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Volumn 314, Issue 15, 2008, Pages 2796-2810

Chromatin context dominates estrogen regulation of pS2 gene expression

Author keywords

Chromatin; Estrogen receptor; flp recombination target; Histone acetylation; Histone methylation; Nuclear receptors; pS2; Steroid receptors

Indexed keywords

BETA GALACTOSIDASE; ESTROGEN; ESTROGEN RECEPTOR ALPHA; HISTONE DEACETYLASE; HISTONE H3; HISTONE H4; LUCIFERASE; LYSINE; PROTEIN PS2; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR;

EID: 50049127216     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.07.006     Document Type: Article
Times cited : (8)

References (70)
  • 1
    • 0022483705 scopus 로고
    • The presence of nucleosomes on a DNA template prevents initiation by RNA polymerase II in vitro
    • Knezetic J.A., and Luse D.S. The presence of nucleosomes on a DNA template prevents initiation by RNA polymerase II in vitro. Cell 45 (1986) 95-104
    • (1986) Cell , vol.45 , pp. 95-104
    • Knezetic, J.A.1    Luse, D.S.2
  • 2
    • 0023663417 scopus 로고
    • Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones
    • Lorch Y., LaPointe J.W., and Kornberg R.D. Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones. Cell 49 (1987) 203-210
    • (1987) Cell , vol.49 , pp. 203-210
    • Lorch, Y.1    LaPointe, J.W.2    Kornberg, R.D.3
  • 3
    • 0026512523 scopus 로고
    • Nucleosome arrays inhibit both initiation and elongation of transcripts by bacteriophage T7 RNA polymerase
    • O'Neill T.E., Roberge M., and Bradbury E.M. Nucleosome arrays inhibit both initiation and elongation of transcripts by bacteriophage T7 RNA polymerase. J. Mol. Biol. 223 (1992) 67-78
    • (1992) J. Mol. Biol. , vol.223 , pp. 67-78
    • O'Neill, T.E.1    Roberge, M.2    Bradbury, E.M.3
  • 4
    • 0026095663 scopus 로고
    • Role of nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II
    • Laybourn P.J., and Kadonaga J.T. Role of nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II. Science 254 (1991) 238-245
    • (1991) Science , vol.254 , pp. 238-245
    • Laybourn, P.J.1    Kadonaga, J.T.2
  • 6
    • 14644406272 scopus 로고    scopus 로고
    • Active chromatin domains are defined by acetylation islands revealed by genome-wide mapping
    • Roh T.Y., Cuddapah S., and Zhao K. Active chromatin domains are defined by acetylation islands revealed by genome-wide mapping. Genes Dev. 19 (2005) 542-552
    • (2005) Genes Dev. , vol.19 , pp. 542-552
    • Roh, T.Y.1    Cuddapah, S.2    Zhao, K.3
  • 7
    • 0031876314 scopus 로고    scopus 로고
    • Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III
    • Tse C., Sera T., Wolffe A.P., and Hansen J.C. Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III. Mol. Cell Biol. 18 (1998) 4629-4638
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4629-4638
    • Tse, C.1    Sera, T.2    Wolffe, A.P.3    Hansen, J.C.4
  • 8
    • 0032525139 scopus 로고    scopus 로고
    • Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin
    • Nightingale K.P., Wellinger R.E., Sogo J.M., and Becker P.B. Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin. Embo. J. 17 (1998) 2865-2876
    • (1998) Embo. J. , vol.17 , pp. 2865-2876
    • Nightingale, K.P.1    Wellinger, R.E.2    Sogo, J.M.3    Becker, P.B.4
  • 11
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson C.L., and Laniel M.A. Histones and histone modifications. Curr. Biol. 14 (2004) R546-551
    • (2004) Curr. Biol. , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 12
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger S.L. Histone modifications in transcriptional regulation. Curr. Opin. Genet. Dev. 12 (2002) 142-148
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 13
    • 0029869172 scopus 로고    scopus 로고
    • Histone deacetylase: a regulator of transcription
    • Wolffe A.P. Histone deacetylase: a regulator of transcription. Science 272 (1996) 371-372
    • (1996) Science , vol.272 , pp. 371-372
    • Wolffe, A.P.1
  • 14
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 389 (1997) 349-352
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 15
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 16
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 17
    • 5444255150 scopus 로고    scopus 로고
    • The epigenetics of cancer etiology
    • Feinberg A.P. The epigenetics of cancer etiology. Semin. Cancer Biol. 14 (2004) 427-432
    • (2004) Semin. Cancer Biol. , vol.14 , pp. 427-432
    • Feinberg, A.P.1
  • 19
    • 35348868573 scopus 로고    scopus 로고
    • Epigenetic regulation of normal and malignant hematopoiesis
    • Rice K.L., Hormaeche I., and Licht J.D. Epigenetic regulation of normal and malignant hematopoiesis. Oncogene 26 (2007) 6697-6714
    • (2007) Oncogene , vol.26 , pp. 6697-6714
    • Rice, K.L.1    Hormaeche, I.2    Licht, J.D.3
  • 20
    • 34250617919 scopus 로고    scopus 로고
    • Cancer susceptibility: epigenetic manifestation of environmental exposures
    • Weidman J.R., Dolinoy D.C., Murphy S.K., and Jirtle R.L. Cancer susceptibility: epigenetic manifestation of environmental exposures. Cancer J. 13 (2007) 9-16
    • (2007) Cancer J. , vol.13 , pp. 9-16
    • Weidman, J.R.1    Dolinoy, D.C.2    Murphy, S.K.3    Jirtle, R.L.4
  • 21
    • 33144481148 scopus 로고    scopus 로고
    • Protein lysine acetylation in normal and leukaemic haematopoiesis: HDACs as possible therapeutic targets in adult AML
    • Bruserud O., Stapnes C., Tronstad K.J., Ryningen A., Anensen N., and Gjertsen B.T. Protein lysine acetylation in normal and leukaemic haematopoiesis: HDACs as possible therapeutic targets in adult AML. Expert Opin. Ther. Targets 10 (2006) 51-68
    • (2006) Expert Opin. Ther. Targets , vol.10 , pp. 51-68
    • Bruserud, O.1    Stapnes, C.2    Tronstad, K.J.3    Ryningen, A.4    Anensen, N.5    Gjertsen, B.T.6
  • 23
    • 0019167247 scopus 로고
    • Estrogen and progesterone receptors in the prediction of response of breast cancer to endocrine therapy
    • Manni A., Arafah B., and Pearson O.H. Estrogen and progesterone receptors in the prediction of response of breast cancer to endocrine therapy. Cancer 46 (1980) 2838-2841
    • (1980) Cancer , vol.46 , pp. 2838-2841
    • Manni, A.1    Arafah, B.2    Pearson, O.H.3
  • 24
    • 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.R., Reid G., Brand H., Kos M., and Gannon F. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115 (2003) 751-763
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 25
    • 0036550954 scopus 로고    scopus 로고
    • The estrogen-regulated protein, TFF1, stimulates migration of human breast cancer cells
    • Prest S.J., May F.E., and Westley B.R. The estrogen-regulated protein, TFF1, stimulates migration of human breast cancer cells. Faseb. J. 16 (2002) 592-594
    • (2002) Faseb. J. , vol.16 , pp. 592-594
    • Prest, S.J.1    May, F.E.2    Westley, B.R.3
  • 28
    • 33846815516 scopus 로고    scopus 로고
    • Identification of novel genes that co-cluster with estrogen receptor alpha in breast tumor biopsy specimens, using a large-scale real-time reverse transcription-PCR approach
    • Tozlu S., Girault I., Vacher S., Vendrell J., Andrieu C., Spyratos F., Cohen P., Lidereau R., and Bieche I. Identification of novel genes that co-cluster with estrogen receptor alpha in breast tumor biopsy specimens, using a large-scale real-time reverse transcription-PCR approach. Endocr. Relat. Cancer 13 (2006) 1109-1120
    • (2006) Endocr. Relat. Cancer , vol.13 , pp. 1109-1120
    • Tozlu, S.1    Girault, I.2    Vacher, S.3    Vendrell, J.4    Andrieu, C.5    Spyratos, F.6    Cohen, P.7    Lidereau, R.8    Bieche, I.9
  • 29
    • 33846815517 scopus 로고    scopus 로고
    • Significance, detection and markers of disseminated breast cancer cells
    • Lacroix M. Significance, detection and markers of disseminated breast cancer cells. Endocr. Relat. Cancer 13 (2006) 1033-1067
    • (2006) Endocr. Relat. Cancer , vol.13 , pp. 1033-1067
    • Lacroix, M.1
  • 30
    • 33747773708 scopus 로고    scopus 로고
    • Histone H3 acetylation and H3 K4 methylation define distinct chromatin regions permissive for transgene expression
    • Yan C., and Boyd D.D. Histone H3 acetylation and H3 K4 methylation define distinct chromatin regions permissive for transgene expression. Mol. Cell Biol. 26 (2006) 6357-6371
    • (2006) Mol. Cell Biol. , vol.26 , pp. 6357-6371
    • Yan, C.1    Boyd, D.D.2
  • 31
    • 0034129679 scopus 로고    scopus 로고
    • Steroid hormone receptors: an update
    • Beato M., and Klug J. Steroid hormone receptors: an update. Hum. Reprod. Update 6 (2000) 225-236
    • (2000) Hum. Reprod. Update , vol.6 , pp. 225-236
    • Beato, M.1    Klug, J.2
  • 32
    • 0031894879 scopus 로고    scopus 로고
    • Hormone action and chromatin remodelling
    • Robyr D., and Wolffe P. Hormone action and chromatin remodelling. Cell Mol. Life Sci. 54 (1998) 113-124
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 113-124
    • Robyr, D.1    Wolffe, P.2
  • 34
    • 33746348338 scopus 로고    scopus 로고
    • Dynamic changes in histone H3 phosphoacetylation during early embryonic stem cell differentiation are directly mediated by mitogen- and stress-activated protein kinase 1 via activation of MAPK pathways
    • Lee E.R., McCool K.W., Murdoch F.E., and Fritsch M.K. Dynamic changes in histone H3 phosphoacetylation during early embryonic stem cell differentiation are directly mediated by mitogen- and stress-activated protein kinase 1 via activation of MAPK pathways. J. Biol. Chem. 281 (2006) 21162-21172
    • (2006) J. Biol. Chem. , vol.281 , pp. 21162-21172
    • Lee, E.R.1    McCool, K.W.2    Murdoch, F.E.3    Fritsch, M.K.4
  • 35
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(- Delta Delta C(T)) Method
    • Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(- Delta Delta C(T)) Method. Methods 25 (2001) 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 36
    • 0036024955 scopus 로고    scopus 로고
    • Identification of unknown target genes of human transcription factors using chromatin immunoprecipitation
    • Weinmann A.S., and Farnham P.J. Identification of unknown target genes of human transcription factors using chromatin immunoprecipitation. Methods 26 (2002) 37-47
    • (2002) Methods , vol.26 , pp. 37-47
    • Weinmann, A.S.1    Farnham, P.J.2
  • 37
    • 0035888026 scopus 로고    scopus 로고
    • Chromatin remodeling, measured by a novel real-time polymerase chain reaction assay, across the proximal promoter region of the IL-2 gene
    • Rao S., Procko E., and Shannon M.F. Chromatin remodeling, measured by a novel real-time polymerase chain reaction assay, across the proximal promoter region of the IL-2 gene. J. Immunol. 167 (2001) 4494-4503
    • (2001) J. Immunol. , vol.167 , pp. 4494-4503
    • Rao, S.1    Procko, E.2    Shannon, M.F.3
  • 38
  • 39
    • 0029034448 scopus 로고
    • Dioxin induces localized, graded changes in chromatin structure: implications for Cyp1A1 gene transcription
    • Okino S.T., and Whitlock Jr. J.P. Dioxin induces localized, graded changes in chromatin structure: implications for Cyp1A1 gene transcription. Mol. Cell Biol. 15 (1995) 3714-3721
    • (1995) Mol. Cell Biol. , vol.15 , pp. 3714-3721
    • Okino, S.T.1    Whitlock Jr., J.P.2
  • 40
    • 2442640603 scopus 로고    scopus 로고
    • A novel homologous recombination system to study 92 kDa type IV collagenase transcription demonstrates that the NF-kappaB motif drives the transition from a repressed to an activated state of gene expression
    • Yan C., Wang H., Aggarwal B., and Boyd D.D. A novel homologous recombination system to study 92 kDa type IV collagenase transcription demonstrates that the NF-kappaB motif drives the transition from a repressed to an activated state of gene expression. Faseb. J. 18 (2004) 540-541
    • (2004) Faseb. J. , vol.18 , pp. 540-541
    • Yan, C.1    Wang, H.2    Aggarwal, B.3    Boyd, D.D.4
  • 41
    • 0024448351 scopus 로고
    • Effects of the antioestrogen, ICI 164,384, on oestrogen induced RNAs in MCF-7 cells
    • Wiseman L.R., Wakeling A.E., May F.E., and Westley B.R. Effects of the antioestrogen, ICI 164,384, on oestrogen induced RNAs in MCF-7 cells. J. Steroid Biochem. 33 (1989) 1-6
    • (1989) J. Steroid Biochem. , vol.33 , pp. 1-6
    • Wiseman, L.R.1    Wakeling, A.E.2    May, F.E.3    Westley, B.R.4
  • 42
    • 20844453021 scopus 로고    scopus 로고
    • Differential regulation of estrogen-inducible proteolysis and transcription by the estrogen receptor alpha N terminus
    • Valley C.C., Metivier R., Solodin N.M., Fowler A.M., Mashek M.T., Hill L., and Alarid E.T. Differential regulation of estrogen-inducible proteolysis and transcription by the estrogen receptor alpha N terminus. Mol. Cell Biol. 25 (2005) 5417-5428
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5417-5428
    • Valley, C.C.1    Metivier, R.2    Solodin, N.M.3    Fowler, A.M.4    Mashek, M.T.5    Hill, L.6    Alarid, E.T.7
  • 44
    • 0001235572 scopus 로고
    • Estrogen-responsive element of the human pS2 gene is an imperfectly palindromic sequence
    • Berry M., Nunez A.M., and Chambon P. Estrogen-responsive element of the human pS2 gene is an imperfectly palindromic sequence. Proc. Natl. Acad. Sci. U S A 86 (1989) 1218-1222
    • (1989) Proc. Natl. Acad. Sci. U S A , vol.86 , pp. 1218-1222
    • Berry, M.1    Nunez, A.M.2    Chambon, P.3
  • 45
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang Y., Hu X., DiRenzo J., Lazar M.A., and Brown M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103 (2000) 843-852
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 46
    • 33748751950 scopus 로고    scopus 로고
    • SET-mediated promoter hypoacetylation is a prerequisite for coactivation of the estrogen-responsive pS2 gene by PRMT1
    • Wagner S., Weber S., Kleinschmidt M.A., Nagata K., and Bauer U.M. SET-mediated promoter hypoacetylation is a prerequisite for coactivation of the estrogen-responsive pS2 gene by PRMT1. J. Biol. Chem. 281 (2006) 27242-27250
    • (2006) J. Biol. Chem. , vol.281 , pp. 27242-27250
    • Wagner, S.1    Weber, S.2    Kleinschmidt, M.A.3    Nagata, K.4    Bauer, U.M.5
  • 47
    • 0024454741 scopus 로고
    • The 5′ flanking region of the pS2 gene contains a complex enhancer region responsive to oestrogens, epidermal growth factor, a tumour promoter (TPA), the c-Ha-ras oncoprotein and the c-jun protein
    • Nunez A.M., Berry M., Imler J.L., and Chambon P. The 5′ flanking region of the pS2 gene contains a complex enhancer region responsive to oestrogens, epidermal growth factor, a tumour promoter (TPA), the c-Ha-ras oncoprotein and the c-jun protein. Embo. J. 8 (1989) 823-829
    • (1989) Embo. J. , vol.8 , pp. 823-829
    • Nunez, A.M.1    Berry, M.2    Imler, J.L.3    Chambon, P.4
  • 48
    • 0035487829 scopus 로고    scopus 로고
    • Intracellular signaling pathways: nongenomic actions of estrogens and ligand-independent activation of estrogen receptors
    • Coleman K.M., and Smith C.L. Intracellular signaling pathways: nongenomic actions of estrogens and ligand-independent activation of estrogen receptors. Front Biosci. 6 (2001) D1379-1391
    • (2001) Front Biosci. , vol.6
    • Coleman, K.M.1    Smith, C.L.2
  • 49
    • 0033926403 scopus 로고    scopus 로고
    • Review: chromatin structural features and targets that regulate transcription
    • Wolffe A.P., and Guschin D. Review: chromatin structural features and targets that regulate transcription. J. Struct. Biol. 129 (2000) 102-122
    • (2000) J. Struct. Biol. , vol.129 , pp. 102-122
    • Wolffe, A.P.1    Guschin, D.2
  • 50
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core particle linking number change
    • Norton V.G., Imai B.S., Yau P., and Bradbury E.M. Histone acetylation reduces nucleosome core particle linking number change. Cell 57 (1989) 449-457
    • (1989) Cell , vol.57 , pp. 449-457
    • Norton, V.G.1    Imai, B.S.2    Yau, P.3    Bradbury, E.M.4
  • 51
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M., Kijima M., Akita M., and Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 265 (1990) 17174-17179
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 52
    • 0037023754 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases alters allelic chromatin conformation at the imprinted U2af1-rs1 locus in mouse embryonic stem cells
    • Gregory R.I., O'Neill L.P., Randall T.E., Fournier C., Khosla S., Turner B.M., and Feil R. Inhibition of histone deacetylases alters allelic chromatin conformation at the imprinted U2af1-rs1 locus in mouse embryonic stem cells. J. Biol. Chem. 277 (2002) 11728-11734
    • (2002) J. Biol. Chem. , vol.277 , pp. 11728-11734
    • Gregory, R.I.1    O'Neill, L.P.2    Randall, T.E.3    Fournier, C.4    Khosla, S.5    Turner, B.M.6    Feil, R.7
  • 53
    • 34250370970 scopus 로고    scopus 로고
    • The role of histone acetylation in regulating early gene expression patterns during early embryonic stem cell differentiation
    • McCool K.W., Xu X., Singer D.B., Murdoch F.E., and Fritsch M.K. The role of histone acetylation in regulating early gene expression patterns during early embryonic stem cell differentiation. J. Biol. Chem. 282 (2007) 6696-6706
    • (2007) J. Biol. Chem. , vol.282 , pp. 6696-6706
    • McCool, K.W.1    Xu, X.2    Singer, D.B.3    Murdoch, F.E.4    Fritsch, M.K.5
  • 54
    • 0032076461 scopus 로고    scopus 로고
    • Beyond the nucleosome: epigenetic aspects of position-effect variegation in Drosophila
    • Wakimoto B.T. Beyond the nucleosome: epigenetic aspects of position-effect variegation in Drosophila. Cell 93 (1998) 321-324
    • (1998) Cell , vol.93 , pp. 321-324
    • Wakimoto, B.T.1
  • 55
    • 0029939592 scopus 로고    scopus 로고
    • The beta-globin locus control region enhances transcription of but does not confer position-independent expression onto the lacZ gene in transgenic mice
    • Guy L.G., Kothary R., DeRepentigny Y., Delvoye N., Ellis J., and Wall L. The beta-globin locus control region enhances transcription of but does not confer position-independent expression onto the lacZ gene in transgenic mice. Embo. J. 15 (1996) 3713-3721
    • (1996) Embo. J. , vol.15 , pp. 3713-3721
    • Guy, L.G.1    Kothary, R.2    DeRepentigny, Y.3    Delvoye, N.4    Ellis, J.5    Wall, L.6
  • 56
    • 0002434883 scopus 로고
    • The phenomenon of position effect
    • Lewis E.B. The phenomenon of position effect. Adv. Genet. 3 (1950) 73-115
    • (1950) Adv. Genet. , vol.3 , pp. 73-115
    • Lewis, E.B.1
  • 57
    • 0034615669 scopus 로고    scopus 로고
    • The SRC family of nuclear receptor coactivators
    • Leo C., and Chen J.D. The SRC family of nuclear receptor coactivators. Gene 245 (2000) 1-11
    • (2000) Gene , vol.245 , pp. 1-11
    • Leo, C.1    Chen, J.D.2
  • 58
    • 0036275233 scopus 로고    scopus 로고
    • Acetylation of nucleosomal histones by p300 facilitates transcription from tax-responsive human T-cell leukemia virus type 1 chromatin template
    • Lu H., Pise-Masison C.A., Fletcher T.M., Schiltz R.L., Nagaich A.K., Radonovich M., Hager G., Cole P.A., and Brady J.N. Acetylation of nucleosomal histones by p300 facilitates transcription from tax-responsive human T-cell leukemia virus type 1 chromatin template. Mol. Cell Biol. 22 (2002) 4450-4462
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4450-4462
    • Lu, H.1    Pise-Masison, C.A.2    Fletcher, T.M.3    Schiltz, R.L.4    Nagaich, A.K.5    Radonovich, M.6    Hager, G.7    Cole, P.A.8    Brady, J.N.9
  • 59
    • 4444383323 scopus 로고    scopus 로고
    • Role for Nhp6, Gcn5, and the Swi/Snf complex in stimulating formation of the TATA-binding protein-TFIIA-DNA complex
    • Biswas D., Imbalzano A.N., Eriksson P., Yu Y., and Stillman D.J. Role for Nhp6, Gcn5, and the Swi/Snf complex in stimulating formation of the TATA-binding protein-TFIIA-DNA complex. Mol. Cell Biol. 24 (2004) 8312-8321
    • (2004) Mol. Cell Biol. , vol.24 , pp. 8312-8321
    • Biswas, D.1    Imbalzano, A.N.2    Eriksson, P.3    Yu, Y.4    Stillman, D.J.5
  • 60
    • 0035146586 scopus 로고    scopus 로고
    • Binding of TATA binding protein to a naturally positioned nucleosome is facilitated by histone acetylation
    • Sewack G.F., Ellis T.W., and Hansen U. Binding of TATA binding protein to a naturally positioned nucleosome is facilitated by histone acetylation. Mol. Cell Biol. 21 (2001) 1404-1415
    • (2001) Mol. Cell Biol. , vol.21 , pp. 1404-1415
    • Sewack, G.F.1    Ellis, T.W.2    Hansen, U.3
  • 62
    • 0034617058 scopus 로고    scopus 로고
    • p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation
    • Fu M., Wang C., Reutens A.T., Wang J., Angeletti R.H., Siconolfi-Baez L., Ogryzko V., Avantaggiati M.L., and Pestell R.G. p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation. J. Biol. Chem. 275 (2000) 20853-20860
    • (2000) J. Biol. Chem. , vol.275 , pp. 20853-20860
    • Fu, M.1    Wang, C.2    Reutens, A.T.3    Wang, J.4    Angeletti, R.H.5    Siconolfi-Baez, L.6    Ogryzko, V.7    Avantaggiati, M.L.8    Pestell, R.G.9
  • 64
    • 33745658056 scopus 로고    scopus 로고
    • Acetylation of estrogen receptor alpha by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor
    • Kim M.Y., Woo E.M., Chong Y.T., Homenko D.R., and Kraus W.L. Acetylation of estrogen receptor alpha by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor. Mol. Endocrinol. 20 (2006) 1479-1493
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1479-1493
    • Kim, M.Y.1    Woo, E.M.2    Chong, Y.T.3    Homenko, D.R.4    Kraus, W.L.5
  • 65
    • 0022799080 scopus 로고
    • Removal of positioned nucleosomes from the yeast PHO5 promoter upon PHO5 induction releases additional upstream activating DNA elements
    • Almer A., Rudolph H., Hinnen A., and Horz W. Removal of positioned nucleosomes from the yeast PHO5 promoter upon PHO5 induction releases additional upstream activating DNA elements. Embo. J. 5 (1986) 2689-2696
    • (1986) Embo. J. , vol.5 , pp. 2689-2696
    • Almer, A.1    Rudolph, H.2    Hinnen, A.3    Horz, W.4
  • 66
    • 0034161435 scopus 로고    scopus 로고
    • Hormone activation induces nucleosome positioning in vivo
    • Belikov S., Gelius B., Almouzni G., and Wrange O. Hormone activation induces nucleosome positioning in vivo. Embo. J. 19 (2000) 1023-1033
    • (2000) Embo. J. , vol.19 , pp. 1023-1033
    • Belikov, S.1    Gelius, B.2    Almouzni, G.3    Wrange, O.4
  • 67
    • 0025815198 scopus 로고
    • Glucocorticoids are required for establishment and maintenance of an alteration in chromatin structure: induction leads to a reversible disruption of nucleosomes over an enhancer
    • Reik A., Schutz G., and Stewart A.F. Glucocorticoids are required for establishment and maintenance of an alteration in chromatin structure: induction leads to a reversible disruption of nucleosomes over an enhancer. Embo. J. 10 (1991) 2569-2576
    • (1991) Embo. J. , vol.10 , pp. 2569-2576
    • Reik, A.1    Schutz, G.2    Stewart, A.F.3
  • 68
    • 0034665624 scopus 로고    scopus 로고
    • Differential remodeling of the HIV-1 nucleosome upon transcription activators and SWI/SNF complex binding
    • Angelov D., Charra M., Seve M., Cote J., Khochbin S., and Dimitrov S. Differential remodeling of the HIV-1 nucleosome upon transcription activators and SWI/SNF complex binding. J. Mol. Biol. 302 (2000) 315-326
    • (2000) J. Mol. Biol. , vol.302 , pp. 315-326
    • Angelov, D.1    Charra, M.2    Seve, M.3    Cote, J.4    Khochbin, S.5    Dimitrov, S.6
  • 69
    • 34247508924 scopus 로고    scopus 로고
    • Unraveling the mechanisms of endocrine resistance in breast cancer: new therapeutic opportunities
    • Massarweh S., and Schiff R. Unraveling the mechanisms of endocrine resistance in breast cancer: new therapeutic opportunities. Clin. Cancer Res. 13 (2007) 1950-1954
    • (2007) Clin. Cancer Res. , vol.13 , pp. 1950-1954
    • Massarweh, S.1    Schiff, R.2
  • 70
    • 6044259839 scopus 로고    scopus 로고
    • Endocrine-resistant breast cancer: underlying mechanisms and strategies for overcoming resistance
    • Kurebayashi J. Endocrine-resistant breast cancer: underlying mechanisms and strategies for overcoming resistance. Breast Cancer 10 (2003) 112-119
    • (2003) Breast Cancer , vol.10 , pp. 112-119
    • Kurebayashi, J.1


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