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Volumn 32, Issue 5, 2011, Pages 597-622

Cracking the estrogen receptor's posttranslational code in breast tumors

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ANASTROZOLE; ARGININE; CYCLIN D1; ESTROGEN RECEPTOR; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; EXEMESTANE; FULVESTRANT; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE 6; LETROZOLE; METHYLTRANSFERASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN P21; RALOXIFENE; TAMOXIFEN; TUBULIN;

EID: 81255186483     PISSN: 0163769X     EISSN: None     Source Type: Journal    
DOI: 10.1210/er.2010-0016     Document Type: Review
Times cited : (230)

References (273)
  • 1
    • 0033305438 scopus 로고    scopus 로고
    • Estrogen receptor null mice: what have we learned and where will they lead us?
    • Couse JF, Korach KS 1999 Estrogen receptor null mice: what have we learned and where will they lead us? Endocr Rev 20:358-417
    • (1999) Endocr Rev , vol.20 , pp. 358-417
    • Couse, J.F.1    Korach, K.S.2
  • 3
    • 0037204724 scopus 로고    scopus 로고
    • Connections and regulation of the human estrogen receptor
    • McDonnell DP, Norris JD 2002 Connections and regulation of the human estrogen receptor. Science 296:1642-1644
    • (2002) Science , vol.296 , pp. 1642-1644
    • McDonnell, D.P.1    Norris, J.D.2
  • 4
    • 70450197247 scopus 로고    scopus 로고
    • Membrane oestrogen receptor α signalling to cell functions
    • Levin ER 2009 Membrane oestrogen receptor α signalling to cell functions. J Physiol 587:5019-5023
    • (2009) J Physiol , vol.587 , pp. 5019-5023
    • Levin, E.R.1
  • 5
    • 0032925166 scopus 로고    scopus 로고
    • Pattern of distribution of cells positive for estrogen receptor α and progesterone receptor in relation to proliferating cells in the mammary gland
    • Russo J, Ao X, Grill C, Russo IH 1999 Pattern of distribution of cells positive for estrogen receptor α and progesterone receptor in relation to proliferating cells in the mammary gland. Breast Cancer Res Treat 53:217-227
    • (1999) Breast Cancer Res Treat , vol.53 , pp. 217-227
    • Russo, J.1    Ao, X.2    Grill, C.3    Russo, I.H.4
  • 6
    • 0034641862 scopus 로고    scopus 로고
    • Estrogen receptor β acts as a dominant regulator of estrogen signaling
    • Pettersson K, Delaunay F, Gustafsson JA 2000 Estrogen receptor β acts as a dominant regulator of estrogen signaling. Oncogene 19:4970-4978
    • (2000) Oncogene , vol.19 , pp. 4970-4978
    • Pettersson, K.1    Delaunay, F.2    Gustafsson, J.A.3
  • 7
  • 8
    • 77950858531 scopus 로고    scopus 로고
    • Estrogen receptorβ exerts growth-inhibitory effects on human mammary epithelial cells
    • Treeck O, Lattrich C, Springwald A, Ortmann O 2010 Estrogen receptorβ exerts growth-inhibitory effects on human mammary epithelial cells. Breast Cancer Res Treat 120:557-565
    • (2010) Breast Cancer Res Treat , vol.120 , pp. 557-565
    • Treeck, O.1    Lattrich, C.2    Springwald, A.3    Ortmann, O.4
  • 9
    • 34547409238 scopus 로고    scopus 로고
    • Loss of tumourigenicity of stably ERβ-transfected MCF-7 breast cancer cells
    • Behrens D, Gill JH, Fichtner I 2007 Loss of tumourigenicity of stably ERβ-transfected MCF-7 breast cancer cells. Mol Cell Endocrinol 274:19-29
    • (2007) Mol Cell Endocrinol , vol.274 , pp. 19-29
    • Behrens, D.1    Gill, J.H.2    Fichtner, I.3
  • 11
    • 38949182981 scopus 로고    scopus 로고
    • Agenome-wide study of the repressive effects of estrogen receptor β on estrogen receptor α signaling in breast cancer cells
    • Williams C, Edvardsson K, Lewandowski SA, Ström A, Gustafsson JA 2008 Agenome-wide study of the repressive effects of estrogen receptor β on estrogen receptor α signaling in breast cancer cells. Oncogene 27:1019-1032
    • (2008) Oncogene , vol.27 , pp. 1019-1032
    • Williams, C.1    Edvardsson, K.2    Lewandowski, S.A.3    Ström, A.4    Gustafsson, J.A.5
  • 12
    • 0032478958 scopus 로고    scopus 로고
    • Relationship between estrogen levels, use of hormone replacement therapy, and breast cancer
    • Colditz GA 1998 Relationship between estrogen levels, use of hormone replacement therapy, and breast cancer. J Natl Cancer Inst 90:814-823
    • (1998) J Natl Cancer Inst , vol.90 , pp. 814-823
    • Colditz, G.A.1
  • 13
    • 0032581419 scopus 로고    scopus 로고
    • Identification of estrogen receptor β RNA in human breast and abdominal subcutaneous adipose tissue
    • Crandall DL, Busler DE, Novak TJ, Weber RV, Kral JG 1998 Identification of estrogen receptor β RNA in human breast and abdominal subcutaneous adipose tissue. Biochem Biophys Res Commun 248:523-526
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 523-526
    • Crandall, D.L.1    Busler, D.E.2    Novak, T.J.3    Weber, R.V.4    Kral, J.G.5
  • 14
    • 0032896905 scopus 로고    scopus 로고
    • Estrogen receptor status by immunohistochemistry is superior to the ligand-binding assay for predicting response to adjuvant endocrine therapy in breast cancer
    • Harvey JM, Clark GM, Osborne CK, Allred DC 1999 Estrogen receptor status by immunohistochemistry is superior to the ligand-binding assay for predicting response to adjuvant endocrine therapy in breast cancer. J Clin Oncol 17:1474-1481
    • (1999) J Clin Oncol , vol.17 , pp. 1474-1481
    • Harvey, J.M.1    Clark, G.M.2    Osborne, C.K.3    Allred, D.C.4
  • 15
    • 0036488531 scopus 로고    scopus 로고
    • Endocrine-responsive breast cancer and strategies for combating resistance
    • Ali S, Coombes RC 2002 Endocrine-responsive breast cancer and strategies for combating resistance. Nat Rev Cancer 2:101-112
    • (2002) Nat Rev Cancer , vol.2 , pp. 101-112
    • Ali, S.1    Coombes, R.C.2
  • 16
    • 74849127936 scopus 로고    scopus 로고
    • Oestrogen receptor splice variants in the pathogenesis of disease
    • Taylor SE, Martin-Hirsch PL, Martin FL 2010 Oestrogen receptor splice variants in the pathogenesis of disease. Cancer Lett 288:133-148
    • (2010) Cancer Lett , vol.288 , pp. 133-148
    • Taylor, S.E.1    Martin-Hirsch, P.L.2    Martin, F.L.3
  • 17
    • 77952397929 scopus 로고    scopus 로고
    • Estrogen receptor mutations and changes in downstream gene expression and signaling
    • Barone I, Brusco L, Fuqua SA 2010 Estrogen receptor mutations and changes in downstream gene expression and signaling. Clin Cancer Res 16:2702-2708
    • (2010) Clin Cancer Res , vol.16 , pp. 2702-2708
    • Barone, I.1    Brusco, L.2    Fuqua, S.A.3
  • 18
    • 10644274482 scopus 로고    scopus 로고
    • Estrogen receptor mutations in human disease
    • Herynk MH, Fuqua SA 2004 Estrogen receptor mutations in human disease. Endocr Rev 25:869-898
    • (2004) Endocr Rev , vol.25 , pp. 869-898
    • Herynk, M.H.1    Fuqua, S.A.2
  • 19
    • 33750316364 scopus 로고    scopus 로고
    • Post-translational modifications of steroid receptors
    • Faus H, Haendler B 2006 Post-translational modifications of steroid receptors. Biomed Pharmacother 60:520-528
    • (2006) Biomed Pharmacother , vol.60 , pp. 520-528
    • Faus, H.1    Haendler, B.2
  • 20
    • 30344479480 scopus 로고    scopus 로고
    • Coregulators in nuclear estrogen receptor action: from concept to therapeutic targeting
    • Hall JM, McDonnell DP 2005 Coregulators in nuclear estrogen receptor action: from concept to therapeutic targeting. Mol Interv 5:343-357
    • (2005) Mol Interv , vol.5 , pp. 343-357
    • Hall, J.M.1    McDonnell, D.P.2
  • 21
    • 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
  • 22
    • 73349085238 scopus 로고    scopus 로고
    • Steroid receptor phosphorylation: assigning function to site-specific phosphorylation
    • Ward RD, Weigel NL 2009 Steroid receptor phosphorylation: assigning function to site-specific phosphorylation. Biofactors 35:528-536
    • (2009) Biofactors , vol.35 , pp. 528-536
    • Ward, R.D.1    Weigel, N.L.2
  • 26
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai MJ, O'Malley BW 1994 Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu Rev Biochem 63:451-486
    • (1994) Annu Rev Biochem , vol.63 , pp. 451-486
    • Tsai, M.J.1    O'Malley, B.W.2
  • 27
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • Tora L, White J, Brou C, Tasset D, Webster N, Scheer E, Chambon P 1989 The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 59:477-487
    • (1989) Cell , vol.59 , pp. 477-487
    • Tora, L.1    White, J.2    Brou, C.3    Tasset, D.4    Webster, N.5    Scheer, E.6    Chambon, P.7
  • 29
    • 0030593681 scopus 로고    scopus 로고
    • ER β: identification and characterization of a novel human estrogen receptor
    • Mosselman S, Polman J, Dijkema R 1996 ER β: identification and characterization of a novel human estrogen receptor. FEBS Lett 392:49-53
    • (1996) FEBS Lett , vol.392 , pp. 49-53
    • Mosselman, S.1    Polman, J.2    Dijkema, R.3
  • 30
    • 77951157335 scopus 로고    scopus 로고
    • The hinge region of the human estrogen receptor determines functional synergy between AF-1 and AF-2 in the quantitative response to estradiol and tamoxifen
    • Zwart W, de Leeuw R, Rondaij M, Neefjes J, Mancini MA, Michalides R 2010 The hinge region of the human estrogen receptor determines functional synergy between AF-1 and AF-2 in the quantitative response to estradiol and tamoxifen. J Cell Sci 123:1253-1261
    • (2010) J Cell Sci , vol.123 , pp. 1253-1261
    • Zwart, W.1    de Leeuw, R.2    Rondaij, M.3    Neefjes, J.4    Mancini, M.A.5    Michalides, R.6
  • 32
    • 2342649469 scopus 로고    scopus 로고
    • Phyto-oestrogens, their mechanism of action: current evidence for a role in breast and prostate cancer
    • Magee PJ, Rowland IR 2004 Phyto-oestrogens, their mechanism of action: current evidence for a role in breast and prostate cancer. Br J Nutr 91:513-531
    • (2004) Br J Nutr , vol.91 , pp. 513-531
    • Magee, P.J.1    Rowland, I.R.2
  • 33
    • 0033036785 scopus 로고    scopus 로고
    • The two phyto-oestrogens genistein and quercetin exert different effects on oestrogen receptor function
    • Miodini P, Fioravanti L, Di Fronzo G, Cappelletti V 1999 The two phyto-oestrogens genistein and quercetin exert different effects on oestrogen receptor function. Br J Cancer 80:1150-1155
    • (1999) Br J Cancer , vol.80 , pp. 1150-1155
    • Miodini, P.1    Fioravanti, L.2    Di Fronzo, G.3    Cappelletti, V.4
  • 34
    • 37649007431 scopus 로고    scopus 로고
    • Selective estrogen-receptor modulators and antihormonal resistance in breast cancer
    • Jordan VC, O'Malley BW 2007 Selective estrogen-receptor modulators and antihormonal resistance in breast cancer. J Clin Oncol 25:5815-5824
    • (2007) J Clin Oncol , vol.25 , pp. 5815-5824
    • Jordan, V.C.1    O'Malley, B.W.2
  • 35
    • 1442351143 scopus 로고    scopus 로고
    • Coregulator function: a key to understanding tissue specificity of selective receptor modulators
    • Smith CL, O'Malley BW 2004 Coregulator function: a key to understanding tissue specificity of selective receptor modulators. Endocr Rev 25:45-71
    • (2004) Endocr Rev , vol.25 , pp. 45-71
    • Smith, C.L.1    O'Malley, B.W.2
  • 36
    • 27644476924 scopus 로고    scopus 로고
    • Biological characteristics of the pure antiestrogen fulvestrant: overcoming endocrine resistance
    • Dowsett M, Nicholson RI, Pietras RJ 2005 Biological characteristics of the pure antiestrogen fulvestrant: overcoming endocrine resistance. Breast Cancer Res Treat 93(Suppl 1):S11-S18
    • (2005) Breast Cancer Res Treat , vol.93 , Issue.SUPPL 1
    • Dowsett, M.1    Nicholson, R.I.2    Pietras, R.J.3
  • 37
    • 0026395885 scopus 로고
    • A potent specific pure antiestrogen with clinical potential
    • Wakeling AE, Dukes M, Bowler J 1991 A potent specific pure antiestrogen with clinical potential. Cancer Res 51:3867-3873
    • (1991) Cancer Res , vol.51 , pp. 3867-3873
    • Wakeling, A.E.1    Dukes, M.2    Bowler, J.3
  • 39
    • 15544376261 scopus 로고    scopus 로고
    • Lessons in estrogen biology from knockout and transgenic animals
    • Hewitt SC, Harrell JC, Korach KS 2005 Lessons in estrogen biology from knockout and transgenic animals. Annu Rev Physiol 67:285-308
    • (2005) Annu Rev Physiol , vol.67 , pp. 285-308
    • Hewitt, S.C.1    Harrell, J.C.2    Korach, K.S.3
  • 41
    • 0027429548 scopus 로고
    • Alteration of reproductive function but not prenatal sexual development after insertional disruption of the mouse estrogen receptor gene
    • Lubahn DB, Moyer JS, Golding TS, Couse JF, Korach KS, Smithies O 1993 Alteration of reproductive function but not prenatal sexual development after insertional disruption of the mouse estrogen receptor gene. Proc Natl Acad Sci USA 90:11162-11166
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11162-11166
    • Lubahn, D.B.1    Moyer, J.S.2    Golding, T.S.3    Couse, J.F.4    Korach, K.S.5    Smithies, O.6
  • 43
    • 0141752761 scopus 로고    scopus 로고
    • Estrogen receptor isoform-specific regulation of endogenous gene expression in human osteoblastic cell lines expressing either ERα or ERβ
    • Monroe DG, Getz BJ, Johnsen SA, Riggs BL, Khosla S, Spelsberg TC 2003 Estrogen receptor isoform-specific regulation of endogenous gene expression in human osteoblastic cell lines expressing either ERα or ERβ. J Cell Biochem 90:315-326
    • (2003) J Cell Biochem , vol.90 , pp. 315-326
    • Monroe, D.G.1    Getz, B.J.2    Johnsen, S.A.3    Riggs, B.L.4    Khosla, S.5    Spelsberg, T.C.6
  • 44
    • 0038318925 scopus 로고    scopus 로고
    • Disruption of the estrogen receptor β gene in mice causes myeloprolifer- ative disease resembling chronic myeloid leukemia with lymphoid blast crisis
    • Shim GJ, Wang L, Andersson S, Nagy N, Kis LL, Zhang Q, Mäkelä S, Warner M, Gustafsson JA 2003 Disruption of the estrogen receptor β gene in mice causes myeloprolifer- ative disease resembling chronic myeloid leukemia with lymphoid blast crisis. Proc Natl Acad Sci USA 100:6694-6699
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6694-6699
    • Shim, G.J.1    Wang, L.2    Andersson, S.3    Nagy, N.4    Kis, L.L.5    Zhang, Q.6    Mäkelä, S.7    Warner, M.8    Gustafsson, J.A.9
  • 46
  • 48
    • 34250191787 scopus 로고    scopus 로고
    • Oestrogen receptors pathways to oestrogen responsive elements: the transactivation function-1 acts as the keystone of oestrogen receptor (ER)β-mediated transcriptional repression of ERα
    • Gougelet A, Mueller SO, Korach KS, Renoir JM 2007 Oestrogen receptors pathways to oestrogen responsive elements: the transactivation function-1 acts as the keystone of oestrogen receptor (ER)β-mediated transcriptional repression of ERα. J Steroid Biochem Mol Biol 104:110-122
    • (2007) J Steroid Biochem Mol Biol , vol.104 , pp. 110-122
    • Gougelet, A.1    Mueller, S.O.2    Korach, K.S.3    Renoir, J.M.4
  • 49
    • 0033304993 scopus 로고    scopus 로고
    • The estrogen receptor β-isoform (ERβ) of the human estrogen receptor modulates ERα transcriptional activity and is a key regulator of the cellular response to estrogens and antiestrogens
    • Hall JM, McDonnell DP 1999 The estrogen receptor β-isoform (ERβ) of the human estrogen receptor modulates ERα transcriptional activity and is a key regulator of the cellular response to estrogens and antiestrogens. Endocrinology 140:5566-5578
    • (1999) Endocrinology , vol.140 , pp. 5566-5578
    • Hall, J.M.1    McDonnell, D.P.2
  • 51
    • 1642535535 scopus 로고    scopus 로고
    • Estrogen receptor β inhibits human breast cancer cell proliferation and tumor formation by causing a G2 cell cycle arrest
    • Paruthiyil S, Parmar H, Kerekatte V, Cunha GR, Firestone GL, Leitman DC 2004 Estrogen receptor β inhibits human breast cancer cell proliferation and tumor formation by causing a G2 cell cycle arrest. Cancer Res 64:423-428
    • (2004) Cancer Res , vol.64 , pp. 423-428
    • Paruthiyil, S.1    Parmar, H.2    Kerekatte, V.3    Cunha, G.R.4    Firestone, G.L.5    Leitman, D.C.6
  • 52
    • 0035208142 scopus 로고    scopus 로고
    • Minireview: genomic organization of the human ERα gene promoter region
    • Kos M, Reid G, Denger S, Gannon F 2001 Minireview: genomic organization of the human ERα gene promoter region. Mol Endocrinol 15:2057-2063
    • (2001) Mol Endocrinol , vol.15 , pp. 2057-2063
    • Kos, M.1    Reid, G.2    Denger, S.3    Gannon, F.4
  • 53
    • 0029791308 scopus 로고    scopus 로고
    • Tamoxifen aziridine labeling of the estrogen receptor-potential utility in detecting biologically aggressive breast tumors
    • Trivedi S, Piccart M, Muquardt C, Gilot N, Hadiy S, Patel D, Leclercq G 1996 Tamoxifen aziridine labeling of the estrogen receptor-potential utility in detecting biologically aggressive breast tumors. Breast Cancer Res Treat 40:231-241
    • (1996) Breast Cancer Res Treat , vol.40 , pp. 231-241
    • Trivedi, S.1    Piccart, M.2    Muquardt, C.3    Gilot, N.4    Hadiy, S.5    Patel, D.6    Leclercq, G.7
  • 55
    • 65949089012 scopus 로고    scopus 로고
    • Estradiol regulates expression of estrogen receptor ERα46 in human macrophages
    • Murphy AJ, Guyre PM, Wira CR, Pioli PA 2009 Estradiol regulates expression of estrogen receptor ERα46 in human macrophages. PLoS One 4:e5539
    • (2009) PLoS One , vol.4
    • Murphy, A.J.1    Guyre, P.M.2    Wira, C.R.3    Pioli, P.A.4
  • 56
    • 0037446887 scopus 로고    scopus 로고
    • Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells
    • Li L, Haynes MP, Bender JR 2003 Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells. Proc Natl Acad Sci USA 100:4807-4812
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4807-4812
    • Li, L.1    Haynes, M.P.2    Bender, J.R.3
  • 57
    • 0034283016 scopus 로고    scopus 로고
    • Identification of a new isoform of the human estrogen receptor-α (hER-α) that is encoded by distinct transcripts and that is able to repress hER-α activation function 1
    • Flouriot G, Brand H, Denger S, Metivier R, Kos M, Reid G, Sonntag-Buck V, Gannon F 2000 Identification of a new isoform of the human estrogen receptor-α (hER-α) that is encoded by distinct transcripts and that is able to repress hER-α activation function 1. EMBO J 19:4688-4700
    • (2000) EMBO J , vol.19 , pp. 4688-4700
    • Flouriot, G.1    Brand, H.2    Denger, S.3    Metivier, R.4    Kos, M.5    Reid, G.6    Sonntag-Buck, V.7    Gannon, F.8
  • 59
    • 0023740699 scopus 로고
    • A variant estrogen receptor messenger ribonucleic acid is associated with reduced levels of estrogen binding in human mammary tumors
    • Garcia T, Lehrer S, Bloomer WD, Schachter B 1988 A variant estrogen receptor messenger ribonucleic acid is associated with reduced levels of estrogen binding in human mammary tumors. Mol Endocrinol 2:785-791
    • (1988) Mol Endocrinol , vol.2 , pp. 785-791
    • Garcia, T.1    Lehrer, S.2    Bloomer, W.D.3    Schachter, B.4
  • 61
    • 0025789867 scopus 로고
    • Estrogen receptor variants in clinical breast cancer
    • McGuire WL, Chamness GC, Fuqua SA 1991 Estrogen receptor variants in clinical breast cancer. Mol Endocrinol 5:1571-1577
    • (1991) Mol Endocrinol , vol.5 , pp. 1571-1577
    • McGuire, W.L.1    Chamness, G.C.2    Fuqua, S.A.3
  • 62
    • 77952951595 scopus 로고    scopus 로고
    • Estrogen receptor α 46 is reduced in tamoxifen resistant breast cancer cells and re-expression inhibits cell proliferation and estrogen receptor α 66-regulated target gene transcription
    • Klinge CM, Riggs KA, Wickramasinghe NS, Emberts CG, McConda DB, Barry PN, Magnusen JE 2010 Estrogen receptor α 46 is reduced in tamoxifen resistant breast cancer cells and re-expression inhibits cell proliferation and estrogen receptor α 66-regulated target gene transcription. Mol Cell Endocrinol 323:268-276
    • (2010) Mol Cell Endocrinol , vol.323 , pp. 268-276
    • Klinge, C.M.1    Riggs, K.A.2    Wickramasinghe, N.S.3    Emberts, C.G.4    McConda, D.B.5    Barry, P.N.6    Magnusen, J.E.7
  • 63
    • 25644437706 scopus 로고    scopus 로고
    • Identification, cloning, and expression of human estrogen receptor-α36, a novel variant of human estrogen receptor-α66
    • Wang Z, Zhang X, Shen P, Loggie BW, Chang Y, Deuel TF 2005 Identification, cloning, and expression of human estrogen receptor-α36, a novel variant of human estrogen receptor-α66. Biochem Biophys Res Commun 336:1023-1027
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 1023-1027
    • Wang, Z.1    Zhang, X.2    Shen, P.3    Loggie, B.W.4    Chang, Y.5    Deuel, T.F.6
  • 64
    • 33745160700 scopus 로고    scopus 로고
    • A variant of estrogen receptor-α, hER-α36: transduction of estrogen- and antiestrogen-dependent membrane- initiated mitogenic signaling
    • Wang Z, Zhang X, Shen P, Loggie BW, Chang Y, Deuel TF 2006 A variant of estrogen receptor-α, hER-α36: transduction of estrogen- and antiestrogen-dependent membrane- initiated mitogenic signaling. Proc Natl Acad Sci USA 103:9063-9068
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 9063-9068
    • Wang, Z.1    Zhang, X.2    Shen, P.3    Loggie, B.W.4    Chang, Y.5    Deuel, T.F.6
  • 65
    • 79951809981 scopus 로고    scopus 로고
    • A positive feedback loop of ER-α36/EGFR promotes malignant growth of ER-negative breast cancer cells
    • Zhang XT, Kang LG, Ding L, Vranic S, Gatalica Z, Wang ZY 2011 A positive feedback loop of ER-α36/EGFR promotes malignant growth of ER-negative breast cancer cells. Oncogene 30:770-780
    • (2011) Oncogene , vol.30 , pp. 770-780
    • Zhang, X.T.1    Kang, L.G.2    Ding, L.3    Vranic, S.4    Gatalica, Z.5    Wang, Z.Y.6
  • 66
    • 69249129572 scopus 로고    scopus 로고
    • Expression of ER-α36, a novel variant of estrogen receptor α, and resistance to tamoxifen treatment in breast cancer
    • Shi L, Dong B, Li Z, Lu Y, Ouyang T, Li J, Wang T, Fan Z, Fan T, Lin B, Wang Z, Xie Y 2009 Expression of ER-α36, a novel variant of estrogen receptor α, and resistance to tamoxifen treatment in breast cancer. J Clin Oncol 27:3423-3429
    • (2009) J Clin Oncol , vol.27 , pp. 3423-3429
    • Shi, L.1    Dong, B.2    Li, Z.3    Lu, Y.4    Ouyang, T.5    Li, J.6    Wang, T.7    Fan, Z.8    Fan, T.9    Lin, B.10    Wang, Z.11    Xie, Y.12
  • 69
    • 11244287448 scopus 로고    scopus 로고
    • Correlation of mRNA for oestrogen receptor β splice variants ERβ1, ERβ2/ERβcx and ERβ5 with outcome in endocrine-treated breast cancer
    • Davies MP, O'Neill PA, Innes H, Sibson DR, Prime W, Holcombe C, Foster CS 2004 Correlation of mRNA for oestrogen receptor β splice variants ERβ1, ERβ2/ERβcx and ERβ5 with outcome in endocrine-treated breast cancer. J Mol Endocrinol 33:773-782
    • (2004) J Mol Endocrinol , vol.33 , pp. 773-782
    • Davies, M.P.1    O'Neill, P.A.2    Innes, H.3    Sibson, D.R.4    Prime, W.5    Holcombe, C.6    Foster, C.S.7
  • 70
    • 33748305646 scopus 로고    scopus 로고
    • Expression of oestrogen receptor- β in oestrogen receptor-α negative human breast tumours
    • Skliris GP, Leygue E, Curtis-Snell L, Watson PH, Murphy LC 2006 Expression of oestrogen receptor- β in oestrogen receptor-α negative human breast tumours. Br J Cancer 95:616-626
    • (2006) Br J Cancer , vol.95 , pp. 616-626
    • Skliris, G.P.1    Leygue, E.2    Curtis-Snell, L.3    Watson, P.H.4    Murphy, L.C.5
  • 71
    • 18144405740 scopus 로고    scopus 로고
    • Estrogen receptor α and β subtype expression and transactivation capacity are differentially affected by receptor-, hsp90- and immunophi- lin-ligands in human breast cancer cells
    • Gougelet A, Bouclier C, Marsaud V, Maillard S, Mueller SO, Korach KS, Renoir JM 2005 Estrogen receptor α and β subtype expression and transactivation capacity are differentially affected by receptor-, hsp90- and immunophi- lin-ligands in human breast cancer cells. J Steroid Biochem Mol Biol 94:71-81
    • (2005) J Steroid Biochem Mol Biol , vol.94 , pp. 71-81
    • Gougelet, A.1    Bouclier, C.2    Marsaud, V.3    Maillard, S.4    Mueller, S.O.5    Korach, K.S.6    Renoir, J.M.7
  • 72
    • 0025928122 scopus 로고
    • Steroid hormone receptors
    • Jensen EV 1991 Steroid hormone receptors. Curr Top Pathol 83:365-431
    • (1991) Curr Top Pathol , vol.83 , pp. 365-431
    • Jensen, E.V.1
  • 73
    • 0023664574 scopus 로고
    • The binding activity of estrogen receptor to DNA and heat shock protein(Mr90,000) is dependent on receptor-bound metal
    • Sabbah M, Redeuilh G, Secco C, Baulieu EE 1987 The binding activity of estrogen receptor to DNA and heat shock protein(Mr90,000) is dependent on receptor-bound metal. J Biol Chem 262:8631-8635
    • (1987) J Biol Chem , vol.262 , pp. 8631-8635
    • Sabbah, M.1    Redeuilh, G.2    Secco, C.3    Baulieu, E.E.4
  • 74
    • 75649135910 scopus 로고    scopus 로고
    • Deconstructing repression: evolving models of co-repressor action
    • Perissi V, Jepsen K, Glass CK, Rosenfeld MG 2010 Deconstructing repression: evolving models of co-repressor action. Nat Rev Genet 11:109-123
    • (2010) Nat Rev Genet , vol.11 , pp. 109-123
    • Perissi, V.1    Jepsen, K.2    Glass, C.K.3    Rosenfeld, M.G.4
  • 75
    • 33646133406 scopus 로고    scopus 로고
    • The expanding cosmos of nuclear receptor coactivators
    • Lonard DM, O'Malley BW 2006 The expanding cosmos of nuclear receptor coactivators. Cell 125:411-414
    • (2006) Cell , vol.125 , pp. 411-414
    • Lonard, D.M.1    O'Malley, B.W.2
  • 76
    • 0034454583 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulators in action: diversity for shared tasks
    • Robyr D, Wolffe AP, Wahli W 2000 Nuclear hormone receptor coregulators in action: diversity for shared tasks. Mol Endocrinol 14:329-347
    • (2000) Mol Endocrinol , vol.14 , pp. 329-347
    • Robyr, D.1    Wolffe, A.P.2    Wahli, W.3
  • 77
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptorregulated transcription
    • Shang Y, Hu X, DiRenzo J, Lazar MA, Brown M 2000 Cofactor dynamics and sufficiency in estrogen receptorregulated transcription. Cell 103:843-852
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 78
    • 19344364880 scopus 로고    scopus 로고
    • Effects of chemotherapy and hormonal therapy for early breast cancer on recurrence and 15-year survival: an overview of the randomised trials
    • Early Breast Cancer Trialists' Collaborative Group (EBCTCG)
    • Early Breast Cancer Trialists' Collaborative Group (EBCTCG) 2005 Effects of chemotherapy and hormonal therapy for early breast cancer on recurrence and 15-year survival: an overview of the randomised trials. Lancet 365:1687-1717
    • (2005) Lancet , vol.365 , pp. 1687-1717
  • 79
    • 16844384340 scopus 로고    scopus 로고
    • The future of breast cancer: the role of prognostic factors
    • Gradishar WJ 2005 The future of breast cancer: the role of prognostic factors. Breast Cancer Res Treat 89(Suppl 1): S17-S26
    • (2005) Breast Cancer Res Treat , vol.89 , Issue.SUPPL 1
    • Gradishar, W.J.1
  • 80
    • 78649846415 scopus 로고    scopus 로고
    • Steroid receptor coactivator (SRC) family: masters of systems biology
    • York B, O'Malley BW 2010 Steroid receptor coactivator (SRC) family: masters of systems biology. J Biol Chem 285:38743-38750
    • (2010) J Biol Chem , vol.285 , pp. 38743-38750
    • York, B.1    O'Malley, B.W.2
  • 85
    • 0034088842 scopus 로고    scopus 로고
    • Ligand-, cell-, and estrogen receptor subtype (α/β)-dependent activation at GC-rich (Sp1) promoter elements
    • Saville B, Wormke M, Wang F, Nguyen T, Enmark E, Kuiper G, Gustafsson JA, Safe S 2000 Ligand-, cell-, and estrogen receptor subtype (α/β)-dependent activation at GC-rich (Sp1) promoter elements. J Biol Chem 275:5379-5387
    • (2000) J Biol Chem , vol.275 , pp. 5379-5387
    • Saville, B.1    Wormke, M.2    Wang, F.3    Nguyen, T.4    Enmark, E.5    Kuiper, G.6    Gustafsson, J.A.7    Safe, S.8
  • 86
    • 4344679375 scopus 로고    scopus 로고
    • Estrogen receptor-dependent activation of AP-1 via non-genomic signalling
    • Björnström L, Sjöberg M 2004 Estrogen receptor-dependent activation of AP-1 via non-genomic signalling. Nucl Recept 2:3
    • (2004) Nucl Recept , vol.2 , pp. 3
    • Björnström, L.1    Sjöberg, M.2
  • 89
    • 0033049975 scopus 로고    scopus 로고
    • Increased activator protein-1 DNA binding and c-Jun NH2-terminal kinase activity in human breast tumors with acquired tamoxifen resistance
    • Johnston SR, Lu B, Scott GK, Kushner PJ, Smith IE, Dowsett M, Benz CC 1999 Increased activator protein-1 DNA binding and c-Jun NH2-terminal kinase activity in human breast tumors with acquired tamoxifen resistance. Clin Cancer Res 5:251-256
    • (1999) Clin Cancer Res , vol.5 , pp. 251-256
    • Johnston, S.R.1    Lu, B.2    Scott, G.K.3    Kushner, P.J.4    Smith, I.E.5    Dowsett, M.6    Benz, C.C.7
  • 93
    • 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, Giguère 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    Giguère, V.4
  • 94
    • 67651005771 scopus 로고    scopus 로고
    • Positive feedback activation of estrogen receptors by the CXCL12-CXCR4 pathway
    • Sauvé K, Lepage J, Sanchez M, Heveker N, Tremblay A 2009 Positive feedback activation of estrogen receptors by the CXCL12-CXCR4 pathway. Cancer Res 69:5793-5800
    • (2009) Cancer Res , vol.69 , pp. 5793-5800
    • Sauvé, K.1    Lepage, J.2    Sanchez, M.3    Heveker, N.4    Tremblay, A.5
  • 96
    • 37349081370 scopus 로고    scopus 로고
    • Extranuclear steroid receptors: nature and actions
    • Hammes SR, Levin ER 2007 Extranuclear steroid receptors: nature and actions. Endocr Rev 28:726-741
    • (2007) Endocr Rev , vol.28 , pp. 726-741
    • Hammes, S.R.1    Levin, E.R.2
  • 97
    • 70349401677 scopus 로고    scopus 로고
    • GPR30/GPER1: searching for a role in estrogen physiology
    • Olde B, Leeb-Lundberg LM 2009 GPR30/GPER1: searching for a role in estrogen physiology. Trends Endocrinol Metab 20:409-416
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 409-416
    • Olde, B.1    Leeb-Lundberg, L.M.2
  • 98
    • 0028925081 scopus 로고
    • Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding
    • Pappas TC, Gametchu B, Watson CS 1995 Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding. FASEB J 9:404-410
    • (1995) FASEB J , vol.9 , pp. 404-410
    • Pappas, T.C.1    Gametchu, B.2    Watson, C.S.3
  • 99
    • 72149133431 scopus 로고    scopus 로고
    • Plasma membrane estrogen receptors
    • Levin ER 2009 Plasma membrane estrogen receptors. Trends Endocrinol Metab 20:477-482
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 477-482
    • Levin, E.R.1
  • 101
    • 33845329220 scopus 로고    scopus 로고
    • An inherent role of integrin-linked kinase-estrogen receptor α interaction in cell migration
    • Acconcia F, Manavathi B, Mascarenhas J, Talukder AH, Mills G, Kumar R 2006 An inherent role of integrin-linked kinase-estrogen receptor α interaction in cell migration. Cancer Res 66:11030-11038
    • (2006) Cancer Res , vol.66 , pp. 11030-11038
    • Acconcia, F.1    Manavathi, B.2    Mascarenhas, J.3    Talukder, A.H.4    Mills, G.5    Kumar, R.6
  • 102
    • 15444368857 scopus 로고    scopus 로고
    • Mechanisms of estrogen receptor signaling: convergence of genomic and nongenomic actions on target genes
    • Björnström L, Sjöberg M 2005 Mechanisms of estrogen receptor signaling: convergence of genomic and nongenomic actions on target genes. Mol Endocrinol 19:833-842
    • (2005) Mol Endocrinol , vol.19 , pp. 833-842
    • Björnström, L.1    Sjöberg, M.2
  • 104
    • 0034727094 scopus 로고    scopus 로고
    • Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase
    • Simoncini T, Hafezi-Moghadam A, Brazil DP, Ley K, Chin WW, Liao JK 2000 Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase. Nature 407:538-541
    • (2000) Nature , vol.407 , pp. 538-541
    • Simoncini, T.1    Hafezi-Moghadam, A.2    Brazil, D.P.3    Ley, K.4    Chin, W.W.5    Liao, J.K.6
  • 105
    • 25144517216 scopus 로고    scopus 로고
    • Estrogen rapid action via protein complex formation involving ERα and Src
    • Song RX, Zhang Z, Santen RJ 2005 Estrogen rapid action via protein complex formation involving ERα and Src. Trends Endocrinol Metab 16:347-353
    • (2005) Trends Endocrinol Metab , vol.16 , pp. 347-353
    • Song, R.X.1    Zhang, Z.2    Santen, R.J.3
  • 106
    • 1242341918 scopus 로고    scopus 로고
    • The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor α to the plasma membrane
    • Song RX, Barnes CJ, Zhang Z, Bao Y, Kumar R, Santen RJ 2004 The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor α to the plasma membrane. Proc Natl Acad Sci USA 101:2076-2081
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2076-2081
    • Song, R.X.1    Barnes, C.J.2    Zhang, Z.3    Bao, Y.4    Kumar, R.5    Santen, R.J.6
  • 109
    • 10344237581 scopus 로고    scopus 로고
    • Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor α
    • Lu Q, Pallas DC, Surks HK, Baur WE, Mendelsohn ME, Karas RH 2004 Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor α. Proc Natl Acad Sci USA 101:17126-17131
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17126-17131
    • Lu, Q.1    Pallas, D.C.2    Surks, H.K.3    Baur, W.E.4    Mendelsohn, M.E.5    Karas, R.H.6
  • 110
    • 3042843668 scopus 로고    scopus 로고
    • Estradiol abrogates apoptosis in breast cancer cells through inactivation of BAD: Ras-dependent nongenomic pathways requiring signaling through ERK and Akt
    • Fernando RI, Wimalasena J 2004 Estradiol abrogates apoptosis in breast cancer cells through inactivation of BAD: Ras-dependent nongenomic pathways requiring signaling through ERK and Akt. Mol Biol Cell 15:3266-3284
    • (2004) Mol Biol Cell , vol.15 , pp. 3266-3284
    • Fernando, R.I.1    Wimalasena, J.2
  • 111
    • 67749137207 scopus 로고    scopus 로고
    • Estrogen inhibits ATR signaling to cell cycle checkpoints and DNA repair
    • Pedram A, Razandi M, Evinger AJ, Lee E, Levin ER 2009 Estrogen inhibits ATR signaling to cell cycle checkpoints and DNA repair. Mol Biol Cell 20:3374-3389
    • (2009) Mol Biol Cell , vol.20 , pp. 3374-3389
    • Pedram, A.1    Razandi, M.2    Evinger, A.J.3    Lee, E.4    Levin, E.R.5
  • 112
    • 66149144380 scopus 로고    scopus 로고
    • Association of estrogen receptor α and histone deacetylase 6 causes rapid deacetylation of tubulin in breast cancer cells
    • Azuma K, Urano T, Horie-Inoue K, Hayashi S, Sakai R, Ouchi Y, Inoue S 2009 Association of estrogen receptor α and histone deacetylase 6 causes rapid deacetylation of tubulin in breast cancer cells. Cancer Res 69:2935-2940
    • (2009) Cancer Res , vol.69 , pp. 2935-2940
    • Azuma, K.1    Urano, T.2    Horie-Inoue, K.3    Hayashi, S.4    Sakai, R.5    Ouchi, Y.6    Inoue, S.7
  • 116
    • 66749105045 scopus 로고    scopus 로고
    • Nuclear receptors: genomic and non-genomic effects converge
    • Ordóñez-Morán P, Muñoz A 2009 Nuclear receptors: genomic and non-genomic effects converge. Cell Cycle 8:1675-1680
    • (2009) Cell Cycle , vol.8 , pp. 1675-1680
    • Ordóñez-Morán, P.1    Muñoz, A.2
  • 117
    • 0031778177 scopus 로고    scopus 로고
    • Basic guide to the mechanisms of antiestrogen action
    • MacGregor JI, Jordan VC 1998 Basic guide to the mechanisms of antiestrogen action. Pharmacol Rev 50:151-196
    • (1998) Pharmacol Rev , vol.50 , pp. 151-196
    • MacGregor, J.I.1    Jordan, V.C.2
  • 119
    • 0033638393 scopus 로고    scopus 로고
    • The 26S proteasome is required for estrogen receptor-α and coactivator turnover and for efficient estrogen receptor-α transactivation
    • Lonard DM, Nawaz Z, Smith CL, O'Malley BW 2000 The 26S proteasome is required for estrogen receptor-α and coactivator turnover and for efficient estrogen receptor-α transactivation. Mol Cell 5:939-948
    • (2000) Mol Cell , vol.5 , pp. 939-948
    • Lonard, D.M.1    Nawaz, Z.2    Smith, C.L.3    O'Malley, B.W.4
  • 120
    • 0035929585 scopus 로고    scopus 로고
    • The human estrogen receptor-α is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators
    • Wijayaratne AL, McDonnell DP 2001 The human estrogen receptor-α is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators. J Biol Chem 276:35684-35692
    • (2001) J Biol Chem , vol.276 , pp. 35684-35692
    • Wijayaratne, A.L.1    McDonnell, D.P.2
  • 121
    • 0142056952 scopus 로고    scopus 로고
    • Various phosphorylation pathways, depending on agonist and antagonist binding to endogenous estrogen receptor α (ERα), differentially affect ERα extractability, proteasome- mediated stability, and transcriptional activity in human breast cancer cells
    • Marsaud V, Gougelet A, Maillard S, Renoir JM 2003 Various phosphorylation pathways, depending on agonist and antagonist binding to endogenous estrogen receptor α (ERα), differentially affect ERα extractability, proteasome- mediated stability, and transcriptional activity in human breast cancer cells. Mol Endocrinol 17:2013-2027
    • (2003) Mol Endocrinol , vol.17 , pp. 2013-2027
    • Marsaud, V.1    Gougelet, A.2    Maillard, S.3    Renoir, J.M.4
  • 123
    • 84995870933 scopus 로고
    • Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions
    • Tzukerman MT, Esty A, Santiso-Mere D, Danielian P, Parker MG, Stein RB, Pike JW, McDonnell DP 1994 Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol Endocrinol 8:21-30
    • (1994) Mol Endocrinol , vol.8 , pp. 21-30
    • Tzukerman, M.T.1    Esty, A.2    Santiso-Mere, D.3    Danielian, P.4    Parker, M.G.5    Stein, R.B.6    Pike, J.W.7    McDonnell, D.P.8
  • 124
    • 0037501319 scopus 로고    scopus 로고
    • The estrogen receptor: a model for molecular medicine
    • Jensen EV, Jordan VC 2003 The estrogen receptor: a model for molecular medicine. Clin Cancer Res 9:1980-1989
    • (2003) Clin Cancer Res , vol.9 , pp. 1980-1989
    • Jensen, E.V.1    Jordan, V.C.2
  • 125
    • 0242499440 scopus 로고    scopus 로고
    • Aromatase inhibitors for breast cancer: lessons from the laboratory
    • Johnston SR, Dowsett M 2003 Aromatase inhibitors for breast cancer: lessons from the laboratory. Nat Rev Cancer 3:821-831
    • (2003) Nat Rev Cancer , vol.3 , pp. 821-831
    • Johnston, S.R.1    Dowsett, M.2
  • 126
    • 1542346355 scopus 로고    scopus 로고
    • Aromatase inhibitors that regulate estrogen target tissues selectively?
    • Jordan VC 2004 Aromatase inhibitors that regulate estrogen target tissues selectively? Bone 34:372-375
    • (2004) Bone , vol.34 , pp. 372-375
    • Jordan, V.C.1
  • 128
    • 69249137029 scopus 로고    scopus 로고
    • Biological determinants of endocrine resistance in breast cancer
    • Musgrove EA, Sutherland RL 2009 Biological determinants of endocrine resistance in breast cancer. Nat Rev Cancer 9:631-643
    • (2009) Nat Rev Cancer , vol.9 , pp. 631-643
    • Musgrove, E.A.1    Sutherland, R.L.2
  • 132
    • 4143087257 scopus 로고    scopus 로고
    • Histone deacetylase inhibition and estrogen signalling in human breast cancer cells
    • Margueron R, Duong V, Castet A, Cavaillès V 2004 Histone deacetylase inhibition and estrogen signalling in human breast cancer cells. Biochem Pharmacol 68:1239-1246
    • (2004) Biochem Pharmacol , vol.68 , pp. 1239-1246
    • Margueron, R.1    Duong, V.2    Castet, A.3    Cavaillès, V.4
  • 134
    • 0019193306 scopus 로고
    • In vitro inactivation of oestrogen receptor by nuclei: prevention by phosphatase inhibitors
    • Auricchio F, Migliaccio A 1980 In vitro inactivation of oestrogen receptor by nuclei: prevention by phosphatase inhibitors. FEBS Lett 117:224-226
    • (1980) FEBS Lett , vol.117 , pp. 224-226
    • Auricchio, F.1    Migliaccio, A.2
  • 135
    • 0021281603 scopus 로고
    • Direct evidence of in vitro phosphorylation-dephosphorylation of the estradiol-17β receptor. Role of Ca2+-calmodulin in the activation of hormone binding sites
    • Auricchio F, Migliaccio A, Castoria G, Rotondi A, Lastoria S 1984 Direct evidence of in vitro phosphorylation-dephosphorylation of the estradiol-17β receptor. Role of Ca2+-calmodulin in the activation of hormone binding sites. J Steroid Biochem 20:31-35
    • (1984) J Steroid Biochem , vol.20 , pp. 31-35
    • Auricchio, F.1    Migliaccio, A.2    Castoria, G.3    Rotondi, A.4    Lastoria, S.5
  • 136
    • 42549131382 scopus 로고    scopus 로고
    • Phosphorylation at serines 104 and 106 by Erk1/2 MAPK is important for estrogen receptor-α activity
    • Thomas RS, Sarwar N, Phoenix F, Coombes RC, Ali S 2008 Phosphorylation at serines 104 and 106 by Erk1/2 MAPK is important for estrogen receptor-α activity. J Mol Endocrinol 40:173-184
    • (2008) J Mol Endocrinol , vol.40 , pp. 173-184
    • Thomas, R.S.1    Sarwar, N.2    Phoenix, F.3    Coombes, R.C.4    Ali, S.5
  • 137
    • 25444468111 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 interacts with and phosphorylates estrogen receptor α and is involved in the regulation of receptor activity
    • Medunjanin S, Hermani A, DeServi B, Grisouard J, Rincke G, Mayer D 2005 Glycogen synthase kinase-3 interacts with and phosphorylates estrogen receptor α and is involved in the regulation of receptor activity. J Biol Chem 280:33006-33014
    • (2005) J Biol Chem , vol.280 , pp. 33006-33014
    • Medunjanin, S.1    Hermani, A.2    DeServi, B.3    Grisouard, J.4    Rincke, G.5    Mayer, D.6
  • 138
    • 0033529557 scopus 로고    scopus 로고
    • Potentiation of human estrogen receptor α transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex
    • Rogatsky I, Trowbridge JM, Garabedian MJ 1999 Potentiation of human estrogen receptor α transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex. J Biol Chem 274:22296-22302
    • (1999) J Biol Chem , vol.274 , pp. 22296-22302
    • Rogatsky, I.1    Trowbridge, J.M.2    Garabedian, M.J.3
  • 140
    • 0038345161 scopus 로고    scopus 로고
    • Mutation of serines 104, 106, and 118 inhibits dimerization of the human estrogen receptor in yeast
    • Sheeler CQ, Singleton DW, Khan SA 2003 Mutation of serines 104, 106, and 118 inhibits dimerization of the human estrogen receptor in yeast. Endocr Res 29:237-255
    • (2003) Endocr Res , vol.29 , pp. 237-255
    • Sheeler, C.Q.1    Singleton, D.W.2    Khan, S.A.3
  • 141
    • 34748864669 scopus 로고    scopus 로고
    • A functional serine 118 phosphorylation site in estrogen receptor-α is required for down-regulation of gene expression by 17β-estradiol and 4-hydroxytamoxifen
    • Cheng J, Zhang C, Shapiro DJ 2007 A functional serine 118 phosphorylation site in estrogen receptor-α is required for down-regulation of gene expression by 17β-estradiol and 4-hydroxytamoxifen. Endocrinology 148:4634-4641
    • (2007) Endocrinology , vol.148 , pp. 4634-4641
    • Cheng, J.1    Zhang, C.2    Shapiro, D.J.3
  • 142
    • 0038648982 scopus 로고    scopus 로고
    • Ligand-independent interactions of p160/steroid receptor coactivators and CREBbinding protein (CBP) with estrogen receptor-α: regulation by phosphorylation sites in the A/B region depends on other receptor domains
    • Dutertre M, Smith CL 2003 Ligand-independent interactions of p160/steroid receptor coactivators and CREBbinding protein (CBP) with estrogen receptor-α: regulation by phosphorylation sites in the A/B region depends on other receptor domains. Mol Endocrinol 17:1296-1314
    • (2003) Mol Endocrinol , vol.17 , pp. 1296-1314
    • Dutertre, M.1    Smith, C.L.2
  • 143
    • 14844325297 scopus 로고    scopus 로고
    • The Src kinase pathway promotes tamoxifen agonist action in Ishikawa endometrial cells through phosphorylation-dependent stabilization of estrogen receptor (α) promoter interaction and elevated steroid receptor coactivator 1 activity
    • Shah YM, Rowan BG 2005 The Src kinase pathway promotes tamoxifen agonist action in Ishikawa endometrial cells through phosphorylation-dependent stabilization of estrogen receptor (α) promoter interaction and elevated steroid receptor coactivator 1 activity. Mol Endocrinol 19:732-748
    • (2005) Mol Endocrinol , vol.19 , pp. 732-748
    • Shah, Y.M.1    Rowan, B.G.2
  • 144
    • 0029877913 scopus 로고    scopus 로고
    • Activation of the unliganded estrogen receptor by EGFinvolves the MAP kinase pathway and direct phosphorylation
    • Bunone G, Briand PA, Miksicek RJ, Picard D 1996 Activation of the unliganded estrogen receptor by EGFinvolves 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
  • 145
    • 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
  • 147
    • 15944379896 scopus 로고    scopus 로고
    • Formation of an IKKα-dependent transcription complex is required for estrogen receptor-mediated gene activation
    • Park KJ, Krishnan V, O'Malley BW, Yamamoto Y, Gaynor RB 2005 Formation of an IKKα-dependent transcription complex is required for estrogen receptor-mediated gene activation. Mol Cell 18:71-82
    • (2005) Mol Cell , vol.18 , pp. 71-82
    • Park, K.J.1    Krishnan, V.2    O'Malley, B.W.3    Yamamoto, Y.4    Gaynor, R.B.5
  • 148
    • 33750552134 scopus 로고    scopus 로고
    • Estrogen receptor-α phosphorylated at Ser118 is present at the promoters of estrogen-regulated genes and is not altered due to HER-2 overexpression
    • Weitsman GE, Li L, Skliris GP, Davie JR, Ung K, Niu Y, Curtis-Snell L, Tomes L, Watson PH, Murphy LC 2006 Estrogen receptor-α phosphorylated at Ser118 is present at the promoters of estrogen-regulated genes and is not altered due to HER-2 overexpression. Cancer Res 66:10162-10170
    • (2006) Cancer Res , vol.66 , pp. 10162-10170
    • Weitsman, G.E.1    Li, L.2    Skliris, G.P.3    Davie, J.R.4    Ung, K.5    Niu, Y.6    Curtis-Snell, L.7    Tomes, L.8    Watson, P.H.9    Murphy, L.C.10
  • 150
    • 0027978187 scopus 로고
    • Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor
    • Arnold SF, Obourn JD, Jaffe H, Notides AC 1994 Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. Mol Endocrinol 8:1208-1214
    • (1994) Mol Endocrinol , vol.8 , pp. 1208-1214
    • Arnold, S.F.1    Obourn, J.D.2    Jaffe, H.3    Notides, A.C.4
  • 151
    • 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
  • 152
    • 0035971181 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/ AKT-mediated activation of estrogen receptor α: a new model for anti-estrogen resistance
    • Campbell RA, Bhat-Nakshatri P, Patel NM, Constantinidou D, Ali S, Nakshatri H 2001 Phosphatidylinositol 3-kinase/ AKT-mediated activation of estrogen receptor α: a new model for anti-estrogen resistance. J Biol Chem 276:9817-9824
    • (2001) J Biol Chem , vol.276 , pp. 9817-9824
    • Campbell, R.A.1    Bhat-Nakshatri, P.2    Patel, N.M.3    Constantinidou, D.4    Ali, S.5    Nakshatri, H.6
  • 153
    • 65249190250 scopus 로고    scopus 로고
    • S6 kinase 1 regulates estrogen receptorα in control of breast cancer cell proliferation
    • Yamnik RL, Digilova A, Davis DC, Brodt ZN, Murphy CJ, Holz MK 2009 S6 kinase 1 regulates estrogen receptorα in control of breast cancer cell proliferation. J Biol Chem284:6361-6369
    • (2009) J Biol Chem , vol.284 , pp. 6361-6369
    • Yamnik, R.L.1    Digilova, A.2    Davis, D.C.3    Brodt, Z.N.4    Murphy, C.J.5    Holz, M.K.6
  • 154
    • 71549166007 scopus 로고    scopus 로고
    • mTOR/S6K1 and MAPK/RSK signaling pathways coordinately regulate estrogen receptor α serine 167 phosphorylation
    • Yamnik RL, Holz MK 2010 mTOR/S6K1 and MAPK/RSK signaling pathways coordinately regulate estrogen receptor α serine 167 phosphorylation. FEBS Lett 584:124-128
    • (2010) FEBS Lett , vol.584 , pp. 124-128
    • Yamnik, R.L.1    Holz, M.K.2
  • 155
    • 0032906876 scopus 로고    scopus 로고
    • Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization
    • Chen D, Pace PE, Coombes RC, Ali S 1999 Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization. Mol Cell Biol 19:1002-1015
    • (1999) Mol Cell Biol , vol.19 , pp. 1002-1015
    • Chen, D.1    Pace, P.E.2    Coombes, R.C.3    Ali, S.4
  • 156
    • 2542501575 scopus 로고    scopus 로고
    • Protein kinase A activation of estrogen receptor α transcription does not require proteasome activity and protects the receptor from ligand-mediated degradation
    • Tsai HW, Katzenellenbogen JA, Katzenellenbogen BS, Shupnik MA 2004 Protein kinase A activation of estrogen receptor α transcription does not require proteasome activity and protects the receptor from ligand-mediated degradation. Endocrinology 145:2730-2738
    • (2004) Endocrinology , vol.145 , pp. 2730-2738
    • Tsai, H.W.1    Katzenellenbogen, J.A.2    Katzenellenbogen, B.S.3    Shupnik, M.A.4
  • 158
    • 54849437262 scopus 로고    scopus 로고
    • Phosphorylation of estrogen receptor α, serine residue 305 enhances activity
    • Tharakan R, Lepont P, Singleton D, Kumar R, Khan S 2008 Phosphorylation of estrogen receptor α, serine residue 305 enhances activity. Mol Cell Endocrinol 295:70-78
    • (2008) Mol Cell Endocrinol , vol.295 , pp. 70-78
    • Tharakan, R.1    Lepont, P.2    Singleton, D.3    Kumar, R.4    Khan, S.5
  • 159
    • 2942568370 scopus 로고    scopus 로고
    • Estrogen receptor activation at serine 305 is sufficient to upregulate cyclin D1 in breast cancer cells
    • Balasenthil S, Barnes CJ, Rayala SK, Kumar R 2004 Estrogen receptor activation at serine 305 is sufficient to upregulate cyclin D1 in breast cancer cells. FEBS Lett 567:243-247
    • (2004) FEBS Lett , vol.567 , pp. 243-247
    • Balasenthil, S.1    Barnes, C.J.2    Rayala, S.K.3    Kumar, R.4
  • 160
    • 0037107380 scopus 로고    scopus 로고
    • P21-activated kinase-1 phosphorylates and transactivates estrogen receptor-α and promotes hyperplasia in mammary epithelium
    • Wang RA, Mazumdar A, Vadlamudi RK, Kumar R 2002 P21-activated kinase-1 phosphorylates and transactivates estrogen receptor-α and promotes hyperplasia in mammary epithelium. EMBO J 21:5437-5447
    • (2002) EMBO J , vol.21 , pp. 5437-5447
    • Wang, R.A.1    Mazumdar, A.2    Vadlamudi, R.K.3    Kumar, R.4
  • 161
    • 34547812560 scopus 로고    scopus 로고
    • PKA-induced resistance to tamoxifen is associated with an altered ori- entation of ERα towards co-activator SRC-1
    • Zwart W, Griekspoor A, Berno V, Lakeman K, Jalink K, Mancini M, Neefjes J, Michalides R 2007 PKA-induced resistance to tamoxifen is associated with an altered ori- entation of ERα towards co-activator SRC-1. EMBO J 26:3534-3544
    • (2007) EMBO J , vol.26 , pp. 3534-3544
    • Zwart, W.1    Griekspoor, A.2    Berno, V.3    Lakeman, K.4    Jalink, K.5    Mancini, M.6    Neefjes, J.7    Michalides, R.8
  • 163
    • 77951557127 scopus 로고    scopus 로고
    • Phosphorylation of the mutant K303R estrogen receptor α at serine 305 affects aromatase inhibitor sensitivity
    • Barone I, Iacopetta D, Covington KR, Cui Y, Tsimelzon A, Beyer A, Andò S, Fuqua SA 2010 Phosphorylation of the mutant K303R estrogen receptor α at serine 305 affects aromatase inhibitor sensitivity. Oncogene 29:2404-2414
    • (2010) Oncogene , vol.29 , pp. 2404-2414
    • Barone, I.1    Iacopetta, D.2    Covington, K.R.3    Cui, Y.4    Tsimelzon, A.5    Beyer, A.6    Andò, S.7    Fuqua, S.A.8
  • 164
    • 72449129179 scopus 로고    scopus 로고
    • Growth factor-induced resistance to tamoxifen is associated with a mutation of estrogen receptor α and its phosphorylation at serine 305
    • Giordano C, Cui Y, Barone I, Ando S, Mancini MA, Berno V, Fuqua SA 2010 Growth factor-induced resistance to tamoxifen is associated with a mutation of estrogen receptor α and its phosphorylation at serine 305. Breast Cancer Res Treat 119:71-85
    • (2010) Breast Cancer Res Treat , vol.119 , pp. 71-85
    • Giordano, C.1    Cui, Y.2    Barone, I.3    Ando, S.4    Mancini, M.A.5    Berno, V.6    Fuqua, S.A.7
  • 165
    • 66349092194 scopus 로고    scopus 로고
    • Expression of the K303R estrogen receptor-α breast cancer mutation induces resistance to an aromatase inhibitor via addiction to the PI3K/Akt kinase pathway
    • Barone I, Cui Y, Herynk MH, Corona-Rodriguez A, Giordano C, Selever J, Beyer A, Andò S, Fuqua SA 2009 Expression of the K303R estrogen receptor-α breast cancer mutation induces resistance to an aromatase inhibitor via addiction to the PI3K/Akt kinase pathway. Cancer Res 69:4724-4732
    • (2009) Cancer Res , vol.69 , pp. 4724-4732
    • Barone, I.1    Cui, Y.2    Herynk, M.H.3    Corona-Rodriguez, A.4    Giordano, C.5    Selever, J.6    Beyer, A.7    Andò, S.8    Fuqua, S.A.9
  • 167
    • 0031790490 scopus 로고    scopus 로고
    • A novel human estrogen receptor β: identification and functional analysis of additional N-terminal amino acids
    • Bhat RA, Harnish DC, Stevis PE, Lyttle CR, Komm BS 1998 A novel human estrogen receptor β: identification and functional analysis of additional N-terminal amino acids. J Steroid Biochem Mol Biol 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    Lyttle, C.R.4    Komm, B.S.5
  • 168
    • 0034718570 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor β
    • Cheng X, Cole RN, Zaia J, Hart GW 2000 Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor β. Biochemistry 39:11609-11620
    • (2000) Biochemistry , vol.39 , pp. 11609-11620
    • Cheng, X.1    Cole, R.N.2    Zaia, J.3    Hart, G.W.4
  • 169
    • 0035971067 scopus 로고    scopus 로고
    • Alternative O-glycosylation/Ophosphorylation of serine-16 in murine estrogen receptor β: post-translational regulation of turnover and transactivation activity
    • Cheng X, Hart GW 2001 Alternative O-glycosylation/Ophosphorylation of serine-16 in murine estrogen receptor β: post-translational regulation of turnover and transactivation activity. J Biol Chem 276:10570-10575
    • (2001) J Biol Chem , vol.276 , pp. 10570-10575
    • Cheng, X.1    Hart, G.W.2
  • 170
    • 38849141014 scopus 로고    scopus 로고
    • Phosphorylation of activation function-1 regulates proteasome-dependent nuclear mobility and E6-associated protein ubiquitin ligase recruitment to the estrogen receptor β
    • Picard N, Charbonneau C, Sanchez M, Licznar A, Busson M, Lazennec G, Tremblay A 2008 Phosphorylation of activation function-1 regulates proteasome-dependent nuclear mobility and E6-associated protein ubiquitin ligase recruitment to the estrogen receptor β. Mol Endocrinol 22:317-330
    • (2008) Mol Endocrinol , vol.22 , pp. 317-330
    • Picard, N.1    Charbonneau, C.2    Sanchez, M.3    Licznar, A.4    Busson, M.5    Lazennec, G.6    Tremblay, A.7
  • 171
    • 0343371427 scopus 로고    scopus 로고
    • Contribution of steroid receptor coactivator-1 and CREB binding protein in ligandindependent activity of estrogen receptor β
    • Tremblay A, Giguère V 2001 Contribution of steroid receptor coactivator-1 and CREB binding protein in ligandindependent activity of estrogen receptor β. J Steroid Biochem Mol Biol 77:19-27
    • (2001) J Steroid Biochem Mol Biol , vol.77 , pp. 19-27
    • Tremblay, A.1    Giguère, V.2
  • 172
    • 18244392910 scopus 로고    scopus 로고
    • Selective hormone-dependent repression of estrogen receptor β by a p38-activated ErbB2/ErbB3 pathway
    • St-Laurent V, Sanchez M, Charbonneau C, Tremblay A 2005 Selective hormone-dependent repression of estrogen receptor β by a p38-activated ErbB2/ErbB3 pathway. J Steroid Biochem Mol Biol 94:23-37
    • (2005) J Steroid Biochem Mol Biol , vol.94 , pp. 23-37
    • St-Laurent, V.1    Sanchez, M.2    Charbonneau, C.3    Tremblay, A.4
  • 173
    • 33947541885 scopus 로고    scopus 로고
    • The hormonal response of estrogen receptor β is decreased by the phosphatidylinositol 3-kinase/Akt pathway via a phosphorylation- dependent release of CREB-binding protein
    • Sanchez M, Sauvé K, Picard N, Tremblay A 2007 The hormonal response of estrogen receptor β is decreased by the phosphatidylinositol 3-kinase/Akt pathway via a phosphorylation- dependent release of CREB-binding protein. J Biol Chem 282:4830-4840
    • (2007) J Biol Chem , vol.282 , pp. 4830-4840
    • Sanchez, M.1    Sauvé, K.2    Picard, N.3    Tremblay, A.4
  • 174
    • 0032031082 scopus 로고    scopus 로고
    • Ligand- independent activation of the estrogen receptors α and β by mutations of a conserved tyrosine can be abolished by antiestrogens
    • Tremblay GB, Tremblay A, Labrie F, Giguère V 1998 Ligand- independent activation of the estrogen receptors α and β by mutations of a conserved tyrosine can be abolished by antiestrogens. Cancer Res 58:877-881
    • (1998) Cancer Res , vol.58 , pp. 877-881
    • Tremblay, G.B.1    Tremblay, A.2    Labrie, F.3    Giguère, V.4
  • 176
    • 0026317212 scopus 로고
    • Dopaminergic and ligand-independent activation of steroid hormone receptors
    • Power RF, Mani SK, Codina J, Conneely OM, O'Malley BW 1991 Dopaminergic and ligand-independent activation of steroid hormone receptors. Science 254:1636-1639
    • (1991) Science , vol.254 , pp. 1636-1639
    • Power, R.F.1    Mani, S.K.2    Codina, J.3    Conneely, O.M.4    O'Malley, B.W.5
  • 179
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • Chen H, Lin RJ, Xie W, Wilpitz D, Evans RM 1999 Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 98:675-686
    • (1999) Cell , vol.98 , pp. 675-686
    • Chen, H.1    Lin, R.J.2    Xie, W.3    Wilpitz, D.4    Evans, R.M.5
  • 180
    • 0035503476 scopus 로고    scopus 로고
    • Arole for coactivators and histone acetylation in estrogen receptor α-mediated transcription initiation
    • Kim MY, Hsiao SJ, Kraus WL 2001 Arole for coactivators and histone acetylation in estrogen receptor α-mediated transcription initiation. EMBO J 20:6084-6094
    • (2001) EMBO J , vol.20 , pp. 6084-6094
    • Kim, M.Y.1    Hsiao, S.J.2    Kraus, W.L.3
  • 181
    • 33745658056 scopus 로고    scopus 로고
    • Acetylation of estrogen receptor α by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor
    • Kim MY, Woo EM, Chong YT, Homenko DR, Kraus WL 2006 Acetylation of estrogen receptor α by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor. Mol Endocrinol 20:1479-1493
    • (2006) Mol Endocrinol , vol.20 , pp. 1479-1493
    • Kim, M.Y.1    Woo, E.M.2    Chong, Y.T.3    Homenko, D.R.4    Kraus, W.L.5
  • 187
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling
    • Reid G, Hübner MR, Métivier R, Brand H, Denger S, Manu D, Beaudouin J, Ellenberg J, Gannon F 2003 Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling. Mol Cell 11:695-707
    • (2003) Mol Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hübner, M.R.2    Métivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6    Beaudouin, J.7    Ellenberg, J.8    Gannon, F.9
  • 188
    • 0029100143 scopus 로고
    • Ubiquitination of the rat uterine estrogen receptor: dependence on estradiol
    • Nirmala PB, Thampan RV 1995 Ubiquitination of the rat uterine estrogen receptor: dependence on estradiol. Biochem Biophys Res Commun 213:24-31
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 24-31
    • Nirmala, P.B.1    Thampan, R.V.2
  • 189
    • 28144439277 scopus 로고    scopus 로고
    • CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor- α
    • Fan M, Park A, Nephew KP 2005 CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor- α. Mol Endocrinol 19:2901-2914
    • (2005) Mol Endocrinol , vol.19 , pp. 2901-2914
    • Fan, M.1    Park, A.2    Nephew, K.P.3
  • 190
    • 34347262483 scopus 로고    scopus 로고
    • Differential regulation of estrogen receptor α turnover and transactivation by Mdm2 and stressinducing agents
    • Duong V, Boulle N, Daujat S, Chauvet J, Bonnet S, Neel H, Cavaillès V 2007 Differential regulation of estrogen receptor α turnover and transactivation by Mdm2 and stressinducing agents. Cancer Res 67:5513-5521
    • (2007) Cancer Res , vol.67 , pp. 5513-5521
    • Duong, V.1    Boulle, N.2    Daujat, S.3    Chauvet, J.4    Bonnet, S.5    Neel, H.6    Cavaillès, V.7
  • 191
    • 0033304776 scopus 로고    scopus 로고
    • Proteasomemediated proteolysis of estrogen receptor: a novel component in autologous down-regulation
    • Alarid ET, Bakopoulos N, Solodin N 1999 Proteasomemediated proteolysis of estrogen receptor: a novel component in autologous down-regulation. Mol Endocrinol 13:1522-1534
    • (1999) Mol Endocrinol , vol.13 , pp. 1522-1534
    • Alarid, E.T.1    Bakopoulos, N.2    Solodin, N.3
  • 193
    • 33748947865 scopus 로고    scopus 로고
    • The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription
    • Zhang H, Sun L, Liang J, Yu W, Zhang Y, Wang Y, Chen Y, Li R, Sun X, Shang Y 2006 The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. EMBO J 25:4223-4233
    • (2006) EMBO J , vol.25 , pp. 4223-4233
    • Zhang, H.1    Sun, L.2    Liang, J.3    Yu, W.4    Zhang, Y.5    Wang, Y.6    Chen, Y.7    Li, R.8    Sun, X.9    Shang, Y.10
  • 194
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Métivier R, Penot G, Hübner MR, Reid G, Brand H, Kos M, Gannon F 2003 Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115:751-763
    • (2003) Cell , vol.115 , pp. 751-763
    • Métivier, R.1    Penot, G.2    Hübner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 195
    • 33644855057 scopus 로고    scopus 로고
    • E6AP and calmodulin reciprocally regulate estrogen receptor stability
    • Li L, Li Z, Howley PM, Sacks DB 2006 E6AP and calmodulin reciprocally regulate estrogen receptor stability. J Biol Chem 281:1978-1985
    • (2006) J Biol Chem , vol.281 , pp. 1978-1985
    • Li, L.1    Li, Z.2    Howley, P.M.3    Sacks, D.B.4
  • 198
    • 4143093854 scopus 로고    scopus 로고
    • Coactivator AIB1 links estrogen receptor transcriptional activity and stability
    • Shao W, Keeton EK, McDonnell DP, Brown M 2004 Coactivator AIB1 links estrogen receptor transcriptional activity and stability. Proc Natl Acad Sci USA 101:11599-11604
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11599-11604
    • Shao, W.1    Keeton, E.K.2    McDonnell, D.P.3    Brown, M.4
  • 199
    • 0033060824 scopus 로고    scopus 로고
    • Implication of proteasome in estrogen receptor degradation
    • El Khissiin A, Leclercq G 1999 Implication of proteasome in estrogen receptor degradation. FEBS Lett 448:160-166
    • (1999) FEBS Lett , vol.448 , pp. 160-166
    • El Khissiin, A.1    Leclercq, G.2
  • 200
    • 33646930743 scopus 로고    scopus 로고
    • Fulvestrant (ICI 182,780)-dependent interacting proteins mediate immobilization and degradation of estrogen receptor-α
    • Long X, Nephew KP 2006 Fulvestrant (ICI 182,780)-dependent interacting proteins mediate immobilization and degradation of estrogen receptor-α. J Biol Chem 281:9607-9615
    • (2006) J Biol Chem , vol.281 , pp. 9607-9615
    • Long, X.1    Nephew, K.P.2
  • 201
    • 46349108800 scopus 로고    scopus 로고
    • Estrogen receptor-α hinge-region lysines 302 and 303 regulate receptor degradation by the proteasome
    • Berry NB, Fan M, Nephew KP 2008 Estrogen receptor-α hinge-region lysines 302 and 303 regulate receptor degradation by the proteasome. Mol Endocrinol 22:1535-1551
    • (2008) Mol Endocrinol , vol.22 , pp. 1535-1551
    • Berry, N.B.1    Fan, M.2    Nephew, K.P.3
  • 202
    • 34347256776 scopus 로고    scopus 로고
    • Estrogen receptor α is a putative substrate for the BRCA1 ubiquitin ligase
    • Eakin CM, Maccoss MJ, Finney GL, Klevit RE 2007 Estrogen receptor α is a putative substrate for the BRCA1 ubiquitin ligase. Proc Natl Acad Sci USA 104:5794-5799
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5794-5799
    • Eakin, C.M.1    Maccoss, M.J.2    Finney, G.L.3    Klevit, R.E.4
  • 203
    • 67650215581 scopus 로고    scopus 로고
    • OTU Domain-containing ubiquitin aldehydebinding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) α and affects ERα transcriptional activity
    • Stanisiæ V, Malovannaya A, Qin J, Lonard DM, O'Malley BW 2009 OTU Domain-containing ubiquitin aldehydebinding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) α and affects ERα transcriptional activity. J Biol Chem 284:16135-16145
    • (2009) J Biol Chem , vol.284 , pp. 16135-16145
    • Stanisiæ, V.1    Malovannaya, A.2    Qin, J.3    Lonard, D.M.4    O'Malley, B.W.5
  • 205
    • 1842425822 scopus 로고    scopus 로고
    • Involvement of suppressor for Gal 1 in the ubiquitin/proteasome-mediated degradation of estrogen receptors
    • Masuyama H, Hiramatsu Y 2004 Involvement of suppressor for Gal 1 in the ubiquitin/proteasome-mediated degradation of estrogen receptors. J Biol Chem 279:12020-12026
    • (2004) J Biol Chem , vol.279 , pp. 12020-12026
    • Masuyama, H.1    Hiramatsu, Y.2
  • 206
    • 27644467440 scopus 로고    scopus 로고
    • Sumoylation of the estrogen receptor α hinge region regulates its transcriptional activity
    • Sentis S, Le Romancer M, Bianchin C, Rostan MC, Corbo L 2005 Sumoylation of the estrogen receptor α hinge region regulates its transcriptional activity. Mol Endocrinol 19:2671-2684
    • (2005) Mol Endocrinol , vol.19 , pp. 2671-2684
    • Sentis, S.1    Le Romancer, M.2    Bianchin, C.3    Rostan, M.C.4    Corbo, L.5
  • 207
    • 73449092853 scopus 로고    scopus 로고
    • SET7/9 mediated methylation of non-histone proteins in mammalian cells
    • Pradhan S, Chin HG, Estève PO, Jacobsen SE 2009 SET7/9 mediated methylation of non-histone proteins in mammalian cells. Epigenetics 4:383-387
    • (2009) Epigenetics , vol.4 , pp. 383-387
    • Pradhan, S.1    Chin, H.G.2    Estève, P.O.3    Jacobsen, S.E.4
  • 209
    • 14044276372 scopus 로고    scopus 로고
    • Rapid nitric oxide-mediated S-nitrosylation of estrogen receptor: regulation of estrogen-dependent gene transcription
    • Garbán HJ, Márquez-Garbán DC, Pietras RJ, Ignarro LJ 2005 Rapid nitric oxide-mediated S-nitrosylation of estrogen receptor: regulation of estrogen-dependent gene transcription. Proc Natl Acad Sci USA 102:2632-2636
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2632-2636
    • Garbán, H.J.1    Márquez-Garbán, D.C.2    Pietras, R.J.3    Ignarro, L.J.4
  • 210
    • 0034671011 scopus 로고    scopus 로고
    • Glycosylation of the murine estrogen receptor-α
    • Cheng X, Hart GW 2000 Glycosylation of the murine estrogen receptor-α. J Steroid Biochem Mol Biol 75:147-158
    • (2000) J Steroid Biochem Mol Biol , vol.75 , pp. 147-158
    • Cheng, X.1    Hart, G.W.2
  • 211
    • 0031017574 scopus 로고    scopus 로고
    • A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine
    • Jiang MS, Hart GW 1997 A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine. J Biol Chem 272:2421-2428
    • (1997) J Biol Chem , vol.272 , pp. 2421-2428
    • Jiang, M.S.1    Hart, G.W.2
  • 213
    • 0017354142 scopus 로고
    • Specific binding sites for oestrogen at the outer surfaces of isolated endometrial cells
    • Pietras RJ, Szego CM 1977 Specific binding sites for oestrogen at the outer surfaces of isolated endometrial cells. Nature 265:69-72
    • (1977) Nature , vol.265 , pp. 69-72
    • Pietras, R.J.1    Szego, C.M.2
  • 216
    • 42549141260 scopus 로고    scopus 로고
    • The nutritional flavanone naringenin triggers antiestrogenic effects by regulating estrogen receptorα-palmitoylation
    • Galluzzo P, Ascenzi P, Bulzomi P, Marino M 2008 The nutritional flavanone naringenin triggers antiestrogenic effects by regulating estrogen receptorα-palmitoylation. Endocrinology 149:2567-2575
    • (2008) Endocrinology , vol.149 , pp. 2567-2575
    • Galluzzo, P.1    Ascenzi, P.2    Bulzomi, P.3    Marino, M.4
  • 217
  • 218
    • 44549088115 scopus 로고    scopus 로고
    • Membrane association of estrogen receptorα andβ influences 17β-estradiol-mediated cancer cell proliferation
    • Marino M, Ascenzi P 2008 Membrane association of estrogen receptorα andβ influences 17β-estradiol-mediated cancer cell proliferation. Steroids 73:853-858
    • (2008) Steroids , vol.73 , pp. 853-858
    • Marino, M.1    Ascenzi, P.2
  • 219
    • 34249682915 scopus 로고    scopus 로고
    • Role of ERβ palmitoylation in the inhibition of human colon cancer cell proliferation
    • Galluzzo P, Caiazza F, Moreno S, Marino M 2007 Role of ERβ palmitoylation in the inhibition of human colon cancer cell proliferation. Endocr Relat Cancer 14:153-167
    • (2007) Endocr Relat Cancer , vol.14 , pp. 153-167
    • Galluzzo, P.1    Caiazza, F.2    Moreno, S.3    Marino, M.4
  • 221
    • 0022820771 scopus 로고
    • Estradiol receptor: phosphorylation on tyrosine in uterus and interaction with anti-phosphotyrosine antibody
    • Migliaccio A, Rotondi A, Auricchio F 1986 Estradiol receptor: phosphorylation on tyrosine in uterus and interaction with anti-phosphotyrosine antibody. EMBO J 5:2867-2872
    • (1986) EMBO J , vol.5 , pp. 2867-2872
    • Migliaccio, A.1    Rotondi, A.2    Auricchio, F.3
  • 223
    • 0028833473 scopus 로고
    • Phos- phorylation 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 Phos- phorylation 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
  • 224
    • 44549087499 scopus 로고    scopus 로고
    • Sex-steroid hormones and EGFsignalling in breast and prostate cancer cells: targeting the association of Src with steroid receptors
    • Auricchio F, Migliaccio A, Castoria G 2008 Sex-steroid hormones and EGFsignalling in breast and prostate cancer cells: targeting the association of Src with steroid receptors. Steroids 73:880-884
    • (2008) Steroids , vol.73 , pp. 880-884
    • Auricchio, F.1    Migliaccio, A.2    Castoria, G.3
  • 226
    • 33751552134 scopus 로고    scopus 로고
    • Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, deoxyribonucleic acid, and coregulators associated with alterations in estrogen and tamoxifen activity
    • Likhite VS, Stossi F, Kim K, Katzenellenbogen BS, Katzenellenbogen JA 2006 Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, deoxyribonucleic acid, and coregulators associated with alterations in estrogen and tamoxifen activity. Mol Endocrinol 20:3120-3132
    • (2006) Mol Endocrinol , vol.20 , pp. 3120-3132
    • Likhite, V.S.1    Stossi, F.2    Kim, K.3    Katzenellenbogen, B.S.4    Katzenellenbogen, J.A.5
  • 229
    • 0030940071 scopus 로고    scopus 로고
    • An estrogen receptor mutant with strong hormoneindependent activity from a metastatic breast cancer
    • Zhang QX, Borg A, Wolf DM, Oesterreich S, Fuqua SA 1997 An estrogen receptor mutant with strong hormoneindependent activity from a metastatic breast cancer. Cancer Res 57:1244-1249
    • (1997) Cancer Res , vol.57 , pp. 1244-1249
    • Zhang, Q.X.1    Borg, A.2    Wolf, D.M.3    Oesterreich, S.4    Fuqua, S.A.5
  • 230
    • 10844286471 scopus 로고    scopus 로고
    • Phosphorylation of estrogen receptor α blocks its acetylation and regulates estrogen sensitivity
    • Cui Y, Zhang M, Pestell R, Curran EM, Welshons WV, Fuqua SA 2004 Phosphorylation of estrogen receptor α blocks its acetylation and regulates estrogen sensitivity. Cancer Res 64:9199-9208
    • (2004) Cancer Res , vol.64 , pp. 9199-9208
    • Cui, Y.1    Zhang, M.2    Pestell, R.3    Curran, E.M.4    Welshons, W.V.5    Fuqua, S.A.6
  • 232
    • 34250681785 scopus 로고    scopus 로고
    • Association between the estrogen receptor α A908G mutation and outcomes in invasive breast cancer
    • Herynk MH, Parra I, Cui Y, Beyer A, Wu MF, Hilsenbeck SG, Fuqua SA 2007 Association between the estrogen receptor α A908G mutation and outcomes in invasive breast cancer. Clin Cancer Res 13:3235-3243
    • (2007) Clin Cancer Res , vol.13 , pp. 3235-3243
    • Herynk, M.H.1    Parra, I.2    Cui, Y.3    Beyer, A.4    Wu, M.F.5    Hilsenbeck, S.G.6    Fuqua, S.A.7
  • 233
    • 32944473985 scopus 로고    scopus 로고
    • P21-activated kinase 1 regulation of estrogen receptor-α activation involves serine 305 activation linked with serine 118 phosphorylation
    • Rayala SK, Talukder AH, Balasenthil S, Tharakan R, Barnes CJ, Wang RA, Aldaz CM, Khan S, Kumar R 2006 P21-activated kinase 1 regulation of estrogen receptor-α activation involves serine 305 activation linked with serine 118 phosphorylation. Cancer Res 66:1694-1701
    • (2006) Cancer Res , vol.66 , pp. 1694-1701
    • Rayala, S.K.1    Talukder, A.H.2    Balasenthil, S.3    Tharakan, R.4    Barnes, C.J.5    Wang, R.A.6    Aldaz, C.M.7    Khan, S.8    Kumar, R.9
  • 234
    • 18944391961 scopus 로고    scopus 로고
    • CSN5/Jab1 is involved in ligand-dependent degradation of estrogen receptor α by the proteasome
    • Calligé M, Kieffer I, Richard-Foy H 2005 CSN5/Jab1 is involved in ligand-dependent degradation of estrogen receptor α by the proteasome. Mol Cell Biol 25:4349-4358
    • (2005) Mol Cell Biol , vol.25 , pp. 4349-4358
    • Calligé, M.1    Kieffer, I.2    Richard-Foy, H.3
  • 235
    • 20844453021 scopus 로고    scopus 로고
    • Differential regulation of estrogen- inducible proteolysis and transcription by the estrogen receptorαNterminus
    • Valley CC, Métivier R, Solodin NM, Fowler AM, Mashek MT, Hill L, Alarid ET 2005 Differential regulation of estrogen- inducible proteolysis and transcription by the estrogen receptorαNterminus. Mol Cell Biol 25:5417-5428
    • (2005) Mol Cell Biol , vol.25 , pp. 5417-5428
    • Valley, C.C.1    Métivier, R.2    Solodin, N.M.3    Fowler, A.M.4    Mashek, M.T.5    Hill, L.6    Alarid, E.T.7
  • 238
    • 0034017798 scopus 로고    scopus 로고
    • Results of two or five years of adjuvant tamoxifen correlated to steroid receptor and S-phase levels. South Sweden Breast Cancer Group, and South-East Sweden Breast Cancer Group
    • Fernö M, Stål O, Baldetorp B, Hatschek T, Källström AC, Malmström P, Nordenskjöld B, Rydën S 2000 Results of two or five years of adjuvant tamoxifen correlated to steroid receptor and S-phase levels. South Sweden Breast Cancer Group, and South-East Sweden Breast Cancer Group. Breast Cancer Res Treat 59:69-76
    • (2000) Breast Cancer Res Treat , vol.59 , pp. 69-76
    • Fernö, M.1    Stål, O.2    Baldetorp, B.3    Hatschek, T.4    Källström, A.C.5    Malmström, P.6    Nordenskjöld, B.7    Rydën, S.8
  • 242
    • 4444324186 scopus 로고    scopus 로고
    • Phosphoserine- 118 estrogen receptor-α expression is associated with better disease outcome in women treated with tamoxifen
    • Murphy LC, Niu Y, Snell L, Watson P 2004 Phosphoserine- 118 estrogen receptor-α expression is associated with better disease outcome in women treated with tamoxifen. Clin Cancer Res 10:5902-5906
    • (2004) Clin Cancer Res , vol.10 , pp. 5902-5906
    • Murphy, L.C.1    Niu, Y.2    Snell, L.3    Watson, P.4
  • 244
    • 50249163362 scopus 로고    scopus 로고
    • Low phosphorylation of estrogen receptor α (ERα) serine 118 and high phosphorylation of ERα serine 167 improve survival in ERpositive breast cancer
    • Yamashita H, Nishio M, Toyama T, Sugiura H, Kondo N, Kobayashi S, Fujii Y, Iwase H 2008 Low phosphorylation of estrogen receptor α (ERα) serine 118 and high phosphorylation of ERα serine 167 improve survival in ERpositive breast cancer. Endocr Relat Cancer 15:755-763
    • (2008) Endocr Relat Cancer , vol.15 , pp. 755-763
    • Yamashita, H.1    Nishio, M.2    Toyama, T.3    Sugiura, H.4    Kondo, N.5    Kobayashi, S.6    Fujii, Y.7    Iwase, H.8
  • 246
    • 35348904493 scopus 로고    scopus 로고
    • Phosphorylation of estrogen receptor- α at Ser167 is indicative of longer disease-free and overall survival in breast cancer patients
    • Jiang J, Sarwar N, Peston D, Kulinskaya E, Shousha S, Coombes RC, Ali S 2007 Phosphorylation of estrogen receptor- α at Ser167 is indicative of longer disease-free and overall survival in breast cancer patients. Clin Cancer Res 13:5769-5776
    • (2007) Clin Cancer Res , vol.13 , pp. 5769-5776
    • Jiang, J.1    Sarwar, N.2    Peston, D.3    Kulinskaya, E.4    Shousha, S.5    Coombes, R.C.6    Ali, S.7
  • 247
    • 25844468319 scopus 로고    scopus 로고
    • Epidermal growth factor receptor/HER2/insulin-like growth factor receptor signalling and oestrogen receptor activity in clinical breast cancer
    • Gee JM, Robertson JF, Gutteridge E, Ellis IO, Pinder SE, Rubini M, Nicholson RI 2005 Epidermal growth factor receptor/HER2/insulin-like growth factor receptor signalling and oestrogen receptor activity in clinical breast cancer. Endocr Relat Cancer 12(Suppl 1):S99-S111
    • (2005) Endocr Relat Cancer , vol.12 , Issue.SUPPL 1
    • Gee, J.M.1    Robertson, J.F.2    Gutteridge, E.3    Ellis, I.O.4    Pinder, S.E.5    Rubini, M.6    Nicholson, R.I.7
  • 249
    • 77956205328 scopus 로고    scopus 로고
    • A phosphorylation code for oestrogen receptor α predicts clinical outcome to endocrine therapy in breast cancer
    • Skliris GP, Nugent ZJ, Rowan BG, Penner CR, Watson PH, Murphy LC 2010 A phosphorylation code for oestrogen receptor α predicts clinical outcome to endocrine therapy in breast cancer. Endocr Relat Cancer 17:589-597
    • (2010) Endocr Relat Cancer , vol.17 , pp. 589-597
    • Skliris, G.P.1    Nugent, Z.J.2    Rowan, B.G.3    Penner, C.R.4    Watson, P.H.5    Murphy, L.C.6
  • 250
    • 33644873967 scopus 로고    scopus 로고
    • Phosphorylation of estrogen receptor α serine 167 is predictive of response to endocrine therapy and increases postrelapse survival in metastatic breast cancer
    • Yamashita H, Nishio M, Kobayashi S, Ando Y, Sugiura H, Zhang Z, Hamaguchi M, Mita K, Fujii Y, Iwase H 2005 Phosphorylation of estrogen receptor α serine 167 is predictive of response to endocrine therapy and increases postrelapse survival in metastatic breast cancer. Breast Cancer Res 7:R753-R764
    • (2005) Breast Cancer Res , vol.7
    • Yamashita, H.1    Nishio, M.2    Kobayashi, S.3    Ando, Y.4    Sugiura, H.5    Zhang, Z.6    Hamaguchi, M.7    Mita, K.8    Fujii, Y.9    Iwase, H.10
  • 252
    • 70449587245 scopus 로고    scopus 로고
    • Immunohistochemical validation of multiple phospho-specific epitopes for estrogen receptor α (ERα) in tissue microarrays of ERα positivehumanbreast carcinomas
    • Skliris GP, Rowan BG, Al-Dhaheri M, Williams C, Troup S, Begic S, Parisien M, Watson PH, Murphy LC 2009 Immunohistochemical validation of multiple phospho-specific epitopes for estrogen receptor α (ERα) in tissue microarrays of ERα positivehumanbreast carcinomas. Breast Cancer Res Treat 118:443-453
    • (2009) Breast Cancer Res Treat , vol.118 , pp. 443-453
    • Skliris, G.P.1    Rowan, B.G.2    Al-Dhaheri, M.3    Williams, C.4    Troup, S.5    Begic, S.6    Parisien, M.7    Watson, P.H.8    Murphy, L.C.9
  • 254
    • 0031418311 scopus 로고    scopus 로고
    • Changes in messenger RNAexpression of protein kinase A regulatory subunit iα in breast cancer patients treated with tamoxifen
    • Miller WR, Hulme MJ, Bartlett JM, MacCallum J, Dixon JM 1997 Changes in messenger RNAexpression of protein kinase A regulatory subunit iα in breast cancer patients treated with tamoxifen. Clin Cancer Res 3:2399-2404
    • (1997) Clin Cancer Res , vol.3 , pp. 2399-2404
    • Miller, W.R.1    Hulme, M.J.2    Bartlett, J.M.3    MacCallum, J.4    Dixon, J.M.5
  • 255
    • 35549002845 scopus 로고    scopus 로고
    • Amplification of CCND1 and PAK1as predictors of recurrence and tamoxifen resistance in postmenopausal breast cancer
    • Bostner J, Ahnström Waltersson M, Fornander T, Skoog L, Nordenskjöld B, Stål O 2007 Amplification of CCND1 and PAK1as predictors of recurrence and tamoxifen resistance in postmenopausal breast cancer. Oncogene 26:6997-7005
    • (2007) Oncogene , vol.26 , pp. 6997-7005
    • Bostner, J.1    Ahnström Waltersson, M.2    Fornander, T.3    Skoog, L.4    Nordenskjöld, B.5    Stål, O.6
  • 256
    • 33646940460 scopus 로고    scopus 로고
    • Association between Pak1 expression and subcellular localization and tamoxifen resistance in breast cancer patients
    • Holm C, Rayala S, Jirström K, Stål O, Kumar R, Landberg G 2006 Association between Pak1 expression and subcellular localization and tamoxifen resistance in breast cancer patients. J Natl Cancer Inst 98:671-680
    • (2006) J Natl Cancer Inst , vol.98 , pp. 671-680
    • Holm, C.1    Rayala, S.2    Jirström, K.3    Stål, O.4    Kumar, R.5    Landberg, G.6
  • 257
    • 77649091619 scopus 로고    scopus 로고
    • Estrogen receptor-α phosphorylation at serine 305, nuclear p21-activated kinase 1 expression, and response to tamoxifen in postmenopausal breast cancer
    • Bostner J, Skoog L, Fornander T, Nordenskjöld B, Stål O 2010 Estrogen receptor-α phosphorylation at serine 305, nuclear p21-activated kinase 1 expression, and response to tamoxifen in postmenopausal breast cancer. Clin Cancer Res 16:1624-1633
    • (2010) Clin Cancer Res , vol.16 , pp. 1624-1633
    • Bostner, J.1    Skoog, L.2    Fornander, T.3    Nordenskjöld, B.4    Stål, O.5
  • 258
    • 36348969300 scopus 로고    scopus 로고
    • Alternative splicing yields protein arginine methyltransferase 1 isoforms with distinct activity, substrate specificity, and subcellular localization
    • Goulet I, Gauvin G, Boisvenue S, Côté J 2007 Alternative splicing yields protein arginine methyltransferase 1 isoforms with distinct activity, substrate specificity, and subcellular localization. J Biol Chem 282:33009-33021
    • (2007) J Biol Chem , vol.282 , pp. 33009-33021
    • Goulet, I.1    Gauvin, G.2    Boisvenue, S.3    Côté, J.4
  • 262
    • 77951081069 scopus 로고    scopus 로고
    • c-Abl regulates estrogen receptor α transcription activity through its stabilization by phosphorylation
    • He X, Zheng Z, Song T, Wei C, Ma H, Ma Q, Zhang Y, Xu Y, Shi W, Ye Q, Zhong H 2010 c-Abl regulates estrogen receptor α transcription activity through its stabilization by phosphorylation. Oncogene 29:2238-2251
    • (2010) Oncogene , vol.29 , pp. 2238-2251
    • He, X.1    Zheng, Z.2    Song, T.3    Wei, C.4    Ma, H.5    Ma, Q.6    Zhang, Y.7    Xu, Y.8    Shi, W.9    Ye, Q.10    Zhong, H.11
  • 263
    • 0033636597 scopus 로고    scopus 로고
    • Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7
    • Chen D, Riedl T, Washbrook E, Pace PE, Coombes RC, Egly JM, Ali S 2000 Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7. Mol Cell 6:127-137
    • (2000) Mol Cell , vol.6 , pp. 127-137
    • Chen, D.1    Riedl, T.2    Washbrook, E.3    Pace, P.E.4    Coombes, R.C.5    Egly, J.M.6    Ali, S.7
  • 264
    • 70350220644 scopus 로고    scopus 로고
    • Reactive oxygen species induce phosphorylation of serine 118 and 167 on estrogen receptor α
    • Weitsman GE, Weebadda W, Ung K, Murphy LC 2009 Reactive oxygen species induce phosphorylation of serine 118 and 167 on estrogen receptor α. Breast Cancer Res Treat 118:269-279
    • (2009) Breast Cancer Res Treat , vol.118 , pp. 269-279
    • Weitsman, G.E.1    Weebadda, W.2    Ung, K.3    Murphy, L.C.4
  • 266
    • 43049162551 scopus 로고    scopus 로고
    • Akt stabilizes estrogen receptor α with the concomitant reduction in its transcriptional activity
    • Park S, Song J, Joe CO, Shin I 2008 Akt stabilizes estrogen receptor α with the concomitant reduction in its transcriptional activity. Cell Signal 20:1368-1374
    • (2008) Cell Signal , vol.20 , pp. 1368-1374
    • Park, S.1    Song, J.2    Joe, C.O.3    Shin, I.4
  • 267
    • 76149105148 scopus 로고    scopus 로고
    • Identification of four novel phosphorylation sites in estrogen receptor α: impact on receptor- dependent gene expression and phosphorylation by protein kinase CK2
    • Williams CC, Basu A, El-Gharbawy A, Carrier LM, Smith CL, Rowan BG 2009 Identification of four novel phosphorylation sites in estrogen receptor α: impact on receptor- dependent gene expression and phosphorylation by protein kinase CK2. BMC Biochem 10:36
    • (2009) BMC Biochem , vol.10 , pp. 36
    • Williams, C.C.1    Basu, A.2    El-Gharbawy, A.3    Carrier, L.M.4    Smith, C.L.5    Rowan, B.G.6
  • 268
    • 0036318571 scopus 로고    scopus 로고
    • Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation
    • Lee H, Bai W 2002 Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation. Mol Cell Biol 22:5835-5845
    • (2002) Mol Cell Biol , vol.22 , pp. 5835-5845
    • Lee, H.1    Bai, W.2
  • 270
    • 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
  • 271
    • 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
  • 272
    • 0035721850 scopus 로고    scopus 로고
    • Epidermal growth factor receptor and tyrosine phosphorylation of estrogen receptor
    • Márquez DC, Lee J, Lin T, Pietras RJ 2001 Epidermal growth factor receptor and tyrosine phosphorylation of estrogen receptor. Endocrine 16:73-81
    • (2001) Endocrine , vol.16 , pp. 73-81
    • Márquez, D.C.1    Lee, J.2    Lin, T.3    Pietras, R.J.4
  • 273
    • 83355162308 scopus 로고    scopus 로고
    • Nanocarriers targeting breast cancers to deliver modulators of estrogen receptor
    • Souto EB, ed., Akron, Ohio: iSmithers Creative Publishing Solutions
    • Urbinati G, Marsaud V, Plassat V, Renoir JM 2011 Nanocarriers targeting breast cancers to deliver modulators of estrogen receptor. In: Souto EB, ed. Lipid nanocarriers in cancer diagnosis and therapy. Akron, Ohio: iSmithers Creative Publishing Solutions 10:279-330
    • (2011) Lipid nanocarriers in cancer diagnosis and therapy , vol.10 , pp. 279-330
    • Urbinati, G.1    Marsaud, V.2    Plassat, V.3    Renoir, J.M.4


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