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Volumn 288, Issue 35, 2013, Pages 25038-25052

Estrogen receptor β (ERβ1) transactivation is differentially modulated by the transcriptional coregulator Tip60 in a cis-acting element-dependent manner

Author keywords

[No Author keywords available]

Indexed keywords

CIS ACTINGS; COACTIVATORS; COREGULATORS; COREPRESSORS; ESTROGEN RECEPTOR; TRANSACTIVATION; TRANSCRIPTIONAL ACTIVITY;

EID: 84883357081     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.476952     Document Type: Article
Times cited : (12)

References (77)
  • 1
    • 80052249325 scopus 로고    scopus 로고
    • Estrogens and prostate cancer: Etiology, mediators, prevention, and management
    • Ho, S. M., Lee, M. T., Lam, H. M., and Leung, Y. K. (2011) Estrogens and prostate cancer: etiology, mediators, prevention, and management. Endocrinol. Metab Clin. North Am. 40, 591-614
    • (2011) Endocrinol. Metab Clin. North Am , vol.40 , pp. 591-614
    • Ho, S.M.1    Lee, M.T.2    Lam, H.M.3    Leung, Y.K.4
  • 2
    • 33746600263 scopus 로고    scopus 로고
    • Estrogen receptor target gene: An evolving concept
    • Carroll, J. S., and Brown, M. (2006) Estrogen receptor target gene: an evolving concept. Mol. Endocrinol. 20, 1707-1714
    • (2006) Mol. Endocrinol , vol.20 , pp. 1707-1714
    • Carroll, J.S.1    Brown, M.2
  • 3
    • 0035878743 scopus 로고    scopus 로고
    • Estrogen receptor interaction with estrogen-response elements
    • Klinge, C. M. (2001) Estrogen receptor interaction with estrogen-response elements. Nucleic Acids Res. 29, 2905-2919
    • (2001) Nucleic Acids Res , vol.29 , pp. 2905-2919
    • Klinge, C.M.1
  • 5
    • 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, J. A., and 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
  • 7
    • 79953905621 scopus 로고    scopus 로고
    • Exploration of dimensions of estrogen potency: Parsing ligand binding and coactivator binding affinities
    • Jeyakumar, M., Carlson, K. E., Gunther, J. R., and Katzenellenbogen, J. A. (2011) Exploration of dimensions of estrogen potency: parsing ligand binding and coactivator binding affinities. J. Biol. Chem. 286, 12971-12982
    • (2011) J. Biol. Chem , vol.286 , pp. 12971-12982
    • Jeyakumar, M.1    Carlson, K.E.2    Gunther, J.R.3    Katzenellenbogen, J.A.4
  • 8
    • 7244247363 scopus 로고    scopus 로고
    • Estrogen-response element-dependent regulation of transcriptional activation of estrogen receptors α and β by coactivators and corepressors
    • Klinge, C. M., Jernigan, S. C., Mattingly, K. A., Risinger, K. E., and 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
  • 9
    • 0035849586 scopus 로고    scopus 로고
    • Structure-function evaluation of ER α and β interplay with SRC family coactivators. ER selective ligands
    • Wong, C. W., Komm, B., and Cheskis, B. J. (2001) Structure-function evaluation of ER α and β interplay with SRC family coactivators. ER selective ligands. Biochemistry 40, 6756-6765
    • (2001) Biochemistry , vol.40 , pp. 6756-6765
    • Wong, C.W.1    Komm, B.2    Cheskis, B.J.3
  • 11
    • 77953740831 scopus 로고    scopus 로고
    • Genome-wide mapping of estrogen receptor-β-binding regions reveals extensive cross-talk with transcription factor activator protein-1
    • Zhao, C., Gao, H., Liu, Y., Papoutsi, Z., Jaffrey, S., Gustafsson, J. A., and Dahlman-Wright, K. (2010) Genome-wide mapping of estrogen receptor-β-binding regions reveals extensive cross-talk with transcription factor activator protein-1. Cancer Res. 70, 5174-5183
    • (2010) Cancer Res , vol.70 , pp. 5174-5183
    • Zhao, C.1    Gao, H.2    Liu, Y.3    Papoutsi, Z.4    Jaffrey, S.5    Gustafsson, J.A.6    Dahlman-Wright, K.7
  • 12
    • 34548252291 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Judges, juries, and executioners of cellular regulation
    • Lonard, D. M., and O'malley, B. W. (2007) Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation. Mol. Cell 27, 691-700
    • (2007) Mol. Cell , vol.27 , pp. 691-700
    • Lonard, D.M.1    O'Malley, B.W.2
  • 14
    • 18844373937 scopus 로고    scopus 로고
    • Transcriptional regulation by steroid receptor coactivator phosphorylation
    • Wu, R. C., Smith, C. L., and O'Malley, B. W. (2005) Transcriptional regulation by steroid receptor coactivator phosphorylation. Endocr. Rev. 26, 393-399
    • (2005) Endocr. Rev , vol.26 , pp. 393-399
    • Wu, R.C.1    Smith, C.L.2    O'Malley, B.W.3
  • 15
    • 4143114765 scopus 로고    scopus 로고
    • Acetylation of nuclear receptors in cellular growth and apoptosis
    • Fu, M., Wang, C., Zhang, X., and Pestell, R. G. (2004) Acetylation of nuclear receptors in cellular growth and apoptosis. Biochem. Pharmacol. 68, 1199-1208
    • (2004) Biochem. Pharmacol , vol.68 , pp. 1199-1208
    • Fu, M.1    Wang, C.2    Zhang, X.3    Pestell, R.G.4
  • 16
    • 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, M. Y., Woo, E. M., Chong, Y. T., Homenko, D. R., and Kraus, W. L. (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
  • 18
    • 10844286471 scopus 로고    scopus 로고
    • Phosphorylation of estrogen receptor α blocks its acetylation and regulates estrogen sensitivity
    • Cui, Y., Zhang, M., Pestell, R., Curran, E. M., Welshons, W. V., and Fuqua, S. A. (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
  • 21
    • 0037242383 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases
    • Utley, R. T., and Côté, J. (2003) The MYST family of histone acetyltransferases. Curr. Top. Microbiol. Immunol. 274, 203-236
    • (2003) Curr. Top. Microbiol. Immunol , vol.274 , pp. 203-236
    • Utley, R.T.1    Côté, J.2
  • 22
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein
    • Baek, S. H., Ohgi, K. A., Rose, D. W., Koo, E. H., Glass, C. K., and Rosenfeld, M. G. (2002) Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein. Cell 110, 55-67
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 24
    • 0037135566 scopus 로고    scopus 로고
    • Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor
    • Gaughan, L., Logan, I. R., Cook, S., Neal, D. E., and Robson, C. N. (2002) Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor. J. Biol. Chem. 277, 25904-25913
    • (2002) J. Biol. Chem , vol.277 , pp. 25904-25913
    • Gaughan, L.1    Logan, I.R.2    Cook, S.3    Neal, D.E.4    Robson, C.N.5
  • 27
    • 0034708355 scopus 로고    scopus 로고
    • Tip60 inhibits activation of CREB protein by protein kinase A
    • Gavaravarapu, S., and Kamine, J. (2000) Tip60 inhibits activation of CREB protein by protein kinase A. Biochem. Biophys. Res. Commun. 269, 758-766
    • (2000) Biochem. Biophys. Res. Commun , vol.269 , pp. 758-766
    • Gavaravarapu, S.1    Kamine, J.2
  • 28
    • 0037837745 scopus 로고    scopus 로고
    • Tip60 is a corepressor for STAT3
    • Xiao, H., Chung, J., Kao, H. Y., and Yang, Y. C. (2003) Tip60 is a corepressor for STAT3. J. Biol. Chem. 278, 11197-11204
    • (2003) J. Biol. Chem , vol.278 , pp. 11197-11204
    • Xiao, H.1    Chung, J.2    Kao, H.Y.3    Yang, Y.C.4
  • 29
    • 82955198464 scopus 로고    scopus 로고
    • Recognition of enhancer element-specific histone methylation by TIP60 in transcriptional activation
    • Jeong, K. W., Kim, K., Situ, A. J., Ulmer, T. S., An, W., and Stallcup, M. R. (2011) Recognition of enhancer element-specific histone methylation by TIP60 in transcriptional activation. Nat. Struct. Mol. Biol. 18, 1358-1365
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 1358-1365
    • Jeong, K.W.1    Kim, K.2    Situ, A.J.3    Ulmer, T.S.4    An, W.5    Stallcup, M.R.6
  • 31
    • 84861203822 scopus 로고    scopus 로고
    • Gene-specific patterns of coregulator requirements by estrogen receptor-α in breast cancer cells
    • Won Jeong, K., Chodankar, R., Purcell, D. J., Bittencourt, D., and Stallcup, M. R. (2012) Gene-specific patterns of coregulator requirements by estrogen receptor-α in breast cancer cells. Mol. Endocrinol. 26, 955-966
    • (2012) Mol. Endocrinol , vol.26 , pp. 955-966
    • Won Jeong, K.1    Chodankar, R.2    Purcell, D.J.3    Bittencourt, D.4    Stallcup, M.R.5
  • 32
    • 0035861571 scopus 로고    scopus 로고
    • Tip60 is a co-activator specific for class i nuclear hormone receptors
    • Gaughan, L., Brady, M. E., Cook, S., Neal, D. E., and Robson, C. N. (2001) Tip60 is a co-activator specific for class I nuclear hormone receptors. J. Biol. Chem. 276, 46841-46848
    • (2001) J. Biol. Chem , vol.276 , pp. 46841-46848
    • Gaughan, L.1    Brady, M.E.2    Cook, S.3    Neal, D.E.4    Robson, C.N.5
  • 33
    • 77956363192 scopus 로고    scopus 로고
    • Estrogen receptorβ2 andβ5 are associated with poor prognosis in prostate cancer and promote cancer cell migration and invasion
    • Leung, Y. K., Lam, H. M., Wu, S., Song, D., Levin, L., Cheng, L., Wu, C. L., and Ho, S. M. (2010) Estrogen receptorβ2 andβ5 are associated with poor prognosis in prostate cancer and promote cancer cell migration and invasion. Endocr. Relat. Cancer 17, 675-689
    • (2010) Endocr. Relat. Cancer , vol.17 , pp. 675-689
    • Leung, Y.K.1    Lam, H.M.2    Wu, S.3    Song, D.4    Levin, L.5    Cheng, L.6    Wu, C.L.7    Ho, S.M.8
  • 34
    • 33646437486 scopus 로고    scopus 로고
    • ICI 182,780-regulated gene expression in DU145 prostate cancer cells is mediated by estrogen receptor-β/NFκB crosstalk
    • Leung, Y. K., Gao, Y., Lau, K. M., Zhang, X., and Ho, S. M. (2006) ICI 182,780-regulated gene expression in DU145 prostate cancer cells is mediated by estrogen receptor-β/NFκB crosstalk. Neoplasia 8, 242-249
    • (2006) Neoplasia , vol.8 , pp. 242-249
    • Leung, Y.K.1    Gao, Y.2    Lau, K.M.3    Zhang, X.4    Ho, S.M.5
  • 35
  • 37
    • 1542299148 scopus 로고    scopus 로고
    • Effects of environmental estrogenic chemicals on AP1-mediated transcription with estrogen receptors α and β
    • Fujimoto, N., Honda, H., and Kitamura, S. (2004) Effects of environmental estrogenic chemicals on AP1-mediated transcription with estrogen receptors α and β. J. Steroid Biochem. Mol. Biol. 88, 53-59
    • (2004) J. Steroid Biochem. Mol. Biol , vol.88 , pp. 53-59
    • Fujimoto, N.1    Honda, H.2    Kitamura, S.3
  • 38
    • 24944516931 scopus 로고    scopus 로고
    • A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM
    • Sun, Y., Jiang, X., Chen, S., Fernandes, N., and Price, B. D. (2005) A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc. Natl. Acad. Sci. U.S.A. 102, 13182-13187
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 13182-13187
    • Sun, Y.1    Jiang, X.2    Chen, S.3    Fernandes, N.4    Price, B.D.5
  • 39
    • 33746581782 scopus 로고    scopus 로고
    • Inhibition of histone acetyltransferase activity by anacardic acid sensitizes tumor cells to ionizing radiation
    • Sun, Y., Jiang, X., Chen, S., and Price, B. D. (2006) Inhibition of histone acetyltransferase activity by anacardic acid sensitizes tumor cells to ionizing radiation. FEBS Lett. 580, 4353-4356
    • (2006) FEBS Lett , vol.580 , pp. 4353-4356
    • Sun, Y.1    Jiang, X.2    Chen, S.3    Price, B.D.4
  • 40
    • 14744303696 scopus 로고    scopus 로고
    • Expanding functional diversity of the coactivators
    • Lonard, D. M., and O'Malley, B. W. (2005) Expanding functional diversity of the coactivators. Trends Biochem. Sci. 30, 126-132
    • (2005) Trends Biochem. Sci , vol.30 , pp. 126-132
    • Lonard, D.M.1    O'Malley, B.W.2
  • 41
  • 42
    • 69249110003 scopus 로고    scopus 로고
    • Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family
    • Xu, J., Wu, R. C., and O'Malley, B. W. (2009) Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family. Nat. Rev. Cancer 9, 615-630
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 615-630
    • Xu, J.1    Wu, R.C.2    O'Malley, B.W.3
  • 44
    • 54749136212 scopus 로고    scopus 로고
    • Nkx3-1 and LEF-1 function as transcriptional inhibitors of estrogen receptor activity
    • Holmes, K. A., Song, J. S., Liu, X. S., Brown, M., and Carroll, J. S. (2008) Nkx3-1 and LEF-1 function as transcriptional inhibitors of estrogen receptor activity. Cancer Res. 68, 7380-7385
    • (2008) Cancer Res , vol.68 , pp. 7380-7385
    • Holmes, K.A.1    Song, J.S.2    Liu, X.S.3    Brown, M.4    Carroll, J.S.5
  • 47
    • 33644550627 scopus 로고    scopus 로고
    • Estrogen receptor (ER)β modulates ERα-mediated transcriptional activation by altering the recruitment of c-Fos and c-Jun to estrogen- responsive promoters
    • Matthews, J., Wihlén, B., Tujague, M., Wan, J., Ström, A., and Gustafsson, J. A. (2006) Estrogen receptor (ER)β modulates ERα-mediated transcriptional activation by altering the recruitment of c-Fos and c-Jun to estrogen- responsive promoters. Mol. Endocrinol. 20, 534-543
    • (2006) Mol. Endocrinol , vol.20 , pp. 534-543
    • Matthews, J.1    Wihlén, B.2    Tujague, M.3    Wan, J.4    Ström, A.5    Gustafsson, J.A.6
  • 48
    • 0033120030 scopus 로고    scopus 로고
    • Ligandindependent recruitment of SRC-1 to estrogen receptor β through phosphorylation of activation function AF-1
    • Tremblay, A., Tremblay, G. B., Labrie, F., and Giguère, V. (1999) Ligandindependent 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
  • 49
    • 38949182981 scopus 로고    scopus 로고
    • A genome-wide study of the repressive effects of estrogen receptor β on estrogen receptor α signaling in breast cancer cells
    • Williams, C., Edvardsson, K., Lewandowski, S. A., Ström, A., and Gustafsson, J. A. (2008) A genome-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
  • 51
    • 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, T. A., Richer, J. K., Bain, D. L., Takimoto, G. S., Tung, L., and Horwitz, K. B. (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
  • 52
    • 0034717075 scopus 로고    scopus 로고
    • Modulation of estrogen receptor-α transcriptional activity by the coactivator PGC-1
    • Tcherepanova, I., Puigserver, P., Norris, J. D., Spiegelman, B. M., and Mc-Donnell, D. P. (2000) Modulation of estrogen receptor-α transcriptional activity by the coactivator PGC-1. J. Biol. Chem. 275, 16302-16308
    • (2000) J. Biol. Chem , vol.275 , pp. 16302-16308
    • Tcherepanova, I.1    Puigserver, P.2    Norris, J.D.3    Spiegelman, B.M.4    Mc-Donnell, D.P.5
  • 53
    • 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 CREBbinding protein
    • Sanchez, M., Sauvé, K., Picard, N., and 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 CREBbinding 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
  • 54
    • 84871977882 scopus 로고    scopus 로고
    • Coordinate regulation of estrogen receptor β degradation by Mdm2 and CREB-binding protein in response to growth signals
    • Sanchez, M., Picard, N., Sauvé, K., and Tremblay, A. (2013) Coordinate regulation of estrogen receptor β degradation by Mdm2 and CREB-binding protein in response to growth signals. Oncogene 32, 117-126
    • (2013) Oncogene , vol.32 , pp. 117-126
    • Sanchez, M.1    Picard, N.2    Sauvé, K.3    Tremblay, A.4
  • 55
    • 79953300720 scopus 로고    scopus 로고
    • Selective mutations in estrogen receptorα D-domain alters nuclear translocation and non-estrogen-response element gene regulatory mechanisms
    • Burns, K. A., Li, Y., Arao, Y., Petrovich, R. M., and Korach, K. S. (2011) Selective mutations in estrogen receptorα D-domain alters nuclear translocation and non-estrogen-response element gene regulatory mechanisms. J. Biol. Chem. 286, 12640-12649
    • (2011) J. Biol. Chem , vol.286 , pp. 12640-12649
    • Burns, K.A.1    Li, Y.2    Arao, Y.3    Petrovich, R.M.4    Korach, K.S.5
  • 56
    • 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, M. A., and 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
  • 58
    • 32444436779 scopus 로고    scopus 로고
    • Distinct roles of unliganded and liganded estrogen receptors in transcriptional repression
    • Cvoro, A., Tzagarakis-Foster, C., Tatomer, D., Paruthiyil, S., Fox, M. S., and Leitman, D. C. (2006) Distinct roles of unliganded and liganded estrogen receptors in transcriptional repression. Mol. Cell 21, 555-564
    • (2006) Mol. Cell , vol.21 , pp. 555-564
    • Cvoro, A.1    Tzagarakis-Foster, C.2    Tatomer, D.3    Paruthiyil, S.4    Fox, M.S.5    Leitman, D.C.6
  • 59
    • 0037168648 scopus 로고    scopus 로고
    • Alternate surfaces of transcriptional coregulator GRIP1 function in different glucocorticoid receptor activation and repression contexts
    • Rogatsky, I., Luecke, H. F., Leitman, D. C., and Yamamoto, K. R. (2002) Alternate surfaces of transcriptional coregulator GRIP1 function in different glucocorticoid receptor activation and repression contexts. Proc. Natl. Acad. Sci. U.S.A. 99, 16701-16706
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16701-16706
    • Rogatsky, I.1    Luecke, H.F.2    Leitman, D.C.3    Yamamoto, K.R.4
  • 60
    • 24144496829 scopus 로고    scopus 로고
    • Phytoestrogens induce differential estrogen receptor α- Or β-mediated responses in transfected breast cancer cells
    • Harris, D. M., Besselink, E., Henning, S. M., Go, V. L., and Heber, D. (2005) Phytoestrogens induce differential estrogen receptor α- or β-mediated responses in transfected breast cancer cells. Exp. Biol. Med. 230, 558-568
    • (2005) Exp. Biol. Med , vol.230 , pp. 558-568
    • Harris, D.M.1    Besselink, E.2    Henning, S.M.3    Go, V.L.4    Heber, D.5
  • 62
    • 0033762869 scopus 로고    scopus 로고
    • Interactions of dietary estrogens with human estrogen receptors and the effect on estrogen receptor-estrogen-response element complex formation
    • Nikov, G. N., Hopkins, N. E., Boue, S., and Alworth, W. L. (2000) Interactions of dietary estrogens with human estrogen receptors and the effect on estrogen receptor-estrogen-response element complex formation. Environ. Health Perspect. 108, 867-872
    • (2000) Environ. Health Perspect , vol.108 , pp. 867-872
    • Nikov, G.N.1    Hopkins, N.E.2    Boue, S.3    Alworth, W.L.4
  • 64
    • 3242798960 scopus 로고    scopus 로고
    • Phytoestrogens and their human metabolites show distinct agonistic and antagonistic properties on estrogen receptor α (ERα) and ERβ in human cells
    • Mueller, S. O., Simon, S., Chae, K., Metzler, M., and Korach, K. S. (2004) Phytoestrogens and their human metabolites show distinct agonistic and antagonistic properties on estrogen receptor α (ERα) and ERβ in human cells. Toxicol. Sci. 80, 14-25
    • (2004) Toxicol. Sci , vol.80 , pp. 14-25
    • Mueller, S.O.1    Simon, S.2    Chae, K.3    Metzler, M.4    Korach, K.S.5
  • 65
    • 0034680924 scopus 로고    scopus 로고
    • Differential effects of xenoestrogens on coactivator recruitment by estrogen receptor (ER) α and ERβ
    • Routledge, E. J., White, R., Parker, M. G., and Sumpter, J. P. (2000) Differential effects of xenoestrogens on coactivator recruitment by estrogen receptor (ER) α and ERβ. J. Biol. Chem. 275, 35986-35993
    • (2000) J. Biol. Chem , vol.275 , pp. 35986-35993
    • Routledge, E.J.1    White, R.2    Parker, M.G.3    Sumpter, J.P.4
  • 66
    • 4344679375 scopus 로고    scopus 로고
    • Estrogen receptor-dependent activation of AP-1 via non-genomic signalling
    • Björnström, L., and Sjöberg, M. (2004) Estrogen receptor-dependent activation of AP-1 via non-genomic signalling. Nucl. Recept. 2, 33
    • (2004) Nucl. Recept , vol.2 , pp. 33
    • Björnström, L.1    Sjöberg, M.2
  • 69
    • 33745632097 scopus 로고    scopus 로고
    • A second binding site for hydroxytamoxifen within the coactivator- binding groove of estrogen receptor β
    • Wang, Y., Chirgadze, N. Y., Briggs, S. L., Khan, S., Jensen, E. V., and Burris, T. P. (2006) A second binding site for hydroxytamoxifen within the coactivator- binding groove of estrogen receptor β. Proc. Natl. Acad. Sci. U.S.A. 103, 9908-9911
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9908-9911
    • Wang, Y.1    Chirgadze, N.Y.2    Briggs, S.L.3    Khan, S.4    Jensen, E.V.5    Burris, T.P.6
  • 70
    • 84883414730 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 71
    • 77951217683 scopus 로고    scopus 로고
    • SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60
    • Wang, J., and Chen, J. (2010) SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60. J. Biol. Chem. 285, 11458-11464
    • (2010) J. Biol. Chem , vol.285 , pp. 11458-11464
    • Wang, J.1    Chen, J.2
  • 72
    • 84859045769 scopus 로고    scopus 로고
    • Function of the active site lysine autoacetylation in Tip60 catalysis
    • Yang, C., Wu, J., and Zheng, Y. G. (2012) Function of the active site lysine autoacetylation in Tip60 catalysis. PLoS One 7, e32886
    • (2012) PLoS One , vol.7
    • Yang, C.1    Wu, J.2    Zheng, Y.G.3
  • 73
    • 33744534726 scopus 로고    scopus 로고
    • GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1α
    • Lerin, C., Rodgers, J. T., Kalume, D. E., Kim, S. H., Pandey, A., and Puigserver, P. (2006) GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1α. Cell Metab. 3, 429-438
    • (2006) Cell Metab , vol.3 , pp. 429-438
    • Lerin, C.1    Rodgers, J.T.2    Kalume, D.E.3    Kim, S.H.4    Pandey, A.5    Puigserver, P.6
  • 75
    • 0032479304 scopus 로고    scopus 로고
    • Steroid receptor coactivator-1 coactivates activating protein- 1-mediated transactivations through interaction with the c-Jun and c-Fos subunits
    • Lee, S. K., Kim, H. J., Na, S. Y., Kim, T. S., Choi, H. S., Im, S. Y., and Lee, J. W. (1998) Steroid receptor coactivator-1 coactivates activating protein- 1-mediated transactivations through interaction with the c-Jun and c-Fos subunits. J. Biol. Chem. 273, 16651-16654
    • (1998) J. Biol. Chem , vol.273 , pp. 16651-16654
    • Lee, S.K.1    Kim, H.J.2    Na, S.Y.3    Kim, T.S.4    Choi, H.S.5    Im, S.Y.6    Lee, J.W.7
  • 76
    • 67651005771 scopus 로고    scopus 로고
    • Positive feedback activation of estrogen receptors by the CXCL12-CXCR4 pathway
    • Sauvé, K., Lepage, J., Sanchez, M., Heveker, N., and 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
  • 77
    • 33748087796 scopus 로고    scopus 로고
    • Coregulation of estrogen receptor by ERBB4/HER4 establishes a growth-promoting autocrine signal in breast tumor cells
    • Zhu, Y., Sullivan, L. L., Nair, S. S., Williams, C. C., Pandey, A. K., Marrero, L., Vadlamudi, R. K., and Jones, F. E. (2006) Coregulation of estrogen receptor by ERBB4/HER4 establishes a growth-promoting autocrine signal in breast tumor cells. Cancer Res. 66, 7991-7998
    • (2006) Cancer Res , vol.66 , pp. 7991-7998
    • Zhu, Y.1    Sullivan, L.L.2    Nair, S.S.3    Williams, C.C.4    Pandey, A.K.5    Marrero, L.6    Vadlamudi, R.K.7    Jones, F.E.8


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