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Volumn 22, Issue 3, 2011, Pages 87-93

Negative regulation by nuclear receptors: A plethora of mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CELL NUCLEUS RECEPTOR; CONSTITUTIVE ANDROSTANE RECEPTOR; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE 3; LIGAND; NUCLEAR RECEPTOR COREPRESSOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR BINDING PROTEIN; PROLACTIN; RECEPTOR INTERACTING PROTEIN 140; SILENCING MEDIATOR OF RETINOID AND THYROID HORMONE RECEPTOR; THYROTROPIN; TRANSCRIPTION FACTOR GATA 2;

EID: 79952103416     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tem.2010.11.004     Document Type: Review
Times cited : (72)

References (56)
  • 1
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen J.D., Evans R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 1995, 377:454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 2
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
    • Hörlein A.J., et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 1995, 377:397-404.
    • (1995) Nature , vol.377 , pp. 397-404
    • Hörlein, A.J.1
  • 3
    • 3242784885 scopus 로고    scopus 로고
    • Mechanism of the nuclear receptor molecular switch
    • Nagy L., Schwabe J.W. Mechanism of the nuclear receptor molecular switch. Trends Biochem. Sci. 2004, 29:317-324.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 317-324
    • Nagy, L.1    Schwabe, J.W.2
  • 4
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna N.J., O'Malley B.W. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 2002, 108:465-474.
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 5
    • 0024080921 scopus 로고
    • Hormone-mediated repression: a negative glucocorticoid response element from the bovine prolactin gene
    • Sakai D.D., et al. Hormone-mediated repression: a negative glucocorticoid response element from the bovine prolactin gene. Genes Dev. 1988, 2:1144-1154.
    • (1988) Genes Dev. , vol.2 , pp. 1144-1154
    • Sakai, D.D.1
  • 6
    • 0024357987 scopus 로고
    • Negative regulation of the thyroid-stimulating hormone alpha gene by thyroid hormone: receptor interaction adjacent to the TATA box
    • Chatterjee V.K., et al. Negative regulation of the thyroid-stimulating hormone alpha gene by thyroid hormone: receptor interaction adjacent to the TATA box. Proc. Natl. Acad. Sci. U. S. A. 1989, 86:9114-9118.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 9114-9118
    • Chatterjee, V.K.1
  • 7
    • 0024456922 scopus 로고
    • Thyroid hormone inhibition of human thyrotropin beta-subunit gene expression is mediated by a cis-acting element located in the first exon
    • Wondisford F.E., et al. Thyroid hormone inhibition of human thyrotropin beta-subunit gene expression is mediated by a cis-acting element located in the first exon. J. Biol. Chem. 1989, 264:14601-14604.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14601-14604
    • Wondisford, F.E.1
  • 8
    • 0037428431 scopus 로고    scopus 로고
    • Thyroid hormone receptor DNA binding is required for both positive and negative gene regulation
    • Shibusawa N., et al. Thyroid hormone receptor DNA binding is required for both positive and negative gene regulation. J. Biol. Chem. 2003, 278:732-738.
    • (2003) J. Biol. Chem. , vol.278 , pp. 732-738
    • Shibusawa, N.1
  • 9
    • 85047692403 scopus 로고    scopus 로고
    • Thyroid hormone action in the absence of thyroid hormone receptor DNA-binding in vivo
    • Shibusawa N., et al. Thyroid hormone action in the absence of thyroid hormone receptor DNA-binding in vivo. J. Clin. Invest. 2003, 112:588-597.
    • (2003) J. Clin. Invest. , vol.112 , pp. 588-597
    • Shibusawa, N.1
  • 10
    • 0032483406 scopus 로고    scopus 로고
    • Glucocorticoids repress transcription from a negative glucocorticoid response element recognized by two homeodomain-containing proteins, Pbx and Oct-1
    • Subramaniam N., et al. Glucocorticoids repress transcription from a negative glucocorticoid response element recognized by two homeodomain-containing proteins, Pbx and Oct-1. J. Biol. Chem. 1998, 273:23567-23574.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23567-23574
    • Subramaniam, N.1
  • 11
    • 1842583520 scopus 로고    scopus 로고
    • A response unit in the first exon of the beta-amyloid precursor protein gene containing thyroid hormone receptor and Sp1 binding sites mediates negative regulation by 3,5,3′-triiodothyronine
    • Villa A., et al. A response unit in the first exon of the beta-amyloid precursor protein gene containing thyroid hormone receptor and Sp1 binding sites mediates negative regulation by 3,5,3′-triiodothyronine. Mol. Endocrinol. 2004, 18:863-873.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 863-873
    • Villa, A.1
  • 12
    • 0033529543 scopus 로고    scopus 로고
    • Mechanisms that mediate negative regulation of the thyroid-stimulating hormone alpha gene by the thyroid hormone receptor
    • Tagami T., et al. Mechanisms that mediate negative regulation of the thyroid-stimulating hormone alpha gene by the thyroid hormone receptor. J. Biol. Chem. 1999, 274:22345-22353.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22345-22353
    • Tagami, T.1
  • 13
    • 0037147224 scopus 로고    scopus 로고
    • Corepressor SMRT functions as a coactivator for thyroid hormone receptor T3Ralpha from a negative hormone response element
    • Berghagen H., et al. Corepressor SMRT functions as a coactivator for thyroid hormone receptor T3Ralpha from a negative hormone response element. J. Biol. Chem. 2002, 277:49517-49522.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49517-49522
    • Berghagen, H.1
  • 14
    • 24644447873 scopus 로고    scopus 로고
    • Negative regulation by thyroid hormone receptor requires an intact coactivator-binding surface
    • Ortiga-Carvalho T.M., et al. Negative regulation by thyroid hormone receptor requires an intact coactivator-binding surface. J. Clin. Invest. 2005, 115:2517-2523.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2517-2523
    • Ortiga-Carvalho, T.M.1
  • 15
    • 33747606243 scopus 로고    scopus 로고
    • Negative regulation of superoxide dismutase-1 promoter by thyroid hormone
    • Santos G.M., et al. Negative regulation of superoxide dismutase-1 promoter by thyroid hormone. Mol. Pharmacol. 2006, 70:793-800.
    • (2006) Mol. Pharmacol. , vol.70 , pp. 793-800
    • Santos, G.M.1
  • 16
    • 0036212262 scopus 로고    scopus 로고
    • 3-regulated transcription of genes in vivo
    • 3-regulated transcription of genes in vivo. Endocrinology 2002, 143:1346-1352.
    • (2002) Endocrinology , vol.143 , pp. 1346-1352
    • Takeuchi, Y.1
  • 17
    • 0033118328 scopus 로고    scopus 로고
    • Mice deficient in the steroid receptor co-activator 1 (SRC-1) are resistant to thyroid hormone
    • Weiss R.E., et al. Mice deficient in the steroid receptor co-activator 1 (SRC-1) are resistant to thyroid hormone. EMBO J. 1999, 18:1900-1904.
    • (1999) EMBO J. , vol.18 , pp. 1900-1904
    • Weiss, R.E.1
  • 18
    • 33745748585 scopus 로고    scopus 로고
    • Absence of the steroid receptor coactivator-3 induces B-cell lymphoma
    • Coste A., et al. Absence of the steroid receptor coactivator-3 induces B-cell lymphoma. EMBO J. 2006, 25:2453-2464.
    • (2006) EMBO J. , vol.25 , pp. 2453-2464
    • Coste, A.1
  • 19
    • 0345564849 scopus 로고    scopus 로고
    • Target-specific utilization of transcriptional regulatory surfaces by the glucocorticoid receptor
    • Rogatsky I., et al. Target-specific utilization of transcriptional regulatory surfaces by the glucocorticoid receptor. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:13845-13850.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13845-13850
    • Rogatsky, I.1
  • 20
    • 65249167505 scopus 로고    scopus 로고
    • DNA binding site sequence directs glucocorticoid receptor structure and activity
    • Meijsing S.H., et al. DNA binding site sequence directs glucocorticoid receptor structure and activity. Science 2009, 324:407-410.
    • (2009) Science , vol.324 , pp. 407-410
    • Meijsing, S.H.1
  • 21
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
    • Metzger E., et al. LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 2005, 437:436-439.
    • (2005) Nature , vol.437 , pp. 436-439
    • Metzger, E.1
  • 22
    • 77950460256 scopus 로고    scopus 로고
    • I controls demethylation at histone H3K4
    • I controls demethylation at histone H3K4. Nature 2010, 464:792-796.
    • (2010) Nature , vol.464 , pp. 792-796
    • Metzger, E.1
  • 23
    • 58149142965 scopus 로고    scopus 로고
    • Multi-modulation of nuclear receptor coactivators through posttranslational modifications
    • Han S.J., et al. Multi-modulation of nuclear receptor coactivators through posttranslational modifications. Trends Endocrinol. Metab. 2009, 20:8-15.
    • (2009) Trends Endocrinol. Metab. , vol.20 , pp. 8-15
    • Han, S.J.1
  • 24
    • 34548252291 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation
    • Lonard D.M., O'Malley B.W. Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation. Mol. Cell 2007, 27:691-700.
    • (2007) Mol. Cell , vol.27 , pp. 691-700
    • Lonard, D.M.1    O'Malley, B.W.2
  • 25
    • 33744792310 scopus 로고    scopus 로고
    • Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response
    • Rosenfeld M.G., et al. Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response. Genes Dev. 2006, 20:1405-1428.
    • (2006) Genes Dev. , vol.20 , pp. 1405-1428
    • Rosenfeld, M.G.1
  • 26
    • 40849114903 scopus 로고    scopus 로고
    • Acetylation in nuclear receptor signaling and the role of sirtuins
    • Wang C., et al. Acetylation in nuclear receptor signaling and the role of sirtuins. Mol. Endocrinol. 2008, 22:539-545.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 539-545
    • Wang, C.1
  • 27
    • 77954832705 scopus 로고    scopus 로고
    • The interaction between nuclear receptor corepressor and histone deacetylase 3 regulates both positive and negative thyroid hormone action in vivo
    • You S.H., et al. The interaction between nuclear receptor corepressor and histone deacetylase 3 regulates both positive and negative thyroid hormone action in vivo. Mol. Endocrinol. 2010, 24:1359-1367.
    • (2010) Mol. Endocrinol. , vol.24 , pp. 1359-1367
    • You, S.H.1
  • 28
    • 0032230248 scopus 로고    scopus 로고
    • A regulatory role for RIP140 in nuclear receptor activation
    • Treuter E., et al. A regulatory role for RIP140 in nuclear receptor activation. Mol. Endocrinol. 1998, 12:864-881.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 864-881
    • Treuter, E.1
  • 29
    • 0034731401 scopus 로고    scopus 로고
    • Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing
    • Wei L.N., et al. Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing. J. Biol. Chem. 2000, 275:40782-40787.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40782-40787
    • Wei, L.N.1
  • 30
    • 33746077514 scopus 로고    scopus 로고
    • Metabolic regulation by the nuclear receptor corepressor RIP140
    • Christian M., et al. Metabolic regulation by the nuclear receptor corepressor RIP140. Trends Endocrinol. Metab. 2006, 17:243-250.
    • (2006) Trends Endocrinol. Metab. , vol.17 , pp. 243-250
    • Christian, M.1
  • 31
    • 0037248643 scopus 로고    scopus 로고
    • Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms
    • Fernandes I., et al. Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms. Mol. Cell 2003, 11:139-150.
    • (2003) Mol. Cell , vol.11 , pp. 139-150
    • Fernandes, I.1
  • 32
    • 22344445394 scopus 로고    scopus 로고
    • The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene
    • Yin L., Lazar M.A. The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene. Mol. Endocrinol. 2005, 19:1452-1459.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 1452-1459
    • Yin, L.1    Lazar, M.A.2
  • 33
    • 36849084107 scopus 로고    scopus 로고
    • Identification of heme as the ligand for the orphan nuclear receptors REV-ERBalpha and REV-ERBbeta
    • Raghuram S., et al. Identification of heme as the ligand for the orphan nuclear receptors REV-ERBalpha and REV-ERBbeta. Nat. Struct. Mol. Biol. 2007, 14:1207-1213.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1207-1213
    • Raghuram, S.1
  • 34
    • 0037379181 scopus 로고    scopus 로고
    • Using nondenaturing mass spectrometry to detect fortuitous ligands in orphan nuclear receptors
    • Potier N., et al. Using nondenaturing mass spectrometry to detect fortuitous ligands in orphan nuclear receptors. Protein Sci. 2003, 12:725-733.
    • (2003) Protein Sci. , vol.12 , pp. 725-733
    • Potier, N.1
  • 35
    • 0141730390 scopus 로고    scopus 로고
    • All-trans retinoic acid is a ligand for the orphan nuclear receptor ROR beta
    • Stehlin-Gaon C., et al. All-trans retinoic acid is a ligand for the orphan nuclear receptor ROR beta. Nat. Struct. Biol. 2003, 10:820-825.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 820-825
    • Stehlin-Gaon, C.1
  • 36
    • 19944372389 scopus 로고    scopus 로고
    • A structural basis for constitutive activity in the human CAR/RXRalpha heterodimer
    • Xu R.X., et al. A structural basis for constitutive activity in the human CAR/RXRalpha heterodimer. Mol. Cell 2004, 16:919-928.
    • (2004) Mol. Cell , vol.16 , pp. 919-928
    • Xu, R.X.1
  • 37
    • 0032497544 scopus 로고    scopus 로고
    • Androstane metabolites bind to and deactivate the nuclear receptor CAR-beta
    • Forman B.M., et al. Androstane metabolites bind to and deactivate the nuclear receptor CAR-beta. Nature 1998, 395:612-615.
    • (1998) Nature , vol.395 , pp. 612-615
    • Forman, B.M.1
  • 38
    • 0036311095 scopus 로고    scopus 로고
    • A structural model of the constitutive androstane receptor defines novel interactions that mediate ligand-independent activity
    • Dussault I., et al. A structural model of the constitutive androstane receptor defines novel interactions that mediate ligand-independent activity. Mol. Cell Biol. 2002, 22:5270-5280.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 5270-5280
    • Dussault, I.1
  • 39
    • 10944229118 scopus 로고    scopus 로고
    • Structure of the murine constitutive androstane receptor complexed to androstenol: a molecular basis for inverse agonism
    • Shan L., et al. Structure of the murine constitutive androstane receptor complexed to androstenol: a molecular basis for inverse agonism. Mol. Cell 2004, 16:907-917.
    • (2004) Mol. Cell , vol.16 , pp. 907-917
    • Shan, L.1
  • 40
    • 0023849563 scopus 로고
    • Steroid receptor-mediated inhibition of rat prolactin gene expression does not require the receptor DNA-binding domain
    • Adler S., et al. Steroid receptor-mediated inhibition of rat prolactin gene expression does not require the receptor DNA-binding domain. Cell 1988, 52:685-695.
    • (1988) Cell , vol.52 , pp. 685-695
    • Adler, S.1
  • 41
    • 33750475959 scopus 로고    scopus 로고
    • Cross-talk between nuclear receptors and nuclear factor kappaB
    • De Bosscher K., et al. Cross-talk between nuclear receptors and nuclear factor kappaB. Oncogene 2006, 25:6868-6886.
    • (2006) Oncogene , vol.25 , pp. 6868-6886
    • De Bosscher, K.1
  • 42
    • 18144444807 scopus 로고    scopus 로고
    • DNA binding of the glucocorticoid receptor is not essential for survival
    • Reichardt H.M., et al. DNA binding of the glucocorticoid receptor is not essential for survival. Cell 1998, 93:531-541.
    • (1998) Cell , vol.93 , pp. 531-541
    • Reichardt, H.M.1
  • 43
    • 0035971434 scopus 로고    scopus 로고
    • Cross-talk between glucocorticoid receptor and AP-1
    • Herrlich P. Cross-talk between glucocorticoid receptor and AP-1. Oncogene 2001, 20:2465-2475.
    • (2001) Oncogene , vol.20 , pp. 2465-2475
    • Herrlich, P.1
  • 44
    • 48249111889 scopus 로고    scopus 로고
    • Restriction to Fos family members of Trip6-dependent coactivation and glucocorticoid receptor-dependent trans-repression of activator protein-1
    • Diefenbacher M., et al. Restriction to Fos family members of Trip6-dependent coactivation and glucocorticoid receptor-dependent trans-repression of activator protein-1. Mol. Endocrinol. 2008, 22:1767-1780.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1767-1780
    • Diefenbacher, M.1
  • 45
    • 0030789420 scopus 로고    scopus 로고
    • I kappaB alpha-independent downregulation of NF-kappaB activity by glucocorticoid receptor
    • Heck S., et al. I kappaB alpha-independent downregulation of NF-kappaB activity by glucocorticoid receptor. EMBO J. 1997, 16:4698-4707.
    • (1997) EMBO J. , vol.16 , pp. 4698-4707
    • Heck, S.1
  • 46
    • 0025130179 scopus 로고
    • Functional antagonism between oncoprotein c-Jun and the glucocorticoid receptor
    • Schüle R., et al. Functional antagonism between oncoprotein c-Jun and the glucocorticoid receptor. Cell 1990, 62:1217-1226.
    • (1990) Cell , vol.62 , pp. 1217-1226
    • Schüle, R.1
  • 47
    • 0025188132 scopus 로고
    • Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction
    • Yang-Yen H.F., et al. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell 1990, 62:1205-1215.
    • (1990) Cell , vol.62 , pp. 1205-1215
    • Yang-Yen, H.F.1
  • 48
    • 34247844378 scopus 로고    scopus 로고
    • Essential role of GATA2 in the negative regulation of thyrotropin beta gene by thyroid hormone and its receptors
    • Matsushita A., et al. Essential role of GATA2 in the negative regulation of thyrotropin beta gene by thyroid hormone and its receptors. Mol. Endocrinol. 2007, 21:865-884.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 865-884
    • Matsushita, A.1
  • 49
    • 77958615259 scopus 로고    scopus 로고
    • Dissecting the relation between a nuclear receptor and GATA: binding affinity studies of thyroid hormone receptor and GATA2 on TSHβ promoter
    • Figueira A.C., et al. Dissecting the relation between a nuclear receptor and GATA: binding affinity studies of thyroid hormone receptor and GATA2 on TSHβ promoter. PLoS ONE 2010, 5:e12628.
    • (2010) PLoS ONE , vol.5
    • Figueira, A.C.1
  • 50
    • 26444471700 scopus 로고    scopus 로고
    • A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-gamma
    • Pascual G., et al. A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-gamma. Nature 2005, 437:759-763.
    • (2005) Nature , vol.437 , pp. 759-763
    • Pascual, G.1
  • 51
    • 41649102323 scopus 로고    scopus 로고
    • A global view of transcriptional regulation by nuclear receptors: gene expression, factor localization, and DNA sequence analysis
    • Kininis M., Kraus W.L. A global view of transcriptional regulation by nuclear receptors: gene expression, factor localization, and DNA sequence analysis. Nucl. Recept. signaling 2008, 6:e005.
    • (2008) Nucl. Recept. signaling , vol.6
    • Kininis, M.1    Kraus, W.L.2
  • 52
    • 34347345081 scopus 로고    scopus 로고
    • Whole-genome cartography of estrogen receptor alpha binding sites
    • Lin C.Y., et al. Whole-genome cartography of estrogen receptor alpha binding sites. PLoS Genet. 2007, 3:e87.
    • (2007) PLoS Genet. , vol.3
    • Lin, C.Y.1
  • 53
    • 44449126207 scopus 로고    scopus 로고
    • Conservation analysis predicts in vivo occupancy of glucocorticoid receptor-binding sequences at glucocorticoid-induced genes
    • So A.Y., et al. Conservation analysis predicts in vivo occupancy of glucocorticoid receptor-binding sequences at glucocorticoid-induced genes. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:5745-5749.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 5745-5749
    • So, A.Y.1
  • 54
    • 0023805741 scopus 로고
    • Negative effect of the transcriptional activator GAL4
    • Gill G., Ptashne M. Negative effect of the transcriptional activator GAL4. Nature 1988, 334:721-724.
    • (1988) Nature , vol.334 , pp. 721-724
    • Gill, G.1    Ptashne, M.2
  • 55
    • 69449102464 scopus 로고    scopus 로고
    • Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
    • Wang Z., et al. Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes. Cell 2009, 138:1019-1031.
    • (2009) Cell , vol.138 , pp. 1019-1031
    • Wang, Z.1
  • 56
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Métivier R., et al. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 2003, 115:751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Métivier, R.1


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