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Volumn 148, Issue 10, 2007, Pages 4634-4641

A functional serine 118 phosphorylation site in estrogen receptor-α is required for down-regulation of gene expression by 17β-estradiol and 4-hydroxytamoxifen

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 4 HYDROXYTAMOXIFEN; ANGIOTENSINOGEN; CYTOKERATIN 13; CYTOKERATIN 19; ESTRADIOL; ESTROGEN RECEPTOR ALPHA; FULVESTRANT; INTERLEUKIN 6; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; NOTCH3 RECEPTOR; PROLACTIN; SMAD3 PROTEIN; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR SP1;

EID: 34748864669     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2007-0148     Document Type: Article
Times cited : (51)

References (63)
  • 2
    • 0033278993 scopus 로고    scopus 로고
    • Transcriptional activation of insulin-like growth factor-binding protein-4 by 17β-estradiol in MCF-7 cells: Role of estrogen receptor-Sp1 complexes
    • Qin C, Singh P, Safe S 1999 Transcriptional activation of insulin-like growth factor-binding protein-4 by 17β-estradiol in MCF-7 cells: role of estrogen receptor-Sp1 complexes. Endocrinology 140:2501-2508
    • (1999) Endocrinology , vol.140 , pp. 2501-2508
    • Qin, C.1    Singh, P.2    Safe, S.3
  • 3
    • 0035228654 scopus 로고    scopus 로고
    • Transcriptional activation of genes by 17β-estradiol through estrogen receptor-Sp1 interactions
    • Safe S 2001 Transcriptional activation of genes by 17β-estradiol through estrogen receptor-Sp1 interactions. Vitam Horm 62:231-252
    • (2001) Vitam Horm , vol.62 , pp. 231-252
    • Safe, S.1
  • 4
    • 0035958041 scopus 로고    scopus 로고
    • Estrogen receptor binding to DNA is not required for its activity through the nonclassical AP1 pathway
    • Jakacka M, Ito M, Weiss J, Chien PY, Gehm BD, Jameson JL 2001 Estrogen receptor binding to DNA is not required for its activity through the nonclassical AP1 pathway. J Biol Chem 276:13615-13621
    • (2001) J Biol Chem , vol.276 , pp. 13615-13621
    • Jakacka, M.1    Ito, M.2    Weiss, J.3    Chien, P.Y.4    Gehm, B.D.5    Jameson, J.L.6
  • 6
    • 33747841976 scopus 로고    scopus 로고
    • Nature of functional estrogen receptors at the plasma membrane
    • Pedram A, Razandi M, Levin ER 2006 Nature of functional estrogen receptors at the plasma membrane. Mol Endocrinol 20:1996-2009
    • (2006) Mol Endocrinol , vol.20 , pp. 1996-2009
    • Pedram, A.1    Razandi, M.2    Levin, E.R.3
  • 7
    • 23744447497 scopus 로고    scopus 로고
    • Integration of the extranuclear and nuclear actions of estrogen
    • Levin ER 2005 Integration of the extranuclear and nuclear actions of estrogen. Mol Endocrinol 19:1951-1959
    • (2005) Mol Endocrinol , vol.19 , pp. 1951-1959
    • Levin, E.R.1
  • 8
    • 3142511046 scopus 로고    scopus 로고
    • Receptor mechanisms of rapid extranuclear signalling initiated by steroid hormones
    • Boonyaratanakornkit V, Edwards DP 2004 Receptor mechanisms of rapid extranuclear signalling initiated by steroid hormones. Essays Biochem 40:105-120
    • (2004) Essays Biochem , vol.40 , pp. 105-120
    • Boonyaratanakornkit, V.1    Edwards, D.P.2
  • 9
    • 0037069418 scopus 로고    scopus 로고
    • Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade
    • Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ 2002 Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci USA 99:14783-14788
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14783-14788
    • Wong, C.W.1    McNally, C.2    Nickbarg, E.3    Komm, B.S.4    Cheskis, B.J.5
  • 10
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG 2000 The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 14:121-141
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 11
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna NJ, O'Malley BW 2002 Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108:465-474
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 12
    • 7244247363 scopus 로고    scopus 로고
    • Estrogen response element-dependent regulation of transcriptional activation of estrogen receptors α and β by coactivators and corepressors
    • Klinge CM, Jernigan SC, Mattingly KA, Risinger KE, Zhang J 2004 Estrogen response element-dependent regulation of transcriptional activation of estrogen receptors α and β by coactivators and corepressors. J Mol Endocrinol 33:387-410
    • (2004) J Mol Endocrinol , vol.33 , pp. 387-410
    • Klinge, C.M.1    Jernigan, S.C.2    Mattingly, K.A.3    Risinger, K.E.4    Zhang, J.5
  • 13
    • 0036185782 scopus 로고    scopus 로고
    • Allosteric regulation of estrogen receptor structure, function, and coactivator recruitment by different estrogen response elements
    • Hall JM, McDonnell DP, Korach KS 2002 Allosteric regulation of estrogen receptor structure, function, and coactivator recruitment by different estrogen response elements. Mol Endocrinol 16:469-486
    • (2002) Mol Endocrinol , vol.16 , pp. 469-486
    • Hall, J.M.1    McDonnell, D.P.2    Korach, K.S.3
  • 14
    • 0035962033 scopus 로고    scopus 로고
    • Estrogen response element sequence impacts the conformation and transcriptional activity of estrogen receptor α
    • Klinge CM, Jernigan SC, Smith SL, Tyulmenkov VV, Kulakosky PC 2001 Estrogen response element sequence impacts the conformation and transcriptional activity of estrogen receptor α. Mol Cell Endocrinol 174:151-166
    • (2001) Mol Cell Endocrinol , vol.174 , pp. 151-166
    • Klinge, C.M.1    Jernigan, S.C.2    Smith, S.L.3    Tyulmenkov, V.V.4    Kulakosky, P.C.5
  • 15
    • 0035976933 scopus 로고    scopus 로고
    • Estrogen response elements alter coactivator recruitment through allosteric modulation of estrogen receptor β conformation
    • Loven MA, Likhite VS, Choi I, Nardulli AM 2001 Estrogen response elements alter coactivator recruitment through allosteric modulation of estrogen receptor β conformation. J Biol Chem 276:45282-45288
    • (2001) J Biol Chem , vol.276 , pp. 45282-45288
    • Loven, M.A.1    Likhite, V.S.2    Choi, I.3    Nardulli, A.M.4
  • 16
    • 0035811531 scopus 로고    scopus 로고
    • Interaction of estrogen receptors α and β with estrogen response elements
    • Loven MA, Wood JR, Nardulli AM 2001 Interaction of estrogen receptors α and β with estrogen response elements. Mol Cell Endocrinol 181:151-163
    • (2001) Mol Cell Endocrinol , vol.181 , pp. 151-163
    • Loven, M.A.1    Wood, J.R.2    Nardulli, A.M.3
  • 17
    • 0031900850 scopus 로고    scopus 로고
    • Estrogen response elements function as allosteric modulators of estrogen receptor conformation
    • Wood JR, Greene GL, Nardulli AM 1998 Estrogen response elements function as allosteric modulators of estrogen receptor conformation. Mol Cell Biol 18:1927-1934
    • (1998) Mol Cell Biol , vol.18 , pp. 1927-1934
    • Wood, J.R.1    Greene, G.L.2    Nardulli, A.M.3
  • 18
    • 0034969440 scopus 로고    scopus 로고
    • Allosteric modulation of estrogen receptor conformation by different estrogen response elements
    • Wood JR, Likhite VS, Loven MA, Nardulli AM 2001 Allosteric modulation of estrogen receptor conformation by different estrogen response elements. Mol Endocrinol 15:1114-1126
    • (2001) Mol Endocrinol , vol.15 , pp. 1114-1126
    • Wood, J.R.1    Likhite, V.S.2    Loven, M.A.3    Nardulli, A.M.4
  • 19
    • 1042301372 scopus 로고    scopus 로고
    • Interplay between estrogen response element sequence and ligands controls in vivo binding of estrogen receptor to regulated genes
    • Krieg AJ, Krieg SA, Ahn BS, Shapiro DJ 2004 Interplay between estrogen response element sequence and ligands controls in vivo binding of estrogen receptor to regulated genes. J Biol Chem 279:5025-5034
    • (2004) J Biol Chem , vol.279 , pp. 5025-5034
    • Krieg, A.J.1    Krieg, S.A.2    Ahn, B.S.3    Shapiro, D.J.4
  • 21
    • 0025062215 scopus 로고
    • Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen
    • Berry M, Metzger D, Chambon P 1990 Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen. EMBO J 9:2811-2818
    • (1990) EMBO J , vol.9 , pp. 2811-2818
    • Berry, M.1    Metzger, D.2    Chambon, P.3
  • 24
    • 0027258030 scopus 로고
    • Peptide growth factors elicit estrogen receptor-dependent transcriptional activation of an estrogen-responsive element
    • Ignar-Trowbridge DM, Teng CT, Ross KA, Parker MG, Korach KS, McLachlan JA 1993 Peptide growth factors elicit estrogen receptor-dependent transcriptional activation of an estrogen-responsive element. Mol Endocrinol 7:992-998
    • (1993) Mol Endocrinol , vol.7 , pp. 992-998
    • Ignar-Trowbridge, D.M.1    Teng, C.T.2    Ross, K.A.3    Parker, M.G.4    Korach, K.S.5    McLachlan, J.A.6
  • 25
    • 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, Picard D 1996 Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. EMBO J 15:2174-2183
    • (1996) EMBO J , vol.15 , pp. 2174-2183
    • Bunone, G.1    Briand, P.A.2    Miksicek, R.J.3    Picard, D.4
  • 27
    • 0035120348 scopus 로고    scopus 로고
    • Signal transduction through the Ras/Erk pathway is essential for the mycoestrogen zearalenone-induced cell-cycle progression in MCF-7 cells
    • Ahamed S, Foster JS, Bukovsky A, Wimalasena J 2001 Signal transduction through the Ras/Erk pathway is essential for the mycoestrogen zearalenone-induced cell-cycle progression in MCF-7 cells. Mol Carcinog 30:88-98
    • (2001) Mol Carcinog , vol.30 , pp. 88-98
    • Ahamed, S.1    Foster, J.S.2    Bukovsky, A.3    Wimalasena, J.4
  • 28
    • 0028111526 scopus 로고
    • Phosphorylation of the human estrogen receptor. Identification of hormone-regulated sites and examination of their influence on transcriptional activity
    • Le Goff P, Montano MM, Schodin DJ, Katzenellenbogen BS 1994 Phosphorylation of the human estrogen receptor. Identification of hormone-regulated sites and examination of their influence on transcriptional activity. J Biol Chem 269:4458-4466
    • (1994) J Biol Chem , vol.269 , pp. 4458-4466
    • Le Goff, P.1    Montano, M.M.2    Schodin, D.J.3    Katzenellenbogen, B.S.4
  • 29
    • 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, Chambon P 1993 Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region. EMBO J 12:1153-1160
    • (1993) EMBO J , vol.12 , pp. 1153-1160
    • Ali, S.1    Metzger, D.2    Bornert, J.M.3    Chambon, P.4
  • 30
    • 0029163578 scopus 로고
    • Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor
    • Joel PB, Traish AM, Lannigan DA 1995 Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Mol Endocrinol 9:1041-1052
    • (1995) Mol Endocrinol , vol.9 , pp. 1041-1052
    • Joel, P.B.1    Traish, A.M.2    Lannigan, D.A.3
  • 31
    • 0033120030 scopus 로고    scopus 로고
    • Ligand-independent recruitment of SRC-1 to estrogen receptor β through phosphorylation of activation function AF-1
    • Tremblay A, Tremblay GB, Labrie F, Giguere V 1999 Ligand-independent recruitment of SRC-1 to estrogen receptor β through phosphorylation of activation function AF-1. Mol Cell 3:513-519
    • (1999) Mol Cell , vol.3 , pp. 513-519
    • Tremblay, A.1    Tremblay, G.B.2    Labrie, F.3    Giguere, V.4
  • 32
    • 0035134504 scopus 로고    scopus 로고
    • Potentiation of estrogen receptor activation function 1 (AF-1) by Src/JNK through a serine 118-independent pathway
    • Feng W, Webb P, Nguyen P, Liu X, Li J, Karin M, Kushner PJ 2001 Potentiation of estrogen receptor activation function 1 (AF-1) by Src/JNK through a serine 118-independent pathway. Mol Endocrinol 15:32-45
    • (2001) Mol Endocrinol , vol.15 , pp. 32-45
    • Feng, W.1    Webb, P.2    Nguyen, P.3    Liu, X.4    Li, J.5    Karin, M.6    Kushner, P.J.7
  • 33
    • 0141785350 scopus 로고    scopus 로고
    • Profiling of estrogen up- and down-regulated gene expression in human breast cancer cells: Insights into gene networks and pathways underlying estrogenic control of proliferation and cell phenotype
    • Frasor J, Danes JM, Komm B, Chang KC, Lyttle CR, Katzenellenbogen BS 2003 Profiling of estrogen up- and down-regulated gene expression in human breast cancer cells: insights into gene networks and pathways underlying estrogenic control of proliferation and cell phenotype. Endocrinology 144:4562-4574
    • (2003) Endocrinology , vol.144 , pp. 4562-4574
    • Frasor, J.1    Danes, J.M.2    Komm, B.3    Chang, K.C.4    Lyttle, C.R.5    Katzenellenbogen, B.S.6
  • 34
    • 33745188029 scopus 로고    scopus 로고
    • Estrogen-occupied estrogen receptor represses cyclin G2 gene expression and recruits a repressor complex at the cyclin G2 promoter
    • Stossi F, Likhite VS, Katzenellenbogen JA, Katzenellenbogen BS 2006 Estrogen-occupied estrogen receptor represses cyclin G2 gene expression and recruits a repressor complex at the cyclin G2 promoter. J Biol Chem 281:16272-16278
    • (2006) J Biol Chem , vol.281 , pp. 16272-16278
    • Stossi, F.1    Likhite, V.S.2    Katzenellenbogen, J.A.3    Katzenellenbogen, B.S.4
  • 35
    • 13944252475 scopus 로고    scopus 로고
    • Transcription factor cross-talk: The estrogen receptor and NF-κB
    • Kalaitzidis D, Gilmore TD 2005 Transcription factor cross-talk: the estrogen receptor and NF-κB. Trends Endocrinol Metab 16:46-52
    • (2005) Trends Endocrinol Metab , vol.16 , pp. 46-52
    • Kalaitzidis, D.1    Gilmore, T.D.2
  • 37
    • 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, Notides AC, Sasson S 1997 Estradiol-binding mechanism and binding capacity of the human estrogen receptor is regulated by tyrosine phosphorylation. Mol Endocrinol 11:48-53
    • (1997) Mol Endocrinol , vol.11 , pp. 48-53
    • Arnold, S.F.1    Melamed, M.2    Vorojeikina, D.P.3    Notides, A.C.4    Sasson, S.5
  • 38
    • 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 1995 Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element. J Biol Chem 270:30205-30212
    • (1995) J Biol Chem , vol.270 , pp. 30205-30212
    • Arnold, S.F.1    Vorojeikina, D.P.2    Notides, A.C.3
  • 39
    • 0028833473 scopus 로고
    • Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro
    • Arnold SF, Obourn JD, Jaffe H, Notides AC 1995 Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro. Mol Endocrinol 9:24-33
    • (1995) Mol Endocrinol , vol.9 , pp. 24-33
    • Arnold, S.F.1    Obourn, J.D.2    Jaffe, H.3    Notides, A.C.4
  • 41
    • 0023761997 scopus 로고
    • Phosphorylation of estradiol receptor on tyrosine and interaction of estradiol and glucocorticoid receptors with antiphosphotyrosine antibodies
    • Auricchio F, Migliaccio A, Castoria G, Rotondi A, Di Domenico M, Pagano M, Nola E 1988 Phosphorylation of estradiol receptor on tyrosine and interaction of estradiol and glucocorticoid receptors with antiphosphotyrosine antibodies. Adv Exp Med Biol 231:519-540
    • (1988) Adv Exp Med Biol , vol.231 , pp. 519-540
    • Auricchio, F.1    Migliaccio, A.2    Castoria, G.3    Rotondi, A.4    Di Domenico, M.5    Pagano, M.6    Nola, E.7
  • 42
    • 0037211754 scopus 로고    scopus 로고
    • Estrogen receptor phosphorylation
    • Lannigan DA 2003 Estrogen receptor phosphorylation. Steroids 68:1-9
    • (2003) Steroids , vol.68 , pp. 1-9
    • Lannigan, D.A.1
  • 43
    • 0026644374 scopus 로고
    • Estrogen receptor phosphorylation. Hormonal dependence and consequence on specific DNA binding
    • Denton RR, Koszewski NJ, Notides AC 1992 Estrogen receptor phosphorylation. Hormonal dependence and consequence on specific DNA binding. J Biol Chem 267:7263-7268
    • (1992) J Biol Chem , vol.267 , pp. 7263-7268
    • Denton, R.R.1    Koszewski, N.J.2    Notides, A.C.3
  • 44
    • 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-I
    • Aronica SM, Katzenellenbogen BS 1993 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-I. Mol Endocrinol 7:743-752
    • (1993) Mol Endocrinol , vol.7 , pp. 743-752
    • Aronica, S.M.1    Katzenellenbogen, B.S.2
  • 45
    • 0025975455 scopus 로고
    • Uterine estrogen receptor in vivo: Phosphorylation of nuclear specific forms on serine residues
    • Washburn T, Hocutt A, Brautigan DL, Korach KS 1991 Uterine estrogen receptor in vivo: phosphorylation of nuclear specific forms on serine residues. Mol Endocrinol 5:235-242
    • (1991) Mol Endocrinol , vol.5 , pp. 235-242
    • Washburn, T.1    Hocutt, A.2    Brautigan, D.L.3    Korach, K.S.4
  • 46
    • 0028049163 scopus 로고
    • Characterization of ligand-dependent phosphorylation of the estrogen receptor
    • Lahooti H, White R, Danielian PS, Parker MG 1994 Characterization of ligand-dependent phosphorylation of the estrogen receptor. Mol Endocrinol 8:182-188
    • (1994) Mol Endocrinol , vol.8 , pp. 182-188
    • Lahooti, H.1    White, R.2    Danielian, P.S.3    Parker, M.G.4
  • 49
    • 0031594574 scopus 로고    scopus 로고
    • pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167
    • Joel PB, Smith J, Sturgill TW, Fisher TL, Blenis J, Lannigan DA 1998 pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167. Mol Cell Biol 18:1978-1984
    • (1998) Mol Cell Biol , vol.18 , pp. 1978-1984
    • Joel, P.B.1    Smith, J.2    Sturgill, T.W.3    Fisher, T.L.4    Blenis, J.5    Lannigan, D.A.6
  • 50
    • 0030822421 scopus 로고    scopus 로고
    • Dimerizing the estrogen receptor DNA binding domain enhances binding to estrogen response elements
    • Kuntz MA, Shapiro DJ 1997 Dimerizing the estrogen receptor DNA binding domain enhances binding to estrogen response elements. J Biol Chem 272:27949-27956
    • (1997) J Biol Chem , vol.272 , pp. 27949-27956
    • Kuntz, M.A.1    Shapiro, D.J.2
  • 51
    • 0033313939 scopus 로고    scopus 로고
    • HMG-1 stimulates estrogen response element binding by estrogen receptor from stably transfected HeLa cells
    • Zhang CC, Krieg S, Shapiro DJ 1999 HMG-1 stimulates estrogen response element binding by estrogen receptor from stably transfected HeLa cells. Mol Endocrinol 13:632-643
    • (1999) Mol Endocrinol , vol.13 , pp. 632-643
    • Zhang, C.C.1    Krieg, S.2    Shapiro, D.J.3
  • 52
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells
    • Schreiber E, Matthias P, Muller MM, Schaffner W 1989 Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells. Nucleic Acids Res 17:6419
    • (1989) Nucleic Acids Res , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 53
    • 0026560435 scopus 로고
    • Antiestrogen ICI 164,384 reduces cellular estrogen receptor content by increasing its turnover
    • Dauvois S, Danielian PS, White R, Parker MG 1992 Antiestrogen ICI 164,384 reduces cellular estrogen receptor content by increasing its turnover. Proc Natl Acad Sci USA 89:4037-4041
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4037-4041
    • Dauvois, S.1    Danielian, P.S.2    White, R.3    Parker, M.G.4
  • 54
    • 0032230245 scopus 로고    scopus 로고
    • Interaction and dissociation by ligands of estrogen receptor and Hsp90: The antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm
    • Devin-Leclerc J, Meng X, Delahaye F, Leclerc P, Baulieu EE, Catelli MG 1998 Interaction and dissociation by ligands of estrogen receptor and Hsp90: the antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm. Mol Endocrinol 12:842-854
    • (1998) Mol Endocrinol , vol.12 , pp. 842-854
    • Devin-Leclerc, J.1    Meng, X.2    Delahaye, F.3    Leclerc, P.4    Baulieu, E.E.5    Catelli, M.G.6
  • 55
    • 2442607924 scopus 로고    scopus 로고
    • Tamoxifen induces the expression of maspin through estrogen receptor-α
    • Liu Z, Shi HY, Nawaz Z, Zhang M 2004 Tamoxifen induces the expression of maspin through estrogen receptor-α. Cancer Lett 209:55-65
    • (2004) Cancer Lett , vol.209 , pp. 55-65
    • Liu, Z.1    Shi, H.Y.2    Nawaz, Z.3    Zhang, M.4
  • 56
    • 33748679908 scopus 로고    scopus 로고
    • A cell-type-specific transcriptional network required for estrogen regulation of cyclin D1 and cell cycle progression in breast cancer
    • Eeckhoute J, Carroll JS, Geistlinger TR, Torres-Arzayus MI, Brown M 2006 A cell-type-specific transcriptional network required for estrogen regulation of cyclin D1 and cell cycle progression in breast cancer. Genes Dev 20:2513-2526
    • (2006) Genes Dev , vol.20 , pp. 2513-2526
    • Eeckhoute, J.1    Carroll, J.S.2    Geistlinger, T.R.3    Torres-Arzayus, M.I.4    Brown, M.5
  • 58
    • 0037135690 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases 1 and 2 participate in interleukin-17 plus tumor necrosis factor-α-induced stabilization of interleukin-6 mRNA in human pancreatic myofibroblasts
    • Andoh A, Shimada M, Bamba S, Okuno T, Araki Y, Fujiyama Y, Bamba T 2002 Extracellular signal-regulated kinases 1 and 2 participate in interleukin-17 plus tumor necrosis factor-α-induced stabilization of interleukin-6 mRNA in human pancreatic myofibroblasts. Biochim Biophys Acta 1591:69-74
    • (2002) Biochim Biophys Acta , vol.1591 , pp. 69-74
    • Andoh, A.1    Shimada, M.2    Bamba, S.3    Okuno, T.4    Araki, Y.5    Fujiyama, Y.6    Bamba, T.7
  • 59
    • 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 1997 Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol Endocrinol 11:657-666
    • (1997) Mol Endocrinol , vol.11 , pp. 657-666
    • Smith, C.L.1    Nawaz, Z.2    O'Malley, B.W.3
  • 60
    • 0037192501 scopus 로고    scopus 로고
    • Molecular determinants for the tissue specificity of SERMs
    • Shang Y, Brown M 2002 Molecular determinants for the tissue specificity of SERMs. Science 295:2465-2468
    • (2002) Science , vol.295 , pp. 2465-2468
    • Shang, Y.1    Brown, M.2
  • 61
    • 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 the corepressors N-CoR or SMRT
    • Jackson TA, Richer JK, Bain DL, Takimoto GS, Tung L, Horwitz KB 1997 The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT. Mol Endocrinol 11:693-705
    • (1997) Mol Endocrinol , vol.11 , pp. 693-705
    • Jackson, T.A.1    Richer, J.K.2    Bain, D.L.3    Takimoto, G.S.4    Tung, L.5    Horwitz, K.B.6
  • 62
    • 0031910827 scopus 로고    scopus 로고
    • The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor
    • Wagner BL, Norris JD, Knotts TA, Weigel NL, McDonnell DP 1998 The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor. Mol Cell Biol 18:1369-1378
    • (1998) Mol Cell Biol , vol.18 , pp. 1369-1378
    • Wagner, B.L.1    Norris, J.D.2    Knotts, T.A.3    Weigel, N.L.4    McDonnell, D.P.5


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