메뉴 건너뛰기




Volumn 40, Issue 5-6, 2008, Pages 199-210

Striatin-3γ inhibits estrogen receptor activity by recruiting a protein phosphatase

Author keywords

[No Author keywords available]

Indexed keywords

ESTRADIOL; ESTROGEN RECEPTOR ALPHA; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; REGULATOR PROTEIN; SMALL INTERFERING RNA; STRIATIN 3 GAMMA; ANTIESTROGEN; AUTOANTIGEN; CALMODULIN BINDING PROTEIN; ESTROGEN RECEPTOR; GS2NA PROTEIN, RAT; ISOPROTEIN; PHOSPHOPROTEIN PHOSPHATASE 2; STRN3 PROTEIN, HUMAN;

EID: 45549086138     PISSN: 09525041     EISSN: None     Source Type: Journal    
DOI: 10.1677/JME-07-0132     Document Type: Article
Times cited : (11)

References (63)
  • 1
    • 0027405070 scopus 로고
    • Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region
    • Ali S, Metzger D, Bornert J & Chambon P 1993 Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region. EMBO Journal 12 1153-1160.
    • (1993) EMBO Journal , vol.12 , pp. 1153-1160
    • Ali, S.1    Metzger, D.2    Bornert, J.3    Chambon, P.4
  • 2
    • 0032575651 scopus 로고    scopus 로고
    • Interaction of calmodulin with striatin, a WD-repeat protein present in neuronal dendritic spines
    • Bartoli M, Monneron A & Ladant D 1998 Interaction of calmodulin with striatin, a WD-repeat protein present in neuronal dendritic spines. Journal of Biological Chemistry 273 22248-22253.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 22248-22253
    • Bartoli, M.1    Monneron, A.2    Ladant, D.3
  • 3
    • 0026642483 scopus 로고
    • Effects of hormone and cellular modulators of protein phosphorylation on transcriptional activity, DNA binding, and phosphorylation of human progesterone receptors
    • Beck C, Weigel N & Edwards D 1992 Effects of hormone and cellular modulators of protein phosphorylation on transcriptional activity, DNA binding, and phosphorylation of human progesterone receptors. Molecular Endocrinology 6 607-620.
    • (1992) Molecular Endocrinology , vol.6 , pp. 607-620
    • Beck, C.1    Weigel, N.2    Edwards, D.3
  • 4
    • 0034935019 scopus 로고    scopus 로고
    • Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling
    • Bhattacharjee R, Banks G, Trotter K, Lee H & Archer T 2001 Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling. Molecular and Cell Biology 21 5417-5425.
    • (2001) Molecular and Cell Biology , vol.21 , pp. 5417-5425
    • Bhattacharjee, R.1    Banks, G.2    Trotter, K.3    Lee, H.4    Archer, T.5
  • 5
    • 0028324907 scopus 로고
    • Differentially regulated immediate early genes in the rat uterus
    • Bigsby R & Li A 1994 Differentially regulated immediate early genes in the rat uterus. Endocrinology 134 1820-1826.
    • (1994) Endocrinology , vol.134 , pp. 1820-1826
    • Bigsby, R.1    Li, A.2
  • 7
    • 0040390304 scopus 로고
    • Activation of pS2 gene transcription is a primary response to estrogen in the human breast cancer cell line MCF-7
    • Brown A, Jeltsch J, Roberts M & Chambon P 1984 Activation of pS2 gene transcription is a primary response to estrogen in the human breast cancer cell line MCF-7. PNAS 81 6344-6348.
    • (1984) PNAS , vol.81 , pp. 6344-6348
    • Brown, A.1    Jeltsch, J.2    Roberts, M.3    Chambon, P.4
  • 11
    • 0024602483 scopus 로고
    • Regulation of cathepsin-D and pS2 gene expression by growth factors in MCF7 human breast cancer cells
    • Cavailles V, Garcia M & Rochefort H 1989 Regulation of cathepsin-D and pS2 gene expression by growth factors in MCF7 human breast cancer cells. Molecular Endocrinology 3 552-558.
    • (1989) Molecular Endocrinology , vol.3 , pp. 552-558
    • Cavailles, V.1    Garcia, M.2    Rochefort, H.3
  • 12
    • 0033636597 scopus 로고    scopus 로고
    • Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7
    • Chen D, Riedl T, Washbrook E, Pace P, Coombes R, Egly J & Ali S 2000 Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7. Molecular Cell 6 127-137.
    • (2000) Molecular Cell , vol.6 , pp. 127-137
    • Chen, D.1    Riedl, T.2    Washbrook, E.3    Pace, P.4    Coombes, R.5    Egly, J.6    Ali, S.7
  • 13
    • 0037173738 scopus 로고    scopus 로고
    • Phosphorylation of human estrogen receptor alpha at serine 118 by two distinct signal transduction pathways revealed by phosphorylation-specific antisera
    • Chen D, Washbrook E, Sarwar N, Bates G, Pace P, Thirunuvakkarasu V, Taylor J, Epstein R, Fuller-Pace F, Egly J et al. 2002 Phosphorylation of human estrogen receptor alpha at serine 118 by two distinct signal transduction pathways revealed by phosphorylation-specific antisera. Oncogene 21 4921-4931.
    • (2002) Oncogene , vol.21 , pp. 4921-4931
    • Chen, D.1    Washbrook, E.2    Sarwar, N.3    Bates, G.4    Pace, P.5    Thirunuvakkarasu, V.6    Taylor, J.7    Epstein, R.8    Fuller-Pace, F.9    Egly, J.10
  • 14
    • 0035796492 scopus 로고    scopus 로고
    • Rsk2 allosterically activates estrogen receptor alpha by docking to the hormone-binding domain
    • Clark D, Poteet-Smith C, Smith J & Lannigan D 2001 Rsk2 allosterically activates estrogen receptor alpha by docking to the hormone-binding domain. EMBO Journal 20 3484-3494.
    • (2001) EMBO Journal , vol.20 , pp. 3484-3494
    • Clark, D.1    Poteet-Smith, C.2    Smith, J.3    Lannigan, D.4
  • 15
    • 0030047451 scopus 로고    scopus 로고
    • High complexity in the expression of the B′ subunit of protein phosphatase 2A0. Evidence for the existence of at least seven novel isoforms
    • Csortos C, Zolnierowicz S, Bako E, Durbin S & DePaoli-Roach A 1996 High complexity in the expression of the B′ subunit of protein phosphatase 2A0. Evidence for the existence of at least seven novel isoforms. Journal of Biological Chemistry 271 2578-2588.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 2578-2588
    • Csortos, C.1    Zolnierowicz, S.2    Bako, E.3    Durbin, S.4    DePaoli-Roach, A.5
  • 16
    • 2342666137 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatase 5 (PP5) participates in the regulation of glucocorticoid receptor nucleocytoplasmic shuttling
    • Dean D, Urban G, Aragon I, Swingle M, Miller B, Rusconi S, Bueno M, Dean N & Honkanen R 2001 Serine/threonine protein phosphatase 5 (PP5) participates in the regulation of glucocorticoid receptor nucleocytoplasmic shuttling. BMC Cell Biology 2 6.
    • (2001) BMC Cell Biology , vol.2 , pp. 6
    • Dean, D.1    Urban, G.2    Aragon, I.3    Swingle, M.4    Miller, B.5    Rusconi, S.6    Bueno, M.7    Dean, N.8    Honkanen, R.9
  • 17
    • 0026406078 scopus 로고
    • Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors
    • DeFranco D, Qi M, Borror K, Garabedian MJ & Brautigan D 1991 Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors. Molecular Endocrinolgy 5 1215-1228.
    • (1991) Molecular Endocrinolgy , vol.5 , pp. 1215-1228
    • DeFranco, D.1    Qi, M.2    Borror, K.3    Garabedian, M.J.4    Brautigan, D.5
  • 19
    • 15744393640 scopus 로고    scopus 로고
    • Regulation of signal transduction pathways by estrogen and progesterone
    • Edwards D 2005 Regulation of signal transduction pathways by estrogen and progesterone. Annual Review of Physiology 67 335-376.
    • (2005) Annual Review of Physiology , vol.67 , pp. 335-376
    • Edwards, D.1
  • 21
    • 0037339988 scopus 로고    scopus 로고
    • The NEDD8 pathway is required for proteasome-mediated degradation of human estrogen receptor (ER)-alpha and essential for the antiproliferative activity of ICI 182,780 in ERα-positive breast cancer cells
    • Fan M, Bigsby R & Nephew K 2003 The NEDD8 pathway is required for proteasome-mediated degradation of human estrogen receptor (ER)-alpha and essential for the antiproliferative activity of ICI 182,780 in ERα-positive breast cancer cells. Molecular Endocrinology 17 356-365.
    • (2003) Molecular Endocrinology , vol.17 , pp. 356-365
    • Fan, M.1    Bigsby, R.2    Nephew, K.3
  • 22
    • 0030924806 scopus 로고    scopus 로고
    • Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin
    • Favre B, Turowski P & Hemmings B 1997 Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin. Journal of Biological Chemistry 272 13856-13863.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 13856-13863
    • Favre, B.1    Turowski, P.2    Hemmings, B.3
  • 23
    • 0001392322 scopus 로고    scopus 로고
    • AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor
    • Font de Mora J & Brown M 2000 AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor. Molecular and Cell Biology 20 5041-5047.
    • (2000) Molecular and Cell Biology , vol.20 , pp. 5041-5047
    • Font de Mora, J.1    Brown, M.2
  • 24
    • 0141785350 scopus 로고    scopus 로고
    • Profiling of estrogen up- and down-regulated gene expression in human breast cancer cells: Insights into gene networks and pathways underlying estrogenic control of proliferation and cell phenotype
    • Frasor J, Danes J, Komm B, Chang K, Lyttle C & Katzenellenbogen B 2003 Profiling of estrogen up- and down-regulated gene expression in human breast cancer cells: insights into gene networks and pathways underlying estrogenic control of proliferation and cell phenotype. Endocrinology 144 4562-4574.
    • (2003) Endocrinology , vol.144 , pp. 4562-4574
    • Frasor, J.1    Danes, J.2    Komm, B.3    Chang, K.4    Lyttle, C.5    Katzenellenbogen, B.6
  • 25
    • 0040175067 scopus 로고    scopus 로고
    • Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction
    • Frodin M & Gammeltoft S 1999 Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction. Molecular and Cellular Endocrinology 151 65-77.
    • (1999) Molecular and Cellular Endocrinology , vol.151 , pp. 65-77
    • Frodin, M.1    Gammeltoft, S.2
  • 26
    • 0033523006 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton
    • Galigniana M, Housley P, DeFranco D & Pratt W 1999 Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton. Journal of Biological Chemistry 274 16222-16227.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 16222-16227
    • Galigniana, M.1    Housley, P.2    DeFranco, D.3    Pratt, W.4
  • 27
    • 0032961449 scopus 로고    scopus 로고
    • Differential distribution of protein phosphatase 2A in human breast carcinoma cell lines and its relation to estrogen receptor status
    • Gopalakrishna R, Gundimeda U, Fontana J & Clarke R 1999 Differential distribution of protein phosphatase 2A in human breast carcinoma cell lines and its relation to estrogen receptor status. Cancer Letters 136 143-151.
    • (1999) Cancer Letters , vol.136 , pp. 143-151
    • Gopalakrishna, R.1    Gundimeda, U.2    Fontana, J.3    Clarke, R.4
  • 28
    • 0037206890 scopus 로고    scopus 로고
    • N-CoR controls differentiation of neural stem cells into astrocytes
    • Hermanson O, Jepsen K & Rosenfeld M 2002 N-CoR controls differentiation of neural stem cells into astrocytes. Nature 419 934-939.
    • (2002) Nature , vol.419 , pp. 934-939
    • Hermanson, O.1    Jepsen, K.2    Rosenfeld, M.3
  • 30
    • 0027994209 scopus 로고
    • Stimulation of androgen-regulated transactivation by modulators of protein phosphorylation
    • Ikonen T, Palvimo J, Kallio P, Reinikainen P & Janne O 1994 Stimulation of androgen-regulated transactivation by modulators of protein phosphorylation. Endocrinology 135 1359-1366.
    • (1994) Endocrinology , vol.135 , pp. 1359-1366
    • Ikonen, T.1    Palvimo, J.2    Kallio, P.3    Reinikainen, P.4    Janne, O.5
  • 32
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens V & Goris J 2001 Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochemical Journal 353 417-439.
    • (2001) Biochemical Journal , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 33
    • 0035235672 scopus 로고    scopus 로고
    • Estrogen receptor-mediated cross-talk with growth factor signaling pathways
    • Kato S 2001 Estrogen receptor-mediated cross-talk with growth factor signaling pathways. Breast Cancer 8 3-9.
    • (2001) Breast Cancer , vol.8 , pp. 3-9
    • Kato, S.1
  • 34
    • 23844463472 scopus 로고    scopus 로고
    • Protein phosphatase 2A (PP2A) regulates estrogen receptor alpha (ER) expression through modulation of ER mRNA stability
    • Keen J, Zhou Q, Park B, Pettit C, Mack K, Blair B, Brenner K & Davidson N 2005 Protein phosphatase 2A (PP2A) regulates estrogen receptor alpha (ER) expression through modulation of ER mRNA stability. Journal of Biological Chemistry 280 29519-29524.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 29519-29524
    • Keen, J.1    Zhou, Q.2    Park, B.3    Pettit, C.4    Mack, K.5    Blair, B.6    Brenner, K.7    Davidson, N.8
  • 35
    • 0028360639 scopus 로고
    • Characterization of a DNA-binding nuclear autoantigen mainly associated with S phase and G2 cells
    • Landberg G & Tan E 1994 Characterization of a DNA-binding nuclear autoantigen mainly associated with S phase and G2 cells. Experimental Cell Research 212 255-261.
    • (1994) Experimental Cell Research , vol.212 , pp. 255-261
    • Landberg, G.1    Tan, E.2
  • 36
    • 0037338707 scopus 로고    scopus 로고
    • Bidirectional signaling between the estrogen receptor and the epidermal growth factor receptor
    • Levin E 2003 Bidirectional signaling between the estrogen receptor and the epidermal growth factor receptor. Molecular Endocrinology 17 309-317.
    • (2003) Molecular Endocrinology , vol.17 , pp. 309-317
    • Levin, E.1
  • 37
    • 33751552134 scopus 로고    scopus 로고
    • Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, deoxyribonucleic acid, and coregulators associated with alterations in estrogen and tamoxifen activity
    • Likhite VS, Stossi F, Kim K, Katzenellenbogen BS & Katzenellenbogen JA 2006 Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, deoxyribonucleic acid, and coregulators associated with alterations in estrogen and tamoxifen activity. Molecular Endocrinology 20 3120-3132.
    • (2006) Molecular Endocrinology , vol.20 , pp. 3120-3132
    • Likhite, V.S.1    Stossi, F.2    Kim, K.3    Katzenellenbogen, B.S.4    Katzenellenbogen, J.A.5
  • 38
    • 0035210802 scopus 로고    scopus 로고
    • Evidence for estrogenic contamination of the MAPK inhibitor PD98059
    • Long X, Gize EA, Nephew K & Bigsby RM 2001 Evidence for estrogenic contamination of the MAPK inhibitor PD98059. Endocrinology 142 5390-5393.
    • (2001) Endocrinology , vol.142 , pp. 5390-5393
    • Long, X.1    Gize, E.A.2    Nephew, K.3    Bigsby, R.M.4
  • 40
    • 0038813724 scopus 로고    scopus 로고
    • Regulation of estrogen receptor alpha -mediated transcription by a direct interaction with protein phosphatase 2A
    • Lu Q, Surks H, Ebling H, Baur W, Brown D, Pallas D & Karas R 2003 Regulation of estrogen receptor alpha -mediated transcription by a direct interaction with protein phosphatase 2A. Journal of Biological Chemistry 278 4639-4645.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 4639-4645
    • Lu, Q.1    Surks, H.2    Ebling, H.3    Baur, W.4    Brown, D.5    Pallas, D.6    Karas, R.7
  • 41
    • 10344237581 scopus 로고    scopus 로고
    • Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor alpha
    • Lu Q, Pallas D, Surks H, Baur W, Mendelsohn M & Karas R 2004 Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor alpha. PNAS 101 17126-17131.
    • (2004) PNAS , vol.101 , pp. 17126-17131
    • Lu, Q.1    Pallas, D.2    Surks, H.3    Baur, W.4    Mendelsohn, M.5    Karas, R.6
  • 43
    • 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 108 465-474.
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 45
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R, Penot G, Hubner M, Reid G, Brand H, Kos M & Gannon F 2003 Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115 751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 47
    • 0034050449 scopus 로고    scopus 로고
    • WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A
    • Moreno C, Park S, Nelson K, Ashby D, Hubalek F, Lane W & Pallas D 2000 WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A. Journal of Biological Chemistry 275 5257-5263.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 5257-5263
    • Moreno, C.1    Park, S.2    Nelson, K.3    Ashby, D.4    Hubalek, F.5    Lane, W.6    Pallas, D.7
  • 48
    • 0035968296 scopus 로고    scopus 로고
    • A mammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes
    • Moreno C, Lane W & Pallas D 2001 A mammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes. Journal of Biological Chemistry 276 24253-24260.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 24253-24260
    • Moreno, C.1    Lane, W.2    Pallas, D.3
  • 49
    • 0028959481 scopus 로고
    • A cell-cycle nuclear autoantigen containing WD-40 motifs expressed mainly in S and G2 phase cells
    • Muro Y, Chan E, Landberg G & Tan E 1995 A cell-cycle nuclear autoantigen containing WD-40 motifs expressed mainly in S and G2 phase cells. Biochemical and Biophysical Research Communications 207 1029-1037.
    • (1995) Biochemical and Biophysical Research Communications , vol.207 , pp. 1029-1037
    • Muro, Y.1    Chan, E.2    Landberg, G.3    Tan, E.4
  • 50
    • 16244382046 scopus 로고    scopus 로고
    • Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity
    • Narayanan R, Edwards D & Weigel N 2005 Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity. Molecular and Cell Biology 25 2885-2898.
    • (2005) Molecular and Cell Biology , vol.25 , pp. 2885-2898
    • Narayanan, R.1    Edwards, D.2    Weigel, N.3
  • 51
    • 0037385535 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors
    • Qiu M, Olsen A, Faivre E, Horwitz K & Lange C 2003 Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors. Molecular Endocrinology 17 628-642.
    • (2003) Molecular Endocrinology , vol.17 , pp. 628-642
    • Qiu, M.1    Olsen, A.2    Faivre, E.3    Horwitz, K.4    Lange, C.5
  • 52
    • 0035840446 scopus 로고    scopus 로고
    • Role of serine/threonine protein phosphatase 2A in cancer
    • Schonthal A 2001 Role of serine/threonine protein phosphatase 2A in cancer. Cancer Letters 170 1-13.
    • (2001) Cancer Letters , vol.170 , pp. 1-13
    • Schonthal, A.1
  • 53
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang Y, Hu X, DiRenzo J, Lazar M & Brown M 2000 Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103 843-852.
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.4    Brown, M.5
  • 54
    • 0031932603 scopus 로고    scopus 로고
    • Cross-talk between peptide growth factor and estrogen receptor signaling pathways
    • Smith C 1998 Cross-talk between peptide growth factor and estrogen receptor signaling pathways. Biological Reproduction 58 627-632.
    • (1998) Biological Reproduction , vol.58 , pp. 627-632
    • Smith, C.1
  • 55
    • 1442351143 scopus 로고    scopus 로고
    • Coregulator function: A key to understanding tissue specificity of selective receptor modulators
    • Smith C & O'Malley B 2004 Coregulator function: a key to understanding tissue specificity of selective receptor modulators. Endocrine Reviews 25 45-71.
    • (2004) Endocrine Reviews , vol.25 , pp. 45-71
    • Smith, C.1    O'Malley, B.2
  • 56
    • 0025781385 scopus 로고
    • p34cdc2 phosphorylation sites in histone H1 are dephosphorylated by protein phosphatase 2A1
    • Sola M, Langan T & Cohen P 1991 p34cdc2 phosphorylation sites in histone H1 are dephosphorylated by protein phosphatase 2A1. Biochimica et Biophysic Acta 1094 211-216.
    • (1991) Biochimica et Biophysic Acta , vol.1094 , pp. 211-216
    • Sola, M.1    Langan, T.2    Cohen, P.3
  • 57
    • 0035100658 scopus 로고    scopus 로고
    • Protein phosphatase 2A: The Trojan Horse of cellular signaling
    • Sontag E 2001 Protein phosphatase 2A: the Trojan Horse of cellular signaling. Cell Signalling 13 7-16.
    • (2001) Cell Signalling , vol.13 , pp. 7-16
    • Sontag, E.1
  • 58
    • 0023786364 scopus 로고
    • Estrogen induces expression of c-fos and c-myc protooncogenes in rat uterus
    • Weisz A & Bresciani F 1988 Estrogen induces expression of c-fos and c-myc protooncogenes in rat uterus. Molecular Endocrinology 2 816-824.
    • (1988) Molecular Endocrinology , vol.2 , pp. 816-824
    • Weisz, A.1    Bresciani, F.2
  • 59
    • 3242881571 scopus 로고    scopus 로고
    • Corepressor recruitment by agonist-bound nuclear receptors
    • White J, Fernandes I, Mader S & Yang X 2004 Corepressor recruitment by agonist-bound nuclear receptors. Vitamins and Hormone 68 123-143.
    • (2004) Vitamins and Hormone , vol.68 , pp. 123-143
    • White, J.1    Fernandes, I.2    Mader, S.3    Yang, X.4
  • 60
    • 4644252581 scopus 로고    scopus 로고
    • Selective phosphorylations of the SRC-3/AIB1 coactivator integrate genomic reponses to multiple cellular signaling pathways
    • Wu R, Qin J, Yi P, Wong J, Tsai S, Tsai M & O'Malley B 2004 Selective phosphorylations of the SRC-3/AIB1 coactivator integrate genomic reponses to multiple cellular signaling pathways. Molecular Cell 15 937-949.
    • (2004) Molecular Cell , vol.15 , pp. 937-949
    • Wu, R.1    Qin, J.2    Yi, P.3    Wong, J.4    Tsai, S.5    Tsai, M.6    O'Malley, B.7
  • 61
    • 0042236405 scopus 로고    scopus 로고
    • Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbital
    • Yoshinari K, Kobayashi K, Moore R, Kawamoto T & Negishi M 2003 Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbital. FEBS Letters 548 17-20.
    • (2003) FEBS Letters , vol.548 , pp. 17-20
    • Yoshinari, K.1    Kobayashi, K.2    Moore, R.3    Kawamoto, T.4    Negishi, M.5
  • 62
    • 0035478692 scopus 로고    scopus 로고
    • Transcription activating property of autoantigen SG2NA and modulating effect of WD-40 repeats
    • Zhu W, Chan E, Li J, Hemmerich P & Tan E 2001 Transcription activating property of autoantigen SG2NA and modulating effect of WD-40 repeats. Experimental Cell Research 269 312-321.
    • (2001) Experimental Cell Research , vol.269 , pp. 312-321
    • Zhu, W.1    Chan, E.2    Li, J.3    Hemmerich, P.4    Tan, E.5
  • 63
    • 0040370216 scopus 로고    scopus 로고
    • Ser/Thr protein phosphatase type 5 (PP5) is a negative regulator of glucocorticoid receptor-mediated growth arrest
    • Zuo Z, Urban G, Scammell J, Dean N, McLean T, Aragon I & Honkanen R 1999 Ser/Thr protein phosphatase type 5 (PP5) is a negative regulator of glucocorticoid receptor-mediated growth arrest. Biochemistry 38 8849-8857.
    • (1999) Biochemistry , vol.38 , pp. 8849-8857
    • Zuo, Z.1    Urban, G.2    Scammell, J.3    Dean, N.4    McLean, T.5    Aragon, I.6    Honkanen, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.