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Volumn 69, Issue , 2007, Pages 171-199

Integration of rapid signaling events with steroid hormone receptor action in breast and prostate cancer

Author keywords

Androgen receptor; Cyclin D1; Epidermal growth factor; Mitogen activated protein kinase; Progesterone receptor

Indexed keywords

ANDROGEN RECEPTOR; BETA CATENIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROGESTERONE RECEPTOR; PROTEIN P300; RAF PROTEIN; RAS PROTEIN; SELECTIVE ESTROGEN RECEPTOR MODULATOR; STEROID RECEPTOR; STEROID RECEPTOR COACTIVATOR 1; STEROID RECEPTOR COACTIVATOR 3; WNT1 PROTEIN;

EID: 33947401482     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.69.031905.160319     Document Type: Review
Times cited : (99)

References (156)
  • 1
    • 33645406947 scopus 로고    scopus 로고
    • Up-regulation of the progesterone receptor (PR)-C isoform in laboring myometrium by activation of nuclear factor-κB may contribute to the onset of labor through inhibition of PR function
    • Condon JC, Hardy DB, Kovaric K, Mendelson CR. 2006. Up-regulation of the progesterone receptor (PR)-C isoform in laboring myometrium by activation of nuclear factor-κB may contribute to the onset of labor through inhibition of PR function. Mol. Endocrinol. 20:764-75
    • (2006) Mol. Endocrinol , vol.20 , pp. 764-775
    • Condon, J.C.1    Hardy, D.B.2    Kovaric, K.3    Mendelson, C.R.4
  • 2
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt VVB, Toft DO. 2003. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. 228:111-33
    • (2003) Exp. Biol. Med , vol.228 , pp. 111-133
    • Pratt, V.V.B.1    Toft, D.O.2
  • 4
    • 0023664688 scopus 로고
    • Fatty acid synthetase and its mRNA are induced by progestins in breast cancer cells
    • Chalbos D, Chambon M, Ailhaud G, Rochefort H. 1987. Fatty acid synthetase and its mRNA are induced by progestins in breast cancer cells. J. Biol. Chem. 262:9923-26
    • (1987) J. Biol. Chem , vol.262 , pp. 9923-9926
    • Chalbos, D.1    Chambon, M.2    Ailhaud, G.3    Rochefort, H.4
  • 5
    • 0026037160 scopus 로고
    • Co-operation of progestational steroids with epidermal growth factor in activation of gene expression in mammary tumor cells
    • Krusekopf S, Chauchereau A, Milgrom E, Henderson D, Cato AC. 1991. Co-operation of progestational steroids with epidermal growth factor in activation of gene expression in mammary tumor cells. J. Steroid Biochem. Mol. Biol. 40:239-45
    • (1991) J. Steroid Biochem. Mol. Biol , vol.40 , pp. 239-245
    • Krusekopf, S.1    Chauchereau, A.2    Milgrom, E.3    Henderson, D.4    Cato, A.C.5
  • 6
    • 33746623315 scopus 로고    scopus 로고
    • Molecular regulation of androgen action in prostate cancer
    • Dehm SM, Tindall DJ. 2006. Molecular regulation of androgen action in prostate cancer. J. Cell Biochem. 99:333-34
    • (2006) J. Cell Biochem , vol.99 , pp. 333-334
    • Dehm, S.M.1    Tindall, D.J.2
  • 7
    • 0032553304 scopus 로고    scopus 로고
    • Convergence of progesterone and epidermal growth factor signaling in breast cancer. Potentiation of mitogen-activated protein kinase pathways
    • Lange CA, Richer J K, Shen T, Horwitz KB. 1998. Convergence of progesterone and epidermal growth factor signaling in breast cancer. Potentiation of mitogen-activated protein kinase pathways. J. Biol. Chem. 273:31308-16
    • (1998) J. Biol. Chem , vol.273 , pp. 31308-31316
    • Lange, C.A.1    Richer, J.K.2    Shen, T.3    Horwitz, K.B.4
  • 8
    • 0029040399 scopus 로고
    • Androgen up-regulates epidermal growth factor receptor expression and binding affinity in PC3 cell lines expressing the human androgen receptor
    • Brass AL, Barnard J, Patai BL, Salvi D, Rukstalis DB. 1995. Androgen up-regulates epidermal growth factor receptor expression and binding affinity in PC3 cell lines expressing the human androgen receptor. Cancer Res. 55:3197-203
    • (1995) Cancer Res , vol.55 , pp. 3197-3203
    • Brass, A.L.1    Barnard, J.2    Patai, B.L.3    Salvi, D.4    Rukstalis, D.B.5
  • 9
    • 17144365000 scopus 로고    scopus 로고
    • Induction of AP-I activity by androgen activation of the androgen receptor in LNCaP human prostate carcinoma cells
    • Church DR, Lee E, Thompson TA, Basu HS, Ripple MO, et al. 2005. Induction of AP-I activity by androgen activation of the androgen receptor in LNCaP human prostate carcinoma cells. Prostate 63:155-68
    • (2005) Prostate , vol.63 , pp. 155-168
    • Church, D.R.1    Lee, E.2    Thompson, T.A.3    Basu, H.S.4    Ripple, M.O.5
  • 10
    • 0032553553 scopus 로고    scopus 로고
    • Convergence or progesterone with growth factor and cytokine signaling in breast cancer. Progesterone receptors regulate signal transducers and activators of transcription expression and activity
    • Richer JK, Lange CA, Manning NG, Owen G, Powell R, Horwitz, KB. 1998. Convergence or progesterone with growth factor and cytokine signaling in breast cancer. Progesterone receptors regulate signal transducers and activators of transcription expression and activity. J. Biol. Chem. 273:31317-26
    • (1998) J. Biol. Chem , vol.273 , pp. 31317-31326
    • Richer, J.K.1    Lange, C.A.2    Manning, N.G.3    Owen, G.4    Powell, R.5    Horwitz, K.B.6
  • 11
    • 0034935259 scopus 로고    scopus 로고
    • Androgen receptor regulation of G1 cyclin and cyclin-dependent kinase function in the CWR22 human prostate cancer xenograft
    • Gregory CW, Johnson RTJ, Presnell SC, Mohler JL, French FS. 2001. Androgen receptor regulation of G1 cyclin and cyclin-dependent kinase function in the CWR22 human prostate cancer xenograft. J. Androl. 22:537-48
    • (2001) J. Androl , vol.22 , pp. 537-548
    • Gregory, C.W.1    Johnson, R.T.J.2    Presnell, S.C.3    Mohler, J.L.4    French, F.S.5
  • 12
    • 0030775651 scopus 로고    scopus 로고
    • Biphasic regulation of breast cancer cell growth by progesterone: Role of the cyclin-dependent kinase inhibitors, p21 and p27 (Kip1)
    • Groshong SD, Owen GI, Grimison B, Schauer IE, Todd MC, et al. 1997. Biphasic regulation of breast cancer cell growth by progesterone: role of the cyclin-dependent kinase inhibitors, p21 and p27 (Kip1). Mol. Endocrinol. 11:1593-607
    • (1997) Mol. Endocrinol , vol.11 , pp. 1593-1607
    • Groshong, S.D.1    Owen, G.I.2    Grimison, B.3    Schauer, I.E.4    Todd, M.C.5
  • 13
    • 0032562712 scopus 로고    scopus 로고
    • Progesterone regulates transcription of the p21 (WAF1) cyclin-dependent kinase inhibitor gene through Sp1 and CBP/p300
    • Owen GI, Richer JK, Tung L, Takimoto G, Horwitz KB. 1998. Progesterone regulates transcription of the p21 (WAF1) cyclin-dependent kinase inhibitor gene through Sp1 and CBP/p300. J. Biol. Chem. 273:10696-701
    • (1998) J. Biol. Chem , vol.273 , pp. 10696-10701
    • Owen, G.I.1    Richer, J.K.2    Tung, L.3    Takimoto, G.4    Horwitz, K.B.5
  • 14
    • 0242351198 scopus 로고    scopus 로고
    • Progesterone receptor (hPR) upregulates the fibronectin promoter activity in human decidual fibroblasts
    • Tseng L, Tang M, Wang Z, Mazella J. 2003. Progesterone receptor (hPR) upregulates the fibronectin promoter activity in human decidual fibroblasts. DNA Cell Biol. 22:633-40
    • (2003) DNA Cell Biol , vol.22 , pp. 633-640
    • Tseng, L.1    Tang, M.2    Wang, Z.3    Mazella, J.4
  • 15
    • 20344391678 scopus 로고    scopus 로고
    • Progestins induce transcriptional activation of signal transducer and activator of transcription 3 (Stat3) via a Jak- and Src-dependent mechanism in breast cancer cells
    • Proietti C, Salatino M, Rosemblit C, Carnevale R, Pecci A, et al. 2005. Progestins induce transcriptional activation of signal transducer and activator of transcription 3 (Stat3) via a Jak- and Src-dependent mechanism in breast cancer cells. Mol. Cell Biol. 25:4826-40
    • (2005) Mol. Cell Biol , vol.25 , pp. 4826-4840
    • Proietti, C.1    Salatino, M.2    Rosemblit, C.3    Carnevale, R.4    Pecci, A.5
  • 16
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna NJ, O'Malley BW. 2002. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108:465-74
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 17
    • 0014486198 scopus 로고
    • Role of the oocyte nucleus in physiological maturation in Rana pipiens
    • Smith LD, Ecker RE. 1969. Role of the oocyte nucleus in physiological maturation in Rana pipiens. Dev. Biol. 19:281-309
    • (1969) Dev. Biol , vol.19 , pp. 281-309
    • Smith, L.D.1    Ecker, R.E.2
  • 18
    • 0035755603 scopus 로고    scopus 로고
    • From oocyte maturation to the in vitro cell cycle: The history of discoveries of Maturation-Promoting Factor (MPF) and Cytostatic Factor (CSF)
    • Masui Y. 2001. From oocyte maturation to the in vitro cell cycle: the history of discoveries of Maturation-Promoting Factor (MPF) and Cytostatic Factor (CSF). Differentiation 69:1-17
    • (2001) Differentiation , vol.69 , pp. 1-17
    • Masui, Y.1
  • 19
    • 1842584190 scopus 로고    scopus 로고
    • Steroids and oocyte maturation - a new look at an old story
    • Hammes SR. 2004. Steroids and oocyte maturation - a new look at an old story. Mol. Endocrinol. 18:769-75
    • (2004) Mol. Endocrinol , vol.18 , pp. 769-775
    • Hammes, S.R.1
  • 20
    • 0035923642 scopus 로고    scopus 로고
    • Evidence that androgens are the primary steroids produced by Xenopus laevis ovaries and may signal through the classical androgen receptor to promote oocyte maturation
    • Lutz LB, Cole LM, Gupta MK, Kwist KW, Auchus RJ, Hammes SR. 2001. Evidence that androgens are the primary steroids produced by Xenopus laevis ovaries and may signal through the classical androgen receptor to promote oocyte maturation. Proc. Natl. Acad. Sci. USA 98:13728-33
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13728-13733
    • Lutz, L.B.1    Cole, L.M.2    Gupta, M.K.3    Kwist, K.W.4    Auchus, R.J.5    Hammes, S.R.6
  • 21
    • 18144363630 scopus 로고    scopus 로고
    • Specific modulation of nongenomic androgen signaling in the ovary
    • White SN, Jamnongjit M, Gill A, Lutz LB, Hammes SR. 2005. Specific modulation of nongenomic androgen signaling in the ovary. Steroids 70:352-60
    • (2005) Steroids , vol.70 , pp. 352-360
    • White, S.N.1    Jamnongjit, M.2    Gill, A.3    Lutz, L.B.4    Hammes, S.R.5
  • 22
    • 23844432614 scopus 로고    scopus 로고
    • Oocyte maturation: The coming of age of a germ cell
    • Jamnongjit M, Hammes SR. 2005. Oocyte maturation: the coming of age of a germ cell. Semin. Reprod. Med. 23:234-41
    • (2005) Semin. Reprod. Med , vol.23 , pp. 234-241
    • Jamnongjit, M.1    Hammes, S.R.2
  • 23
    • 0037441315 scopus 로고    scopus 로고
    • Quantitation of apoptotic activity following castration in human prostatic tissue in vivo
    • Staack A, Kassis AP, Olshen A, Wang Y, Wu D, et al. 2003. Quantitation of apoptotic activity following castration in human prostatic tissue in vivo. Prostate 54:212-19
    • (2003) Prostate , vol.54 , pp. 212-219
    • Staack, A.1    Kassis, A.P.2    Olshen, A.3    Wang, Y.4    Wu, D.5
  • 24
    • 0033988067 scopus 로고    scopus 로고
    • Endocrine treatment in prostate cancer
    • Denis LJ, Griffiths K. 2000. Endocrine treatment in prostate cancer. Semin. Surg. Oncol. 18:52-74
    • (2000) Semin. Surg. Oncol , vol.18 , pp. 52-74
    • Denis, L.J.1    Griffiths, K.2
  • 25
  • 26
    • 1842612441 scopus 로고    scopus 로고
    • Molecular determinants of resistance to antiandrogen therapy
    • Chen CD, Welsbie DS, Tran C, Baek SH, Chen R, et al. 2004. Molecular determinants of resistance to antiandrogen therapy. Nat. Med. 10:33-39
    • (2004) Nat. Med , vol.10 , pp. 33-39
    • Chen, C.D.1    Welsbie, D.S.2    Tran, C.3    Baek, S.H.4    Chen, R.5
  • 28
    • 20444403792 scopus 로고    scopus 로고
    • The androgen receptor and signal-transduction pathways in hormone-refractory prostate cancer. Part 1: Modifications to the androgen receptor
    • Edwards J, Bartlett JM. 2005. The androgen receptor and signal-transduction pathways in hormone-refractory prostate cancer. Part 1: Modifications to the androgen receptor. BJU Int. 95:1320-26
    • (2005) BJU Int , vol.95 , pp. 1320-1326
    • Edwards, J.1    Bartlett, J.M.2
  • 29
    • 20444368837 scopus 로고    scopus 로고
    • The androgen receptor and signal-transduction pathways in hormone-refractory prostate cancer. Part 2: Androgen-receptor cofactors and bypass pathways
    • Edwards J, Bartlett JM. 2005. The androgen receptor and signal-transduction pathways in hormone-refractory prostate cancer. Part 2: Androgen-receptor cofactors and bypass pathways. BJU Int. 95:1327-35
    • (2005) BJU Int , vol.95 , pp. 1327-1335
    • Edwards, J.1    Bartlett, J.M.2
  • 30
    • 17144364645 scopus 로고    scopus 로고
    • Signal transduction in prostate cancer progression
    • Gioeli D. 2005. Signal transduction in prostate cancer progression. Clin. Sci. 108:293-308
    • (2005) Clin. Sci , vol.108 , pp. 293-308
    • Gioeli, D.1
  • 31
    • 0028272478 scopus 로고
    • Androgen-independent cancer progression and bone metastasis in the LNCaP model of human prostate cancer
    • Thalmann GN, Anezinis PE, Chang SM, Zhau HE, Kim EE, et al. 1994. Androgen-independent cancer progression and bone metastasis in the LNCaP model of human prostate cancer. Cancer Res. 54:2577-81
    • (1994) Cancer Res , vol.54 , pp. 2577-2581
    • Thalmann, G.N.1    Anezinis, P.E.2    Chang, S.M.3    Zhau, H.E.4    Kim, E.E.5
  • 32
    • 0026848294 scopus 로고
    • Prostate and bone fibroblasts induce human prostate cancer growth in vivo: Implications for bidirectional tumor-stromal cell interaction in prostate carcinoma growth and metastasis
    • Gleave ME, Hsieh JT, von Eschenbach AC, Chung LW. 1992. Prostate and bone fibroblasts induce human prostate cancer growth in vivo: implications for bidirectional tumor-stromal cell interaction in prostate carcinoma growth and metastasis. J. Urol. 147:1151-59
    • (1992) J. Urol , vol.147 , pp. 1151-1159
    • Gleave, M.E.1    Hsieh, J.T.2    von Eschenbach, A.C.3    Chung, L.W.4
  • 33
    • 0027407639 scopus 로고
    • Inhibition of growth of prostatic cancer cell lines by peptide analogues of insulin-like growth factor 1
    • Pietrzkowski Z, Mulholland G, Gomella L, Jameson BA, Wernicke D, Baserga R. 1993. Inhibition of growth of prostatic cancer cell lines by peptide analogues of insulin-like growth factor 1. Cancer Res. 53:1102-6
    • (1993) Cancer Res , vol.53 , pp. 1102-1106
    • Pietrzkowski, Z.1    Mulholland, G.2    Gomella, L.3    Jameson, B.A.4    Wernicke, D.5    Baserga, R.6
  • 34
    • 0033022342 scopus 로고    scopus 로고
    • A mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase
    • Craft N, Shostak Y, Carey M, Sawyers CL. 1999. A mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase. Nat. Med. 5:280-85
    • (1999) Nat. Med , vol.5 , pp. 280-285
    • Craft, N.1    Shostak, Y.2    Carey, M.3    Sawyers, C.L.4
  • 35
    • 0037105743 scopus 로고    scopus 로고
    • Growth inhibitory effects of the dual ErbB1/ErbB2 tyrosine kinase inhibitor PKI-166 on human prostate cancer xenografts
    • Mellinghoff IK, Tran C, Sawyers CL. 2002. Growth inhibitory effects of the dual ErbB1/ErbB2 tyrosine kinase inhibitor PKI-166 on human prostate cancer xenografts. Cancer Res. 62:5254-59
    • (2002) Cancer Res , vol.62 , pp. 5254-5259
    • Mellinghoff, I.K.1    Tran, C.2    Sawyers, C.L.3
  • 36
    • 19044380618 scopus 로고    scopus 로고
    • Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth
    • Agus DB, Akita RW, Fox WD, Lewis GD, Higgins B, et al. 2002. Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth. Cancer Cell 2:121-37
    • (2002) Cancer Cell , vol.2 , pp. 121-137
    • Agus, D.B.1    Akita, R.W.2    Fox, W.D.3    Lewis, G.D.4    Higgins, B.5
  • 37
    • 7944234374 scopus 로고    scopus 로고
    • HER2/neu kinase-dependent modulation of androgen receptor function through effects on DNA binding and stability
    • McIlinghoff IK, Vivancol, Kwon A, Tran C, Wongvipat J, Sawyers CL. 2004. HER2/neu kinase-dependent modulation of androgen receptor function through effects on DNA binding and stability. Cancer Cell 6:517-27
    • (2004) Cancer Cell , vol.6 , pp. 517-527
    • McIlinghoff, I.K.1    Vivancol2    Kwon, A.3    Tran, C.4    Wongvipat, J.5    Sawyers, C.L.6
  • 38
    • 0025186176 scopus 로고
    • ras gene mutations in human prostate cancer
    • Carter BS, Epstein JI, Isaacs WB. 1990. ras gene mutations in human prostate cancer. Cancer Res. 50:6830-32
    • (1990) Cancer Res , vol.50 , pp. 6830-6832
    • Carter, B.S.1    Epstein, J.I.2    Isaacs, W.B.3
  • 39
    • 0025924862 scopus 로고
    • v-rasH expression confers hormone-independent in vitro growth to LNCaP prostate carcinoma cells
    • Voeller HJ, Wilding G, Gelmann EP. 1991. v-rasH expression confers hormone-independent in vitro growth to LNCaP prostate carcinoma cells. Mol. Endocrinol. 5:209-16
    • (1991) Mol. Endocrinol , vol.5 , pp. 209-216
    • Voeller, H.J.1    Wilding, G.2    Gelmann, E.P.3
  • 40
    • 0037447330 scopus 로고    scopus 로고
    • Constitutive activation of the Ras/mitogen-activated protein kinase signaling pathway promotes androgen hypersensitivity in LNCaP prostate cancer cells
    • Bakin RE, Giocli D, Sikes RA, Bissonette EA, Weber MJ. 2003. Constitutive activation of the Ras/mitogen-activated protein kinase signaling pathway promotes androgen hypersensitivity in LNCaP prostate cancer cells. Cancer Res. 63:1981-89
    • (2003) Cancer Res , vol.63 , pp. 1981-1989
    • Bakin, R.E.1    Giocli, D.2    Sikes, R.A.3    Bissonette, E.A.4    Weber, M.J.5
  • 41
    • 0034234571 scopus 로고    scopus 로고
    • LNCaP progression model of human prostate cancer: Androgen-independence and osseous metastasis
    • Thalmann GN, Sikes RA, Wu TT, Degeorges A, Chang SM, et al. 2000. LNCaP progression model of human prostate cancer: androgen-independence and osseous metastasis. Prostate 44:91-103
    • (2000) Prostate , vol.44 , pp. 91-103
    • Thalmann, G.N.1    Sikes, R.A.2    Wu, T.T.3    Degeorges, A.4    Chang, S.M.5
  • 42
    • 0037447154 scopus 로고    scopus 로고
    • Attenuation of Ras signaling restores androgen sensitivity to hormone-refractory C4-2 prostate cancer cells
    • Bakin RE, Gioeli D, Bissonette EA, Weber MJ. 2003. Attenuation of Ras signaling restores androgen sensitivity to hormone-refractory C4-2 prostate cancer cells. Cancer Res. 63:1975-80
    • (2003) Cancer Res , vol.63 , pp. 1975-1980
    • Bakin, R.E.1    Gioeli, D.2    Bissonette, E.A.3    Weber, M.J.4
  • 43
  • 44
    • 0036235788 scopus 로고    scopus 로고
    • Regulation of proliferation/apoptosis equilibrium by mitogen-activated protein kinases in normal, hyperplastic, and carcinomatous human prostate
    • Royuela M, Arenas MI, Bethencourt FR, Sanchez-Chapado M, Fraile B, Paniagua R. 2002. Regulation of proliferation/apoptosis equilibrium by mitogen-activated protein kinases in normal, hyperplastic, and carcinomatous human prostate. Hum. Pathol. 33:299-306
    • (2002) Hum. Pathol , vol.33 , pp. 299-306
    • Royuela, M.1    Arenas, M.I.2    Bethencourt, F.R.3    Sanchez-Chapado, M.4    Fraile, B.5    Paniagua, R.6
  • 45
    • 19044380048 scopus 로고    scopus 로고
    • Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites
    • Gioeli D, Ficarro SB, Kwiek JJ, Aaronson D, Hancock M, et al. 2002. Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites. J. Biol. Chem. 277:29304-14
    • (2002) J. Biol. Chem , vol.277 , pp. 29304-29314
    • Gioeli, D.1    Ficarro, S.B.2    Kwiek, J.J.3    Aaronson, D.4    Hancock, M.5
  • 46
    • 0034811237 scopus 로고    scopus 로고
    • Identification of a novel phosphorylation site in human androgen receptor by mass spectrometry
    • Zhu Z, Becklin RR, Desiderio DM, Dalton JT. 2001. Identification of a novel phosphorylation site in human androgen receptor by mass spectrometry. Biochem. Biophys. Res. Commun. 284:836-44
    • (2001) Biochem. Biophys. Res. Commun , vol.284 , pp. 836-844
    • Zhu, Z.1    Becklin, R.R.2    Desiderio, D.M.3    Dalton, J.T.4
  • 47
    • 0029041681 scopus 로고
    • Identification of three proline-directed phosphorylation sites in the human androgen receptor
    • Zhou ZX, Kemppainen JA, Wilson EM. 1995. Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol. Endocrinol. 9:605-15
    • (1995) Mol. Endocrinol , vol.9 , pp. 605-615
    • Zhou, Z.X.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 48
    • 0033545848 scopus 로고    scopus 로고
    • From HER2/Neu signal cascade to androgen receptor and its coactivators: A novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells
    • Yeh S, Lin HK, Kang HY, Thin TH, Lin MF, Chang C. 1999. From HER2/Neu signal cascade to androgen receptor and its coactivators: a novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells. Proc. Natl. Acad. Sci. USA 96:5458-63
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5458-5463
    • Yeh, S.1    Lin, H.K.2    Kang, H.Y.3    Thin, T.H.4    Lin, M.F.5    Chang, C.6
  • 49
    • 0035912833 scopus 로고    scopus 로고
    • Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor
    • Lin HK, Yeh S, Kang HY, Chang C. 2001. Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Proc. Natl. Acad. Sci. USA 98:7200-5
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7200-7205
    • Lin, H.K.1    Yeh, S.2    Kang, H.Y.3    Chang, C.4
  • 50
    • 0034671668 scopus 로고    scopus 로고
    • HER-2/neu promotes androgen-independent survival and growth of prostate cancer cells through the Akt pathway
    • Wen Y, Hu MC, Makino K, Spohn B, Bartholomeusz G, et al. 2000. HER-2/neu promotes androgen-independent survival and growth of prostate cancer cells through the Akt pathway. Cancer Res. 60:6841-45
    • (2000) Cancer Res , vol.60 , pp. 6841-6845
    • Wen, Y.1    Hu, M.C.2    Makino, K.3    Spohn, B.4    Bartholomeusz, G.5
  • 51
    • 33344467745 scopus 로고    scopus 로고
    • Stress kinase signaling regulates androgen receptor phosphorylation, transcription, and localization
    • Gioeli D, Black BE, Gordon V, Spencer A, Kesler CT, et al. 2006. Stress kinase signaling regulates androgen receptor phosphorylation, transcription, and localization. Mol. Endocrinol. 20:503-15
    • (2006) Mol. Endocrinol , vol.20 , pp. 503-515
    • Gioeli, D.1    Black, B.E.2    Gordon, V.3    Spencer, A.4    Kesler, C.T.5
  • 52
    • 28844467498 scopus 로고    scopus 로고
    • Cell-specific regulation of androgen receptor phosphorylation in vivo
    • Taneja SS, Ha S, Swenson NK, Huang HY, Lee P, et al. 2005. Cell-specific regulation of androgen receptor phosphorylation in vivo. J. Biol. Chem. 280:40916-24
    • (2005) J. Biol. Chem , vol.280 , pp. 40916-40924
    • Taneja, S.S.1    Ha, S.2    Swenson, N.K.3    Huang, H.Y.4    Lee, P.5
  • 53
    • 0347696003 scopus 로고    scopus 로고
    • Suppression versus induction of androgen receptor functions by the phosphatidylinositol 3-kinase/Akt pathway in prostate cancer LNCaP cells with different passage numbers
    • Lin HK, Hu YC, Yang L, Altuwaijri S, Chen YT, et al. 2003. Suppression versus induction of androgen receptor functions by the phosphatidylinositol 3-kinase/Akt pathway in prostate cancer LNCaP cells with different passage numbers. J. Biol. Chem. 278:50902-7
    • (2003) J. Biol. Chem , vol.278 , pp. 50902-50907
    • Lin, H.K.1    Hu, Y.C.2    Yang, L.3    Altuwaijri, S.4    Chen, Y.T.5
  • 54
    • 0036794281 scopus 로고    scopus 로고
    • Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation
    • Itoh M, Adachi M, Yasui H, Takekawa M, Tanaka H, Imai K. 2002. Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation. Mol. Endocrinol. 16:2382-92
    • (2002) Mol. Endocrinol , vol.16 , pp. 2382-2392
    • Itoh, M.1    Adachi, M.2    Yasui, H.3    Takekawa, M.4    Tanaka, H.5    Imai, K.6
  • 55
    • 0037385535 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors
    • Qiu M, Olsen A, Faivre E, Horwitz KB, Lange CA. 2003. Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors. Mol. Endocrinol. 17:628-42
    • (2003) Mol. Endocrinol , vol.17 , pp. 628-642
    • Qiu, M.1    Olsen, A.2    Faivre, E.3    Horwitz, K.B.4    Lange, C.A.5
  • 56
    • 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. 22:5835-45
    • (2002) Mol. Cell Biol , vol.22 , pp. 5835-5845
    • Lee, H.1    Bai, W.2
  • 57
    • 0034635553 scopus 로고    scopus 로고
    • Phosphorylation of steroid receptor coactivator-I. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway
    • Rowan BG, Weigel NL, O'Malley BW. 2000. Phosphorylation of steroid receptor coactivator-I. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway. J. Biol. Chem. 275:4475-83
    • (2000) J. Biol. Chem , vol.275 , pp. 4475-4483
    • Rowan, B.G.1    Weigel, N.L.2    O'Malley, B.W.3
  • 58
    • 1342325380 scopus 로고    scopus 로고
    • Epidermal growth factor increases coactivation of the androgen receptor in recurrent prostate cancer
    • Gregory CW, Fei X, Ponguta LA, He B, Bill HM, et al. 2004. Epidermal growth factor increases coactivation of the androgen receptor in recurrent prostate cancer. J. Biol. Chem. 279:7119-30
    • (2004) J. Biol. Chem , vol.279 , pp. 7119-7130
    • Gregory, C.W.1    Fei, X.2    Ponguta, L.A.3    He, B.4    Bill, H.M.5
  • 59
    • 0032549744 scopus 로고    scopus 로고
    • Partial hormone resistance in mice with disruption ofthe steroid receptor coactivator-1 (SRC-I) gene
    • Xu J, Qiu Y, DeMayo FJ, Tsai SY, Tsai MJ, O'Malley BW. 1998, Partial hormone resistance in mice with disruption ofthe steroid receptor coactivator-1 (SRC-I) gene. Science 279:1922-25
    • (1998) Science , vol.279 , pp. 1922-1925
    • Xu, J.1    Qiu, Y.2    DeMayo, F.J.3    Tsai, S.Y.4    Tsai, M.J.5    O'Malley, B.W.6
  • 60
    • 0035361340 scopus 로고    scopus 로고
    • A mechanism for androgen receptor-mediated prostate cancer recurrence after androgen deprivation therapy
    • Gregory CW, He B, Johnson RT, Ford OH, Mohler JL, et al. 2001. A mechanism for androgen receptor-mediated prostate cancer recurrence after androgen deprivation therapy. Cancer Res. 61:4315-19
    • (2001) Cancer Res , vol.61 , pp. 4315-4319
    • Gregory, C.W.1    He, B.2    Johnson, R.T.3    Ford, O.H.4    Mohler, J.L.5
  • 61
    • 0036219918 scopus 로고    scopus 로고
    • Androgen receptor (AR) coregulators: An overview
    • Heinlein CA, Chang C. 2002. Androgen receptor (AR) coregulators: an overview. Endocr. Rev. 23:175-200
    • (2002) Endocr. Rev , vol.23 , pp. 175-200
    • Heinlein, C.A.1    Chang, C.2
  • 62
    • 0033398962 scopus 로고    scopus 로고
    • Differential induction of androgen receptor transactivation by different androgen receptor coactivators in human prostate cancer DU145 cells
    • Yeh S, Kang HY, Miyamoto H, Nishimura K, Chang HC, et al. 1999. Differential induction of androgen receptor transactivation by different androgen receptor coactivators in human prostate cancer DU145 cells. Endocrine 11:195-202
    • (1999) Endocrine , vol.11 , pp. 195-202
    • Yeh, S.1    Kang, H.Y.2    Miyamoto, H.3    Nishimura, K.4    Chang, H.C.5
  • 63
    • 0037108955 scopus 로고    scopus 로고
    • P300 mediates androgen-independent transactivation of the androgen receptor by interleukin 6
    • Debes JD, Schmidt LJ, Huang H, Tindall DJ. 2002. P300 mediates androgen-independent transactivation of the androgen receptor by interleukin 6. Cancer Res. 62:5632-36
    • (2002) Cancer Res , vol.62 , pp. 5632-5636
    • Debes, J.D.1    Schmidt, L.J.2    Huang, H.3    Tindall, D.J.4
  • 64
    • 0038112654 scopus 로고    scopus 로고
    • The role of the androgen receptor in prostate cancer
    • Huang H, Tindall DJ. 2002. The role of the androgen receptor in prostate cancer. Crit. Rev. Enkaryot. Gene Expr. 12:193-207
    • (2002) Crit. Rev. Enkaryot. Gene Expr , vol.12 , pp. 193-207
    • Huang, H.1    Tindall, D.J.2
  • 65
    • 0344464720 scopus 로고    scopus 로고
    • Wnts and Hedgehogs: Lipid-modified proteins and similarities in signaling mechanisms at the cell surface
    • Nusse R. 2003. Wnts and Hedgehogs: lipid-modified proteins and similarities in signaling mechanisms at the cell surface. Development 130:5297-305
    • (2003) Development , vol.130 , pp. 5297-5305
    • Nusse, R.1
  • 66
    • 0036794477 scopus 로고    scopus 로고
    • Increasingly complex: New players enter the Wnt signaling network
    • Pandur P, Maurus D, Kuhl M. 2002. Increasingly complex: New players enter the Wnt signaling network. Bioessays 24:881-84
    • (2002) Bioessays , vol.24 , pp. 881-884
    • Pandur, P.1    Maurus, D.2    Kuhl, M.3
  • 67
  • 68
    • 0034283030 scopus 로고    scopus 로고
    • Beta-catenin affects androgen receptor transcriptional activity and ligand specificity
    • Truica CI, Byers S, Gelmann EP. 2000. Beta-catenin affects androgen receptor transcriptional activity and ligand specificity. Cancer Res. 60:4709-13
    • (2000) Cancer Res , vol.60 , pp. 4709-4713
    • Truica, C.I.1    Byers, S.2    Gelmann, E.P.3
  • 69
    • 0037124062 scopus 로고    scopus 로고
    • The androgen receptor can promote beta-catenin nuclear translocation independently of adenomatous polyposis coli
    • Mulholland DJ, Cheng H, Reid K, Rennie PS, Nelson CC. 2002. The androgen receptor can promote beta-catenin nuclear translocation independently of adenomatous polyposis coli. J. Biol Chem. 277:17933-43
    • (2002) J. Biol Chem , vol.277 , pp. 17933-17943
    • Mulholland, D.J.1    Cheng, H.2    Reid, K.3    Rennie, P.S.4    Nelson, C.C.5
  • 70
    • 10844230334 scopus 로고    scopus 로고
    • Wnt3a growth factor induces androgen receptor-mediated transcription and enhances cell growth in human prostate cancer cells
    • Verras M, Brown J, Li X, Nusse R, Sun Z. 2004. Wnt3a growth factor induces androgen receptor-mediated transcription and enhances cell growth in human prostate cancer cells. Cancer Res. 64:8860-66
    • (2004) Cancer Res , vol.64 , pp. 8860-8866
    • Verras, M.1    Brown, J.2    Li, X.3    Nusse, R.4    Sun, Z.5
  • 71
    • 0025222517 scopus 로고
    • The transforming growth factor-beta family
    • Massague J. 1990. The transforming growth factor-beta family. Annu. Rev. Cell Biol. 6:597-641
    • (1990) Annu. Rev. Cell Biol , vol.6 , pp. 597-641
    • Massague, J.1
  • 72
    • 0030598681 scopus 로고    scopus 로고
    • TGFβ1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice
    • Cui W, Fowlis DJ, Bryson S, Duffie E, Ireland H, et al. 1996. TGFβ1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice. Cell 86:531-42
    • (1996) Cell , vol.86 , pp. 531-542
    • Cui, W.1    Fowlis, D.J.2    Bryson, S.3    Duffie, E.4    Ireland, H.5
  • 73
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massague J. 1998. TGF-β signal transduction. Annu. Rev. Biochem. 67:753-91
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 753-791
    • Massague, J.1
  • 74
    • 27244445059 scopus 로고    scopus 로고
    • Transforming growth factor β and prostate cancer
    • Zhu B, Kyprianou N. 2005. Transforming growth factor β and prostate cancer. Cancer Treat. Res. 126:157-73
    • (2005) Cancer Treat. Res , vol.126 , pp. 157-173
    • Zhu, B.1    Kyprianou, N.2
  • 75
  • 76
    • 27844610897 scopus 로고    scopus 로고
    • Androgen receptor and TGFβ1/Smad signaling are mutually inhibitory in prostate cancer
    • van der Poel HG. 2005. Androgen receptor and TGFβ1/Smad signaling are mutually inhibitory in prostate cancer. Eur. Urol. 48:1051-58
    • (2005) Eur. Urol , vol.48 , pp. 1051-1058
    • van der Poel, H.G.1
  • 77
    • 0035853055 scopus 로고    scopus 로고
    • From transforming growth factor-β signaling to androgen action: Identification of Smad3 as an androgen receptor coregulator in prostate cancer cells
    • Kang HY, Lin HK, Hu YC, Yeh S, Huang KF, Chang C. 2001. From transforming growth factor-β signaling to androgen action: identification of Smad3 as an androgen receptor coregulator in prostate cancer cells. Proc. Natl. Acad. Sci. USA 98:3018-23
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3018-3023
    • Kang, H.Y.1    Lin, H.K.2    Hu, Y.C.3    Yeh, S.4    Huang, K.F.5    Chang, C.6
  • 78
    • 0037113990 scopus 로고    scopus 로고
    • Differential modulation of androgen receptor-mediated transactivation by Smad3 and tumor suppressor Smad4
    • Kang HY, Huang KF, Chang SY, Ma WL, Lin WJ, Chang C. 2002. Differential modulation of androgen receptor-mediated transactivation by Smad3 and tumor suppressor Smad4. J. Biol. Chem. 277:43749-56
    • (2002) J. Biol. Chem , vol.277 , pp. 43749-43756
    • Kang, H.Y.1    Huang, K.F.2    Chang, S.Y.3    Ma, W.L.4    Lin, W.J.5    Chang, C.6
  • 79
    • 0037059735 scopus 로고    scopus 로고
    • The androgen receptor represses transforming growth factor-β signaling through interaction with Smad3
    • Chipuk JE, Cornelius SC, Pultz NJ, Jorgensen JS, Bonham MJ, et al. 2002. The androgen receptor represses transforming growth factor-β signaling through interaction with Smad3. J. Biol. Chem. 277:1240-48
    • (2002) J. Biol. Chem , vol.277 , pp. 1240-1248
    • Chipuk, J.E.1    Cornelius, S.C.2    Pultz, N.J.3    Jorgensen, J.S.4    Bonham, M.J.5
  • 80
    • 0036369222 scopus 로고    scopus 로고
    • Establishing a framework for the functional mammary gland: From endocrinology to morphology
    • Hovey RC, Trott JF, Vonderhaar BK. 2002. Establishing a framework for the functional mammary gland: from endocrinology to morphology. J. Mammary Gland Biol. Neoplasia 7:17-38
    • (2002) J. Mammary Gland Biol. Neoplasia , vol.7 , pp. 17-38
    • Hovey, R.C.1    Trott, J.F.2    Vonderhaar, B.K.3
  • 81
    • 0027537676 scopus 로고
    • Effects of epidermal growth factor, estrogen, and progestin on DNA synthesis in mammary cells in vivo are determined by the developmental state of the gland
    • Haslam SZ, Counterman LJ, Nummy KA. 1993. Effects of epidermal growth factor, estrogen, and progestin on DNA synthesis in mammary cells in vivo are determined by the developmental state of the gland. J. Cell Physiol. 155:72-78
    • (1993) J. Cell Physiol , vol.155 , pp. 72-78
    • Haslam, S.Z.1    Counterman, L.J.2    Nummy, K.A.3
  • 82
    • 0031938326 scopus 로고    scopus 로고
    • Role of epidermal growth factor in the acquisition of ovarian steroid hormone responsiveness in the normal mouse mammary gland
    • Ankrapp DP, Bennett JM, Haslam SZ. 1998. Role of epidermal growth factor in the acquisition of ovarian steroid hormone responsiveness in the normal mouse mammary gland. J. Cell Physiol. 174:251-60
    • (1998) J. Cell Physiol , vol.174 , pp. 251-260
    • Ankrapp, D.P.1    Bennett, J.M.2    Haslam, S.Z.3
  • 83
    • 0034656368 scopus 로고    scopus 로고
    • Side-branching in the mammary gland: The progesterone-Wnt connection
    • Robinson GW, Hennighausen L, Johnson PF. 2000. Side-branching in the mammary gland: the progesterone-Wnt connection. Genes Dev. 14:889-94
    • (2000) Genes Dev , vol.14 , pp. 889-894
    • Robinson, G.W.1    Hennighausen, L.2    Johnson, P.F.3
  • 84
    • 19444385094 scopus 로고    scopus 로고
    • Stem/progenitor cells in mouse mammary gland development and breast cancer
    • Li Y, Rosen JM. 2005. Stem/progenitor cells in mouse mammary gland development and breast cancer. J. Mammary Gland Biol. Neoplasia 10:17-24
    • (2005) J. Mammary Gland Biol. Neoplasia , vol.10 , pp. 17-24
    • Li, Y.1    Rosen, J.M.2
  • 85
    • 23044500236 scopus 로고    scopus 로고
    • Progesterone receptor isoforms A and B: Temporal and spatial differences in expression during murine mammary gland development
    • Aupperlee MD, Smith KT, Kariagina A, Haslam SZ. 2005. Progesterone receptor isoforms A and B: temporal and spatial differences in expression during murine mammary gland development. Endocrinology 146:3577-88
    • (2005) Endocrinology , vol.146 , pp. 3577-3588
    • Aupperlee, M.D.1    Smith, K.T.2    Kariagina, A.3    Haslam, S.Z.4
  • 86
    • 0037830132 scopus 로고    scopus 로고
    • Influence of estrogen plus progestin on breast cancer and mammography in healthy postmenopausal women: The Women's Health Initiative Randomized Trial
    • Chlebowski RT, Hendrix SL, Longer RD, Stefanick ML, Gass M, et al. 2003. Influence of estrogen plus progestin on breast cancer and mammography in healthy postmenopausal women: the Women's Health Initiative Randomized Trial. JAMA 289:3243-53
    • (2003) JAMA , vol.289 , pp. 3243-3253
    • Chlebowski, R.T.1    Hendrix, S.L.2    Longer, R.D.3    Stefanick, M.L.4    Gass, M.5
  • 87
    • 0036369960 scopus 로고    scopus 로고
    • Postmenopausal hormone replacement therapy: Effects on normal mammary gland in humans and in a mouse postmenopausal model
    • Haslam SZ, Osuch JR, Raafat AM, Hofseth LJ. 2002. Postmenopausal hormone replacement therapy: effects on normal mammary gland in humans and in a mouse postmenopausal model. J. Mammary Gland Biol. Neoplasia 7:93-105
    • (2002) J. Mammary Gland Biol. Neoplasia , vol.7 , pp. 93-105
    • Haslam, S.Z.1    Osuch, J.R.2    Raafat, A.M.3    Hofseth, L.J.4
  • 88
    • 33748134717 scopus 로고    scopus 로고
    • Estrogen receptor-α and progesterone receptor are expressed in label-retaining mammary epithelial cells that divide asymmetrically and retain their template DNA strands
    • Booth BW, Smith GH. 2006. Estrogen receptor-α and progesterone receptor are expressed in label-retaining mammary epithelial cells that divide asymmetrically and retain their template DNA strands. Breast Cancer Res. 8:R49
    • (2006) Breast Cancer Res , vol.8
    • Booth, B.W.1    Smith, G.H.2
  • 89
    • 33745685565 scopus 로고    scopus 로고
    • Ovarian steroids and the human breast: Regulation of stem cells and cell proliferation
    • Clarke RB. 2006. Ovarian steroids and the human breast: regulation of stem cells and cell proliferation. Maturitas 54: 327-34
    • (2006) Maturitas , vol.54 , pp. 327-334
    • Clarke, R.B.1
  • 90
    • 18344390450 scopus 로고    scopus 로고
    • The Ras-MAPK signal transduction pathway, cancer and chromatin remodeling
    • Dunn KL, Espino PS, Drobic B, He S, Davie JR. 2005. The Ras-MAPK signal transduction pathway, cancer and chromatin remodeling. Biochem. Cell Biol. 83:1-14
    • (2005) Biochem. Cell Biol , vol.83 , pp. 1-14
    • Dunn, K.L.1    Espino, P.S.2    Drobic, B.3    He, S.4    Davie, J.R.5
  • 91
    • 1642564339 scopus 로고    scopus 로고
    • Novel agents for the prevention of breast cancer: Targeting transcription factors and signal transduction pathways
    • Shen Q, Brown PH. 2003. Novel agents for the prevention of breast cancer: targeting transcription factors and signal transduction pathways. J. Mammary Gland Biol. Neoplasia 8:45-73
    • (2003) J. Mammary Gland Biol. Neoplasia , vol.8 , pp. 45-73
    • Shen, Q.1    Brown, P.H.2
  • 92
    • 28744431757 scopus 로고    scopus 로고
    • Advanced concepts in estrogen receptor biology and breast cancer endocrine resistance: Implicated role of growth factor signaling and estrogen receptor coregulators
    • Schiff R, Massarweh SA, Shou J, Bharwani L, Arpino G, et al. 2005. Advanced concepts in estrogen receptor biology and breast cancer endocrine resistance: implicated role of growth factor signaling and estrogen receptor coregulators. Cancer Chemother. Pharmacol. 56(Suppl. 1):10-20
    • (2005) Cancer Chemother. Pharmacol , vol.56 , Issue.SUPPL. 1 , pp. 10-20
    • Schiff, R.1    Massarweh, S.A.2    Shou, J.3    Bharwani, L.4    Arpino, G.5
  • 93
    • 0842291441 scopus 로고    scopus 로고
    • Making sense of cross-talk between steroid hormone receptors and intracellular signaling pathways: Who will have the last word?
    • Lange CA. 2004. Making sense of cross-talk between steroid hormone receptors and intracellular signaling pathways: Who will have the last word? Mol. Endocrinol. 18:269-78
    • (2004) Mol. Endocrinol , vol.18 , pp. 269-278
    • Lange, C.A.1
  • 94
    • 0030923066 scopus 로고    scopus 로고
    • Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo
    • Zhang Y, Beck CA, Poletti A, Clement JP, Prendergast P, et al. 1997. Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo. Mol. Endocrinol. 11:823-32
    • (1997) Mol. Endocrinol , vol.11 , pp. 823-832
    • Zhang, Y.1    Beck, C.A.2    Poletti, A.3    Clement, J.P.4    Prendergast, P.5
  • 95
    • 0029168036 scopus 로고
    • Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor
    • Zhang Y, Beck CA, Poletti A, Edwards DP, Weigel NL. 1995. Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor. Mol. Endocrinol. 9:1029-40
    • (1995) Mol. Endocrinol , vol.9 , pp. 1029-1040
    • Zhang, Y.1    Beck, C.A.2    Poletti, A.3    Edwards, D.P.4    Weigel, N.L.5
  • 96
    • 0026559680 scopus 로고
    • Hormone-induced progesterone receptor phosphorylation consists of sequential DNA-independent and DNA-dependent stages: Analysis with zinc-finger mutants and the progesterone antagonist ZK89299
    • Takimoto GS, Tasser DM, Eppert AC, and Horwitz KB. 1992. Hormone-induced progesterone receptor phosphorylation consists of sequential DNA-independent and DNA-dependent stages: analysis with zinc-finger mutants and the progesterone antagonist ZK89299. Proc. Natl. Acad. Sci. USA 89:3050-54
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3050-3054
    • Takimoto, G.S.1    Tasser, D.M.2    Eppert, A.C.3    Horwitz, K.B.4
  • 97
    • 0034027552 scopus 로고    scopus 로고
    • Association of the Ku autoantigen/DNA-dependent protein kinase holoenzyme and poly(ADP-ribose) polymerase with the DNA binding-domain of progesterone receptors
    • Sartorius CA, Takimoto GS, Richer JK, Tung L, Horwitz KB. 2000. Association of the Ku autoantigen/DNA-dependent protein kinase holoenzyme and poly(ADP-ribose) polymerase with the DNA binding-domain of progesterone receptors. J. Mol. Endocrinol. 24:165-82
    • (2000) J. Mol. Endocrinol , vol.24 , pp. 165-182
    • Sartorius, C.A.1    Takimoto, G.S.2    Richer, J.K.3    Tung, L.4    Horwitz, K.B.5
  • 98
    • 0027988153 scopus 로고
    • Identification of phosphorylation sites unique to the B form of human progesterone receptor. In vitro phosphorylation by casein kinase II
    • Zhang Y, Beck CA, Poletti A, Edwards DP, Weigel NL. 1994. Identification of phosphorylation sites unique to the B form of human progesterone receptor. In vitro phosphorylation by casein kinase II. J. Biol. Chem. 269:31034-40
    • (1994) J. Biol. Chem , vol.269 , pp. 31034-31040
    • Zhang, Y.1    Beck, C.A.2    Poletti, A.3    Edwards, D.P.4    Weigel, N.L.5
  • 99
    • 0033967491 scopus 로고    scopus 로고
    • Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome
    • Lange CA, Shen T, Horwitz KB. 2000. Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome. Proc. Natl. Acad. Sci. USA 97:1032-37
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1032-1037
    • Lange, C.A.1    Shen, T.2    Horwitz, K.B.3
  • 100
    • 0035726623 scopus 로고    scopus 로고
    • Transcriptional hyperactivity of human progesterone receptors is coupled to their ligand-dependent down-regulation by mitogen-activated protein kinase-dependent phosphorylation of serine 294
    • Shen T, Horwitz KB, Lange CA. 2001. Transcriptional hyperactivity of human progesterone receptors is coupled to their ligand-dependent down-regulation by mitogen-activated protein kinase-dependent phosphorylation of serine 294. Mol. Cell Biol. 21:6122-31
    • (2001) Mol. Cell Biol , vol.21 , pp. 6122-6131
    • Shen, T.1    Horwitz, K.B.2    Lange, C.A.3
  • 101
    • 0035896651 scopus 로고    scopus 로고
    • Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites
    • Knotts TA, Orkiszewski RS, Cook RG, Edwards DP, Weigel NL. 2001. Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites. J. Biol. Chem. 276:8475-83
    • (2001) J. Biol. Chem , vol.276 , pp. 8475-8483
    • Knotts, T.A.1    Orkiszewski, R.S.2    Cook, R.G.3    Edwards, D.P.4    Weigel, N.L.5
  • 102
    • 0001392322 scopus 로고    scopus 로고
    • AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor
    • Font de Mora J, Broun M. 2000. AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor. Mol. Cell Biol. 20:5041-47
    • (2000) Mol. Cell Biol , vol.20 , pp. 5041-5047
    • Font de Mora, J.1    Broun, M.2
  • 103
    • 11144274562 scopus 로고    scopus 로고
    • Cyclin-dependent kinase activity is required for progesterone receptor function: Novel role for cyelin A/Cdk2 as a progesterone receptor coactivator
    • Narayanan R, Adigun AA, Edwards DP, Weigel NL. 2005. Cyclin-dependent kinase activity is required for progesterone receptor function: novel role for cyelin A/Cdk2 as a progesterone receptor coactivator. Mol. Cell Biol. 25:264-77
    • (2005) Mol. Cell Biol , vol.25 , pp. 264-277
    • Narayanan, R.1    Adigun, A.A.2    Edwards, D.P.3    Weigel, N.L.4
  • 104
    • 0037305884 scopus 로고    scopus 로고
    • Heregulin induces transcriptional activation of the progesterone receptor by a mechanism that requires functional ErbB-2 and mitogen-activated protein kinase activation in breast cancer cells
    • Labriola L, Salatino M, Proietti CJ, Pecci A, Coso OA, et al. 2003. Heregulin induces transcriptional activation of the progesterone receptor by a mechanism that requires functional ErbB-2 and mitogen-activated protein kinase activation in breast cancer cells. Mol. Cell Biol. 23:1095-111
    • (2003) Mol. Cell Biol , vol.23 , pp. 1095-1111
    • Labriola, L.1    Salatino, M.2    Proietti, C.J.3    Pecci, A.4    Coso, O.A.5
  • 105
    • 10044257416 scopus 로고    scopus 로고
    • Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase 2
    • Pierson-Mullany LK, Lange CA. 2004. Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase 2. Mol. Cell Biol. 24:10542-57
    • (2004) Mol. Cell Biol , vol.24 , pp. 10542-10557
    • Pierson-Mullany, L.K.1    Lange, C.A.2
  • 106
    • 0029976989 scopus 로고    scopus 로고
    • Role of phosphorylation on DNA binding and transcriptional functions of human progesterone receptors
    • Takimoto CIS, Hovland AR, Tasset DM, Melville MY, Tung L, Horwitz KB. 1996. Role of phosphorylation on DNA binding and transcriptional functions of human progesterone receptors. J. Biol. Chem. 271:13308-16
    • (1996) J. Biol. Chem , vol.271 , pp. 13308-13316
    • Takimoto, C.I.S.1    Hovland, A.R.2    Tasset, D.M.3    Melville, M.Y.4    Tung, L.5    Horwitz, K.B.6
  • 107
    • 33646153793 scopus 로고    scopus 로고
    • How much is enough? Modulation of dose-response curve for steroid receptor-regulated gene expression by changing concentrations of transcription factor
    • Simons SSJ. 2006. How much is enough? Modulation of dose-response curve for steroid receptor-regulated gene expression by changing concentrations of transcription factor. Curr Top Med. Chem. 6:271-85
    • (2006) Curr Top Med. Chem , vol.6 , pp. 271-285
    • Simons, S.S.J.1
  • 108
    • 0042978662 scopus 로고    scopus 로고
    • MAP kinases couple multiple functions of human progesterone receptors: Degradation, transcriptional synergy, and nuclear association
    • Qiu M, Lange CA. 2003. MAP kinases couple multiple functions of human progesterone receptors: degradation, transcriptional synergy, and nuclear association. J. Steroid Biochem. Mol. Biol. 85:147-57
    • (2003) J. Steroid Biochem. Mol. Biol , vol.85 , pp. 147-157
    • Qiu, M.1    Lange, C.A.2
  • 109
    • 0024382236 scopus 로고
    • Phosphorylation on tyrosine of in vitro synthesized human estrogen receptor activates its hormone binding
    • Migliaccio A, Di Domenico M, Green S, de Falco A, Kajtaniak EL, et al. 1989. Phosphorylation on tyrosine of in vitro synthesized human estrogen receptor activates its hormone binding. Mol. Endocrinol. 3:1061-69
    • (1989) Mol. Endocrinol , vol.3 , pp. 1061-1069
    • Migliaccio, A.1    Di Domenico, M.2    Green, S.3    de Falco, A.4    Kajtaniak, E.L.5
  • 110
    • 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. 12:1150-60
    • (1993) EMBO J , vol.12 , pp. 1150-1160
    • Ali, S.1    Metzger, D.2    Bornert, J.M.3    Chambon, P.4
  • 111
    • 16244382046 scopus 로고    scopus 로고
    • Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity
    • Narayanan R, Edwards DP, Weigel NL. 2005. Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity. Mol. Cell Biol. 25:2885-98
    • (2005) Mol. Cell Biol , vol.25 , pp. 2885-2898
    • Narayanan, R.1    Edwards, D.P.2    Weigel, N.L.3
  • 112
    • 0023878411 scopus 로고
    • Progesterone receptor regulation in T47D human breast cancer cells: Analysis by density labeling of progesterone receptor synthesis and degradation and their modulation by progestin
    • Nardulli AM, Katzenellenbogen BS. 1988. Progesterone receptor regulation in T47D human breast cancer cells: analysis by density labeling of progesterone receptor synthesis and degradation and their modulation by progestin. Endocrinology 122:1532-40
    • (1988) Endocrinology , vol.122 , pp. 1532-1540
    • Nardulli, A.M.1    Katzenellenbogen, B.S.2
  • 113
    • 0024226756 scopus 로고
    • Human progesterone receptor transformation and nuclear down-regulation are independent of phosphorylation
    • Sheridan PL, Krett NL, Gordon JA, Horwitz KB. 1988. Human progesterone receptor transformation and nuclear down-regulation are independent of phosphorylation. Mol. Endo. 2:1329-42
    • (1988) Mol. Endo , vol.2 , pp. 1329-1342
    • Sheridan, P.L.1    Krett, N.L.2    Gordon, J.A.3    Horwitz, K.B.4
  • 115
    • 0027490328 scopus 로고
    • Modulators of cellular protein phosphorylation alter the trans-activation function of human progesterone receptor and the biological activity of progesterone antagonists
    • Edwards DP, Weigel NL, Nordeen SK, Beck CA. 1993. Modulators of cellular protein phosphorylation alter the trans-activation function of human progesterone receptor and the biological activity of progesterone antagonists. Breast Cancer Res. Treat. 27:41-56
    • (1993) Breast Cancer Res. Treat , vol.27 , pp. 41-56
    • Edwards, D.P.1    Weigel, N.L.2    Nordeen, S.K.3    Beck, C.A.4
  • 116
    • 0036683093 scopus 로고    scopus 로고
    • Phosphorylation- dependent ubiquitinylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase
    • Lin HK, Wang L, Hu YC, Altuwaijri S, Chang C. 2002. Phosphorylation- dependent ubiquitinylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase. EMBO J. 21:4037-48
    • (2002) EMBO J , vol.21 , pp. 4037-4048
    • Lin, H.K.1    Wang, L.2    Hu, Y.C.3    Altuwaijri, S.4    Chang, C.5
  • 117
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani M, Tansey WP. 2003. How the ubiquitin-proteasome system controls transcription. Nat. Rev. Mol. Cell Biol. 4:192-201
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 118
    • 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 5:939-48
    • (2000) Mol. Cell , vol.5 , pp. 939-948
    • Lonard, D.M.1    Nawaz, Z.2    Smith, C.L.3    O'Malley, B.W.4
  • 119
    • 0029669930 scopus 로고    scopus 로고
    • Tyrosine kinase/p21 tras/MAP-kinase pathway activation by estradiol-receptor complex in MCE-7 cells
    • Migliaccio A, Di Domenico M, Castoria G, de Falco A, Bontempo P, et al. 1996. Tyrosine kinase/p21 tras/MAP-kinase pathway activation by estradiol-receptor complex in MCE-7 cells. EMBO J. 15:1292-300
    • (1996) EMBO J , vol.15 , pp. 1292-1300
    • Migliaccio, A.1    Di Domenico, M.2    Castoria, G.3    de Falco, A.4    Bontempo, P.5
  • 120
    • 0032036584 scopus 로고
    • Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-talk with estrogen receptor
    • 2008
    • Migliaccio A, Piccolo D, Castoria G, Di Domenico M, Bilancio A, et al. 1998. Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-talk with estrogen receptor. EMBO J. 17:2008-18
    • (1918) EMBO J , vol.17
    • Migliaccio, A.1    Piccolo, D.2    Castoria, G.3    Di Domenico, M.4    Bilancio, A.5
  • 121
    • 0034852802 scopus 로고    scopus 로고
    • Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases
    • Boonyaratanakornkit V, Scott MP, Ribon V, Sherman L, Anderson SM, et al. 2001. Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases. Mol. Cell8:269-80
    • (2001) Mol. Cell , vol.8 , pp. 269-280
    • Boonyaratanakornkit, V.1    Scott, M.P.2    Ribon, V.3    Sherman, L.4    Anderson, S.M.5
  • 122
    • 0034675994 scopus 로고    scopus 로고
    • Steroid-induced androgen receptor-estradiol receptor p-Src complex triggers prostate cancel-cell proliferation
    • Migliaccio A, Castoria G, Di Domenico M, de Faleo A, Bilancio A, et al. 2000. Steroid-induced androgen receptor-estradiol receptor p-Src complex triggers prostate cancel-cell proliferation. EMBO J. 19:5406-17
    • (2000) EMBO J , vol.19 , pp. 5406-5417
    • Migliaccio, A.1    Castoria, G.2    Di Domenico, M.3    de Faleo, A.4    Bilancio, A.5
  • 124
    • 0037371863 scopus 로고    scopus 로고
    • Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Frk pathway in mammalian cells
    • Ballare C, Uhrig M, Bechtold T, Sancho E, Di Domenico M, et al. 2003. Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Frk pathway in mammalian cells. Mol. Cell Biol. 23:1994-2008
    • (2003) Mol. Cell Biol , vol.23 , pp. 1994-2008
    • Ballare, C.1    Uhrig, M.2    Bechtold, T.3    Sancho, E.4    Di Domenico, M.5
  • 125
    • 0037069418 scopus 로고    scopus 로고
    • Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade
    • Wong C, McNally C, Nickbarg E, Komm B, Cheskis B. 2002. Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc. Natl. Acad. Sci. USA 99:14783-88
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14783-14788
    • Wong, C.1    McNally, C.2    Nickbarg, E.3    Komm, B.4    Cheskis, B.5
  • 126
    • 23744506856 scopus 로고    scopus 로고
    • The modulator of nongenomic actions ofthe estrogen receptor (MNAR) regulates transcription- independent androgen receptor-mediated signaling: Evidence that MNAR participates in G protein-regulated meiosis in Xenopus laevis oocytes
    • Haas D, White SN, Lutz LB, Rasar M, Hammes SR. 2005. The modulator of nongenomic actions ofthe estrogen receptor (MNAR) regulates transcription- independent androgen receptor-mediated signaling: evidence that MNAR participates in G protein-regulated meiosis in Xenopus laevis oocytes. Mol. Endocrinol. 19:2035-46
    • (2005) Mol. Endocrinol , vol.19 , pp. 2035-2046
    • Haas, D.1    White, S.N.2    Lutz, L.B.3    Rasar, M.4    Hammes, S.R.5
  • 127
    • 4944237502 scopus 로고    scopus 로고
    • Changes in androgen receptor nongenotropic signaling correlate with transition of LNCaP cells to androgen independence
    • Unni E, Sun S, Nan B, McPhaul MJ, Cheskis B, et al. 2004. Changes in androgen receptor nongenotropic signaling correlate with transition of LNCaP cells to androgen independence. Cancer Res. 64:7156-68
    • (2004) Cancer Res , vol.64 , pp. 7156-7168
    • Unni, E.1    Sun, S.2    Nan, B.3    McPhaul, M.J.4    Cheskis, B.5
  • 128
    • 27544435790 scopus 로고    scopus 로고
    • The role of DOC-2/DAB2 in modulating androgen receptor-mediated cell growth via the nongenomic c-Src-mediated pathway in normal prostatic epithelium and cancer
    • Zhoul J, Hernandez G, Tu SW, Huang CL, Tseng CP, Hsieh JT. 2005. The role of DOC-2/DAB2 in modulating androgen receptor-mediated cell growth via the nongenomic c-Src-mediated pathway in normal prostatic epithelium and cancer. Cancer Res. 65:9906-13
    • (2005) Cancer Res , vol.65 , pp. 9906-9913
    • Zhoul, J.1    Hernandez, G.2    Tu, S.W.3    Huang, C.L.4    Tseng, C.P.5    Hsieh, J.T.6
  • 129
    • 0344885580 scopus 로고    scopus 로고
    • Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor
    • Zhu Y, Bond J, Thomas P. 2003. Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor. Proc. Natl. Acad. Sci. USA 100:2237-42
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2237-2242
    • Zhu, Y.1    Bond, J.2    Thomas, P.3
  • 130
    • 13544276888 scopus 로고    scopus 로고
    • Progesterone receptors induce cell cycle progression via activation of mitogen-activated protein kinases
    • Skildum A, Faivre E, Lange CA. 2005. Progesterone receptors induce cell cycle progression via activation of mitogen-activated protein kinases. Mol. Endocrinol. 19:327-39
    • (2005) Mol. Endocrinol , vol.19 , pp. 327-339
    • Skildum, A.1    Faivre, E.2    Lange, C.A.3
  • 131
    • 33646336602 scopus 로고    scopus 로고
    • MAPK signal specificity: The right place at the right time
    • Murphy LO, Blenis J. 2006. MAPK signal specificity: the right place at the right time. Trends Biochem. Sci. 31:268-75
    • (2006) Trends Biochem. Sci , vol.31 , pp. 268-275
    • Murphy, L.O.1    Blenis, J.2
  • 132
    • 0035714726 scopus 로고    scopus 로고
    • Adaptive hypersensitivity to estradiol: Potential mechanism for secondary hormonal responses in breast cancer patients
    • Santen R, Jeng MH, Wang JP, Song R, Masamura S, et al. 2001. Adaptive hypersensitivity to estradiol: potential mechanism for secondary hormonal responses in breast cancer patients. J. Steroid Biochem. Mol. Biol. 79:115-25
    • (2001) J. Steroid Biochem. Mol. Biol , vol.79 , pp. 115-125
    • Santen, R.1    Jeng, M.H.2    Wang, J.P.3    Song, R.4    Masamura, S.5
  • 133
    • 33745601067 scopus 로고    scopus 로고
    • Evaluation of the prognostic significance of androgen receptor expression in metastatic breast cancer
    • Schippinger W, Regitnig P, Dandachi N, Wernecke KD, Bauernhofer T, et al. 2006. Evaluation of the prognostic significance of androgen receptor expression in metastatic breast cancer. Virchows Arch. 449:24-30
    • (2006) Virchows Arch , vol.449 , pp. 24-30
    • Schippinger, W.1    Regitnig, P.2    Dandachi, N.3    Wernecke, K.D.4    Bauernhofer, T.5
  • 134
    • 33745603978 scopus 로고    scopus 로고
    • An estrogen receptor-negative breast cancer subset characterized by a hormonally regulated transcriptional program and response to androgen
    • Doane AS, Danso M, Lal P, Donaton M, Zhang L, et al. 2006. An estrogen receptor-negative breast cancer subset characterized by a hormonally regulated transcriptional program and response to androgen. Oncogene 25:3994-4008
    • (2006) Oncogene , vol.25 , pp. 3994-4008
    • Doane, A.S.1    Danso, M.2    Lal, P.3    Donaton, M.4    Zhang, L.5
  • 136
    • 0032493489 scopus 로고    scopus 로고
    • Multiple G1 regulatory elements control the androgen-dependent proliferation of prostatic carcinoma cells
    • Knudsen KE, Arden KC, Cavenee WK. 1998. Multiple G1 regulatory elements control the androgen-dependent proliferation of prostatic carcinoma cells. J. Biol. Chem. 273:20213-22
    • (1998) J. Biol. Chem , vol.273 , pp. 20213-20222
    • Knudsen, K.E.1    Arden, K.C.2    Cavenee, W.K.3
  • 137
    • 0028331092 scopus 로고
    • Amplification and overexpression of cyclin D1 in breast cancer detected by immunohistochemical staining
    • Gillett C, Fantl V, Smith R, Fisher C, Bartek J, et al. 1994. Amplification and overexpression of cyclin D1 in breast cancer detected by immunohistochemical staining. Cancer Res. 54:1812-17
    • (1994) Cancer Res , vol.54 , pp. 1812-1817
    • Gillett, C.1    Fantl, V.2    Smith, R.3    Fisher, C.4    Bartek, J.5
  • 138
    • 0033833295 scopus 로고    scopus 로고
    • Kaltz-Wittmer C, Klenk U, Glaessgen A, Aust DE, Diebold J, et al. 2000. FISH analysis of gene aberrations (MYC, CCND1, ERBB2, RB, and AR) in advanced prostatic carcinomas before and after androgen deprivation therapy. Lab. Invest. 80:1455-64
    • Kaltz-Wittmer C, Klenk U, Glaessgen A, Aust DE, Diebold J, et al. 2000. FISH analysis of gene aberrations (MYC, CCND1, ERBB2, RB, and AR) in advanced prostatic carcinomas before and after androgen deprivation therapy. Lab. Invest. 80:1455-64
  • 139
    • 0033563091 scopus 로고    scopus 로고
    • D-type cyclins complex with the androgen receptor and inhibit its transcriptional transactivation ability
    • Knudsen KE, Cavenee WK, Arden KC. 1999. D-type cyclins complex with the androgen receptor and inhibit its transcriptional transactivation ability. Cancer Res. 59:2297-301
    • (1999) Cancer Res , vol.59 , pp. 2297-2301
    • Knudsen, K.E.1    Cavenee, W.K.2    Arden, K.C.3
  • 140
    • 33144474074 scopus 로고    scopus 로고
    • Cyclin D1b variant influences prostate cancer growth through aberrant androgen receptor regulation
    • Burd CJ, Petre CE, Morey LM, Wang Y, Revelo MP, et al. 2006. Cyclin D1b variant influences prostate cancer growth through aberrant androgen receptor regulation. Proc. Natl. Acad. Sci. USA 103:2190-95
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2190-2195
    • Burd, C.J.1    Petre, C.E.2    Morey, L.M.3    Wang, Y.4    Revelo, M.P.5
  • 141
    • 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
  • 142
    • 33746600263 scopus 로고    scopus 로고
    • Estrogen receptor target gene: An evolving concept
    • Carroll JS, Brown M. 2006. Estrogen receptor target gene: an evolving concept. Mol. Endocrinol. 20:1707-14
    • (2006) Mol. Endocrinol , vol.20 , pp. 1707-1714
    • Carroll, J.S.1    Brown, M.2
  • 143
    • 0036799626 scopus 로고    scopus 로고
    • Distinct nongenomic signal transduction pathways controlled by 17β-estradiol regulate DNA synthesis and cyclin D, gene transcription in HepG2 cells
    • Marino M, Acconcia F, Bresciani F, Weisz A, Trentalance A. 2002. Distinct nongenomic signal transduction pathways controlled by 17β-estradiol regulate DNA synthesis and cyclin D, gene transcription in HepG2 cells. Mol. Biol. Cell 13:3720-29
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3720-3729
    • Marino, M.1    Acconcia, F.2    Bresciani, F.3    Weisz, A.4    Trentalance, A.5
  • 144
    • 0034463134 scopus 로고    scopus 로고
    • Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody
    • Clemm DL, Sherman L, Boonyaratanakornkit V, Schrader WT, Weigel NL, Edwards DP. 2000. Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody. Mol. Endocrinol. 14:52-65
    • (2000) Mol. Endocrinol , vol.14 , pp. 52-65
    • Clemm, D.L.1    Sherman, L.2    Boonyaratanakornkit, V.3    Schrader, W.T.4    Weigel, N.L.5    Edwards, D.P.6
  • 145
    • 0028970609 scopus 로고
    • Transforming p21 ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions
    • Albanese C, Johnson J, Watanabe C, Eklund N, Vu D, et al. 1995. Transforming p21 ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions. J. Biol. Chem. 270:23589-97
    • (1995) J. Biol. Chem , vol.270 , pp. 23589-23597
    • Albanese, C.1    Johnson, J.2    Watanabe, C.3    Eklund, N.4    Vu, D.5
  • 146
    • 0030612164 scopus 로고    scopus 로고
    • Control of the G1/S transition
    • Reed SI. 1997. Control of the G1/S transition. Cancer Surv. 29:7-23
    • (1997) Cancer Surv , vol.29 , pp. 7-23
    • Reed, S.I.1
  • 147
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr CJ. 1996. Cancer cell cycles. Science 274:1672-77
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 148
    • 0029910364 scopus 로고    scopus 로고
    • Convergence of mitogenic signaling cascades from diverse classes of receptors at the cyclin D-cyclin-dependent kinase-pRb-controlled G1 checkpoint
    • Lukas J, Bartkova J, Bartek J. 1996. Convergence of mitogenic signaling cascades from diverse classes of receptors at the cyclin D-cyclin-dependent kinase-pRb-controlled G1 checkpoint. Mol. Cell Biol. 16:6917-25
    • (1996) Mol. Cell Biol , vol.16 , pp. 6917-6925
    • Lukas, J.1    Bartkova, J.2    Bartek, J.3
  • 149
    • 0032477854 scopus 로고    scopus 로고
    • Assembly of cyclin D-dependent kinase and titration of p27Kip1 regulated by mitogen-activated protein kinase kinase (MEK1)
    • Cheng M, Sexl V, Sherr CJ, Roussel MF. 1998. Assembly of cyclin D-dependent kinase and titration of p27Kip1 regulated by mitogen-activated protein kinase kinase (MEK1). Proc. Natl. Acad. Sci. USA 95:1091-96
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1091-1096
    • Cheng, M.1    Sexl, V.2    Sherr, C.J.3    Roussel, M.F.4
  • 150
    • 0033959495 scopus 로고    scopus 로고
    • Relation of Bcl-2 expression to androgen receptor, p21WF1/C1P1, and cyclin D1 status in prostate cancer
    • Kolar Z, Murray PG, Scott K, Harrison A, Vojtesek B, Dusek J. 2000. Relation of Bcl-2 expression to androgen receptor, p21WF1/C1P1, and cyclin D1 status in prostate cancer. Mol. Pathol. 53:15-18
    • (2000) Mol. Pathol , vol.53 , pp. 15-18
    • Kolar, Z.1    Murray, P.G.2    Scott, K.3    Harrison, A.4    Vojtesek, B.5    Dusek, J.6
  • 151
    • 0033520806 scopus 로고    scopus 로고
    • Prostate cancer cell cycle regulators: Response to androgen withdrawal and development of androgen independence
    • Agus DB, Cordon-Cardo CC, Fox W, Drobnjak M, Koff A, et al. 1999. Prostate cancer cell cycle regulators: response to androgen withdrawal and development of androgen independence. J. Natl. Cancer lust. 91:1869-76
    • (1999) J. Natl. Cancer lust , vol.91 , pp. 1869-1876
    • Agus, D.B.1    Cordon-Cardo, C.C.2    Fox, W.3    Drobnjak, M.4    Koff, A.5
  • 152
    • 0028889751 scopus 로고
    • Mice lacking cyclin D1 are small and show defects in eve and mammary gland development
    • Fantl V, Stamp G, Andrews A, Rosewell I, Dickson C. 1995. Mice lacking cyclin D1 are small and show defects in eve and mammary gland development. Genes Dev. 9:2364-72
    • (1995) Genes Dev , vol.9 , pp. 2364-2372
    • Fantl, V.1    Stamp, G.2    Andrews, A.3    Rosewell, I.4    Dickson, C.5
  • 153
    • 0029111934 scopus 로고
    • Cyclin D1 provides a link between development and oncogenesis in the retina and breast
    • Sicinski P, Donaher JL, Parker SB, Li T, Fazeli A, et al. 1995. Cyclin D1 provides a link between development and oncogenesis in the retina and breast. Cell 82:621-30
    • (1995) Cell , vol.82 , pp. 621-630
    • Sicinski, P.1    Donaher, J.L.2    Parker, S.B.3    Li, T.4    Fazeli, A.5
  • 155
    • 0042354669 scopus 로고    scopus 로고
    • A mechanism of cyclin D1 action encoded in the patterns of gene expression in human cancer
    • Lamb J, Ramaswamy S, Ford HL, Contreras B, Martinez RV, et al. 2003. A mechanism of cyclin D1 action encoded in the patterns of gene expression in human cancer. Cell 114:323-34
    • (2003) Cell , vol.114 , pp. 323-334
    • Lamb, J.1    Ramaswamy, S.2    Ford, H.L.3    Contreras, B.4    Martinez, R.V.5
  • 156
    • 0032525340 scopus 로고    scopus 로고
    • C/EBPβ, but not C/EBPα, is essential tor ductal morphogenesis, lobuloalveolar proliferation, and functional differentiation in the mouse mammary gland
    • Seagroves TN, Krnacik S, Raught B, Gay J, Burgess-Beusse B, et al. 1998. C/EBPβ, but not C/EBPα, is essential tor ductal morphogenesis, lobuloalveolar proliferation, and functional differentiation in the mouse mammary gland. Genes Dev. 12:1917-28
    • (1998) Genes Dev , vol.12 , pp. 1917-1928
    • Seagroves, T.N.1    Krnacik, S.2    Raught, B.3    Gay, J.4    Burgess-Beusse, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.