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Volumn 85, Issue 2-5, 2003, Pages 147-157

MAP kinases couple multiple functions of human progesterone receptors: Degradation, transcriptional synergy, and nuclear association

Author keywords

Breast cancer; Mitogen activated protein kinase; Phosphorylation; Progesterone receptors; Ubiquitin

Indexed keywords

GESTAGEN; GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; PEPTIDE; PROGESTERONE RECEPTOR; PROTEASOME; SERINE; STEROID HORMONE; STEROID RECEPTOR; UBIQUITIN;

EID: 0042978662     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(03)00221-8     Document Type: Conference Paper
Times cited : (85)

References (72)
  • 4
    • 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 A.C. Co-operation of progestational steroids with epidermal growth factor in activation of gene expression in mammary tumor cells. J. Steroid Biochem. Mol. Biol. 40(1-3):1991;239-245.
    • (1991) J. Steroid Biochem. Mol. Biol. , vol.40 , Issue.1-3 , pp. 239-245
    • Krusekopf, S.1    Chauchereau, A.2    Milgrom, E.3    Henderson, D.4    Cato, A.C.5
  • 5
    • 0026086987 scopus 로고
    • Progesterone augments proliferation induced by epidermal growth factor in a feline mammary adenocarcinoma cell line
    • Modiano J.F., Kokai Y., Weiner D.B., Pykett M.J., Nowell P.C., Lyttle C.R. Progesterone augments proliferation induced by epidermal growth factor in a feline mammary adenocarcinoma cell line. J. Cell. Biochem. 45(2):1991;196-206.
    • (1991) J. Cell. Biochem. , vol.45 , Issue.2 , pp. 196-206
    • Modiano, J.F.1    Kokai, Y.2    Weiner, D.B.3    Pykett, M.J.4    Nowell, P.C.5    Lyttle, C.R.6
  • 6
    • 0028266876 scopus 로고
    • EGF receptor expression, regulation, and function in breast cancer
    • Chrysogelos S.A., Dickson R.B. EGF receptor expression, regulation, and function in breast cancer. Breast Cancer Res. Treat. 29(1):1994;29-40.
    • (1994) Breast Cancer Res. Treat. , vol.29 , Issue.1 , pp. 29-40
    • Chrysogelos, S.A.1    Dickson, R.B.2
  • 7
    • 0022638071 scopus 로고
    • Progestin regulation of epidermal growth factor receptor in human mammary carcinoma cells
    • Murphy L.J., Sutherland R.L., Stead B., Murphy L.C., Lazarus L. Progestin regulation of epidermal growth factor receptor in human mammary carcinoma cells. Cancer Res. 46(2):1986;728-734.
    • (1986) Cancer Res. , vol.46 , Issue.2 , pp. 728-734
    • Murphy, L.J.1    Sutherland, R.L.2    Stead, B.3    Murphy, L.C.4    Lazarus, L.5
  • 8
    • 0023780295 scopus 로고
    • Decreased progesterone binding and attenuated progesterone action in cultured human breast carcinoma cells treated with epidermal growth factor
    • Sarup J.C., Rao K.V., Fox C.F. Decreased progesterone binding and attenuated progesterone action in cultured human breast carcinoma cells treated with epidermal growth factor. Cancer Res. 48(18):1988;5071-5078.
    • (1988) Cancer Res. , vol.48 , Issue.18 , pp. 5071-5078
    • Sarup, J.C.1    Rao, K.V.2    Fox, C.F.3
  • 9
    • 0032553304 scopus 로고    scopus 로고
    • Convergence of progesterone and epidermal growth factor signaling in breast cancer. Potentiation of mitogen-activated protein kinase pathways
    • Lange C.A., Richer J.K., Shen T., Horwitz K.B. Convergence of progesterone and epidermal growth factor signaling in breast cancer. Potentiation of mitogen-activated protein kinase pathways. J. Biol. Chem. 273(47):1998;31308-31316.
    • (1998) J. Biol. Chem. , vol.273 , Issue.47 , pp. 31308-31316
    • Lange, C.A.1    Richer, J.K.2    Shen, T.3    Horwitz, K.B.4
  • 10
    • 0032553553 scopus 로고    scopus 로고
    • Convergence of progesterone with growth factor and cytokine signaling in breast cancer. Progesterone receptors regulate signal transducers and activators of transcription expression and activity
    • Richer J.K., Lange C.A., Manning N.G., Owen G., Powell R., Horwitz K.B. Convergence of 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(47):1998;31317-31326.
    • (1998) J. Biol. Chem. , vol.273 , Issue.47 , 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
    • 0033305372 scopus 로고    scopus 로고
    • Hypothesis: Progesterone primes breast cancer cells for cross-talk with proliferative or antiproliferative signals
    • Lange C.A., Richer J.K., Horwitz K.B. Hypothesis: progesterone primes breast cancer cells for cross-talk with proliferative or antiproliferative signals. Mol. Endocrinol. 13(6):1999;829-836.
    • (1999) Mol. Endocrinol. , vol.13 , Issue.6 , pp. 829-836
    • Lange, C.A.1    Richer, J.K.2    Horwitz, K.B.3
  • 12
    • 0034614490 scopus 로고    scopus 로고
    • Signaling - 2000 and beyond
    • Hunter T. Signaling - 2000 and beyond. Cell. 100(1):2000;113-127.
    • (2000) Cell , vol.100 , Issue.1 , pp. 113-127
    • Hunter, T.1
  • 13
    • 0028074621 scopus 로고
    • Ras-dependent growth factor regulation of MEK kinase in PC12 cells
    • Lange-Carter C.A., Johnson G.L. Ras-dependent growth factor regulation of MEK kinase in PC12 cells. Science. 265(5177):1994;1458-1461.
    • (1994) Science , vol.265 , Issue.5177 , pp. 1458-1461
    • Lange-Carter, C.A.1    Johnson, G.L.2
  • 15
    • 0035726623 scopus 로고    scopus 로고
    • Transcriptional hyperactivity of human progesterone receptors is coupled to their ligand-dependent downregulation by mitogen-activated protein kinase-dependent phosphorylation of serine 294
    • Shen T., Horwitz K.B., Lange C.A. Transcriptional hyperactivity of human progesterone receptors is coupled to their ligand-dependent downregulation by mitogen-activated protein kinase-dependent phosphorylation of serine 294. Mol. Cell. Biol. 21(18):2001;6122-6131.
    • (2001) Mol. Cell. Biol. , vol.21 , Issue.18 , pp. 6122-6131
    • Shen, T.1    Horwitz, K.B.2    Lange, C.A.3
  • 18
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-ras that binds and phosphorylates the c-jun activation domain
    • Derijard B., Hibi M., Wu I.H., Barrett T., Su B., Deng T., Karin M., Davis R.J. JNK1: a protein kinase stimulated by UV light and Ha-ras that binds and phosphorylates the c-jun activation domain. Cell. 76(6):1994;1025-1037.
    • (1994) Cell , vol.76 , Issue.6 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 19
    • 0023609199 scopus 로고
    • Stimulation of c-myc oncogene expression associated with estrogen induced proliferation of human breast cancer cells
    • Dubik D., Dembinski T.C., Shiu R.P.C. Stimulation of c-myc oncogene expression associated with estrogen induced proliferation of human breast cancer cells. Cancer Res. 47:1987;6517-6521.
    • (1987) Cancer Res. , vol.47 , pp. 6517-6521
    • Dubik, D.1    Dembinski, T.C.2    Shiu, R.P.C.3
  • 20
    • 0025912060 scopus 로고
    • Differential regulation of c-myc by progestins and antiestrogens in T47D human breast cancer cells
    • Wong M.S., Murphy L.C. Differential regulation of c-myc by progestins and antiestrogens in T47D human breast cancer cells. J. Steroid Biochem. Mol. Biol. 39(1):1991;39-44.
    • (1991) J. Steroid Biochem. Mol. Biol. , vol.39 , Issue.1 , pp. 39-44
    • Wong, M.S.1    Murphy, L.C.2
  • 21
    • 0027527240 scopus 로고
    • Effects of the progestin antagonist Ru 486 on T47D breast cancer cell cycle kinetics and cell cycle regulatory genes
    • Musgrove E.A., Sutherland R.L. Effects of the progestin antagonist Ru 486 on T47D breast cancer cell cycle kinetics and cell cycle regulatory genes. Biochem. Biophys. Res. Commun. 195(3):1993;1184-1190.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , Issue.3 , pp. 1184-1190
    • Musgrove, E.A.1    Sutherland, R.L.2
  • 22
    • 0025504571 scopus 로고
    • Neoplastic transformation of mouse mammary epithelial cells by deregulated myc expression
    • Telang N.T., Osborne M.P., Sweterlitch L.A., Narayaman R. Neoplastic transformation of mouse mammary epithelial cells by deregulated myc expression. Cell. Regul. 1(11):1990;863-872.
    • (1990) Cell. Regul. , vol.1 , Issue.11 , pp. 863-872
    • Telang, N.T.1    Osborne, M.P.2    Sweterlitch, L.A.3    Narayaman, R.4
  • 24
    • 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 C.A., Shen T., Horwitz K.B. Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 97(3):2000;1032-1037.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.3 , pp. 1032-1037
    • Lange, C.A.1    Shen, T.2    Horwitz, K.B.3
  • 26
    • 0030916647 scopus 로고    scopus 로고
    • Prolactin, epidermal growth factor or transforming growth factor-alpha activate a mammary cell-specific enhancer in mouse mammary tumor virus-long terminal repeat
    • Haraguchi S., Good R.A., Engelman R.W., Greene S., Day N.K. Prolactin, epidermal growth factor or transforming growth factor-alpha activate a mammary cell-specific enhancer in mouse mammary tumor virus-long terminal repeat. Mol. Cell. Endocrinol. 129(2):1997;145-155.
    • (1997) Mol. Cell. Endocrinol. , vol.129 , Issue.2 , pp. 145-155
    • Haraguchi, S.1    Good, R.A.2    Engelman, R.W.3    Greene, S.4    Day, N.K.5
  • 27
    • 0035896651 scopus 로고    scopus 로고
    • Identification of a phosphorylation site in the hinge region of human progesterone receptor and additional amino-terminal phosphorylation sites
    • Knotts T.A., Orkiszewski R.S., Cook R.G., Edwards D.P., Weigel N.L. Identification of a phosphorylation site in the hinge region of human progesterone receptor and additional amino-terminal phosphorylation sites. J. Biol. Chem. 276(11):2001;8475-8483.
    • (2001) J. Biol. Chem. , vol.276 , Issue.11 , pp. 8475-8483
    • Knotts, T.A.1    Orkiszewski, R.S.2    Cook, R.G.3    Edwards, D.P.4    Weigel, N.L.5
  • 28
    • 0023640540 scopus 로고
    • Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases
    • Rao K.V., Peralta W.D., Greene G.L., Fox C.F. Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases. Biochem. Biophys. Res. Commun. 146(3):1987;1357-1365.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , Issue.3 , pp. 1357-1365
    • Rao, K.V.1    Peralta, W.D.2    Greene, G.L.3    Fox, C.F.4
  • 29
    • 0027499790 scopus 로고
    • Progesterone receptor phosphorylation - Complexities in defining a functional role
    • Takimoto G., Horwitz K. Progesterone receptor phosphorylation - complexities in defining a functional role. Trends Endocrinol. Metab. 4:1993;1-7.
    • (1993) Trends Endocrinol. Metab. , vol.4 , pp. 1-7
    • Takimoto, G.1    Horwitz, K.2
  • 30
    • 0029855010 scopus 로고    scopus 로고
    • Steroid hormone receptors and their regulation by phosphorylation
    • Weigel N.L. Steroid hormone receptors and their regulation by phosphorylation. Biochem. J. 319(3):1996;657-667.
    • (1996) Biochem. J. , vol.319 , Issue.3 , pp. 657-667
    • Weigel, N.L.1
  • 31
    • 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 C.A., Poletti A., Edwards D.P., Weigel N.L. Identification of phosphorylation sites unique to the B form of human progesterone receptor. In vitro phosphorylation by casein kinase II. J. Biol. Chem. 269(49):1994;31034-31040.
    • (1994) J. Biol. Chem. , vol.269 , Issue.49 , pp. 31034-31040
    • Zhang, Y.1    Beck, C.A.2    Poletti, A.3    Edwards, D.P.4    Weigel, N.L.5
  • 32
    • 0033651439 scopus 로고    scopus 로고
    • MEKK1 activation of human estrogen receptor-alpha and stimulation of the agonistic activity of 4-hydroxytamoxifen in endometrial and ovarian cancer cells (in process citation)
    • Lee H., Jiang F., Wang Q., Nicosia S.V., Yang J., Su B., Bai W. MEKK1 activation of human estrogen receptor-alpha and stimulation of the agonistic activity of 4-hydroxytamoxifen in endometrial and ovarian cancer cells (in process citation). Mol. Endocrinol. 14(11):2000;1882-1896.
    • (2000) Mol. Endocrinol. , vol.14 , Issue.11 , pp. 1882-1896
    • Lee, H.1    Jiang, F.2    Wang, Q.3    Nicosia, S.V.4    Yang, J.5    Su, B.6    Bai, W.7
  • 34
    • 0030946366 scopus 로고    scopus 로고
    • Hyperexpression of mitogen-activated protein kinase in human breast cancer
    • Sivaraman V.S., Wang H., Nuovo G.J., Malbon C.C. Hyperexpression of mitogen-activated protein kinase in human breast cancer. J. Clin. Invest. 99(7):1997;1478-1483.
    • (1997) J. Clin. Invest. , vol.99 , Issue.7 , pp. 1478-1483
    • Sivaraman, V.S.1    Wang, H.2    Nuovo, G.J.3    Malbon, C.C.4
  • 35
    • 0027215820 scopus 로고
    • A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf
    • Lange-Carter C.A., Pleiman C.M., Gardner A.M., Blumer K.J., Johnson G.L. A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf. Science. 260(5106):1993;315-319.
    • (1993) Science , vol.260 , Issue.5106 , pp. 315-319
    • Lange-Carter, C.A.1    Pleiman, C.M.2    Gardner, A.M.3    Blumer, K.J.4    Johnson, G.L.5
  • 36
    • 0035929585 scopus 로고    scopus 로고
    • The human estrogen receptor-alpha is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators
    • Wijayaratne A.L., McDonnell D.P. The human estrogen receptor-alpha is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators. J. Biol. Chem. 276(38):2001;35684-35692.
    • (2001) J. Biol. Chem. , vol.276 , Issue.38 , pp. 35684-35692
    • Wijayaratne, A.L.1    McDonnell, D.P.2
  • 38
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize myc
    • Salghetti S.E., Kim S.Y., Tansey W.P. Destruction of myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize myc. EMBO J. 18(3):1999;717-726.
    • (1999) EMBO J. , vol.18 , Issue.3 , pp. 717-726
    • Salghetti, S.E.1    Kim, S.Y.2    Tansey, W.P.3
  • 39
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the scf ubiquitin-ligase complex
    • Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W. F-box proteins are receptors that recruit phosphorylated substrates to the scf ubiquitin-ligase complex. Cell. 91(2):1997;209-219.
    • (1997) Cell , vol.91 , Issue.2 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 41
    • 0034724166 scopus 로고    scopus 로고
    • Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis
    • Salghetti S.E., Muratani M., Wijnen H., Futcher B., Tansey W.P. Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis. Proc. Natl. Acad. Sci. U.S.A. 97(7):2000;3118-3123.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.7 , pp. 3118-3123
    • Salghetti, S.E.1    Muratani, M.2    Wijnen, H.3    Futcher, B.4    Tansey, W.P.5
  • 42
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • (see comments)
    • Glotzer M., Murray A.W., Kirschner M.W. Cyclin is degraded by the ubiquitin pathway. Nature. 349(6305):1991;132-138. (see comments).
    • (1991) Nature , vol.349 , Issue.6305 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 43
    • 0029787091 scopus 로고    scopus 로고
    • Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates
    • King R.W., Glotzer M., Kirschner M.W. Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates. Mol. Biol. Cell. 7(9):1996;1343-1357.
    • (1996) Mol. Biol. Cell , vol.7 , Issue.9 , pp. 1343-1357
    • King, R.W.1    Glotzer, M.2    Kirschner, M.W.3
  • 44
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • Hershko A. Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr. Opin. Cell Biol. 9(6):1997;788-799.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , Issue.6 , pp. 788-799
    • Hershko, A.1
  • 45
    • 0030727466 scopus 로고    scopus 로고
    • Cell cycle regulation by the ubiquitin pathway
    • Pagano M. Cell cycle regulation by the ubiquitin pathway. FASEB J. 11(13):1997;1067-1075.
    • (1997) FASEB J. , vol.11 , Issue.13 , pp. 1067-1075
    • Pagano, M.1
  • 46
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G., Standaert R.F., Lane W.S., Choi S., Corey E.J., Schreiber S.L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science. 268(5211):1995;726-731.
    • (1995) Science , vol.268 , Issue.5211 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 47
    • 0037385535 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors
    • Qiu M., Olsen A., Faivre E., Horwitz K.B., Lange C.A. Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors. Mol. Endocrinol. 17:2003;628-642.
    • (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
  • 48
    • 0029976989 scopus 로고    scopus 로고
    • Role of phosphorylation on DNA binding and transcriptional functions of human progesterone receptors
    • Takimoto G.S., Hovland A.R., Tasset D.M., Melville M.Y., Tung L., Horwitz K.B. Role of phosphorylation on DNA binding and transcriptional functions of human progesterone receptors. J. Biol. Chem. 271(23):1996;13308-13316.
    • (1996) J. Biol. Chem. , vol.271 , Issue.23 , pp. 13308-13316
    • Takimoto, G.S.1    Hovland, A.R.2    Tasset, D.M.3    Melville, M.Y.4    Tung, L.5    Horwitz, K.B.6
  • 50
    • 0026051580 scopus 로고
    • Progestins both stimulate and inhibit breast cancer cell cycle progression while increasing expression of transforming growth factor-alpha, epidermal growth factor receptor, c-fos, and c-myc genes
    • Musgrove E.A., Lee C.S., Sutherland R.L. Progestins both stimulate and inhibit breast cancer cell cycle progression while increasing expression of transforming growth factor-alpha, epidermal growth factor receptor, c-fos, and c-myc genes. Mol. Cell. Biol. 11(10):1991;5032-5043.
    • (1991) Mol. Cell. Biol. , vol.11 , Issue.10 , pp. 5032-5043
    • Musgrove, E.A.1    Lee, C.S.2    Sutherland, R.L.3
  • 51
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • McNally J.G., Muller W.G., Walker D., Wolford R., Hager G.L. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science. 287(5456):2000;1262-1265.
    • (2000) Science , vol.287 , Issue.5456 , pp. 1262-1265
    • McNally, J.G.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 52
    • 0030061512 scopus 로고    scopus 로고
    • Identification of the Gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome
    • Rubin D.M., Coux O., Wefes I., Hengartner C., Young R.A., Goldberg A.L., Finley D. Identification of the Gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome. Nature. 379(6566):1996;655-657.
    • (1996) Nature , vol.379 , Issue.6566 , pp. 655-657
    • Rubin, D.M.1    Coux, O.2    Wefes, I.3    Hengartner, C.4    Young, R.A.5    Goldberg, A.L.6    Finley, D.7
  • 53
    • 0030464067 scopus 로고    scopus 로고
    • Isolation and characterization of Sug2. A novel ATPase family component of the yeast 26S proteasome
    • Russell S.J., Sathyanarayana U.G., Johnston S.A. Isolation and characterization of Sug2. A novel ATPase family component of the yeast 26S proteasome. J. Biol. Chem. 271(51):1996;32810-32817.
    • (1996) J. Biol. Chem. , vol.271 , Issue.51 , pp. 32810-32817
    • Russell, S.J.1    Sathyanarayana, U.G.2    Johnston, S.A.3
  • 54
    • 0028890360 scopus 로고
    • A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein
    • Swaffield J.C., Melcher K., Johnston S.A. A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein. Nature. 374(6517):1995;88-91.
    • (1995) Nature , vol.374 , Issue.6517 , pp. 88-91
    • Swaffield, J.C.1    Melcher, K.2    Johnston, S.A.3
  • 55
    • 0030739911 scopus 로고    scopus 로고
    • The XPB subunit of repair/transcription factor TFIIH directly interacts with Sug1, a subunit of the 26S proteasome and putative transcription factor
    • Weeda G., Rossignol M., Fraser R.A., Winkler G.S., Vermeulen W., van't Veer L.J., Ma L., Hoeijmakers J.H., Egly J.M. The XPB subunit of repair/transcription factor TFIIH directly interacts with Sug1, a subunit of the 26S proteasome and putative transcription factor. Nucleic Acids Res. 25(12):1997;2274-2283.
    • (1997) Nucleic Acids Res. , vol.25 , Issue.12 , pp. 2274-2283
    • Weeda, G.1    Rossignol, M.2    Fraser, R.A.3    Winkler, G.S.4    Vermeulen, W.5    Van't Veer, L.J.6    Ma, L.7    Hoeijmakers, J.H.8    Egly, J.M.9
  • 56
    • 0029953663 scopus 로고    scopus 로고
    • Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors
    • Imhof M.O., McDonnell D.P. Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors. Mol. Cell. Biol. 16(6):1996;2594-2605.
    • (1996) Mol. Cell. Biol. , vol.16 , Issue.6 , pp. 2594-2605
    • Imhof, M.O.1    McDonnell, D.P.2
  • 57
    • 0032907106 scopus 로고    scopus 로고
    • The angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily
    • Nawaz Z., Lonard D.M., Smith C.L., Lev-Lehman E., Tsai S.Y., Tsai M.J., O'Malley B.W. The angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily. Mol. Cell. Biol. 19(2):1999;1182-1189.
    • (1999) Mol. Cell. Biol. , vol.19 , Issue.2 , pp. 1182-1189
    • Nawaz, Z.1    Lonard, D.M.2    Smith, C.L.3    Lev-Lehman, E.4    Tsai, S.Y.5    Tsai, M.J.6    O'Malley, B.W.7
  • 58
    • 0037066790 scopus 로고    scopus 로고
    • Ubc9 is a novel modulator of the induction properties of glucocorticoid receptors
    • Kaul S., Blackford J.A. Jr., Cho S., Simons S.S. Jr. Ubc9 is a novel modulator of the induction properties of glucocorticoid receptors. J. Biol. Chem. 277(15):2002;12541-12549.
    • (2002) J. Biol. Chem. , vol.277 , Issue.15 , pp. 12541-12549
    • Kaul, S.1    Blackford J.A., Jr.2    Cho, S.3    Simons S.S., Jr.4
  • 59
    • 0025341218 scopus 로고
    • Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription
    • Davie J.R., Murphy L.C. Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription. Biochemistry. 29(20):1990;4752-4757.
    • (1990) Biochemistry , vol.29 , Issue.20 , pp. 4752-4757
    • Davie, J.R.1    Murphy, L.C.2
  • 60
    • 0028068093 scopus 로고
    • Inhibition of transcription selectively reduces the level of ubiquitinated histone H2B in chromatin
    • Davie J.R., Murphy L.C. Inhibition of transcription selectively reduces the level of ubiquitinated histone H2B in chromatin. Biochem. Biophys. Res. Commun. 203(1):1994;344-350.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , Issue.1 , pp. 344-350
    • Davie, J.R.1    Murphy, L.C.2
  • 61
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • Salghetti S.E., Caudy A.A., Chenoweth J.G., Tansey W.P. Regulation of transcriptional activation domain function by ubiquitin. Science. 293(5535):2001;1651-1653.
    • (2001) Science , vol.293 , Issue.5535 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 62
    • 0033638393 scopus 로고    scopus 로고
    • The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation
    • Lonard D.M., Nawaz Z., Smith C.L., O'Malley B.W. The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation. Mol. Cell. 5(6):2000;939-948.
    • (2000) Mol. Cell , vol.5 , Issue.6 , pp. 939-948
    • Lonard, D.M.1    Nawaz, Z.2    Smith, C.L.3    O'Malley, B.W.4
  • 63
    • 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 D.L., Sherman L., Boonyaratanakornkit V., Schrader W.T., Weigel N.L., Edwards D.P. Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody. Mol. Endocrinol. 14(1):2000;52-65.
    • (2000) Mol. Endocrinol. , vol.14 , Issue.1 , 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
  • 64
    • 0029168036 scopus 로고
    • Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor
    • Zhang Y., Beck C.A., Poletti A., Edwards D.P., Weigel N.L. Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor. Mol. Endocrinol. 9(8):1995;1029-1040.
    • (1995) Mol. Endocrinol. , vol.9 , Issue.8 , pp. 1029-1040
    • Zhang, Y.1    Beck, C.A.2    Poletti, A.3    Edwards, D.P.4    Weigel, N.L.5
  • 65
    • 0029982567 scopus 로고    scopus 로고
    • Modulation of AP-1 activity by the human progesterone receptor in endometrial adenocarcinoma cells
    • Bamberger A.M., Bamberger C.M., Gellersen B., Schulte H.M. Modulation of AP-1 activity by the human progesterone receptor in endometrial adenocarcinoma cells. Proc. Natl. Acad. Sci. U.S.A. 93(12):1996;6169-6174.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , Issue.12 , pp. 6169-6174
    • Bamberger, A.M.1    Bamberger, C.M.2    Gellersen, B.3    Schulte, H.M.4
  • 66
    • 0037305884 scopus 로고    scopus 로고
    • Heregulin induces transcriptional activation of the progesterone receptor by a mechanism that requires a functional erbB2 and MAPK activation in breast cancer cells
    • Labriola L., Salatino M., Proietti C.J., Pecci A., Kornblihtt A.R., Charreau E.H., Elidalde P.V. Heregulin induces transcriptional activation of the progesterone receptor by a mechanism that requires a functional erbB2 and MAPK activation in breast cancer cells. Mol. Cell. Biol. 23(3):2003;1095-1111.
    • (2003) Mol. Cell. Biol. , vol.23 , Issue.3 , pp. 1095-1111
    • Labriola, L.1    Salatino, M.2    Proietti, C.J.3    Pecci, A.4    Kornblihtt, A.R.5    Charreau, E.H.6    Elidalde, P.V.7
  • 68
    • 0028840057 scopus 로고
    • When tamoxifen turns bad
    • Horwitz K.B. When tamoxifen turns bad. Endocrinology. 136(3):1995;821-823.
    • (1995) Endocrinology , vol.136 , Issue.3 , pp. 821-823
    • Horwitz, K.B.1
  • 69
    • 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 S.Z., Counterman L.J., Nummy K.A. 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(1):1993;72-78.
    • (1993) J. Cell. Physiol. , vol.155 , Issue.1 , pp. 72-78
    • Haslam, S.Z.1    Counterman, L.J.2    Nummy, K.A.3
  • 71
    • 0034673201 scopus 로고    scopus 로고
    • Effect of hormone replacement therapy on breast cancer risk: Estrogen versus estrogen plus progestin
    • Ross R.K., Paganini-Hill A., Wan P.C., Pike M.C. Effect of hormone replacement therapy on breast cancer risk: estrogen versus estrogen plus progestin. J. Natl. Cancer Inst. 92(4):2000;328-332.
    • (2000) J. Natl. Cancer Inst. , vol.92 , Issue.4 , pp. 328-332
    • Ross, R.K.1    Paganini-Hill, A.2    Wan, P.C.3    Pike, M.C.4
  • 72
    • 0028026693 scopus 로고
    • New T47D breast cancer cell lines for the independent study of progesterone B- and A-receptors: Only antiprogestin-occupied B-receptors are switched to transcriptional agonists by camp
    • Sartorius C.A., Groshong S.D., Miller L.A., Powell R.L., Tung L., Takimoto G.S., Horwitz K.B. New T47D breast cancer cell lines for the independent study of progesterone B- and A-receptors: only antiprogestin-occupied B-receptors are switched to transcriptional agonists by camp. Cancer Res. 54(14):1994;3868-3877.
    • (1994) Cancer Res. , vol.54 , Issue.14 , pp. 3868-3877
    • Sartorius, C.A.1    Groshong, S.D.2    Miller, L.A.3    Powell, R.L.4    Tung, L.5    Takimoto, G.S.6    Horwitz, K.B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.