메뉴 건너뛰기




Volumn 75, Issue , 2013, Pages 225-240

Estrogen and cancer

Author keywords

Breast cancer; Endocrine resistance; Estrogen receptor; Tamoxifen

Indexed keywords

ANASTROZOLE; ANTIESTROGEN; AROMATASE INHIBITOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; ESTROGEN; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; EXEMESTANE; FULVESTRANT; HISTONE DEACETYLASE INHIBITOR; LETROZOLE; MITOGEN ACTIVATED PROTEIN KINASE; RALOXIFENE; SELECTIVE ESTROGEN RECEPTOR MODULATOR; TAMOXIFEN; TOREMIFENE;

EID: 84873675307     PISSN: 00664278     EISSN: 15451585     Source Type: Book Series    
DOI: 10.1146/annurev-physiol-030212-183708     Document Type: Review
Times cited : (249)

References (89)
  • 1
    • 82355188243 scopus 로고    scopus 로고
    • Minireview: Putting physiology back into estrogens' mechanism of action
    • Koos RD. 2011. Minireview: putting physiology back into estrogens' mechanism of action. Endocrinology 152:4481-88
    • (2011) Endocrinology , vol.152 , pp. 4481-4488
    • Koos, R.D.1
  • 2
    • 33646371740 scopus 로고    scopus 로고
    • Molecular mechanisms of oestrogen and SERMs in endometrial carcinogenesis
    • Shang Y. 2006. Molecular mechanisms of oestrogen and SERMs in endometrial carcinogenesis. Nat. Rev. Cancer 6:360-68
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 360-368
    • Shang, Y.1
  • 3
    • 34247378586 scopus 로고    scopus 로고
    • Hormones and cancer
    • Shang Y. 2007. Hormones and cancer. Cell Res. 17:277-79
    • (2007) Cell Res. , vol.17 , pp. 277-279
    • Shang, Y.1
  • 5
    • 84856700317 scopus 로고    scopus 로고
    • Human steroid biosynthesis for the oncologist
    • Auchus ML, Auchus RJ. 2012. Human steroid biosynthesis for the oncologist. J. Investig. Med. 60:495-503
    • (2012) J. Investig. Med. , vol.60 , pp. 495-503
    • Auchus, M.L.1    Auchus, R.J.2
  • 6
    • 79951665862 scopus 로고    scopus 로고
    • The molecular biology, biochemistry, and physiology of human steroido-genesis and its disorders
    • Miller WL, Auchus RJ. 2011. The molecular biology, biochemistry, and physiology of human steroido-genesis and its disorders. Endocr. Rev. 32:81-151
    • (2011) Endocr. Rev. , vol.32 , pp. 81-151
    • Miller, W.L.1    Auchus, R.J.2
  • 8
    • 0035464108 scopus 로고    scopus 로고
    • Aromatase, aromatase inhibitors, and breast cancer
    • Brueggemeier RW. 2001. Aromatase, aromatase inhibitors, and breast cancer. Am. J. Ther. 8:333-44
    • (2001) Am. J. Ther. , vol.8 , pp. 333-344
    • Brueggemeier, R.W.1
  • 9
    • 66649098171 scopus 로고    scopus 로고
    • Minireview: Obesity and breast cancer: The estrogen connection
    • Cleary MP, Grossmann ME. 2009. Minireview: obesity and breast cancer: the estrogen connection. Endocrinology 150:2537-42
    • (2009) Endocrinology , vol.150 , pp. 2537-2542
    • Cleary, M.P.1    Grossmann, M.E.2
  • 10
    • 78650014370 scopus 로고    scopus 로고
    • Role of estrogen in normal male function: Clinical implications for patients with prostate cancer on androgen deprivation therapy
    • Wibowo E, Schellhammer P, Wassersug RJ. 2011. Role of estrogen in normal male function: clinical implications for patients with prostate cancer on androgen deprivation therapy. J. Urol. 185:17-23
    • (2011) J. Urol. , vol.185 , pp. 17-23
    • Wibowo, E.1    Schellhammer, P.2    Wassersug, R.J.3
  • 11
    • 77956944344 scopus 로고    scopus 로고
    • Influence of sex hormones on cancer progression
    • Folkerd EJ, Dowsett M. 2010. Influence of sex hormones on cancer progression. J. Clin. Oncol. 28:4038-44
    • (2010) J. Clin. Oncol. , vol.28 , pp. 4038-4044
    • Folkerd, E.J.1    Dowsett, M.2
  • 12
    • 72649087326 scopus 로고    scopus 로고
    • Estrogen action: A historic perspective on the implications of considering alternative approaches
    • Jensen EV, Jacobson HI, Walf AA, Frye CA. 2010. Estrogen action: a historic perspective on the implications of considering alternative approaches. Physiol. Behav. 99:151-62
    • (2010) Physiol. Behav. , vol.99 , pp. 151-162
    • Jensen, E.V.1    Jacobson, H.I.2    Walf, A.A.3    Frye, C.A.4
  • 13
    • 34447523339 scopus 로고    scopus 로고
    • Estrogen receptors: How do they signal and what are their targets
    • Heldring N, Pike A, Andersson S, Matthews J, Cheng G, et al. 2007. Estrogen receptors: How do they signal and what are their targets. Physiol. Rev. 87:905-31
    • (2007) Physiol. Rev. , vol.87 , pp. 905-931
    • Heldring, N.1    Pike, A.2    Andersson, S.3    Matthews, J.4    Cheng, G.5
  • 14
    • 15444368857 scopus 로고    scopus 로고
    • Mechanisms of estrogen receptor signaling: Convergence of genomic and nongenomic actions on target genes
    • Bjornstrom L, Sjoberg M. 2005. Mechanisms of estrogen receptor signaling: convergence of genomic and nongenomic actions on target genes. Mol. Endocrinol. 19:833-42
    • (2005) Mol. Endocrinol. , vol.19 , pp. 833-842
    • Bjornstrom, L.1    Sjoberg, M.2
  • 15
    • 82355163442 scopus 로고    scopus 로고
    • Minireview: Recent advances in extranuclear steroid receptor actions
    • Hammes SR, Levin ER. 2011. Minireview: recent advances in extranuclear steroid receptor actions. Endocrinology 152:4489-95
    • (2011) Endocrinology , vol.152 , pp. 4489-4495
    • Hammes, S.R.1    Levin, E.R.2
  • 16
    • 79960832381 scopus 로고    scopus 로고
    • The different roles of ER subtypes in cancer biology and therapy
    • Thomas C, Gustafsson JA. 2011. The different roles of ER subtypes in cancer biology and therapy. Nat. Rev. Cancer 11:597-608
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 597-608
    • Thomas, C.1    Gustafsson, J.A.2
  • 17
    • 80053562371 scopus 로고    scopus 로고
    • Development of subtype-selective oestrogen receptor-based therapeutics
    • Nilsson S, Koehler KF, Gustafsson JA. 2011. Development of subtype-selective oestrogen receptor-based therapeutics. Nat. Rev. Drug Discov. 10:778-92
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 778-792
    • Nilsson, S.1    Koehler, K.F.2    Gustafsson, J.A.3
  • 19
    • 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 9:631-43
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 631-643
    • Musgrove, E.A.1    Sutherland, R.L.2
  • 20
    • 0842334473 scopus 로고    scopus 로고
    • /-diindolylmethane is mediated by cross talk between the protein kinase A and mitogen-activated protein kinase signaling pathways
    • /- diindolylmethane is mediated by cross talk between the protein kinase A and mitogen-activated protein kinase signaling pathways. Mol. Endocrinol. 18:291-302
    • (2004) Mol. Endocrinol. , vol.18 , pp. 291-302
    • Leong, H.1    Riby, J.E.2    Firestone, G.L.3    Bjeldanes, L.F.4
  • 21
    • 77955629953 scopus 로고    scopus 로고
    • Genome-wide analysis of estrogen receptor ex DNA binding and tethering mechanisms identifies Runx1 as a novel tethering factor in receptor-mediated transcriptional activation
    • Stender JD, Kim K, Charn TH, Komm B, Chang KC, et al. 2010. Genome-wide analysis of estrogen receptor ex DNA binding and tethering mechanisms identifies Runx1 as a novel tethering factor in receptor-mediated transcriptional activation. Mol. Cell. Biol. 30:3943-55
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3943-3955
    • Stender, J.D.1    Kim, K.2    Charn, T.H.3    Komm, B.4    Chang, K.C.5
  • 22
    • 77950598697 scopus 로고    scopus 로고
    • Estrogens, regulation of p53 and breast cancer risk: A balancing act
    • Jerry DJ, Dunphy KA, Hagen MJ. 2010. Estrogens, regulation of p53 and breast cancer risk: a balancing act. Cell. Mol. Life Sci. 67:1017-23
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 1017-1023
    • Jerry, D.J.1    Dunphy, K.A.2    Hagen, M.J.3
  • 23
    • 0033767836 scopus 로고    scopus 로고
    • Effect of single and compound knockouts of estrogen receptors cx(ERcx) and |3 (ER|3) on mouse reproductive phenotypes
    • Dupont S, Krust A, Gansmuller A, Dierich A, Chambon P, Mark M. 2000. Effect of single and compound knockouts of estrogen receptors cx(ERcx) and |3 (ER|3) on mouse reproductive phenotypes. Development 127:4277-91
    • (2000) Development , vol.127 , pp. 4277-4291
    • Dupont, S.1    Krust, A.2    Gansmuller, A.3    Dierich, A.4    Chambon, P.5    Mark, M.6
  • 25
    • 0345382876 scopus 로고    scopus 로고
    • Involvement of estrogen receptor |3 in terminal differentiation of mammary gland epithelium
    • Forster C, Makela S, Warri A, Kietz S, Becker D, et al. 2002. Involvement of estrogen receptor |3 in terminal differentiation of mammary gland epithelium. Proc. Natl. Acad. Sci. USA 99:15578-83
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15578-15583
    • Forster, C.1    Makela, S.2    Warri, A.3    Kietz, S.4    Becker, D.5
  • 26
    • 40649084350 scopus 로고    scopus 로고
    • Sterility and absence of histopathological defects in nonreproductive organs of a mouse ER|3-null mutant
    • Antal MC, Krust A, Chambon P, Mark M. 2008. Sterility and absence of histopathological defects in nonreproductive organs of a mouse ER|3-null mutant. Proc. Natl. Acad. Sci. USA 105:2433-38
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2433-2438
    • Antal, M.C.1    Krust, A.2    Chambon, P.3    Mark, M.4
  • 27
    • 25644437706 scopus 로고    scopus 로고
    • Identification, cloning, and expression of human estrogen receptor-cx36, a novel variant of human estrogen receptor-cx66
    • Wang Z, Zhang X, Shen P, Loggie BW, Chang Y, Deuel TF. 2005. Identification, cloning, and expression of human estrogen receptor-cx36, a novel variant of human estrogen receptor-cx66. Biochem. Biophys. Res. Commun. 336:1023-27
    • (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
  • 28
    • 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. 25:5815-24
    • (2007) J. Clin. Oncol. , vol.25 , pp. 5815-5824
    • Jordan, V.C.1    O'Malley, B.W.2
  • 29
    • 34147112806 scopus 로고    scopus 로고
    • Regulation of SRC family coactivators by post-translational modifications
    • Li S, Shang Y. 2007. Regulation of SRC family coactivators by post-translational modifications. Cell. Signal. 19:1101-12
    • (2007) Cell. Signal. , vol.19 , pp. 1101-1112
    • Li, S.1    Shang, Y.2
  • 30
    • 0030768745 scopus 로고    scopus 로고
    • Steroid receptor coactivator-1 is a histone acetyltransferase
    • Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, et al. 1997. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389:194-98
    • (1997) Nature , vol.389 , pp. 194-198
    • Spencer, T.E.1    Jenster, G.2    Burcin, M.M.3    Allis, C.D.4    Zhou, J.5
  • 31
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, et al. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569-80
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5
  • 32
    • 58049093386 scopus 로고    scopus 로고
    • GAS, a new glutamate-rich protein, interacts differentially with SRCs and is involved in oestrogen receptor function
    • Liang J, Zhang H, Zhang Y, Zhang Y, Shang Y. 2009. GAS, a new glutamate-rich protein, interacts differentially with SRCs and is involved in oestrogen receptor function. EMBO Rep. 10:51-57
    • (2009) EMBO Rep. , vol.10 , pp. 51-57
    • Liang, J.1    Zhang, H.2    Zhang, Y.3    Zhang, Y.4    Shang, Y.5
  • 33
    • 2542501575 scopus 로고    scopus 로고
    • Protein kinase A activation of estrogen receptor ex 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 ex transcription does not require proteasome activity and protects the receptor from ligand-mediated degradation. Endocrinology 145:2730-38
    • (2004) Endocrinology , vol.145 , pp. 2730-2738
    • Tsai, H.W.1    Katzenellenbogen, J.A.2    Katzenellenbogen, B.S.3    Shupnik, M.A.4
  • 34
    • 0029877913 scopus 로고    scopus 로고
    • Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation
    • Bunone G, Briand PA, Miksicek RJ, Picard D. 1996. Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. EMBO J. 15:2174-83
    • (1996) EMBO J. , vol.15 , pp. 2174-2183
    • Bunone, G.1    Briand, P.A.2    Miksicek, R.J.3    Picard, D.4
  • 35
    • 0242637101 scopus 로고    scopus 로고
    • Direct acetylation of the estrogen receptor ex hinge region by p300 regulates transactivation and hormone sensitivity
    • Wang C, Fu M, Angeletti RH, Siconolfi-Baez L, Reutens AT, et al. 2001. Direct acetylation of the estrogen receptor ex hinge region by p300 regulates transactivation and hormone sensitivity. J. Biol. Chem. 276:18375-83
    • (2001) J. Biol. Chem. , vol.276 , pp. 18375-18383
    • Wang, C.1    Fu, M.2    Angeletti, R.H.3    Siconolfi-Baez, L.4    Reutens, A.T.5
  • 36
    • 46349108800 scopus 로고    scopus 로고
    • Estrogen receptor-tx hinge-region lysines 302 and 303 regulate receptor degradation by the proteasome
    • Berry NB, Fan M, Nephew KP. 2008. Estrogen receptor-tx hinge-region lysines 302 and 303 regulate receptor degradation by the proteasome. Mol. Endocrinol. 22:1535-51
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1535-1551
    • Berry, N.B.1    Fan, M.2    Nephew, K.P.3
  • 38
    • 0033603396 scopus 로고    scopus 로고
    • Regulation of transcription by a protein methyltransferase
    • Chen D, Ma H, Hong H, Koh SS, Huang SM, et al. 1999. Regulation of transcription by a protein methyltransferase. Science 284:2174-77
    • (1999) Science , vol.284 , pp. 2174-2177
    • Chen, D.1    Ma, H.2    Hong, H.3    Koh, S.S.4    Huang, S.M.5
  • 39
    • 0035873803 scopus 로고    scopus 로고
    • Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
    • Schurter BT, Koh SS, Chen D, Bunick GJ, Harp JM, et al. 2001. Methylation of histone H3 by coactivator-associated arginine methyltransferase 1. Biochemistry 40:5747-56
    • (2001) Biochemistry , vol.40 , pp. 5747-5756
    • Schurter, B.T.1    Koh, S.S.2    Chen, D.3    Bunick, G.J.4    Harp, J.M.5
  • 40
    • 0037107417 scopus 로고    scopus 로고
    • Control of CBP co-activating activity by arginine methylation
    • Chevillard-Briet M, Trouche D, Vandel L. 2002. Control of CBP co-activating activity by arginine methylation. EMBO J. 21:5457-66
    • (2002) EMBO J. , vol.21 , pp. 5457-5466
    • Chevillard-Briet, M.1    Trouche, D.2    Vandel, L.3
  • 41
    • 33845789120 scopus 로고    scopus 로고
    • The activity and stability of the tran-scriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation
    • Naeem H, Cheng D, Zhao Q, Underhill C, Tini M, et al. 2007. The activity and stability of the tran-scriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation. Mol. Cell. Biol. 27:120-34
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 120-134
    • Naeem, H.1    Cheng, D.2    Zhao, Q.3    Underhill, C.4    Tini, M.5
  • 42
    • 79953288782 scopus 로고    scopus 로고
    • The C-terminal domain of RNA polymerase II is modified by site-specific methylation
    • Sims RJ 3rd, Rojas LA, Beck D, Bonasio R, Schuller R, et al. 2011. The C-terminal domain of RNA polymerase II is modified by site-specific methylation. Science 332:99-103
    • (2011) Science , vol.332 , pp. 99-103
    • Sims III, R.J.1    Rojas, L.A.2    Beck, D.3    Bonasio, R.4    Schuller, R.5
  • 43
    • 77950470137 scopus 로고    scopus 로고
    • CARM1 mediates the ligand-independent and tamoxifen-resistant activation of the estrogen receptor αby cAMP
    • Carascossa S, Dudek P, Cenni B, Briand PA, Picard D. 2010. CARM1 mediates the ligand-independent and tamoxifen-resistant activation of the estrogen receptor αby cAMP. Genes Dev. 24:708-19
    • (2010) Genes Dev. , vol.24 , pp. 708-719
    • Carascossa, S.1    Dudek, P.2    Cenni, B.3    Briand, P.A.4    Picard, D.5
  • 44
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang Y, Hu X, DiRenzo J, Lazar MA, Brown M. 2000. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103:843-52
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    Direnzo, J.3    Lazar, M.A.4    Brown, M.5
  • 46
    • 22144486551 scopus 로고    scopus 로고
    • Chromosome-wide mapping of estrogen receptor binding reveals long-range regulation requiring the forkhead protein FoxA1
    • Carroll JS, Liu XS, Brodsky AS, Li W, Meyer CA, et al. 2005. Chromosome-wide mapping of estrogen receptor binding reveals long-range regulation requiring the forkhead protein FoxA1. Cell 122:33-43
    • (2005) Cell , vol.122 , pp. 33-43
    • Carroll, J.S.1    Liu, X.S.2    Brodsky, A.S.3    Li, W.4    Meyer, C.A.5
  • 47
    • 70449103609 scopus 로고    scopus 로고
    • An oestrogen-receptor-α-bound human chro-matin interactome
    • Fullwood MJ, Liu MH, Pan YF, Liu J, Xu H, et al. 2009. An oestrogen-receptor-α-bound human chro-matin interactome. Nature 462:58-64
    • (2009) Nature , vol.462 , pp. 58-64
    • Fullwood, M.J.1    Liu, M.H.2    Pan, Y.F.3    Liu, J.4    Xu, H.5
  • 48
    • 73349143638 scopus 로고    scopus 로고
    • Microarray analysis of altered gene expression in ERβ-overexpressing HEK293 cells
    • Zhao C, Putnik M, Gustafsson J-A, Dahlman-Wright K. 2009. Microarray analysis of altered gene expression in ERβ-overexpressing HEK293 cells. Endocrine 36:224-32
    • (2009) Endocrine , vol.36 , pp. 224-232
    • Zhao, C.1    Putnik, M.2    Gustafsson, J.-A.3    Dahlman-Wright, K.4
  • 50
    • 77953626325 scopus 로고    scopus 로고
    • Cell cycle proteins in epithelial cell differentiation: Implications for breast cancer
    • Caldon CE, Sutherland RL, Musgrove E. 2010. Cell cycle proteins in epithelial cell differentiation: implications for breast cancer. Cell Cycle 9:1918-28
    • (2010) Cell Cycle , vol.9 , pp. 1918-1928
    • Caldon, C.E.1    Sutherland, R.L.2    Musgrove, E.3
  • 51
    • 25844515780 scopus 로고    scopus 로고
    • Downstream targets of growth factor and oestrogen signalling and endocrine resistance: The potential roles of c-Myc, cyclin D1 and cyclin e
    • Butt AJ, McNeil CM, Musgrove EA, Sutherland RL. 2005. Downstream targets of growth factor and oestrogen signalling and endocrine resistance: the potential roles of c-Myc, cyclin D1 and cyclin E. Endocr. Relat. Cancer 12(Suppl. 1):47-59
    • (2005) Endocr. Relat. Cancer , vol.12 , Issue.SUPPL. 1 , pp. 47-59
    • Butt, A.J.1    McNeil, C.M.2    Musgrove, E.A.3    Sutherland, R.L.4
  • 52
    • 80052290466 scopus 로고    scopus 로고
    • Estrogen induces c-myc gene expression via an upstream enhancer activated by the estrogen receptor and the AP-1 transcription factor
    • Wang C, Mayer JA, Mazumdar A, Fertuck K, Kim H, et al. 2011. Estrogen induces c-myc gene expression via an upstream enhancer activated by the estrogen receptor and the AP-1 transcription factor. Mol. Endocrinol. 25:1527-38
    • (2011) Mol. Endocrinol. , vol.25 , pp. 1527-1538
    • Wang, C.1    Mayer, J.A.2    Mazumdar, A.3    Fertuck, K.4    Kim, H.5
  • 55
    • 82755168809 scopus 로고    scopus 로고
    • Estrogen induces apopto-sis in estrogen deprivation-resistant breast cancer through stress responses as identified by global gene expression across time
    • Ariazi EA, Cunliffe HE, Lewis-Wambi JS, Slifker MJ, Willis AL, et al. 2011. Estrogen induces apopto-sis in estrogen deprivation-resistant breast cancer through stress responses as identified by global gene expression across time. Proc. Natl. Acad. Sci. USA 108:18879-86
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 18879-18886
    • Ariazi, E.A.1    Cunliffe, H.E.2    Lewis-Wambi, J.S.3    Slifker, M.J.4    Willis, A.L.5
  • 56
    • 74049104166 scopus 로고    scopus 로고
    • Estrogen regulation of apoptosis: How can one hormone stimulate and inhibit?
    • Lewis-Wambi JS, Jordan VC. 2009. Estrogen regulation of apoptosis: How can one hormone stimulate and inhibit? Breast Cancer Res. 11:206
    • (2009) Breast Cancer Res. , vol.11 , pp. 206
    • Lewis-Wambi, J.S.1    Jordan, V.C.2
  • 58
    • 46949109892 scopus 로고    scopus 로고
    • Vascular actions of estrogens: Functional implications
    • Miller VM, Duckles SP. 2008. Vascular actions of estrogens: functional implications. Pharmacol. Rev. 60:210-41
    • (2008) Pharmacol. Rev. , vol.60 , pp. 210-241
    • Miller, V.M.1    Duckles, S.P.2
  • 59
    • 59849090487 scopus 로고    scopus 로고
    • Estradiol increases IL-8 secretion of normal human breast tissue and breast cancer in vivo
    • Bendrik C, Dabrosin C. 2009. Estradiol increases IL-8 secretion of normal human breast tissue and breast cancer in vivo. J. Immunol. 182:371-78
    • (2009) J. Immunol. , vol.182 , pp. 371-378
    • Bendrik, C.1    Dabrosin, C.2
  • 60
    • 78651398665 scopus 로고    scopus 로고
    • Tamoxifen, flaxseed, and the lignan entero-lactone increase stroma-and cancer cell-derived IL-1Ra and decrease tumor angiogenesis in estrogen-dependent breast cancer
    • Lindahl G, Saarinen N, Abrahamsson A, Dabrosin C. 2012. Tamoxifen, flaxseed, and the lignan entero-lactone increase stroma-and cancer cell-derived IL-1Ra and decrease tumor angiogenesis in estrogen-dependent breast cancer. Cancer Res. 71:51-60
    • (2012) Cancer Res. , vol.71 , pp. 51-60
    • Lindahl, G.1    Saarinen, N.2    Abrahamsson, A.3    Dabrosin, C.4
  • 61
    • 78149343486 scopus 로고    scopus 로고
    • Loss of ERαand FOXA1 expression in a progression model of luminal type breast cancer: Insights from PyMT transgenic mouse model
    • McCune K, Mehta R, Thorat MA, Badve S, Nakshatri H. 2010. Loss of ERαand FOXA1 expression in a progression model of luminal type breast cancer: insights from PyMT transgenic mouse model. Oncol. Rep. 24:1233-39
    • (2010) Oncol. Rep. , vol.24 , pp. 1233-1239
    • McCune, K.1    Mehta, R.2    Thorat, M.A.3    Badve, S.4    Nakshatri, H.5
  • 62
    • 34047095373 scopus 로고    scopus 로고
    • Oestrogen signalling inhibits invasive phenotype by repressing RelB and its target BCL2
    • Wang X, Belguise K, Kersual N, Kirsch KH, Mineva ND, et al. 2007. Oestrogen signalling inhibits invasive phenotype by repressing RelB and its target BCL2. Nat. Cell Biol. 9:470-78
    • (2007) Nat. Cell Biol. , vol.9 , pp. 470-478
    • Wang, X.1    Belguise, K.2    Kersual, N.3    Kirsch, K.H.4    Mineva, N.D.5
  • 63
    • 84856447171 scopus 로고    scopus 로고
    • ERα, microRNAs, and the epithelial-mesenchymal transition in breast cancer
    • Guttilla IK, Adams BD, White BA. 2012. ERα, microRNAs, and the epithelial-mesenchymal transition in breast cancer. Trends Endocrinol. Metab. 23:73-82
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 73-82
    • Guttilla, I.K.1    Adams, B.D.2    White, B.A.3
  • 64
    • 84862883653 scopus 로고    scopus 로고
    • Role of estrogen receptor signaling in breast cancer metastasis
    • Saha Roy S, Vadlamudi RK. 2012. Role of estrogen receptor signaling in breast cancer metastasis. Int. J. Breast Cancer 2012:654698
    • (2012) Int. J. Breast Cancer , vol.2012 , pp. 654698
    • Saha Roy, S.1    Vadlamudi, R.K.2
  • 65
    • 0034704202 scopus 로고    scopus 로고
    • Regulation of invasive cell behavior by taiman, a Drosophila protein related to AIB1, a steroid receptor coactivator amplified in breast cancer
    • Bai J, Uehara Y, Montell DJ. 2000. Regulation of invasive cell behavior by taiman, a Drosophila protein related to AIB1, a steroid receptor coactivator amplified in breast cancer. Cell 103:1047-58
    • (2000) Cell , vol.103 , pp. 1047-1058
    • Bai, J.1    Uehara, Y.2    Montell, D.J.3
  • 66
    • 48549086542 scopus 로고    scopus 로고
    • Steroid receptor coactivator-3/AIB1 promotes cell migration and invasiveness through focal adhesion turnover and matrix metalloproteinase expression
    • Yan J, Erdem H, Li R, Cai Y, Ayala G, et al. 2008. Steroid receptor coactivator-3/AIB1 promotes cell migration and invasiveness through focal adhesion turnover and matrix metalloproteinase expression. Cancer Res. 68:5460-68
    • (2008) Cancer Res. , vol.68 , pp. 5460-5468
    • Yan, J.1    Erdem, H.2    Li, R.3    Cai, Y.4    Ayala, G.5
  • 67
    • 78650842398 scopus 로고    scopus 로고
    • Minireview: Steroid receptor coactivator-3: A multifarious coregulator in mammary gland metastasis
    • Lydon JP, O'Malley BW. 2011. Minireview: steroid receptor coactivator-3: a multifarious coregulator in mammary gland metastasis. Endocrinology 152:19-25
    • (2011) Endocrinology , vol.152 , pp. 19-25
    • Lydon, J.P.1    O'Malley, B.W.2
  • 68
    • 80053938505 scopus 로고    scopus 로고
    • American Society of Clinical Oncology endorsement of the cancer care Ontario practice guideline on adjuvant ovarian ablation in the treatment of premenopausal women with early-stage invasive breast cancer
    • Griggs JJ, Somerfield MR, Anderson H, Henry NL, Hudis CA, et al. 2011. American Society of Clinical Oncology endorsement of the cancer care Ontario practice guideline on adjuvant ovarian ablation in the treatment of premenopausal women with early-stage invasive breast cancer. J. Clin. Oncol. 29:3939-42
    • (2011) J. Clin. Oncol. , vol.29 , pp. 3939-3942
    • Griggs, J.J.1    Somerfield, M.R.2    Anderson, H.3    Henry, N.L.4    Hudis, C.A.5
  • 69
    • 79960842378 scopus 로고    scopus 로고
    • Toremifene is an effective and safe alternative to tamoxifen in adjuvant endocrine therapy for breast cancer: Results of four randomized trials
    • Zhou WB, Ding Q, Chen L, Liu XA, Wang S. 2011. Toremifene is an effective and safe alternative to tamoxifen in adjuvant endocrine therapy for breast cancer: results of four randomized trials. Breast Cancer Res. Treat. 128:625-31
    • (2011) Breast Cancer Res. Treat. , vol.128 , pp. 625-631
    • Zhou, W.B.1    Ding, Q.2    Chen, L.3    Liu, X.A.4    Wang, S.5
  • 70
    • 79958149945 scopus 로고    scopus 로고
    • The turnover of estrogen receptor α by the selective estrogen receptor degrader (SERD) fulvestrant is a saturable process that is not required for antagonist efficacy
    • Wardell SE, Marks JR, McDonnell DP. 2011. The turnover of estrogen receptor α by the selective estrogen receptor degrader (SERD) fulvestrant is a saturable process that is not required for antagonist efficacy. Biochem. Pharmacol. 82:122-30
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 122-130
    • Wardell, S.E.1    Marks, J.R.2    McDonnell, D.P.3
  • 71
    • 35148869577 scopus 로고    scopus 로고
    • Definition of functionally important mechanistic differences among selective estrogen receptor down-regulators
    • Wittmann BM, Sherk A, McDonnell DP. 2007. Definition of functionally important mechanistic differences among selective estrogen receptor down-regulators. Cancer Res. 67:9549-60
    • (2007) Cancer Res. , vol.67 , pp. 9549-9560
    • Wittmann, B.M.1    Sherk, A.2    McDonnell, D.P.3
  • 72
    • 33750123955 scopus 로고    scopus 로고
    • STAR trial reports
    • 2006. STAR trial reports. Eur. J. Cancer 42:1694
    • (2006) Eur. J. Cancer , vol.42 , pp. 1694
  • 73
    • 78149501152 scopus 로고    scopus 로고
    • The molecular mechanisms underlying the pharmacological actions of ER modulators: Implications for new drug discovery in breast cancer
    • McDonnell DP, Wardell SE. 2010. The molecular mechanisms underlying the pharmacological actions of ER modulators: implications for new drug discovery in breast cancer. Curr. Opin. Pharmacol. 10:620-28
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 620-628
    • McDonnell, D.P.1    Wardell, S.E.2
  • 74
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, et al. 1998. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95:927-37
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5
  • 75
    • 0037192501 scopus 로고    scopus 로고
    • Molecular determinants for the tissue specificity of SERMs
    • Shang Y, Brown M. 2002. Molecular determinants for the tissue specificity of SERMs. Science 295:2465-68
    • (2002) Science , vol.295 , pp. 2465-2468
    • Shang, Y.1    Brown, M.2
  • 76
    • 30144433414 scopus 로고    scopus 로고
    • Hypomethylation-linked activation of PAX2 mediates tamoxifen-stimulated endometrial carcinogenesis
    • Wu H, Chen Y, Liang J, Shi B, Wu G, et al. 2005. Hypomethylation-linked activation of PAX2 mediates tamoxifen-stimulated endometrial carcinogenesis. Nature 438:981-87
    • (2005) Nature , vol.438 , pp. 981-987
    • Wu, H.1    Chen, Y.2    Liang, J.3    Shi, B.4    Wu, G.5
  • 77
    • 82955170653 scopus 로고    scopus 로고
    • Addition of a histone deacetylase inhibitor redirects tamoxifen-treated breast cancer cells into apoptosis, which is opposed by the induction of autophagy
    • Thomas S, Thurn KT, Bicaku E, Marchion DC, Munster PN. 2011. Addition of a histone deacetylase inhibitor redirects tamoxifen-treated breast cancer cells into apoptosis, which is opposed by the induction of autophagy. Breast Cancer Res. Treat. 130:437-47
    • (2011) Breast Cancer Res. Treat. , vol.130 , pp. 437-447
    • Thomas, S.1    Thurn, K.T.2    Bicaku, E.3    Marchion, D.C.4    Munster, P.N.5
  • 78
    • 34548638977 scopus 로고    scopus 로고
    • New insights into the metabolism of tamoxifen and its role in the treatment and prevention of breast cancer
    • Jordan VC. 2007. New insights into the metabolism of tamoxifen and its role in the treatment and prevention of breast cancer. Steroids 72:829-42
    • (2007) Steroids , vol.72 , pp. 829-842
    • Jordan, V.C.1
  • 79
    • 67749114265 scopus 로고    scopus 로고
    • CYP2D6 and tamoxifen: DNA matters in breast cancer
    • Hoskins JM, Carey LA, McLeod HL. 2009. CYP2D6 and tamoxifen: DNA matters in breast cancer. Nat. Rev. Cancer 9:576-86
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 576-586
    • Hoskins, J.M.1    Carey, L.A.2    McLeod, H.L.3
  • 80
    • 34548248572 scopus 로고    scopus 로고
    • Oestrogen-receptor-mediated transcription and the influence of co-factors and chromatin state
    • Green KA, Carroll JS. 2007. Oestrogen-receptor-mediated transcription and the influence of co-factors and chromatin state. Nat. Rev. Cancer 7:713-22
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 713-722
    • Green, K.A.1    Carroll, J.S.2
  • 82
    • 84855339741 scopus 로고    scopus 로고
    • Tamoxifen downregulation of miR-451 increases 14-3-3ζ and promotes breast cancer cell survival and endocrine resistance
    • Bergamaschi A, Katzenellenbogen BS. 2012. Tamoxifen downregulation of miR-451 increases 14-3-3ζ and promotes breast cancer cell survival and endocrine resistance. Oncogene 31:39-47
    • (2012) Oncogene , vol.31 , pp. 39-47
    • Bergamaschi, A.1    Katzenellenbogen, B.S.2
  • 83
    • 77149135270 scopus 로고    scopus 로고
    • Breast cancer epigenetics: From DNA methylation to microRNAs
    • Veeck J, Esteller M. 2010. Breast cancer epigenetics: from DNA methylation to microRNAs. J. Mammary Gland Biol. Neoplasia 15:5-17
    • (2010) J. Mammary Gland Biol. Neoplasia , vol.15 , pp. 5-17
    • Veeck, J.1    Esteller, M.2
  • 85
    • 77149122714 scopus 로고    scopus 로고
    • Epigenetic regulation in estrogen receptor positive breast cancer-role in treatment response
    • Pathiraja TN, Stearns V, Oesterreich S. 2010. Epigenetic regulation in estrogen receptor positive breast cancer-role in treatment response. J. Mammary Gland Biol. Neoplasia 15:35-47
    • (2010) J. Mammary Gland Biol. Neoplasia , vol.15 , pp. 35-47
    • Pathiraja, T.N.1    Stearns, V.2    Oesterreich, S.3
  • 86
    • 81555216077 scopus 로고    scopus 로고
    • Gene expression profiling in breast cancer: Classification, prognostication, and prediction
    • Reis-Filho JS, Pusztai L. 2011. Gene expression profiling in breast cancer: classification, prognostication, and prediction. Lancet 378:1812-23
    • (2011) Lancet , vol.378 , pp. 1812-1823
    • Reis-Filho, J.S.1    Pusztai, L.2
  • 87
    • 77149156308 scopus 로고    scopus 로고
    • The role of histone modifications and variants in regulating gene expression in breast cancer
    • Dalvai M, Bystricky K. 2010. The role of histone modifications and variants in regulating gene expression in breast cancer. J. Mammary Gland Biol. Neoplasia 15:19-33
    • (2010) J. Mammary Gland Biol. Neoplasia , vol.15 , pp. 19-33
    • Dalvai, M.1    Bystricky, K.2
  • 88
    • 36849020052 scopus 로고    scopus 로고
    • Tamoxifen resistance and epigenetic modifications in breast cancer cell lines
    • Badia E, Oliva J, Balaguer P, Cavailles V. 2007. Tamoxifen resistance and epigenetic modifications in breast cancer cell lines. Curr. Med. Chem. 14:3035-45
    • (2007) Curr. Med. Chem. , vol.14 , pp. 3035-3045
    • Badia, E.1    Oliva, J.2    Balaguer, P.3    Cavailles, V.4
  • 89
    • 84856564293 scopus 로고    scopus 로고
    • ERα phenotype, estrogen level, and benzo[a]pyrene exposure modulate tumor growth and metabolism of lung adenocarcinoma cells
    • Lin S, Lin CJ, Hsieh DP, Li LA. 2012. ERα phenotype, estrogen level, and benzo[a]pyrene exposure modulate tumor growth and metabolism of lung adenocarcinoma cells. Lung Cancer 75:285-92
    • (2012) Lung Cancer , vol.75 , pp. 285-292
    • Lin, S.1    Lin, C.J.2    Hsieh, D.P.3    Li, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.