메뉴 건너뛰기




Volumn 19, Issue 15, 2000, Pages 4074-4090

Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-ErbA yields a chromatin infrastructure-dependent transcriptional repression pathway

Author keywords

Histone deacetylase (HDAC)3; N CoR; Thyroid hormone receptor; Transcriptional repression; v ErbA

Indexed keywords

ENZYME INHIBITOR; HISTONE DEACETYLASE; MUTANT PROTEIN; ONCOPROTEIN; REPRESSOR PROTEIN; THYROID HORMONE RECEPTOR; TRANSCRIPTION FACTOR;

EID: 0034254668     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.15.4074     Document Type: Article
Times cited : (64)

References (87)
  • 1
    • 0033118950 scopus 로고    scopus 로고
    • Chromatin assembly: Biochemical identities and genetic redundancy
    • Adams, C.R. and Kamakaka, R.T. (1999) Chromatin assembly: biochemical identities and genetic redundancy. Curr. Opin. Genet. Dev., 9, 185-190.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 185-190
    • Adams, C.R.1    Kamakaka, R.T.2
  • 2
    • 0027258499 scopus 로고
    • Nuclear assembly, structure, and function: The use of Xenopus in vitro systems
    • Almouzni, G. and Wolffe, A.P. (1993a) Nuclear assembly, structure, and function: the use of Xenopus in vitro systems. Exp. Cell Res., 205, 1-15.
    • (1993) Exp. Cell Res. , vol.205 , pp. 1-15
    • Almouzni, G.1    Wolffe, A.P.2
  • 3
    • 0027385167 scopus 로고
    • Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo
    • Almouzni, G. and Wolffe, A.P. (1993b) Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo. Genes Dev., 7, 2033-2047.
    • (1993) Genes Dev. , vol.7 , pp. 2033-2047
    • Almouzni, G.1    Wolffe, A.P.2
  • 4
    • 0025055091 scopus 로고
    • Competition between transcription complex assembly and chromatin assembly on replicating DNA
    • Almouzni, G., Mechali, M. and Wolffe, A.P. (1990) Competition between transcription complex assembly and chromatin assembly on replicating DNA. EMBO J., 9, 573-582.
    • (1990) EMBO J. , vol.9 , pp. 573-582
    • Almouzni, G.1    Mechali, M.2    Wolffe, A.P.3
  • 5
    • 0027435514 scopus 로고
    • Interaction of human thyroid hormone receptor β with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone
    • Baniahmad, A., Ha, I., Reinberg, D., Tsai, S., Tsai, M.J. and O'Malley, B.W. (1993) Interaction of human thyroid hormone receptor β with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone. Proc. Natl Acad. Sci. USA, 90, 8832-8836.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8832-8836
    • Baniahmad, A.1    Ha, I.2    Reinberg, D.3    Tsai, S.4    Tsai, M.J.5    O'Malley, B.W.6
  • 6
    • 0032480015 scopus 로고    scopus 로고
    • The thyroid hormone receptor functions as a ligand-operated developmental switch between proliferation and differentiation of erythroid progenitors
    • Bauer, A., Mikulits, W., Lagger, G., Stengl, G., Brosch, G. and Beug, H. (1998) The thyroid hormone receptor functions as a ligand-operated developmental switch between proliferation and differentiation of erythroid progenitors. EMBO J., 17, 4291-4303.
    • (1998) EMBO J. , vol.17 , pp. 4291-4303
    • Bauer, A.1    Mikulits, W.2    Lagger, G.3    Stengl, G.4    Brosch, G.5    Beug, H.6
  • 7
    • 0028053577 scopus 로고
    • Insights into erythroid differentiation obtained from studies on avian erythroblastosis virus
    • Beug, H., Mullner, E.W. and Hayman, M.J. (1994) Insights into erythroid differentiation obtained from studies on avian erythroblastosis virus. Curr. Opin. Cell Biol., 6, 816-824.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 816-824
    • Beug, H.1    Mullner, E.W.2    Hayman, M.J.3
  • 9
    • 0032484989 scopus 로고    scopus 로고
    • Retinoblastoma protein recruits histone deacetylase to repress transcription
    • Brehm, A., Miska, E.A., McCance, D.J., Reid, J.L., Bannister, A.J. and Kouzarides, T. (1998) Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature, 391, 597-601.
    • (1998) Nature , vol.391 , pp. 597-601
    • Brehm, A.1    Miska, E.A.2    McCance, D.J.3    Reid, J.L.4    Bannister, A.J.5    Kouzarides, T.6
  • 10
    • 0029205528 scopus 로고
    • Amphibian metamorphosis: A complex program of gene expression changes controlled by the thyroid hormone
    • Brown, D.D., Wang, Z., Kanamori, A., Eliceiri, B., Furlow, J.D. and Schwartzman, R. (1995) Amphibian metamorphosis: a complex program of gene expression changes controlled by the thyroid hormone. Recent Prog. Horm. Res., 50, 309-315.
    • (1995) Recent Prog. Horm. Res. , vol.50 , pp. 309-315
    • Brown, D.D.1    Wang, Z.2    Kanamori, A.3    Eliceiri, B.4    Furlow, J.D.5    Schwartzman, R.6
  • 11
    • 0033200392 scopus 로고    scopus 로고
    • A functional interaction between the histone deacetylase rpd3 and the corepressor groucho in Drosophila development
    • Chen, G., Fernandez, J., Mische, S. and Courey, A.J. (1999) A functional interaction between the histone deacetylase rpd3 and the corepressor groucho in Drosophila development. Genes Dev., 13, 2218-2230.
    • (1999) Genes Dev. , vol.13 , pp. 2218-2230
    • Chen, G.1    Fernandez, J.2    Mische, S.3    Courey, A.J.4
  • 12
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen, J.D. and Evans, R.M. (1995) A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature, 377, 454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 13
    • 0002882756 scopus 로고    scopus 로고
    • Counting nucleosome cores on circular DNA using topoisomerase I
    • Gould, H. (ed.), Oxford University Press, Oxford, UK
    • Clark, D.J. (1998) Counting nucleosome cores on circular DNA using topoisomerase I. In Gould, H. (ed.), Chromatin. IRL Practical Approach Series. Oxford University Press, Oxford, UK, pp. 139-152.
    • (1998) Chromatin. IRL Practical Approach Series , pp. 139-152
    • Clark, D.J.1
  • 14
    • 0025938598 scopus 로고
    • Superhelical stress and nucleosome-mediated repression of 5S RNA gene transcription in vitro
    • Clark, D.J. and Wolffe, A.P. (1991) Superhelical stress and nucleosome-mediated repression of 5S RNA gene transcription in vitro. EMBO J., 10, 3419-3428.
    • (1991) EMBO J. , vol.10 , pp. 3419-3428
    • Clark, D.J.1    Wolffe, A.P.2
  • 15
    • 0033574663 scopus 로고    scopus 로고
    • A unified nomenclature system for the nuclear receptor superfamily
    • Committee (1999) A unified nomenclature system for the nuclear receptor superfamily. Cell, 97, 161-163.
    • (1999) Cell , vol.97 , pp. 161-163
  • 16
    • 0024336324 scopus 로고
    • Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist
    • Damm, K., Thompson, C.C. and Evans, R.M. (1989) Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist. Nature, 339, 593-597.
    • (1989) Nature , vol.339 , pp. 593-597
    • Damm, K.1    Thompson, C.C.2    Evans, R.M.3
  • 18
    • 0026600841 scopus 로고
    • Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
    • Danielian, P.S., White, R., Lees, J.A. and Parker, M.G. (1992) Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J., 11, 1025-1033.
    • (1992) EMBO J. , vol.11 , pp. 1025-1033
    • Danielian, P.S.1    White, R.2    Lees, J.A.3    Parker, M.G.4
  • 22
    • 0027240151 scopus 로고
    • Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: Implications for active repression
    • Fondell, J.D., Roy, A.L. and Roeder, R.G. (1993) Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: implications for active repression. Genes Dev., 7, 1400-1410.
    • (1993) Genes Dev. , vol.7 , pp. 1400-1410
    • Fondell, J.D.1    Roy, A.L.2    Roeder, R.G.3
  • 23
    • 0029656208 scopus 로고    scopus 로고
    • Unliganded thyroid hormone receptor α can target TATA-binding protein for transcriptional repression
    • Fondell, J.D., Brunel, F., Hisatake, K. and Roeder, R.G. (1996) Unliganded thyroid hormone receptor α can target TATA-binding protein for transcriptional repression. Mol. Cell. Biol., 16, 281-287.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 281-287
    • Fondell, J.D.1    Brunel, F.2    Hisatake, K.3    Roeder, R.G.4
  • 24
    • 11944266626 scopus 로고
    • Ectopic expression of the erythrocyte band 3 anion exchange protein, using a new avian retrovirus vector
    • Fuerstenberg, S. et al. (1990) Ectopic expression of the erythrocyte band 3 anion exchange protein, using a new avian retrovirus vector. J. Virol., 64, 5891-5902.
    • (1990) J. Virol. , vol.64 , pp. 5891-5902
    • Fuerstenberg, S.1
  • 25
    • 0028303884 scopus 로고
    • The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein
    • Ge, H. and Roeder, R.G. (1994) The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein. J. Biol. Chem., 269, 17136-17140.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17136-17140
    • Ge, H.1    Roeder, R.G.2
  • 26
    • 0034192756 scopus 로고    scopus 로고
    • A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness
    • Guenther, M.G., Lane, W.S., Fischle, W., Verdin, E., Lazar, M.A. and Shiekhattar, R. (2000) A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness. Genes Dev., 14, 1048-1057.
    • (2000) Genes Dev. , vol.14 , pp. 1048-1057
    • Guenther, M.G.1    Lane, W.S.2    Fischle, W.3    Verdin, E.4    Lazar, M.A.5    Shiekhattar, R.6
  • 27
    • 0014351957 scopus 로고
    • Changes in somatic cell nuclei inserted into growing and maturing amphibian oocytes
    • Gurdon, J.B. (1968) Changes in somatic cell nuclei inserted into growing and maturing amphibian oocytes. J. Embryol. Exp. Morphol., 20, 401-414.
    • (1968) J. Embryol. Exp. Morphol. , vol.20 , pp. 401-414
    • Gurdon, J.B.1
  • 28
    • 0029978521 scopus 로고    scopus 로고
    • Active repression mechanisms of eukaryotic transcription repressors
    • Hanna-Rose, W. and Hansen, U. (1996) Active repression mechanisms of eukaryotic transcription repressors. Trends Genet., 12, 229-234.
    • (1996) Trends Genet. , vol.12 , pp. 229-234
    • Hanna-Rose, W.1    Hansen, U.2
  • 30
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin3A
    • Hassig, C.A., Fleischer, T.C, Billin, A.N., Schreiber, S.L. and Ayer, D.E. (1997) Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell, 89, 341-347.
    • (1997) Cell , vol.89 , pp. 341-347
    • Hassig, C.A.1    Fleischer, T.C.2    Billin, A.N.3    Schreiber, S.L.4    Ayer, D.E.5
  • 32
    • 17744413444 scopus 로고    scopus 로고
    • A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
    • Heinzel, T. et al. (1997) A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature, 387, 43-48.
    • (1997) Nature , vol.387 , pp. 43-48
    • Heinzel, T.1
  • 33
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
    • Hoerlein, A.J. et al. (1995) Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature, 377, 397-404.
    • (1995) Nature , vol.377 , pp. 397-404
    • Hoerlein, A.J.1
  • 34
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • Huang, E.Y., Zhang, J., Miska, E.A., Guenther, M.G., Kouzarides, T. and Lazar, M.A. (2000) Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev., 14, 45-54.
    • (2000) Genes Dev. , vol.14 , pp. 45-54
    • Huang, E.Y.1    Zhang, J.2    Miska, E.A.3    Guenther, M.G.4    Kouzarides, T.5    Lazar, M.A.6
  • 36
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao, H.Y., Downes, M., Ordentlich, P. and Evans, R.M. (2000) Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev., 14, 55-66.
    • (2000) Genes Dev. , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 37
    • 0031104930 scopus 로고    scopus 로고
    • DNA methylation directs a time-dependent repression of transcription initiation
    • Kass, S.U., Landsberger, N. and Wolffe, A.P. (1997) DNA methylation directs a time-dependent repression of transcription initiation. Curr. Biol., 7, 157-165.
    • (1997) Curr. Biol. , vol.7 , pp. 157-165
    • Kass, S.U.1    Landsberger, N.2    Wolffe, A.P.3
  • 38
    • 0033152491 scopus 로고    scopus 로고
    • Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes
    • Koipally, J., Renold, A., Kim, J. and Georgopoulos, K. (1999) Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes. EMBO J., 18, 3090-3100.
    • (1999) EMBO J. , vol.18 , pp. 3090-3100
    • Koipally, J.1    Renold, A.2    Kim, J.3    Georgopoulos, K.4
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
    • Laherty, C.D., Yang, W.M., Sun, J.M., Davie, J.R., Seto, E. and Eisenman, R.N. (1997) Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell, 89, 349-356.
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 42
    • 0032849352 scopus 로고    scopus 로고
    • RBPI recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins
    • Lai, A., Lee, J.M., Yang, W.-M., DeCaprio, J.A., Kaelin, W.G., Seto, E. and Branton, P.E. (1999) RBPI recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins. Mol. Cell. Biol., 19, 6632-6641.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6632-6641
    • Lai, A.1    Lee, J.M.2    Yang, W.-M.3    DeCaprio, J.A.4    Kaelin, W.G.5    Seto, E.6    Branton, P.E.7
  • 43
    • 0032802247 scopus 로고    scopus 로고
    • 3 and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties
    • 3 and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties. Mol. Cell. Biol., 19, 5486-5494.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5486-5494
    • Lavigne, A.C.1    Mengus, G.2    Gangloff, Y.G.3    Wurtz, J.M.4    Davidson, I.5
  • 44
    • 0028876893 scopus 로고
    • Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor
    • Lee, J.W., Choi, H.S., Gyuris, J., Brent, R. and Moore, D.D. (1995) Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol. Endocrinol., 9, 243-254.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 243-254
    • Lee, J.W.1    Choi, H.S.2    Gyuris, J.3    Brent, R.4    Moore, D.D.5
  • 45
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo, R.X., Postigo, A.A. and Dean, D.C. (1998) Rb interacts with histone deacetylase to repress transcription. Cell, 92, 463-473.
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 46
    • 0028853058 scopus 로고
    • Analysis of structure and expression of the Xenopus thyroid hormone receptor β gene to explain its autoinduction
    • Machuca, I., Esslemont, G., Fairclough, L. and Tata, J.R. (1995) Analysis of structure and expression of the Xenopus thyroid hormone receptor β gene to explain its autoinduction. Mol. Endocrinol., 9, 96-107.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 96-107
    • Machuca, I.1    Esslemont, G.2    Fairclough, L.3    Tata, J.R.4
  • 48
    • 0033535957 scopus 로고    scopus 로고
    • The Rpd3 histone deacetylase is required for segmentation of the Drosophila embryo
    • Mannervik, M. and Levine, M. (1999) The Rpd3 histone deacetylase is required for segmentation of the Drosophila embryo. Proc. Natl Acad. Sci. USA, 96, 6797-6801.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6797-6801
    • Mannervik, M.1    Levine, M.2
  • 49
    • 0031833450 scopus 로고    scopus 로고
    • The nuclear receptor ligand-binding domain: Structure and function
    • Moras, D. and Gronemeyer, H. (1998) The nuclear receptor ligand-binding domain: structure and function. Curr. Opin. Cell Biol., 10, 384-391.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 384-391
    • Moras, D.1    Gronemeyer, H.2
  • 50
    • 0023797883 scopus 로고
    • Characterization of the hormone-binding domain of the chicken c-erbA/thyroid hormone receptor protein
    • Munoz, A., Zenke, M., Gehring, U., Sap, J., Beug, H. and Vennstrom, B. (1988) Characterization of the hormone-binding domain of the chicken c-erbA/thyroid hormone receptor protein. EMBO J., 7, 155-159.
    • (1988) EMBO J. , vol.7 , pp. 155-159
    • Munoz, A.1    Zenke, M.2    Gehring, U.3    Sap, J.4    Beug, H.5    Vennstrom, B.6
  • 51
    • 0032526615 scopus 로고    scopus 로고
    • The corepressor N-CoR and its variants RIP13a and RIP13Δ1 directly interact with the basal transcription factors TFIIB, TAFII32 and TAFII70
    • Muscat, G.E., Burke, L.J. and Downes, M. (1998) The corepressor N-CoR and its variants RIP13a and RIP13Δ1 directly interact with the basal transcription factors TFIIB, TAFII32 and TAFII70. Nucleic Acids Res., 26, 2899-2907.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2899-2907
    • Muscat, G.E.1    Burke, L.J.2    Downes, M.3
  • 52
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • Nagy, L., Kao, H.Y., Chakravarti, D., Lin, R.J., Hassig, C.A., Ayer, D.E., Schreiber, S.L. and Evans, R.M. (1997) Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell, 89, 373-380.
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.Y.2    Chakravarti, D.3    Lin, R.J.4    Hassig, C.A.5    Ayer, D.E.6    Schreiber, S.L.7    Evans, R.M.8
  • 53
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan, X., Ng, H.H., Johnson, C.A., Laherty, C.D., Turner, B.M., Eisenman, R.N. and Bird, A. (1998) Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature, 393, 386-389.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 54
    • 0032525781 scopus 로고    scopus 로고
    • A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system
    • Rachez, C., Suldan, Z., Ward, J., Chang, C.P., Burakov, D., Erdjument-Bromage, H., Tempst, P. and Freedman, L.P. (1998) A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system. Genes Dev., 12, 1787-1800.
    • (1998) Genes Dev. , vol.12 , pp. 1787-1800
    • Rachez, C.1    Suldan, Z.2    Ward, J.3    Chang, C.P.4    Burakov, D.5    Erdjument-Bromage, H.6    Tempst, P.7    Freedman, L.P.8
  • 55
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
    • Rundlett, S.E., Carmen, A.A., Kobayashi, R., Bavykin, S., Turner, B.M. and Grunstein, M. (1996) HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc. Natl Acad. Sci. USA, 93, 14503-14508.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14503-14508
    • Rundlett, S.E.1    Carmen, A.A.2    Kobayashi, R.3    Bavykin, S.4    Turner, B.M.5    Grunstein, M.6
  • 56
    • 0027175503 scopus 로고
    • A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor)
    • Saatcioglu, F., Bartunek, P., Deng, T., Zenke, M. and Karin, M. (1993) A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor). Mol. Cell. Biol., 13, 3675-3685.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3675-3685
    • Saatcioglu, F.1    Bartunek, P.2    Deng, T.3    Zenke, M.4    Karin, M.5
  • 59
    • 0024400724 scopus 로고
    • Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product
    • Sap, J., Munoz, A., Schmitt, J., Stunnenberg, H. and Vennstrom, B. (1989) Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product. Nature, 340, 242-244.
    • (1989) Nature , vol.340 , pp. 242-244
    • Sap, J.1    Munoz, A.2    Schmitt, J.3    Stunnenberg, H.4    Vennstrom, B.5
  • 60
    • 0028836714 scopus 로고
    • Isolation of proteins that interact specifically with the retinoid X receptor: Two novel orphan receptors
    • Seol, W., Choi, H.S. and Moore, D.D. (1995) Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors. Mol. Endocrinol., 9, 72-85.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 72-85
    • Seol, W.1    Choi, H.S.2    Moore, D.D.3
  • 61
    • 0026516657 scopus 로고
    • Genomic organization and alternative promoter usage of the two thyroid hormone receptor β genes in Xenopus laevis
    • Shi, Y.B., Yaoita, Y. and Brown, D.D. (1992) Genomic organization and alternative promoter usage of the two thyroid hormone receptor β genes in Xenopus laevis. J. Biol. Chem., 267, 733-738.
    • (1992) J. Biol. Chem. , vol.267 , pp. 733-738
    • Shi, Y.B.1    Yaoita, Y.2    Brown, D.D.3
  • 62
    • 0024384868 scopus 로고
    • The assembly of regularly spaced nucleosomes in the Xenopus oocyte S-150 extract is accompanied by deacetylation of histone H4
    • Shimamura, A. and Worcel, A. (1989) The assembly of regularly spaced nucleosomes in the Xenopus oocyte S-150 extract is accompanied by deacetylation of histone H4. J. Biol. Chem., 264, 14524-14530.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14524-14530
    • Shimamura, A.1    Worcel, A.2
  • 63
    • 0033613706 scopus 로고    scopus 로고
    • Leukemia: The sophisticated subversion of hematopoiesis by nuclear receptor oncoproteins
    • Stunnenberg, H.G., Garcia-Jimenez, C. and Betz, J.L. (1999) Leukemia: the sophisticated subversion of hematopoiesis by nuclear receptor oncoproteins. Biochim. Biophys. Acta, 1423, F15-F33.
    • (1999) Biochim. Biophys. Acta , vol.1423
    • Stunnenberg, H.G.1    Garcia-Jimenez, C.2    Betz, J.L.3
  • 64
    • 0029281195 scopus 로고
    • Retinoic acid and retinoic acid receptors in development
    • Sucov, H.M. and Evans, R.M. (1995) Retinoic acid and retinoic acid receptors in development. Mol. Neurobiol., 10, 169-184.
    • (1995) Mol. Neurobiol. , vol.10 , pp. 169-184
    • Sucov, H.M.1    Evans, R.M.2
  • 65
    • 0030331282 scopus 로고    scopus 로고
    • Metamorphosis: An exquisite model for hormonal regulation of post-embryonic development
    • Tata, J.R. (1996) Metamorphosis: an exquisite model for hormonal regulation of post-embryonic development. Biochem. Soc. Symp., 62, 123-136.
    • (1996) Biochem. Soc. Symp. , vol.62 , pp. 123-136
    • Tata, J.R.1
  • 66
    • 0027996382 scopus 로고
    • Functional analysis of a transactivation domain in the thyroid hormone β receptor
    • Tone, Y., Collingwood, T.N., Adams, M. and Chatterjee, V.K. (1994) Functional analysis of a transactivation domain in the thyroid hormone β receptor. J. Biol. Chem., 269, 31157-31161.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31157-31161
    • Tone, Y.1    Collingwood, T.N.2    Adams, M.3    Chatterjee, V.K.4
  • 67
    • 0028970198 scopus 로고
    • Ligand modulates the interaction of thyroid hormone receptor β with the basal transcription machinery
    • Tong, G.X., Tanen, M.R. and Bagchi, M.K. (1995) Ligand modulates the interaction of thyroid hormone receptor β with the basal transcription machinery. J. Biol. Chem., 270, 10601-10611.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10601-10611
    • Tong, G.X.1    Tanen, M.R.2    Bagchi, M.K.3
  • 68
    • 0031835267 scopus 로고    scopus 로고
    • Co-activators and co-repressors in the integration of transcriptional responses
    • Torchia, J., Glass, C. and Rosenfeld, M.G. (1998) Co-activators and co-repressors in the integration of transcriptional responses. Curr. Opin. Cell Biol., 10, 373-383.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 373-383
    • Torchia, J.1    Glass, C.2    Rosenfeld, M.G.3
  • 69
    • 0030998534 scopus 로고    scopus 로고
    • Histone acetylation: Influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression
    • Ura, K., Kurumizaka, H., Dimitrov, S., Almouzni, G. and Wolffe, A.P. (1997) Histone acetylation: influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression. EMBO J., 16, 2096-2107.
    • (1997) EMBO J. , vol.16 , pp. 2096-2107
    • Ura, K.1    Kurumizaka, H.2    Dimitrov, S.3    Almouzni, G.4    Wolffe, A.P.5
  • 70
    • 0033513096 scopus 로고    scopus 로고
    • Translation of maternal TATA-binding protein mRNA potentiates basal but not activated transcription in Xenopus embryos at the midblastula transition
    • Veenstra, G.J., Destree, O.H. and Wolffe, A.P. (1999) Translation of maternal TATA-binding protein mRNA potentiates basal but not activated transcription in Xenopus embryos at the midblastula transition. Mol. Cell. Biol., 19, 7972-7982.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7972-7982
    • Veenstra, G.J.1    Destree, O.H.2    Wolffe, A.P.3
  • 71
    • 0032812342 scopus 로고    scopus 로고
    • Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte
    • Vermaak, D., Wade, P.A., Jones, P.L., Shi, Y.B. and Wolffe, A.P. (1999) Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte. Mol. Cell. Biol., 19, 5847-5860.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5847-5860
    • Vermaak, D.1    Wade, P.A.2    Jones, P.L.3    Shi, Y.B.4    Wolffe, A.P.5
  • 72
    • 0032474826 scopus 로고    scopus 로고
    • A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase
    • Wade, P.A., Jones, P.L., Vermaak, D. and Wolffe, A.P. (1998) A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase. Curr. Biol., 8, 843-846.
    • (1998) Curr. Biol. , vol.8 , pp. 843-846
    • Wade, P.A.1    Jones, P.L.2    Vermaak, D.3    Wolffe, A.P.4
  • 73
    • 0032845039 scopus 로고    scopus 로고
    • Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation
    • Wade, P.A., Gegonne, A., Jones, P.L., Ballestar, E., Aubry, F. and Wolffe, A.P. (1999a) Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation. Nature Genet., 23, 62-66.
    • (1999) Nature Genet. , vol.23 , pp. 62-66
    • Wade, P.A.1    Gegonne, A.2    Jones, P.L.3    Ballestar, E.4    Aubry, F.5    Wolffe, A.P.6
  • 74
    • 0033039348 scopus 로고    scopus 로고
    • Purification of a histone deacetylase complex from Xenopus laevis: Preparation of substrates and assay procedures
    • Wade, P.A., Jones, P.L., Vermaak, D. and Wolffe, A.P. (1999b) Purification of a histone deacetylase complex from Xenopus laevis: preparation of substrates and assay procedures. Methods Enzymol., 304, 715-725.
    • (1999) Methods Enzymol. , vol.304 , pp. 715-725
    • Wade, P.A.1    Jones, P.L.2    Vermaak, D.3    Wolffe, A.P.4
  • 76
    • 0030922545 scopus 로고    scopus 로고
    • Transcriptional control. Sinful repression
    • Wolffe, A.P. ( 1997) Transcriptional control. Sinful repression. Nature, 387, 16-17.
    • (1997) Nature , vol.387 , pp. 16-17
    • Wolffe, A.P.1
  • 77
    • 0031839177 scopus 로고    scopus 로고
    • Transcriptional repression by the SMRT-mSin3 corepressor: Multiple interactions, multiple mechanisms, and a potential role for TFIIB
    • Wong, C.W. and Privalsky, M.L. (1998) Transcriptional repression by the SMRT-mSin3 corepressor: multiple interactions, multiple mechanisms, and a potential role for TFIIB. Mol. Cell. Biol., 18, 5500-5510.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5500-5510
    • Wong, C.W.1    Privalsky, M.L.2
  • 78
    • 0028860925 scopus 로고
    • A role for nucleosome assembly in both silencing and activation of the Xenopus TRβ A gene by the thyroid hormone receptor
    • Wong, J., Shi, Y.B. and Wolffe, A.P. (1995) A role for nucleosome assembly in both silencing and activation of the Xenopus TRβ A gene by the thyroid hormone receptor. Genes Dev., 9, 2696-2711.
    • (1995) Genes Dev. , vol.9 , pp. 2696-2711
    • Wong, J.1    Shi, Y.B.2    Wolffe, A.P.3
  • 79
    • 0030946171 scopus 로고    scopus 로고
    • Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: Hormone-regulated chromatin disruption is not sufficient for transcriptional activation
    • Wong, J., Shi, Y.B. and Wolffe, A.P. (1997) Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: hormone-regulated chromatin disruption is not sufficient for transcriptional activation. EMBO J., 16, 3158-3171.
    • (1997) EMBO J. , vol.16 , pp. 3158-3171
    • Wong, J.1    Shi, Y.B.2    Wolffe, A.P.3
  • 80
    • 0032486275 scopus 로고    scopus 로고
    • Transcription from the thyroid hormone-dependent promoter of the Xenopus laevis thyroid hormone receptor βA gene requires a novel upstream element and the initiator, but not a TATA box
    • Wong, J., Liang, V.C., Sachs, L.M. and Shi, Y.B. (1998a) Transcription from the thyroid hormone-dependent promoter of the Xenopus laevis thyroid hormone receptor βA gene requires a novel upstream element and the initiator, but not a TATA box. J. Biol. Chem., 273, 14186-14193.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14186-14193
    • Wong, J.1    Liang, V.C.2    Sachs, L.M.3    Shi, Y.B.4
  • 81
    • 0032518799 scopus 로고    scopus 로고
    • Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase
    • Wong, J., Patterton, D., Imhof, A., Guschin, D., Shi, Y.B. and Wolffe, A.P. (1998b) Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase. EMBO J., 17, 520-534.
    • (1998) EMBO J. , vol.17 , pp. 520-534
    • Wong, J.1    Patterton, D.2    Imhof, A.3    Guschin, D.4    Shi, Y.B.5    Wolffe, A.P.6
  • 82
    • 0033119162 scopus 로고    scopus 로고
    • Coactivator and corepressor complexes in nuclear receptor function
    • Xu, L., Glass, C.K. and Rosenfeld, M.G. (1999) Coactivator and corepressor complexes in nuclear receptor function. Curr. Opin. Genet. Dev., 9, 140-147.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 140-147
    • Xu, L.1    Glass, C.K.2    Rosenfeld, M.G.3
  • 83
    • 0032252209 scopus 로고    scopus 로고
    • NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities
    • Xue, Y., Wong, J., Moreno, G.T., Young, M.K., Cote, J. and Wang, W. (1998) NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities. Mol. Cell, 2, 851-861.
    • (1998) Mol. Cell , vol.2 , pp. 851-861
    • Xue, Y.1    Wong, J.2    Moreno, G.T.3    Young, M.K.4    Cote, J.5    Wang, W.6
  • 84
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang, W.M., Yao, Y.L., Sun, J.M., Davie, J.R. and Seto, E. (1997) Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J. Biol. Chem., 272, 28001-28007.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5
  • 85
    • 0025339079 scopus 로고
    • A oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA
    • Zenke, M., Munoz, A., Sap, J., Vennstrom, B. and Beug, H. (1990) v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA. Cell, 61, 1035-1049.
    • (1990) Cell , vol.61 , pp. 1035-1049
    • Zenke, M.1    Munoz, A.2    Sap, J.3    Vennstrom, B.4    Beug, H.5
  • 86
    • 0030916729 scopus 로고    scopus 로고
    • Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
    • Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P. and Reinberg, D. (1997) Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell, 89, 357-364.
    • (1997) Cell , vol.89 , pp. 357-364
    • Zhang, Y.1    Iratni, R.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 87
    • 0030961189 scopus 로고    scopus 로고
    • The KH domain protein encoded by quaking functions as a dimer and is essential for notochord development in Xenopus embryos
    • Zorn, A.M. and Krieg, P.A. (1997) The KH domain protein encoded by quaking functions as a dimer and is essential for notochord development in Xenopus embryos. Genes Dev., 11, 2176-2190.
    • (1997) Genes Dev. , vol.11 , pp. 2176-2190
    • Zorn, A.M.1    Krieg, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.