0032961682 scopus 로고    scopus 로고
    • Estrogen receptor domains E and F: Role in dimerization and interaction with coactivator RIP-140
    • PETERS GA and KHAN SA: Estrogen receptor domains E and F: Role in dimerization and interaction with coactivator RIP-140. Mol. Endocrinol. 13, 286-296, 1999
    • (1999) Mol. Endocrinol. , vol.13 , pp. 286-296
    • Peters, G.A.1    Khan, S.A.2
  • 94
    • 0030747070 scopus 로고    scopus 로고
    • Mouse estrogen receptor âforms estrogen response element-binding heterodimers with estrogen receptor a
    • PETTERSSON K, GRANDIEN K, KUIPER GGJM et al.: Mouse estrogen receptor âforms estrogen response element-binding heterodimers with estrogen receptor a. Mol. Endocrinol. 11, 1486-1496, 1997
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1486-1496
    • Pettersson, K.1    Grandien, K.2    Kuiper, G.G.J.M.3
  • 95
    • 0025382801 scopus 로고
    • Signal transduction by steroid hormones: Nuclear localisation is differently regulated in estrogen and glucocorticoid receptor
    • PICARD D, KUMAR V, CHAMBON P et al.: Signal transduction by steroid hormones: Nuclear localisation is differently regulated in estrogen and glucocorticoid receptor. Cell Regul. 1, 291-299, 1992
    • (1992) Cell Regul. , vol.1 , pp. 291-299
    • Picard, D.1    Kumar, V.2    Chambon, P.3
  • 96
    • 0017354142 scopus 로고
    • Specific binding sites for oestrogen at the outer surfaces of isolated endometrial cells
    • PIETRAS RJ and SZEGO CM: Specific binding sites for oestrogen at the outer surfaces of isolated endometrial cells. Nature 265, 69-72, 1977
    • (1977) Nature , vol.265 , pp. 69-72
    • Pietras, R.J.1    Szego, C.M.2
  • 97
    • 0026556328 scopus 로고
    • Cytosolic type II estrogen binding site in rat uterus: Specific photolabeling with estrone
    • POIROT M, CHAILLEUX C, BAYARD F: Cytosolic type II estrogen binding site in rat uterus: Specific photolabeling with estrone. J. Receptor Res. 12, 217-231, 1992
    • (1992) J. Receptor Res. , vol.12 , pp. 217-231
    • Poirot, M.1    Chailleux, C.2    Bayard, F.3
  • 98
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interaction with heat shock protein and immunophilin chaperones
    • PRATT WB and TOFT DO: Steroid receptor interaction with heat shock protein and immunophilin chaperones. Endocrine Rev. 18, 306-360, 1997
    • (1997) Endocrine Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 99
    • 0032052830 scopus 로고    scopus 로고
    • Isolation and characterisation of an estrogen binding protein which may integrate the plethora of estrogenic actions in non-reproductive organs
    • RAO BR: Isolation and characterisation of an estrogen binding protein which may integrate the plethora of estrogenic actions in non-reproductive organs. J. Steroid Biochem. Molec. Biol. 65, 3-41, 1998
    • (1998) J. Steroid Biochem. Molec. Biol. , vol.65 , pp. 3-41
    • Rao, B.R.1
  • 100
    • 0032462138 scopus 로고    scopus 로고
    • Nongenomic actions of steroids hormones in reproductive tissues
    • REVELLI A, MASSOBRIO M, TESARIK J: Nongenomic actions of steroids hormones in reproductive tissues. Endocrine Rev. 19, 3-17, 1998
    • (1998) Endocrine Rev. , vol.19 , pp. 3-17
    • Revelli, A.1    Massobrio, M.2    Tesarik, J.3
  • 101
    • 0034454583 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulators in action: Diversity for shared tasks
    • ROBYR D, WOLFFE AP, WAHLI W: Nuclear hormone receptor coregulators in action: Diversity for shared tasks. Mol. Endocrinol. 14, 329-347, 2000
    • (2000) Mol. Endocrinol. , vol.14 , pp. 329-347
    • Robyr, D.1    Wolffe, A.P.2    Wahli, W.3
  • 102
    • 0028838714 scopus 로고
    • Intracellular receptors and signal transducers and activators of transcription superfamilies: Novel target for small-molecule drug discovery
    • ROSEN J, DAY A, JONES TJ et al.: Intracellular receptors and signal transducers and activators of transcription superfamilies: Novel target for small-molecule drug discovery. J. Med. Chem. 38, 4855-4874, 1995
    • (1995) J. Med. Chem. , vol.38 , pp. 4855-4874
    • Rosen, J.1    Day, A.2    Jones, T.J.3
  • 103
    • 0034635553 scopus 로고    scopus 로고
    • Phosphorylation of steroid receptor coactivator-1. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway
    • ROWAN BG, WEIGEL NL, O'MALLEY BW: Phosphorylation of steroid receptor coactivator-1. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway. J. Biol. Chem. 275, 4475-4483, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 4475-4483
    • Rowan, B.G.1    Weigel, N.L.2    O'Malley, B.W.3
  • 104
    • 0032535024 scopus 로고    scopus 로고
    • Oestrogen receptor facilitates the formation of preinitiation complex assembly: Involvement of the general transcription factor TFIIB
    • SABBAH M, KANG KI, TORA L et al.: Oestrogen receptor facilitates the formation of preinitiation complex assembly: involvement of the general transcription factor TFIIB. Biochem. J.336, 639-646, 1998
    • (1998) Biochem. J. , vol.336 , pp. 639-646
    • Sabbah, M.1    Kang, K.I.2    Tora, L.3
  • 105
    • 0033051945 scopus 로고    scopus 로고
    • Messenger ribonucleic acid in situ hybridization analysis of estrogen receptor alpha and beta in human breast carcinoma
    • SASANO H, SUZUKI T, MATSUZAKI Y et al.: Messenger ribonucleic acid in situ hybridization analysis of estrogen receptor alpha and beta in human breast carcinoma. J. Clin. Endocrinol. Metab. 84, 781-785, 1999
    • (1999) J. Clin. Endocrinol. Metab. , vol.84 , pp. 781-785
    • Sasano, H.1    Suzuki, T.2    Matsuzaki, Y.3
  • 106
    • 0029417005 scopus 로고
    • Multiple TAFIIs directing synergistic activation of transcription
    • SAUER F, HANSEN SK, TJIAN R: Multiple TAFIIs directing synergistic activation of transcription. Science, 270, 1783-1788, 1995
    • (1995) Science , vol.270 , pp. 1783-1788
    • Sauer, F.1    Hansen, S.K.2    Tjian, R.3
  • 108
    • 0031764890 scopus 로고    scopus 로고
    • Changes in the structure of the ligand or substitutions to AF2 residues in the estrogen receptor make independent contributions to coactivator sensitivity by SRC-1
    • SCHWARTZ JA and BROOKS SC: Changes in the structure of the ligand or substitutions to AF2 residues in the estrogen receptor make independent contributions to coactivator sensitivity by SRC-1. J. Steroid Biochem. Molec. Biol. 67, 223-232, 1998
    • (1998) J. Steroid Biochem. Molec. Biol. , vol.67 , pp. 223-232
    • Schwartz, J.A.1    Brooks, S.C.2
  • 109
    • 0030789691 scopus 로고    scopus 로고
    • NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor - 2
    • SEM DS, CASIMIRO DR, KLIEWER SA et al.: NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor - 2. J. Biol. Chem. 272, 18038-18043, 1997
    • (1997) J. Biol. Chem. , vol.272 , pp. 18038-18043
    • Sem, D.S.1    Casimiro, D.R.2    Kliewer, S.A.3
  • 110
    • 0031571669 scopus 로고    scopus 로고
    • Human estrogen receptor-like 1 (ESRL1) gene: Genomic organization, chromosomal localization, and promoter characterization
    • SHI H, SHIGETA H, YANG N et al.: Human estrogen receptor-like 1 (ESRL1) gene: genomic organization, chromosomal localization, and promoter characterization. Genomics 44, 52-60, 1997
    • (1997) Genomics , vol.44 , pp. 52-60
    • Shi, H.1    Shigeta, H.2    Yang, N.3
  • 111
    • 0030787844 scopus 로고    scopus 로고
    • The orphan nuclear receptor estrogen-related receptor α is a transcriptional regulator of the human medium-chain acyl coenzyme A dehydrogenase gene
    • SLADEK R, BADER JA, GIGUERE V: The orphan nuclear receptor estrogen-related receptor α is a transcriptional regulator of the human medium-chain acyl coenzyme A dehydrogenase gene. MoL. Cell. Biol. 17, 5400-5409, 1997
    • (1997) MoL. Cell. Biol. , vol.17 , pp. 5400-5409
    • Sladek, R.1    Bader, J.A.2    Giguere, V.3
  • 112
    • 0024239029 scopus 로고
    • Assignment of estradiol receptor gene to mouse chromosome 10
    • SLUYSTER M, RIJKERS AW, DE GOEIJ CC et al.: Assignment of estradiol receptor gene to mouse chromosome 10. J. Steroid Biochem. 31, 757-761, 1988
    • (1988) J. Steroid Biochem. , vol.31 , pp. 757-761
    • Sluyster, M.1    Rijkers, A.W.2    De Goeij, C.C.3
  • 113
    • 0033083820 scopus 로고    scopus 로고
    • Coexpression of estrogen receptor alpha and beta: Poor prognostic factors in human breast cancer?
    • SPEIRS V, PARKES AT, KERIN MJ et al.: Coexpression of estrogen receptor alpha and beta: poor prognostic factors in human breast cancer? Cancer Res. 59, 525-528, 1999
    • (1999) Cancer Res. , vol.59 , pp. 525-528
    • Speirs, V.1    Parkes, A.T.2    Kerin, M.J.3
  • 114
    • 0342470960 scopus 로고    scopus 로고
    • Alternative splicing and expression of the mouse estrogen receptor-related receptor gamma
    • SUESENS U, HERMANSBORGMEYER I, BORGMEYER U: Alternative splicing and expression of the mouse estrogen receptor-related receptor gamma. Biochem. Biophys. Res. Commun. 267, 532-535, 2000
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 532-535
    • Suesens, U.1    Hermansborgmeyer, I.2    Borgmeyer, U.3
  • 115
    • 0033347396 scopus 로고    scopus 로고
    • Opposing effects of corepressors and coactivators in determining the doseresponse curve of agonists, and residual agonist activity of antagonists, for glucocorticoid receptor-regulated gene expression
    • SZAPARY D, HUANG Y, SIMONS SS: Opposing effects of corepressors and coactivators in determining the doseresponse curve of agonists, and residual agonist activity of antagonists, for glucocorticoid receptor-regulated gene expression. Mol. Endocrinol. 13, 2108-2121, 1999
    • (1999) Mol. Endocrinol. , vol.13 , pp. 2108-2121
    • Szapary, D.1    Huang, Y.2    Simons, S.S.3
  • 116
    • 0003032256 scopus 로고
    • Parallels in the models of action of peptide and steroid hormones: Membrane effects and cellular entry
    • (Ed. Kearns KW) Pleum Publishing, New York
    • SZEGO CM: Parallels in the models of action of peptide and steroid hormones: membrane effects and cellular entry. In: Structure and Function of the Gonadotropins, (Ed. Kearns KW) pp. 431-472, Pleum Publishing, New York, 1978
    • (1978) Structure and Function of the Gonadotropins , pp. 431-472
    • Szego, C.M.1
  • 117
    • 0034002645 scopus 로고    scopus 로고
    • Immunolocalisation of estrogen receptor beta in human tissues
    • TAYLOR AH and ALAZZAWI F: Immunolocalisation of estrogen receptor beta in human tissues. J. Mol. Endocrin. 24, 145-155, 2000
    • (2000) J. Mol. Endocrin. , vol.24 , pp. 145-155
    • Taylor, A.H.1    Alazzawi, F.2
  • 118
    • 0029985338 scopus 로고    scopus 로고
    • Nuclear orphan receptor as a represser of glucocorticoid receptor transcriptional activity
    • TRAPP T and HOLSBOER F: Nuclear orphan receptor as a represser of glucocorticoid receptor transcriptional activity. J. Biol. Chem. 271, 9879-9882, 1996
    • (1996) J. Biol. Chem. , vol.271 , pp. 9879-9882
    • Trapp, T.1    Holsboer, F.2
  • 119
    • 0031043390 scopus 로고    scopus 로고
    • Cloning, chromosomal localisation, and functional analysis of the murine estrogen receptor β
    • TREMBLAY GB, TREMBLAY A, COPELAND NG et al.: Cloning, chromosomal localisation, and functional analysis of the murine estrogen receptor β. Mol. Endocrinol. 11, 353-365, 1997
    • (1997) Mol. Endocrinol. , vol.11 , pp. 353-365
    • Tremblay, G.B.1    Tremblay, A.2    Copeland, N.G.3
  • 120
    • 0033053616 scopus 로고    scopus 로고
    • Dominant activity of activation function (AF1) and differential stoichiometric requirements for AF-1 and - 2 in the estrogen receptor α-β heterodimeric complex
    • TREMBLAY GB, TREMBLAY A, LABRIE F et al.: Dominant activity of activation function (AF1) and differential stoichiometric requirements for AF-1 and - 2 in the estrogen receptor α-β heterodimeric complex. Mol. Cell. Biol. 19, 1919-1927, 1999
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1919-1927
    • Tremblay, G.B.1    Tremblay, A.2    Labrie, F.3
  • 121
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • TSAI MJ and O'MALLEY BW: Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63, 451-486, 1994
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-486
    • Tsai, M.J.1    O'Malley, B.W.2
  • 122
    • 0032941148 scopus 로고    scopus 로고
    • Ontogeny of estrogen receptor-beta expression in rat testis
    • VANPELT AMM, DEROOIJ DG, VANDERBURG B et al.: Ontogeny of estrogen receptor-beta expression in rat testis. Endocrinology 140, 478-483, 1999
    • (1999) Endocrinology , vol.140 , pp. 478-483
    • Vanpelt, A.M.M.1    Derooij, D.G.2    Vanderburg, B.3
  • 124
    • 0033305460 scopus 로고    scopus 로고
    • Transcriptional activities of the orphan nuclear receptor ERRα (estrogen receptor-related receptor-α)
    • VANACKER JM, BONNELYE E, CHOPIN-DELANNOY S et al.: Transcriptional activities of the orphan nuclear receptor ERRα (estrogen receptor-related receptor-α). Mol. Endocrinol. 13, 764-773, 1999
    • (1999) Mol. Endocrinol. , vol.13 , pp. 764-773
    • Vanacker, J.M.1    Bonnelye, E.2    Chopin-Delannoy, S.3
  • 125
    • 0031561119 scopus 로고    scopus 로고
    • Agonistic effect of tamoxifen is dependent on cell type, ERE-promoter context, and estrogen receptor subtype: Functional difference between estrogen receptors α and β
    • WATANABE T, INOUE S, SUMITO O et al: Agonistic effect of tamoxifen is dependent on cell type, ERE-promoter context, and estrogen receptor subtype: Functional difference between estrogen receptors α and β. Biochem. Biophys. Res. Commun. 236, 140-145, 1997
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 140-145
    • Watanabe, T.1    Inoue, S.2    Sumito, O.3
  • 126
    • 0028783678 scopus 로고
    • The other estrogen receptor in the plasma inembrane: Implication for the action of environmental estrogens
    • WATSON CS, PAPPAS TC, GAMETCHU B: The other estrogen receptor in the plasma inembrane: Implication for the action of environmental estrogens. Environ. Health Perspect. 103, (Suppl. 7), 41-50, 1995
    • (1995) Environ. Health Perspect. , vol.103 , Issue.7 SUPPL. , pp. 41-50
    • Watson, C.S.1    Pappas, T.C.2    Gametchu, B.3
  • 127
    • 0032951143 scopus 로고    scopus 로고
    • Membrane-initiated steroid actions and the proteins that mediate them
    • WATSON CS and GAMETCHU B: Membrane-initiated steroid actions and the proteins that mediate them. P. S. E. B. M. 220, 9-19, 1999
    • (1999) P. S. E. B. M. , vol.220 , pp. 9-19
    • Watson, C.S.1    Gametchu, B.2
  • 128
    • 0032929779 scopus 로고    scopus 로고
    • Rapid actions of estrogens in GH(3)/6 pituitary tumor cells via a plasma membrane version of estrogen receptor-alpha
    • WATSON CS, NORFLEET AM, PAPPAS TC et al.: Rapid actions of estrogens in GH(3)/6 pituitary tumor cells via a plasma membrane version of estrogen receptor-alpha. Steroids 64, 1-2, 1999
    • (1999) Steroids , vol.64 , pp. 1-2
    • Watson, C.S.1    Norfleet, A.M.2    Pappas, T.C.3
  • 129
    • 0028901194 scopus 로고
    • Tamoxifen activation of the estrogen receptor/AP-1 pathway: Potential origin for the cell-specific estrogen-like effects of antiestrogens
    • WEBB P, LOPEZ GN, UHT RM et al.: Tamoxifen activation of the estrogen receptor/AP-1 pathway: Potential origin for the cell-specific estrogen-like effects of antiestrogens. Mol. Endocrinol. 9, 443-456, 1995
    • (1995) Mol. Endocrinol. , vol.9 , pp. 443-456
    • Webb, P.1    Lopez, G.N.2    Uht, R.M.3
  • 130
    • 0029855010 scopus 로고    scopus 로고
    • Steroid hormone receptors and their regulation by phosphorylation
    • WEIGEL NLW: Steroid hormone receptors and their regulation by phosphorylation. Biochem. J. 319, 657-667, 1996
    • (1996) Biochem. J. , vol.319 , pp. 657-667
    • Weigel, N.L.W.1
  • 131
    • 0034705032 scopus 로고    scopus 로고
    • Estrogen receptor (ER) β, a modulator of ERα in the uterus
    • WEIHUA Z. SAJI S, MAKINEN S et al.: Estrogen receptor (ER) β, a modulator of ERα in the uterus. PNAS, 97, 5936-5941, 2000
    • (2000) PNAS , vol.97 , pp. 5936-5941
    • Weihua, Z.1    Saji, S.2    Makinen, S.3
  • 132
    • 0033305525 scopus 로고    scopus 로고
    • Comparative analyses of mechanistic differences among antiestrogens
    • WIJAVARATNE AL, NAGEL SC, PAIGE LA et al.: Comparative analyses of mechanistic differences among antiestrogens. Endocrinology 140, 5828-5840, 1999
    • (1999) Endocrinology , vol.140 , pp. 5828-5840
    • Wijavaratne, A.L.1    Nagel, S.C.2    Paige, L.A.3
  • 133
    • 0027429921 scopus 로고
    • ESV40 early-to-late switch involves titration of cellular transcriptional repressors
    • WILEY SR, KRAUS RJ, Zuo F et al.: ESV40 early-to-late switch involves titration of cellular transcriptional repressors. Genes Dev. 7, 2206-2219, 1993
    • (1993) Genes Dev. , vol.7 , pp. 2206-2219
    • Wiley, S.R.1    Kraus, R.J.2    Zuo, F.3
  • 134
    • 0033981644 scopus 로고    scopus 로고
    • Increased expression of estrogen receptor beta in human uterine smooth muslce at term
    • WU JJ, GEIMONEN E, ANDERSEN J: Increased expression of estrogen receptor beta in human uterine smooth muslce at term. Europ. J. Endocrinol. 142, 92-99, 2000
    • (2000) Europ. J. Endocrinol. , vol.142 , pp. 92-99
    • Wu, J.J.1    Geimonen, E.2    Andersen, J.3
  • 135
    • 0032913586 scopus 로고    scopus 로고
    • Cloning, in vitro expression, and novel phylogenetic classification of a channel catfish estrogen receptor
    • XIA ZF, PATINO R, GALE WL et al.: Cloning, in vitro expression, and novel phylogenetic classification of a channel catfish estrogen receptor. General Comp. Endocrin. 113, 360-368, 1999
    • (1999) General Comp. Endocrin. , vol.113 , pp. 360-368
    • Xia, Z.F.1    Patino, R.2    Gale, W.L.3
  • 136
    • 0033345059 scopus 로고    scopus 로고
    • Constitutive activation of transcription and binding of coactivator by estrogen-related receptors 1 and 2
    • XIE W, HONG H, YANG NN et al.: Constitutive activation of transcription and binding of coactivator by estrogen-related receptors 1 and 2. Mol. Endocrinol. 13, 2151-2162, 2000
    • (2000) Mol. Endocrinol. , vol.13 , pp. 2151-2162
    • Xie, W.1    Hong, H.2    Yang, N.N.3
  • 137
    • 0029965083 scopus 로고    scopus 로고
    • Estrogen-related receptor, hERR1, modulates estrogen receptor-mediated response of human lactoferrin gene promoter
    • YANG N, SHIGETA H, SHI H et al.: Estrogen-related receptor, hERR1, modulates estrogen receptor-mediated response of human lactoferrin gene promoter. J. Biol. Chem. 271, 5795-5804, 1996
    • (1996) J. Biol. Chem. , vol.271 , pp. 5795-5804
    • Yang, N.1    Shigeta, H.2    Shi, H.3
  • 138
    • 0032535306 scopus 로고    scopus 로고
    • Modulation of aromatase expression in the breast tissue by ERRα-1 orphan receptor
    • YANG CH, ZHOU D, CHEN S: Modulation of aromatase expression in the breast tissue by ERRα-1 orphan receptor. Cancer Res. 58, 5695-5700, 1998
    • (1998) Cancer Res. , vol.58 , pp. 5695-5700
    • Yang, C.H.1    Zhou, D.2    Chen, S.3
  • 139
    • 0026713869 scopus 로고
    • Cooperation of protosignals for nuclear accumulation of estrogen and progesterone receptors
    • YLIKOMI T, BOCQUEL MT, BERRY M et al.: Cooperation of protosignals for nuclear accumulation of estrogen and progesterone receptors. EMBO J. 11, 3681-3694, 1992
    • (1992) EMBO J. , vol.11 , pp. 3681-3694
    • Ylikomi, T.1    Bocquel, M.T.2    Berry, M.3
  • 140
    • 0029042392 scopus 로고
    • Common themes in assembly and function of eukaryotic transcription complexes
    • ZAWEL L and RIENBERG D: Common themes in assembly and function of eukaryotic transcription complexes. Annu. Rev. Biochem. 64, 533-561, 1995
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 533-561
    • Zawel, L.1    Rienberg, D.2
  • 141
    • 0030968438 scopus 로고    scopus 로고
    • CDK-independent activation of estrogen receptor by cyclin Dl
    • ZWIJSEN RML, WIENTJENS E, KLOMPMAKER R et al.: CDK-independent activation of estrogen receptor by cyclin Dl. Cell 88, 405-415, 1997
    • (1997) Cell , vol.88 , pp. 405-415
    • Rml, Z.1    Wientjens, E.2    Klompmaker, R.3


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