메뉴 건너뛰기




Volumn 87, Issue C, 2009, Pages 193-234

Chapter 6 Chromatin Remodeling and Nuclear Receptor Signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL RECEPTOR; TRANSACTIVATOR PROTEIN;

EID: 77957800880     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1877-1173(09)87006-3     Document Type: Review
Times cited : (7)

References (203)
  • 4
    • 8844262660 scopus 로고    scopus 로고
    • Principles for modulation of the nuclear receptor superfamily
    • 64
    • Gronemeyer H., Gustafsson J.A., and Laudet V. Principles for modulation of the nuclear receptor superfamily. Nat Rev Drug Discov 3 (2004) 950 64
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 950
    • Gronemeyer, H.1    Gustafsson, J.A.2    Laudet, V.3
  • 5
    • 0037501319 scopus 로고    scopus 로고
    • The estrogen receptor: a model for molecular medicine
    • 9
    • Jensen E.V., and Jordan V.C. The estrogen receptor: a model for molecular medicine. Clin Cancer Res 9 (2003) 1980 9
    • (2003) Clin Cancer Res , vol.9 , pp. 1980
    • Jensen, E.V.1    Jordan, V.C.2
  • 6
    • 0022393794 scopus 로고
    • Primary structure and expression of a functional human glucocorticoid receptor cDNA
    • 41
    • Hollenberg S.M., Weinberger C., Ong E.S., Cerelli G., Oro A., Lebo R., et al. Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature 318 (1985) 635 41
    • (1985) Nature , vol.318 , pp. 635
    • Hollenberg, S.M.1    Weinberger, C.2    Ong, E.S.3    Cerelli, G.4    Oro, A.5    Lebo, R.6
  • 7
    • 0032919564 scopus 로고    scopus 로고
    • Direct visualization of the human estrogen receptor alpha reveals a role for ligand in the nuclear distribution of the receptor
    • 86
    • Htun H., Holth L.T., Walker D., Davie J.R., and Hager G.L. Direct visualization of the human estrogen receptor alpha reveals a role for ligand in the nuclear distribution of the receptor. Mol Biol Cell 10 (1999) 471 86
    • (1999) Mol Biol Cell , vol.10 , pp. 471
    • Htun, H.1    Holth, L.T.2    Walker, D.3    Davie, J.R.4    Hager, G.L.5
  • 8
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • 86
    • Tsai M.J., and O'Malley B.W. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu Rev Biochem 63 (1994) 451 86
    • (1994) Annu Rev Biochem , vol.63 , pp. 451
    • Tsai, M.J.1    O'Malley, B.W.2
  • 9
    • 0024337858 scopus 로고
    • Determinants of target gene specificity for steroid/thyroid hormone receptors
    • 46
    • Umesono K., and Evans R.M. Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell 57 (1989) 1139 46
    • (1989) Cell , vol.57 , pp. 1139
    • Umesono, K.1    Evans, R.M.2
  • 10
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • 41
    • Glass C.K., and Rosenfeld M.G. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 14 (2000) 121 41
    • (2000) Genes Dev , vol.14 , pp. 121
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 11
    • 0026748811 scopus 로고
    • Thyroid hormone alters in vitro DNA binding of monomers and dimers of thyroid hormone receptors
    • 52
    • Ribeiro R.C., Kushner P.J., Apriletti J.W., West B.L., and Baxter J.D. Thyroid hormone alters in vitro DNA binding of monomers and dimers of thyroid hormone receptors. Mol Endocrinol 6 (1992) 1142 52
    • (1992) Mol Endocrinol , vol.6 , pp. 1142
    • Ribeiro, R.C.1    Kushner, P.J.2    Apriletti, J.W.3    West, B.L.4    Baxter, J.D.5
  • 12
    • 0029240326 scopus 로고
    • Nuclear receptors. Lonesome orphans
    • 7
    • Laudet V., and Adelmant G. Nuclear receptors. Lonesome orphans. Curr Biol 5 (1995) 124 7
    • (1995) Curr Biol , vol.5 , pp. 124
    • Laudet, V.1    Adelmant, G.2
  • 13
    • 37249086610 scopus 로고    scopus 로고
    • Rev-erbalpha, a heme sensor that coordinates metabolic and circadian pathways
    • 9
    • Yin L., Wu N., Curtin J.C., Qatanani M., Szwergold N.R., Reid R.A., et al. Rev-erbalpha, a heme sensor that coordinates metabolic and circadian pathways. Science 318 (2007) 1786 9
    • (2007) Science , vol.318 , pp. 1786
    • Yin, L.1    Wu, N.2    Curtin, J.C.3    Qatanani, M.4    Szwergold, N.R.5    Reid, R.A.6
  • 14
    • 36849084107 scopus 로고    scopus 로고
    • Identification of heme as the ligand for the orphan nuclear receptors REV-ERBalpha and REV-ERBbeta
    • 13
    • Raghuram S., Stayrook K.R., Huang P., Rogers P.M., Nosie A.K., McClure D.B., et al. Identification of heme as the ligand for the orphan nuclear receptors REV-ERBalpha and REV-ERBbeta. Nat Struct Mol Biol 14 (2007) 1207 13
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1207
    • Raghuram, S.1    Stayrook, K.R.2    Huang, P.3    Rogers, P.M.4    Nosie, A.K.5    McClure, D.B.6
  • 15
    • 40049109300 scopus 로고    scopus 로고
    • Nuclear hormone receptors for heme: REV-ERBalpha and REV-ERBbeta are ligand-regulated components of the mammalian clock
    • 20
    • Burris T.P. Nuclear hormone receptors for heme: REV-ERBalpha and REV-ERBbeta are ligand-regulated components of the mammalian clock. Mol Endocrinol 22 (2008) 1509 20
    • (2008) Mol Endocrinol , vol.22 , pp. 1509
    • Burris, T.P.1
  • 16
    • 3042753852 scopus 로고    scopus 로고
    • Digging deep into the pockets of orphan nuclear receptors: insights from structural studies
    • 76
    • Benoit G., Malewicz M., and Perlmann T. Digging deep into the pockets of orphan nuclear receptors: insights from structural studies. Trends Cell Biol 14 (2004) 369 76
    • (2004) Trends Cell Biol , vol.14 , pp. 369
    • Benoit, G.1    Malewicz, M.2    Perlmann, T.3
  • 17
    • 0034306499 scopus 로고    scopus 로고
    • Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications
    • 8
    • Bourguet W., Germain P., and Gronemeyer H. Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications. Trends Pharmacol Sci 21 (2000) 381 8
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 381
    • Bourguet, W.1    Germain, P.2    Gronemeyer, H.3
  • 18
    • 0022453518 scopus 로고
    • Functional domains of the human glucocorticoid receptor
    • 52
    • Giguere V., Hollenberg S.M., Rosenfeld M.G., and Evans R.M. Functional domains of the human glucocorticoid receptor. Cell 46 (1986) 645 52
    • (1986) Cell , vol.46 , pp. 645
    • Giguere, V.1    Hollenberg, S.M.2    Rosenfeld, M.G.3    Evans, R.M.4
  • 20
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto K.R., and Sigler P.B. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 352 (1991) 497-505
    • (1991) Nature , vol.352 , pp. 497-505
    • Luisi, B.F.1    Xu, W.X.2    Otwinowski, Z.3    Freedman, L.P.4    Yamamoto, K.R.5    Sigler, P.B.6
  • 21
    • 0028233763 scopus 로고
    • Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor
    • 49
    • Barettino D., Vivanco Ruiz M.M., and Stunnenberg H.G. Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor. EMBO J 13 (1994) 3039 49
    • (1994) EMBO J , vol.13 , pp. 3039
    • Barettino, D.1    Vivanco Ruiz, M.M.2    Stunnenberg, H.G.3
  • 22
    • 0026600841 scopus 로고
    • Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
    • 33
    • Danielian P.S., White R., Lees J.A., and Parker M.G. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J 11 (1992) 1025 33
    • (1992) EMBO J , vol.11 , pp. 1025
    • Danielian, P.S.1    White, R.2    Lees, J.A.3    Parker, M.G.4
  • 23
    • 0027941792 scopus 로고
    • Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity
    • 82
    • Durand B., Saunders M., Gaudon C., Roy B., Losson R., and Chambon P. Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity. EMBO J 13 (1994) 5370 82
    • (1994) EMBO J , vol.13 , pp. 5370
    • Durand, B.1    Saunders, M.2    Gaudon, C.3    Roy, B.4    Losson, R.5    Chambon, P.6
  • 24
    • 56749130032 scopus 로고    scopus 로고
    • Structure of the intact PPAR-gamma-RXR-alpha nuclear receptor complex on DNA
    • Chandra V., Huang P., Hamuro Y., Raghuram S., Wang Y., Burris T.P., et al. Structure of the intact PPAR-gamma-RXR-alpha nuclear receptor complex on DNA. Nature (2008) 350-356
    • (2008) Nature , pp. 350-356
    • Chandra, V.1    Huang, P.2    Hamuro, Y.3    Raghuram, S.4    Wang, Y.5    Burris, T.P.6
  • 25
    • 0026722537 scopus 로고
    • Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II)
    • 23
    • Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., and O'Malley B.W. Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II). J Biol Chem 267 (1992) 17617 23
    • (1992) J Biol Chem , vol.267 , pp. 17617
    • Ing, N.H.1    Beekman, J.M.2    Tsai, S.Y.3    Tsai, M.J.4    O'Malley, B.W.5
  • 26
    • 0027314091 scopus 로고
    • Different TBP-associated factors are required for mediating the stimulation of transcription in vitro by the acidic transactivator GAL-VP16 and the two nonacidic activation functions of the estrogen receptor
    • Brou C., Wu J., Ali S., Scheer E., Lang C., Davidson I., et al. Different TBP-associated factors are required for mediating the stimulation of transcription in vitro by the acidic transactivator GAL-VP16 and the two nonacidic activation functions of the estrogen receptor. Nucleic Acids Res 21 (1993) 5-12
    • (1993) Nucleic Acids Res , vol.21 , pp. 5-12
    • Brou, C.1    Wu, J.2    Ali, S.3    Scheer, E.4    Lang, C.5    Davidson, I.6
  • 27
    • 0031841028 scopus 로고    scopus 로고
    • Targets of activated steroid hormone receptors: basal transcription factors and receptor interacting proteins
    • 6
    • Klein-Hitpass L., Schwerk C., Kahmann S., and Vassen L. Targets of activated steroid hormone receptors: basal transcription factors and receptor interacting proteins. J Mol Med 76 (1998) 490 6
    • (1998) J Mol Med , vol.76 , pp. 490
    • Klein-Hitpass, L.1    Schwerk, C.2    Kahmann, S.3    Vassen, L.4
  • 29
    • 61749092693 scopus 로고    scopus 로고
    • Postrecruitment regulation of RNA polymerase II directs rapid signaling responses at the promoters of estrogen target genes
    • 33
    • Kininis M., Isaacs G.D., Core L.J., Hah N., and Kraus W.L. Postrecruitment regulation of RNA polymerase II directs rapid signaling responses at the promoters of estrogen target genes. Mol Cell Biol 29 (2009) 1123 33
    • (2009) Mol Cell Biol , vol.29 , pp. 1123
    • Kininis, M.1    Isaacs, G.D.2    Core, L.J.3    Hah, N.4    Kraus, W.L.5
  • 30
    • 33646829646 scopus 로고    scopus 로고
    • Role of the mediator complex in nuclear hormone receptor signaling
    • Belakavadi M., and Fondell J.D. Role of the mediator complex in nuclear hormone receptor signaling. Rev Physiol Biochem Pharmacol 156 (2006) 23-43
    • (2006) Rev Physiol Biochem Pharmacol , vol.156 , pp. 23-43
    • Belakavadi, M.1    Fondell, J.D.2
  • 31
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • 7
    • Onate S.A., Tsai S.Y., Tsai M.J., and O'Malley B.W. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270 (1995) 1354 7
    • (1995) Science , vol.270 , pp. 1354
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3    O'Malley, B.W.4
  • 32
    • 0242587820 scopus 로고    scopus 로고
    • A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors
    • 14
    • Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., et al. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85 (1996) 403 14
    • (1996) Cell , vol.85 , pp. 403
    • Kamei, Y.1    Xu, L.2    Heinzel, T.3    Torchia, J.4    Kurokawa, R.5    Gloss, B.6
  • 34
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • 86
    • Chen H., Lin R.J., Xie W., Wilpitz D., and Evans R.M. Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 98 (1999) 675 86
    • (1999) Cell , vol.98 , pp. 675
    • Chen, H.1    Lin, R.J.2    Xie, W.3    Wilpitz, D.4    Evans, R.M.5
  • 35
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • 52
    • 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 52
    • (2000) Cell , vol.103 , pp. 843
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 36
    • 0037062460 scopus 로고    scopus 로고
    • Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo
    • 9
    • Sharma D., and Fondell J.D. Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo. Proc Natl Acad Sci USA 99 (2002) 7934 9
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7934
    • Sharma, D.1    Fondell, J.D.2
  • 37
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities
    • 98
    • Koh S.S., Chen D., Lee Y.H., and Stallcup M.R. Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. J Biol Chem 276 (2001) 1089 98
    • (2001) J Biol Chem , vol.276 , pp. 1089
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 38
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • 80
    • Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074 80
    • (2001) Science , vol.293 , pp. 1074
    • Jenuwein, T.1    Allis, C.D.2
  • 39
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • 5
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41 5
    • (2000) Nature , vol.403 , pp. 41
    • Strahl, B.D.1    Allis, C.D.2
  • 40
    • 29444461024 scopus 로고    scopus 로고
    • Changes in attitude, changes in latitude: nuclear receptors remodeling chromatin to regulate transcription
    • Chen J., Kinyamu H.K., and Archer T.K. Changes in attitude, changes in latitude: nuclear receptors remodeling chromatin to regulate transcription. Mol Endocrinol 20 (2006) 1-13
    • (2006) Mol Endocrinol , vol.20 , pp. 1-13
    • Chen, J.1    Kinyamu, H.K.2    Archer, T.K.3
  • 41
    • 0035134963 scopus 로고    scopus 로고
    • A necessary good: nuclear hormone receptors and their chromatin templates
    • Urnov F.D., and Wolffe A.P. A necessary good: nuclear hormone receptors and their chromatin templates. Mol Endocrinol 15 (2001) 1-16
    • (2001) Mol Endocrinol , vol.15 , pp. 1-16
    • Urnov, F.D.1    Wolffe, A.P.2
  • 42
    • 0033636323 scopus 로고    scopus 로고
    • ATP-driven chromatin remodeling activity and histone acetyltransferases act sequentially during transactivation by RAR/RXR In vitro
    • 58
    • Dilworth F.J., Fromental-Ramain C., Yamamoto K., and Chambon P. ATP-driven chromatin remodeling activity and histone acetyltransferases act sequentially during transactivation by RAR/RXR In vitro. Mol Cell 6 (2000) 1049 58
    • (2000) Mol Cell , vol.6 , pp. 1049
    • Dilworth, F.J.1    Fromental-Ramain, C.2    Yamamoto, K.3    Chambon, P.4
  • 43
    • 0032492846 scopus 로고    scopus 로고
    • Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex
    • Fryer C.J., and Archer T.K. Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature 393 (1998) 88-91
    • (1998) Nature , vol.393 , pp. 88-91
    • Fryer, C.J.1    Archer, T.K.2
  • 44
    • 0038558164 scopus 로고    scopus 로고
    • A role for cofactor-cofactor and cofactor-histone interactions in targeting p300, SWI/SNF and Mediator for transcription
    • 55
    • Huang Z.Q., Li J., Sachs L.M., Cole P.A., and Wong J. A role for cofactor-cofactor and cofactor-histone interactions in targeting p300, SWI/SNF and Mediator for transcription. EMBO J 22 (2003) 2146 55
    • (2003) EMBO J , vol.22 , pp. 2146
    • Huang, Z.Q.1    Li, J.2    Sachs, L.M.3    Cole, P.A.4    Wong, J.5
  • 45
    • 0032742874 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodelling: SWI/SNF and Co. are on the job
    • 98
    • Muchardt C., and Yaniv M. ATP-dependent chromatin remodelling: SWI/SNF and Co. are on the job. J Mol Biol 293 (1999) 187 98
    • (1999) J Mol Biol , vol.293 , pp. 187
    • Muchardt, C.1    Yaniv, M.2
  • 46
    • 0027048595 scopus 로고
    • Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors
    • 604
    • Yoshinaga S.K., Peterson C.L., Herskowitz I., and Yamamoto K.R. Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors. Science 258 (1992) 1598 604
    • (1992) Science , vol.258 , pp. 1598
    • Yoshinaga, S.K.1    Peterson, C.L.2    Herskowitz, I.3    Yamamoto, K.R.4
  • 47
    • 27744561591 scopus 로고    scopus 로고
    • Chromatin remodeling complexes: ATP-dependent machines in action
    • 17
    • Johnson C.N., Adkins N.L., and Georgel P. Chromatin remodeling complexes: ATP-dependent machines in action. Biochem Cell Biol 83 (2005) 405 17
    • (2005) Biochem Cell Biol , vol.83 , pp. 405
    • Johnson, C.N.1    Adkins, N.L.2    Georgel, P.3
  • 48
    • 18044374488 scopus 로고    scopus 로고
    • Nuclear hormone receptor co-repressors
    • Baniahmad A. Nuclear hormone receptor co-repressors. J Steroid Biochem Mol Biol 93 (2005) 89-97
    • (2005) J Steroid Biochem Mol Biol , vol.93 , pp. 89-97
    • Baniahmad, A.1
  • 49
    • 0028988482 scopus 로고
    • The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing
    • Baniahmad A., Leng X., Burris T.P., Tsai S.Y., Tsai M.J., and O'Malley B.W. The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing. Mol Cell Biol 15 (1995) 76-86
    • (1995) Mol Cell Biol , vol.15 , pp. 76-86
    • Baniahmad, A.1    Leng, X.2    Burris, T.P.3    Tsai, S.Y.4    Tsai, M.J.5    O'Malley, B.W.6
  • 50
    • 0028144960 scopus 로고
    • Functional evidence for ligand-dependent dissociation of thyroid hormone and retinoic acid receptors from an inhibitory cellular factor
    • 65
    • Casanova J., Helmer E., Selmi-Ruby S., Qi J.S., Au-Fliegner M., Desai-Yajnik V., et al. Functional evidence for ligand-dependent dissociation of thyroid hormone and retinoic acid receptors from an inhibitory cellular factor. Mol Cell Biol 14 (1994) 5756 65
    • (1994) Mol Cell Biol , vol.14 , pp. 5756
    • Casanova, J.1    Helmer, E.2    Selmi-Ruby, S.3    Qi, J.S.4    Au-Fliegner, M.5    Desai-Yajnik, V.6
  • 51
    • 0029976309 scopus 로고    scopus 로고
    • Transcriptional silencing by unliganded thyroid hormone receptor beta requires a soluble corepressor that interacts with the ligand-binding domain of the receptor
    • 20
    • Tong G.X., Jeyakumar M., Tanen M.R., and Bagchi M.K. Transcriptional silencing by unliganded thyroid hormone receptor beta requires a soluble corepressor that interacts with the ligand-binding domain of the receptor. Mol Cell Biol 16 (1996) 1909 20
    • (1996) Mol Cell Biol , vol.16 , pp. 1909
    • Tong, G.X.1    Jeyakumar, M.2    Tanen, M.R.3    Bagchi, M.K.4
  • 52
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • 7
    • Chen J.D., and Evans R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377 (1995) 454 7
    • (1995) Nature , vol.377 , pp. 454
    • Chen, J.D.1    Evans, R.M.2
  • 53
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
    • Horlein A.J., Naar A.M., Heinzel T., Torchia J., Gloss B., Kurokawa R., et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 377 (1995) 397-404
    • (1995) Nature , vol.377 , pp. 397-404
    • Horlein, A.J.1    Naar, A.M.2    Heinzel, T.3    Torchia, J.4    Gloss, B.5    Kurokawa, R.6
  • 54
    • 0037084392 scopus 로고    scopus 로고
    • Biological roles and mechanistic actions of co-repressor complexes
    • 98
    • Jepsen K., and Rosenfeld M.G. Biological roles and mechanistic actions of co-repressor complexes. J Cell Sci 115 (2002) 689 98
    • (2002) J Cell Sci , vol.115 , pp. 689
    • Jepsen, K.1    Rosenfeld, M.G.2
  • 55
    • 2342573009 scopus 로고    scopus 로고
    • The role of corepressors in transcriptional regulation by nuclear hormone receptors
    • 60
    • Privalsky M.L. The role of corepressors in transcriptional regulation by nuclear hormone receptors. Annu Rev Physiol 66 (2004) 315 60
    • (2004) Annu Rev Physiol , vol.66 , pp. 315
    • Privalsky, M.L.1
  • 56
    • 0033523917 scopus 로고    scopus 로고
    • The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors
    • 6
    • Hu X., and Lazar M.A. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 402 (1999) 93 6
    • (1999) Nature , vol.402 , pp. 93
    • Hu, X.1    Lazar, M.A.2
  • 57
    • 17544398986 scopus 로고    scopus 로고
    • Mechanism of corepressor binding and release from nuclear hormone receptors
    • 16
    • Nagy L., Kao H.Y., Love J.D., Li C., Banayo E., Gooch J.T., et al. Mechanism of corepressor binding and release from nuclear hormone receptors. Genes Dev 13 (1999) 3209 16
    • (1999) Genes Dev , vol.13 , pp. 3209
    • Nagy, L.1    Kao, H.Y.2    Love, J.D.3    Li, C.4    Banayo, E.5    Gooch, J.T.6
  • 59
    • 0034975063 scopus 로고    scopus 로고
    • The specificity of interactions between nuclear hormone receptors and corepressors is mediated by distinct amino acid sequences within the interacting domains
    • 61
    • Cohen R.N., Brzostek S., Kim B., Chorev M., Wondisford F.E., and Hollenberg A.N. The specificity of interactions between nuclear hormone receptors and corepressors is mediated by distinct amino acid sequences within the interacting domains. Mol Endocrinol 15 (2001) 1049 61
    • (2001) Mol Endocrinol , vol.15 , pp. 1049
    • Cohen, R.N.1    Brzostek, S.2    Kim, B.3    Chorev, M.4    Wondisford, F.E.5    Hollenberg, A.N.6
  • 60
    • 0035138513 scopus 로고    scopus 로고
    • Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors
    • 58
    • Hu X., Li Y., and Lazar M.A. Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors. Mol Cell Biol 21 (2001) 1747 58
    • (2001) Mol Cell Biol , vol.21 , pp. 1747
    • Hu, X.1    Li, Y.2    Lazar, M.A.3
  • 61
    • 0042592941 scopus 로고    scopus 로고
    • The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor
    • 31
    • Ishizuka T., and Lazar M.A. The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor. Mol Cell Biol 23 (2003) 5122 31
    • (2003) Mol Cell Biol , vol.23 , pp. 5122
    • Ishizuka, T.1    Lazar, M.A.2
  • 63
    • 0035724413 scopus 로고    scopus 로고
    • The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3
    • 101
    • Guenther M.G., Barak O., and Lazar M.A. The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol Cell Biol 21 (2001) 6091 101
    • (2001) Mol Cell Biol , vol.21 , pp. 6091
    • Guenther, M.G.1    Barak, O.2    Lazar, M.A.3
  • 64
    • 22344453589 scopus 로고    scopus 로고
    • The nuclear receptor corepressor deacetylase activating domain is essential for repression by thyroid hormone receptor
    • 51
    • Ishizuka T., and Lazar M.A. The nuclear receptor corepressor deacetylase activating domain is essential for repression by thyroid hormone receptor. Mol Endocrinol 19 (2005) 1443 51
    • (2005) Mol Endocrinol , vol.19 , pp. 1443
    • Ishizuka, T.1    Lazar, M.A.2
  • 65
    • 0034536085 scopus 로고    scopus 로고
    • The nuclear receptor corepressor (N-CoR) contains three isoleucine motifs (I/LXXII) that serve as receptor interaction domains (IDs)
    • 85
    • Webb P., Anderson C.M., Valentine C., Nguyen P., Marimuthu A., West B.L., et al. The nuclear receptor corepressor (N-CoR) contains three isoleucine motifs (I/LXXII) that serve as receptor interaction domains (IDs). Mol Endocrinol 14 (2000) 1976 85
    • (2000) Mol Endocrinol , vol.14 , pp. 1976
    • Webb, P.1    Anderson, C.M.2    Valentine, C.3    Nguyen, P.4    Marimuthu, A.5    West, B.L.6
  • 66
    • 20044380937 scopus 로고    scopus 로고
    • The histone-binding code of nuclear receptor co-repressors matches the substrate specificity of histone deacetylase 3
    • 51
    • Hartman H.B., Yu J., Alenghat T., Ishizuka T., and Lazar M.A. The histone-binding code of nuclear receptor co-repressors matches the substrate specificity of histone deacetylase 3. EMBO Rep 6 (2005) 445 51
    • (2005) EMBO Rep , vol.6 , pp. 445
    • Hartman, H.B.1    Yu, J.2    Alenghat, T.3    Ishizuka, T.4    Lazar, M.A.5
  • 67
    • 0037925529 scopus 로고    scopus 로고
    • A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation
    • 10
    • Yu J., Li Y., Ishizuka T., Guenther M.G., and Lazar M.A. A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation. EMBO J 22 (2003) 3403 10
    • (2003) EMBO J , vol.22 , pp. 3403
    • Yu, J.1    Li, Y.2    Ishizuka, T.3    Guenther, M.G.4    Lazar, M.A.5
  • 68
    • 0034663815 scopus 로고    scopus 로고
    • Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3
    • 50
    • Li J., Wang J., Nawaz Z., Liu J.M., Qin J., and Wong J. Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3. EMBO J 19 (2000) 4342 50
    • (2000) EMBO J , vol.19 , pp. 4342
    • Li, J.1    Wang, J.2    Nawaz, Z.3    Liu, J.M.4    Qin, J.5    Wong, J.6
  • 69
    • 0344405718 scopus 로고    scopus 로고
    • Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1
    • 46
    • Yoon H.G., Chan D.W., Huang Z.Q., Li J., Fondell J.D., Qin J., et al. Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1. EMBO J 22 (2003) 1336 46
    • (2003) EMBO J , vol.22 , pp. 1336
    • Yoon, H.G.1    Chan, D.W.2    Huang, Z.Q.3    Li, J.4    Fondell, J.D.5    Qin, J.6
  • 70
    • 0036211850 scopus 로고    scopus 로고
    • The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2
    • 23
    • Zhang J., Kalkum M., Chait B.T., and Roeder R.G. The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2. Mol Cell 9 (2002) 611 23
    • (2002) Mol Cell , vol.9 , pp. 611
    • Zhang, J.1    Kalkum, M.2    Chait, B.T.3    Roeder, R.G.4
  • 71
    • 1342264315 scopus 로고    scopus 로고
    • A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors
    • 26
    • Perissi V., Aggarwal A., Glass C.K., Rose D.W., and Rosenfeld M.G. A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors. Cell 116 (2004) 511 26
    • (2004) Cell , vol.116 , pp. 511
    • Perissi, V.1    Aggarwal, A.2    Glass, C.K.3    Rose, D.W.4    Rosenfeld, M.G.5
  • 72
    • 17744413444 scopus 로고    scopus 로고
    • A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
    • 8
    • Heinzel T., Lavinsky R.M., Mullen T.M., Soderstrom M., Laherty C.D., Torchia J., et al. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387 (1997) 43 8
    • (1997) Nature , vol.387 , pp. 43
    • Heinzel, T.1    Lavinsky, R.M.2    Mullen, T.M.3    Soderstrom, M.4    Laherty, C.D.5    Torchia, J.6
  • 73
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • 80
    • Nagy L., Kao H.Y., Chakravarti D., Lin R.J., Hassig C.A., Ayer D.E., et al. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89 (1997) 373 80
    • (1997) Cell , vol.89 , pp. 373
    • Nagy, L.1    Kao, H.Y.2    Chakravarti, D.3    Lin, R.J.4    Hassig, C.A.5    Ayer, D.E.6
  • 74
    • 0034192756 scopus 로고    scopus 로고
    • A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness
    • 57
    • Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A., and Shiekhattar R. A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness. Genes Dev 14 (2000) 1048 57
    • (2000) Genes Dev , vol.14 , pp. 1048
    • Guenther, M.G.1    Lane, W.S.2    Fischle, W.3    Verdin, E.4    Lazar, M.A.5    Shiekhattar, R.6
  • 75
    • 0037087573 scopus 로고    scopus 로고
    • Specific targeting and constitutive association of histone deacetylase complexes during transcriptional repression
    • 92
    • Li J., Lin Q., Wang W., Wade P., and Wong J. Specific targeting and constitutive association of histone deacetylase complexes during transcriptional repression. Genes Dev 16 (2002) 687 92
    • (2002) Genes Dev , vol.16 , pp. 687
    • Li, J.1    Lin, Q.2    Wang, W.3    Wade, P.4    Wong, J.5
  • 76
    • 0035937783 scopus 로고    scopus 로고
    • Multiple N-CoR complexes contain distinct histone deacetylases
    • 11
    • Jones P.L., Sachs L.M., Rouse N., Wade P.A., and Shi Y.B. Multiple N-CoR complexes contain distinct histone deacetylases. J Biol Chem 276 (2001) 8807 11
    • (2001) J Biol Chem , vol.276 , pp. 8807
    • Jones, P.L.1    Sachs, L.M.2    Rouse, N.3    Wade, P.A.4    Shi, Y.B.5
  • 77
    • 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. Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev 14 (2000) 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
  • 78
    • 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. Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev 14 (2000) 55-66
    • (2000) Genes Dev , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 79
    • 33846409855 scopus 로고    scopus 로고
    • Adamantyl-substituted retinoid-related molecules bind small heterodimer partner and modulate the Sin3A repressor
    • 25
    • Farhana L., Dawson M.I., Leid M., Wang L., Moore D.D., Liu G., et al. Adamantyl-substituted retinoid-related molecules bind small heterodimer partner and modulate the Sin3A repressor. Cancer Res 67 (2007) 318 25
    • (2007) Cancer Res , vol.67 , pp. 318
    • Farhana, L.1    Dawson, M.I.2    Leid, M.3    Wang, L.4    Moore, D.D.5    Liu, G.6
  • 80
    • 0034045480 scopus 로고    scopus 로고
    • Transcriptional repression by nuclear hormone receptors
    • Hu X., and Lazar M.A. Transcriptional repression by nuclear hormone receptors. Trends Endocrinol Metab 11 (2000) 6-10
    • (2000) Trends Endocrinol Metab , vol.11 , pp. 6-10
    • Hu, X.1    Lazar, M.A.2
  • 81
    • 0141638426 scopus 로고    scopus 로고
    • N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso
    • 34
    • Yoon H.G., Chan D.W., Reynolds A.B., Qin J., and Wong J. N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso. Mol Cell 12 (2003) 723 34
    • (2003) Mol Cell , vol.12 , pp. 723
    • Yoon, H.G.1    Chan, D.W.2    Reynolds, A.B.3    Qin, J.4    Wong, J.5
  • 82
    • 0034704078 scopus 로고    scopus 로고
    • A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1
    • 70
    • Underhill C., Qutob M.S., Yee S.P., and Torchia J. A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1. J Biol Chem 275 (2000) 40463 70
    • (2000) J Biol Chem , vol.275 , pp. 40463
    • Underhill, C.1    Qutob, M.S.2    Yee, S.P.3    Torchia, J.4
  • 83
    • 0036712390 scopus 로고    scopus 로고
    • Evidence that Swi/Snf directly represses transcription in S. cerevisiae
    • 6
    • Martens J.A., and Winston F. Evidence that Swi/Snf directly represses transcription in S. cerevisiae. Genes Dev 16 (2002) 2231 6
    • (2002) Genes Dev , vol.16 , pp. 2231
    • Martens, J.A.1    Winston, F.2
  • 84
    • 33748363908 scopus 로고    scopus 로고
    • The N-CoR complex enables chromatin remodeler SNF2H to enhance repression by thyroid hormone receptor
    • 74
    • Alenghat T., Yu J., and Lazar M.A. The N-CoR complex enables chromatin remodeler SNF2H to enhance repression by thyroid hormone receptor. EMBO J 25 (2006) 3966 74
    • (2006) EMBO J , vol.25 , pp. 3966
    • Alenghat, T.1    Yu, J.2    Lazar, M.A.3
  • 85
    • 34547447286 scopus 로고    scopus 로고
    • Novel regulatory role for human Acf1 in transcriptional repression of vitamin D3 receptor-regulated genes
    • 806
    • Ewing A.K., Attner M., and Chakravarti D. Novel regulatory role for human Acf1 in transcriptional repression of vitamin D3 receptor-regulated genes. Mol Endocrinol 21 (2007) 1791 806
    • (2007) Mol Endocrinol , vol.21 , pp. 1791
    • Ewing, A.K.1    Attner, M.2    Chakravarti, D.3
  • 86
    • 0034664769 scopus 로고    scopus 로고
    • Combinatorial roles of the nuclear receptor corepressor in transcription and development
    • 63
    • Jepsen K., Hermanson O., Onami T.M., Gleiberman A.S., Lunyak V., McEvilly R.J., et al. Combinatorial roles of the nuclear receptor corepressor in transcription and development. Cell 102 (2000) 753 63
    • (2000) Cell , vol.102 , pp. 753
    • Jepsen, K.1    Hermanson, O.2    Onami, T.M.3    Gleiberman, A.S.4    Lunyak, V.5    McEvilly, R.J.6
  • 87
    • 0018267877 scopus 로고
    • The histone core complex: an octamer assembled by two sets of protein-protein interactions
    • 64
    • Eickbush T.H., and Moudrianakis E.N. The histone core complex: an octamer assembled by two sets of protein-protein interactions. Biochemistry 17 (1978) 4955 64
    • (1978) Biochemistry , vol.17 , pp. 4955
    • Eickbush, T.H.1    Moudrianakis, E.N.2
  • 88
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • 60
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., and Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389 (1997) 251 60
    • (1997) Nature , vol.389 , pp. 251
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 89
    • 0034711232 scopus 로고    scopus 로고
    • The core histone N termini function independently of linker histones during chromatin condensation
    • 90
    • Carruthers L.M., and Hansen J.C. The core histone N termini function independently of linker histones during chromatin condensation. J Biol Chem 275 (2000) 37285 90
    • (2000) J Biol Chem , vol.275 , pp. 37285
    • Carruthers, L.M.1    Hansen, J.C.2
  • 90
    • 60349089645 scopus 로고    scopus 로고
    • Nucleosome positioning and gene regulation: advances through genomics
    • 72
    • Jiang C., and Pugh B.F. Nucleosome positioning and gene regulation: advances through genomics. Nat Rev Genet 10 (2009) 161 72
    • (2009) Nat Rev Genet , vol.10 , pp. 161
    • Jiang, C.1    Pugh, B.F.2
  • 91
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome: from genomic organization to genomic regulation
    • 72
    • Khorasanizadeh S. The nucleosome: from genomic organization to genomic regulation. Cell 116 (2004) 259 72
    • (2004) Cell , vol.116 , pp. 259
    • Khorasanizadeh, S.1
  • 92
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: requirement for the histone H4 N-terminal tail
    • Dorigo B., Schalch T., Bystricky K., and Richmond T.J. Chromatin fiber folding: requirement for the histone H4 N-terminal tail. J Mol Biol 327 (2003) 85-96
    • (2003) J Mol Biol , vol.327 , pp. 85-96
    • Dorigo, B.1    Schalch, T.2    Bystricky, K.3    Richmond, T.J.4
  • 93
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: an acetyl-lysine binding domain
    • 8
    • Zeng L., and Zhou M.M. Bromodomain: an acetyl-lysine binding domain. FEBS Lett 513 (2002) 124 8
    • (2002) FEBS Lett , vol.513 , pp. 124
    • Zeng, L.1    Zhou, M.M.2
  • 95
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • 3
    • Bannister A.J., and Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature 384 (1996) 641 3
    • (1996) Nature , vol.384 , pp. 641
    • Bannister, A.J.1    Kouzarides, T.2
  • 97
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • 9
    • Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., and Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87 (1996) 953 9
    • (1996) Cell , vol.87 , pp. 953
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 98
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • 24
    • Yang X.J., Ogryzko V.V., Nishikawa J., Howard B.H., and Nakatani Y. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382 (1996) 319 24
    • (1996) Nature , vol.382 , pp. 319
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 99
  • 101
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin3A
    • 7
    • Hassig C.A., Fleischer T.C., Billin A.N., Schreiber S.L., and Ayer D.E. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 89 (1997) 341 7
    • (1997) Cell , vol.89 , pp. 341
    • Hassig, C.A.1    Fleischer, T.C.2    Billin, A.N.3    Schreiber, S.L.4    Ayer, D.E.5
  • 102
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: a new partnership for signaling
    • 87
    • Yang X.J. Lysine acetylation and the bromodomain: a new partnership for signaling. Bioessays 26 (2004) 1076 87
    • (2004) Bioessays , vol.26 , pp. 1076
    • Yang, X.J.1
  • 103
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • 79
    • Hassan A.H., Prochasson P., Neely K.E., Galasinski S.C., Chandy M., Carrozza M.J., et al. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell 111 (2002) 369 79
    • (2002) Cell , vol.111 , pp. 369
    • Hassan, A.H.1    Prochasson, P.2    Neely, K.E.3    Galasinski, S.C.4    Chandy, M.5    Carrozza, M.J.6
  • 105
    • 3142730622 scopus 로고    scopus 로고
    • A signaling role of histone-binding proteins and INHAT subunits pp32 and Set/TAF-Ibeta in integrating chromatin hypoacetylation and transcriptional repression
    • 5
    • Kutney S.N., Hong R., Macfarlan T., and Chakravarti D. A signaling role of histone-binding proteins and INHAT subunits pp32 and Set/TAF-Ibeta in integrating chromatin hypoacetylation and transcriptional repression. J Biol Chem 279 (2004) 30850 5
    • (2004) J Biol Chem , vol.279 , pp. 30850
    • Kutney, S.N.1    Hong, R.2    Macfarlan, T.3    Chakravarti, D.4
  • 106
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • 49
    • Martin C., and Zhang Y. The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol 6 (2005) 838 49
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 838
    • Martin, C.1    Zhang, Y.2
  • 107
    • 0031984480 scopus 로고    scopus 로고
    • SET domain proteins modulate chromatin domains in eu- and heterochromatin
    • Jenuwein T., Laible G., Dorn R., and Reuter G. SET domain proteins modulate chromatin domains in eu- and heterochromatin. Cell Mol Life Sci 54 (1998) 80-93
    • (1998) Cell Mol Life Sci , vol.54 , pp. 80-93
    • Jenuwein, T.1    Laible, G.2    Dorn, R.3    Reuter, G.4
  • 108
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • 9
    • Rea S., Eisenhaber F., O'Carroll D., Strahl B.D., Sun Z.W., Schmid M., et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406 (2000) 593 9
    • (2000) Nature , vol.406 , pp. 593
    • Rea, S.1    Eisenhaber, F.2    O'Carroll, D.3    Strahl, B.D.4    Sun, Z.W.5    Schmid, M.6
  • 109
    • 0034107379 scopus 로고    scopus 로고
    • Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres
    • 29
    • Aagaard L., Schmid M., Warburton P., and Jenuwein T. Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres. J Cell Sci 113 Pt 5 (2000) 817 29
    • (2000) J Cell Sci , vol.113 , Issue.PART 5 , pp. 817
    • Aagaard, L.1    Schmid, M.2    Warburton, P.3    Jenuwein, T.4
  • 111
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • 20
    • Lachner M., O'Carroll D., Rea S., Mechtler K., and Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410 (2001) 116 20
    • (2001) Nature , vol.410 , pp. 116
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 112
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • 3
    • Nakayama J., Rice J.C., Strahl B.D., Allis C.D., and Grewal S.I. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292 (2001) 110 3
    • (2001) Science , vol.292 , pp. 110
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.5
  • 113
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • 43
    • Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298 (2002) 1039 43
    • (2002) Science , vol.298 , pp. 1039
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 114
    • 0037099413 scopus 로고    scopus 로고
    • G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
    • 91
    • Tachibana M., Sugimoto K., Nozaki M., Ueda J., Ohta T., Ohki M., et al. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev 16 (2002) 1779 91
    • (2002) Genes Dev , vol.16 , pp. 1779
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3    Ueda, J.4    Ohta, T.5    Ohki, M.6
  • 115
    • 0033524942 scopus 로고    scopus 로고
    • A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity
    • Chakravarti D., Ogryzko V., Kao H.Y., Nash A., Chen H., Nakatani Y., et al. A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity. Cell 96 (1999) 393-403
    • (1999) Cell , vol.96 , pp. 393-403
    • Chakravarti, D.1    Ogryzko, V.2    Kao, H.Y.3    Nash, A.4    Chen, H.5    Nakatani, Y.6
  • 116
    • 0033525094 scopus 로고    scopus 로고
    • Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A
    • 13
    • Hamamori Y., Sartorelli V., Ogryzko V., Puri P.L., Wu H.Y., Wang J.Y., et al. Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A. Cell 96 (1999) 405 13
    • (1999) Cell , vol.96 , pp. 405
    • Hamamori, Y.1    Sartorelli, V.2    Ogryzko, V.3    Puri, P.L.4    Wu, H.Y.5    Wang, J.Y.6
  • 117
    • 0032511884 scopus 로고    scopus 로고
    • Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A
    • 6
    • Ait-Si-Ali S., Ramirez S., Barre F.X., Dkhissi F., Magnaghi-Jaulin L., Girault J.A., et al. Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A. Nature 396 (1998) 184 6
    • (1998) Nature , vol.396 , pp. 184
    • Ait-Si-Ali, S.1    Ramirez, S.2    Barre, F.X.3    Dkhissi, F.4    Magnaghi-Jaulin, L.5    Girault, J.A.6
  • 119
    • 0035846894 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein
    • 30
    • Seo S.B., McNamara P., Heo S., Turner A., Lane W.S., and Chakravarti D. Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein. Cell 104 (2001) 119 30
    • (2001) Cell , vol.104 , pp. 119
    • Seo, S.B.1    McNamara, P.2    Heo, S.3    Turner, A.4    Lane, W.S.5    Chakravarti, D.6
  • 120
    • 0037134538 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex
    • 10
    • Seo S.B., Macfarlan T., McNamara P., Hong R., Mukai Y., Heo S., et al. Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex. J Biol Chem 277 (2002) 14005 10
    • (2002) J Biol Chem , vol.277 , pp. 14005
    • Seo, S.B.1    Macfarlan, T.2    McNamara, P.3    Hong, R.4    Mukai, Y.5    Heo, S.6
  • 121
    • 12244256087 scopus 로고    scopus 로고
    • A novel estrogen receptor alpha-associated protein, template-activating factor Ibeta, inhibits acetylation and transactivation
    • Loven M.A., Muster N., Yates J.R., and Nardulli A.M. A novel estrogen receptor alpha-associated protein, template-activating factor Ibeta, inhibits acetylation and transactivation. Mol Endocrinol 17 (2003) 67-78
    • (2003) Mol Endocrinol , vol.17 , pp. 67-78
    • Loven, M.A.1    Muster, N.2    Yates, J.R.3    Nardulli, A.M.4
  • 122
    • 8344256470 scopus 로고    scopus 로고
    • A novel estrogen receptor alpha-associated protein alters receptor-deoxyribonucleic acid interactions and represses receptor-mediated transcription
    • 59
    • Loven M.A., Davis R.E., Curtis C.D., Muster N., Yates J.R., and Nardulli A.M. A novel estrogen receptor alpha-associated protein alters receptor-deoxyribonucleic acid interactions and represses receptor-mediated transcription. Mol Endocrinol 18 (2004) 2649 59
    • (2004) Mol Endocrinol , vol.18 , pp. 2649
    • Loven, M.A.1    Davis, R.E.2    Curtis, C.D.3    Muster, N.4    Yates, J.R.5    Nardulli, A.M.6
  • 123
    • 0037423949 scopus 로고    scopus 로고
    • SET-ting the stage for life and death
    • 91
    • Chakravarti D., and Hong R. SET-ting the stage for life and death. Cell 112 (2003) 589 91
    • (2003) Cell , vol.112 , pp. 589
    • Chakravarti, D.1    Hong, R.2
  • 124
    • 56649089874 scopus 로고    scopus 로고
    • Isolation of novel coregulatory protein networks associated with DNA-bound estrogen receptor alpha
    • Schultz-Norton J.R., Ziegler Y.S., Likhite V.S., Yates J.R., and Nardulli A.M. Isolation of novel coregulatory protein networks associated with DNA-bound estrogen receptor alpha. BMC Mol Biol 9 (2008) 97
    • (2008) BMC Mol Biol , vol.9 , pp. 97
    • Schultz-Norton, J.R.1    Ziegler, Y.S.2    Likhite, V.S.3    Yates, J.R.4    Nardulli, A.M.5
  • 125
    • 2642536094 scopus 로고    scopus 로고
    • Direct binding of INHAT to H3 tails disrupted by modifications
    • 62
    • Schneider R., Bannister A.J., Weise C., and Kouzarides T. Direct binding of INHAT to H3 tails disrupted by modifications. J Biol Chem 279 (2004) 23859 62
    • (2004) J Biol Chem , vol.279 , pp. 23859
    • Schneider, R.1    Bannister, A.J.2    Weise, C.3    Kouzarides, T.4
  • 126
    • 39149111943 scopus 로고    scopus 로고
    • Activated glucocorticoid receptor interacts with the INHAT component Set/TAF-Ibeta and releases it from a glucocorticoid-responsive gene promoter, relieving repression: implications for the pathogenesis of glucocorticoid resistance in acute undifferentiated leukemia with Set-Can translocation
    • Ichijo T., Chrousos G.P., and Kino T. Activated glucocorticoid receptor interacts with the INHAT component Set/TAF-Ibeta and releases it from a glucocorticoid-responsive gene promoter, relieving repression: implications for the pathogenesis of glucocorticoid resistance in acute undifferentiated leukemia with Set-Can translocation. Mol Cell Endocrinol 283 (2008) 19-31
    • (2008) Mol Cell Endocrinol , vol.283 , pp. 19-31
    • Ichijo, T.1    Chrousos, G.P.2    Kino, T.3
  • 127
    • 0028123786 scopus 로고
    • Identification and characterization of SET, a nuclear phosphoprotein encoded by the translocation break point in acute undifferentiated leukemia
    • 62
    • Adachi Y., Pavlakis G.N., and Copeland T.D. Identification and characterization of SET, a nuclear phosphoprotein encoded by the translocation break point in acute undifferentiated leukemia. J Biol Chem 269 (1994) 2258 62
    • (1994) J Biol Chem , vol.269 , pp. 2258
    • Adachi, Y.1    Pavlakis, G.N.2    Copeland, T.D.3
  • 128
    • 65549132937 scopus 로고    scopus 로고
    • Neuronal differentiation is regulated by leucine-rich acidic nuclear protein (LANP), a member of the inhibitor of histone acetyltransferase complex
    • 92
    • Kular R.K., Cvetanovic M., Siferd S., Kini A.R., and Opal P. Neuronal differentiation is regulated by leucine-rich acidic nuclear protein (LANP), a member of the inhibitor of histone acetyltransferase complex. J Biol Chem 284 (2009) 7783 92
    • (2009) J Biol Chem , vol.284 , pp. 7783
    • Kular, R.K.1    Cvetanovic, M.2    Siferd, S.3    Kini, A.R.4    Opal, P.5
  • 129
    • 33747059905 scopus 로고    scopus 로고
    • Tumor suppressor pp32 represses cell growth through inhibition of transcription by blocking acetylation and phosphorylation of histone H3 and initiating its proapoptotic activity
    • 94
    • Fan Z., Zhang H., and Zhang Q. Tumor suppressor pp32 represses cell growth through inhibition of transcription by blocking acetylation and phosphorylation of histone H3 and initiating its proapoptotic activity. Cell Death Differ 13 (2006) 1485 94
    • (2006) Cell Death Differ , vol.13 , pp. 1485
    • Fan, Z.1    Zhang, H.2    Zhang, Q.3
  • 130
    • 22144483767 scopus 로고    scopus 로고
    • A pp32-retinoblastoma protein complex modulates androgen receptor-mediated transcription and associates with components of the splicing machinery
    • 8
    • Adegbola O., and Pasternack G.R. A pp32-retinoblastoma protein complex modulates androgen receptor-mediated transcription and associates with components of the splicing machinery. Biochem Biophys Res Commun 334 (2005) 702 8
    • (2005) Biochem Biophys Res Commun , vol.334 , pp. 702
    • Adegbola, O.1    Pasternack, G.R.2
  • 131
    • 11844263936 scopus 로고    scopus 로고
    • The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates
    • Gamble M.J., Erdjument-Bromage H., Tempst P., Freedman L.P., and Fisher R.P. The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates. Mol Cell Biol 25 (2005) 797-807
    • (2005) Mol Cell Biol , vol.25 , pp. 797-807
    • Gamble, M.J.1    Erdjument-Bromage, H.2    Tempst, P.3    Freedman, L.P.4    Fisher, R.P.5
  • 132
    • 0029009403 scopus 로고
    • Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis
    • 83
    • Nagata K., Kawase H., Handa H., Yano K., Yamasaki M., Ishimi Y., et al. Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis. Proc Natl Acad Sci USA 92 (1995) 4279 83
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4279
    • Nagata, K.1    Kawase, H.2    Handa, H.3    Yano, K.4    Yamasaki, M.5    Ishimi, Y.6
  • 133
    • 34248351582 scopus 로고    scopus 로고
    • Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity
    • 90
    • Muto S., Senda M., Akai Y., Sato L., Suzuki T., Nagai R., et al. Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity. Proc Natl Acad Sci USA 104 (2007) 4285 90
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4285
    • Muto, S.1    Senda, M.2    Akai, Y.3    Sato, L.4    Suzuki, T.5    Nagai, R.6
  • 134
    • 0037512311 scopus 로고    scopus 로고
    • Distinct strategies to make nucleosomal DNA accessible
    • 22
    • Fan H.Y., He X., Kingston R.E., and Narlikar G.J. Distinct strategies to make nucleosomal DNA accessible. Mol Cell 11 (2003) 1311 22
    • (2003) Mol Cell , vol.11 , pp. 1311
    • Fan, H.Y.1    He, X.2    Kingston, R.E.3    Narlikar, G.J.4
  • 135
    • 0037428217 scopus 로고    scopus 로고
    • Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway
    • 6
    • Jiang X., Kim H.E., Shu H., Zhao Y., Zhang H., Kofron J., et al. Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway. Science 299 (2003) 223 6
    • (2003) Science , vol.299 , pp. 223
    • Jiang, X.1    Kim, H.E.2    Shu, H.3    Zhao, Y.4    Zhang, H.5    Kofron, J.6
  • 136
    • 0037423932 scopus 로고    scopus 로고
    • Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor
    • 72
    • Fan Z., Beresford P.J., Oh D.Y., Zhang D., and Lieberman J. Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell 112 (2003) 659 72
    • (2003) Cell , vol.112 , pp. 659
    • Fan, Z.1    Beresford, P.J.2    Oh, D.Y.3    Zhang, D.4    Lieberman, J.5
  • 137
    • 32944474371 scopus 로고    scopus 로고
    • Human lymphoblastoid proteome analysis reveals a role for the inhibitor of acetyltransferases complex in DNA double-strand break response
    • 80
    • Dirksen E.H., Cloos J., Braakhuis B.J., Brakenhoff R.H., Heck A.J., and Slijper M. Human lymphoblastoid proteome analysis reveals a role for the inhibitor of acetyltransferases complex in DNA double-strand break response. Cancer Res 66 (2006) 1473 80
    • (2006) Cancer Res , vol.66 , pp. 1473
    • Dirksen, E.H.1    Cloos, J.2    Braakhuis, B.J.3    Brakenhoff, R.H.4    Heck, A.J.5    Slijper, M.6
  • 138
    • 0036094806 scopus 로고    scopus 로고
    • Inhibition of CBP-mediated protein acetylation by the Ets family oncoprotein PU.1
    • 43
    • Hong W., Kim A.Y., Ky S., Rakowski C., Seo S.B., Chakravarti D., et al. Inhibition of CBP-mediated protein acetylation by the Ets family oncoprotein PU.1. Mol Cell Biol 22 (2002) 3729 43
    • (2002) Mol Cell Biol , vol.22 , pp. 3729
    • Hong, W.1    Kim, A.Y.2    Ky, S.3    Rakowski, C.4    Seo, S.B.5    Chakravarti, D.6
  • 139
    • 33646538106 scopus 로고    scopus 로고
    • Regulation of histone acetyltransferase activity of p300 and PCAF by proto-oncogene protein DEK
    • 22
    • Ko S.I., Lee I.S., Kim J.Y., Kim S.M., Kim D.W., Lee K.S., et al. Regulation of histone acetyltransferase activity of p300 and PCAF by proto-oncogene protein DEK. FEBS Lett 580 (2006) 3217 22
    • (2006) FEBS Lett , vol.580 , pp. 3217
    • Ko, S.I.1    Lee, I.S.2    Kim, J.Y.3    Kim, S.M.4    Kim, D.W.5    Lee, K.S.6
  • 140
    • 0036272787 scopus 로고    scopus 로고
    • JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells
    • 26
    • Jin C., Li H., Murata T., Sun K., Horikoshi M., Chiu R., et al. JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells. Mol Cell Biol 22 (2002) 4815 26
    • (2002) Mol Cell Biol , vol.22 , pp. 4815
    • Jin, C.1    Li, H.2    Murata, T.3    Sun, K.4    Horikoshi, M.5    Chiu, R.6
  • 141
  • 142
    • 34447648044 scopus 로고    scopus 로고
    • JDP2 suppresses adipocyte differentiation by regulating histone acetylation
    • 405
    • Nakade K., Pan J., Yoshiki A., Ugai H., Kimura M., Liu B., et al. JDP2 suppresses adipocyte differentiation by regulating histone acetylation. Cell Death Differ 14 (2007) 1398 405
    • (2007) Cell Death Differ , vol.14 , pp. 1398
    • Nakade, K.1    Pan, J.2    Yoshiki, A.3    Ugai, H.4    Kimura, M.5    Liu, B.6
  • 143
    • 28444474846 scopus 로고    scopus 로고
    • NIR is a novel INHAT repressor that modulates the transcriptional activity of p53
    • 24
    • Hublitz P., Kunowska N., Mayer U.P., Muller J.M., Heyne K., Yin N., et al. NIR is a novel INHAT repressor that modulates the transcriptional activity of p53. Genes Dev 19 (2005) 2912 24
    • (2005) Genes Dev , vol.19 , pp. 2912
    • Hublitz, P.1    Kunowska, N.2    Mayer, U.P.3    Muller, J.M.4    Heyne, K.5    Yin, N.6
  • 144
    • 0019842812 scopus 로고
    • DNAase I-hypersensitive sites of chromatin
    • 5
    • Elgin S.C. DNAase I-hypersensitive sites of chromatin. Cell 27 (1981) 413 5
    • (1981) Cell , vol.27 , pp. 413
    • Elgin, S.C.1
  • 145
    • 0023899769 scopus 로고
    • Nuclease hypersensitive sites in chromatin
    • 97
    • Gross D.S., and Garrard W.T. Nuclease hypersensitive sites in chromatin. Annu Rev Biochem 57 (1988) 159 97
    • (1988) Annu Rev Biochem , vol.57 , pp. 159
    • Gross, D.S.1    Garrard, W.T.2
  • 146
    • 0019787269 scopus 로고
    • A 200 base pair region at the 5′ end of the chicken adult beta-globin gene is accessible to nuclease digestion
    • McGhee J.D., Wood W.I., Dolan M., Engel J.D., and Felsenfeld G. A 200 base pair region at the 5′ end of the chicken adult beta-globin gene is accessible to nuclease digestion. Cell 27 (1981) 45-55
    • (1981) Cell , vol.27 , pp. 45-55
    • McGhee, J.D.1    Wood, W.I.2    Dolan, M.3    Engel, J.D.4    Felsenfeld, G.5
  • 147
    • 22744432660 scopus 로고    scopus 로고
    • Genome-scale identification of nucleosome positions in S. cerevisiae
    • 30
    • Yuan G.C., Liu Y.J., Dion M.F., Slack M.D., Wu L.F., Altschuler S.J., et al. Genome-scale identification of nucleosome positions in S. cerevisiae. Science 309 (2005) 626 30
    • (2005) Science , vol.309 , pp. 626
    • Yuan, G.C.1    Liu, Y.J.2    Dion, M.F.3    Slack, M.D.4    Wu, L.F.5    Altschuler, S.J.6
  • 149
    • 3543023310 scopus 로고    scopus 로고
    • Evidence for nucleosome depletion at active regulatory regions genome-wide
    • 5
    • Lee C.K., Shibata Y., Rao B., Strahl B.D., and Lieb J.D. Evidence for nucleosome depletion at active regulatory regions genome-wide. Nat Genet 36 (2004) 900 5
    • (2004) Nat Genet , vol.36 , pp. 900
    • Lee, C.K.1    Shibata, Y.2    Rao, B.3    Strahl, B.D.4    Lieb, J.D.5
  • 150
    • 16244411972 scopus 로고    scopus 로고
    • Histone dynamics on the interleukin-2 gene in response to T-cell activation
    • 19
    • Chen X., Wang J., Woltring D., Gerondakis S., and Shannon M.F. Histone dynamics on the interleukin-2 gene in response to T-cell activation. Mol Cell Biol 25 (2005) 3209 19
    • (2005) Mol Cell Biol , vol.25 , pp. 3209
    • Chen, X.1    Wang, J.2    Woltring, D.3    Gerondakis, S.4    Shannon, M.F.5
  • 151
  • 152
    • 0021233482 scopus 로고
    • The role of stable complexes that repress and activate eucaryotic genes
    • 65
    • Brown D.D. The role of stable complexes that repress and activate eucaryotic genes. Cell 37 (1984) 359 65
    • (1984) Cell , vol.37 , pp. 359
    • Brown, D.D.1
  • 154
    • 0038094501 scopus 로고    scopus 로고
    • Nucleosomes unfold completely at a transcriptionally active promoter
    • 98
    • Boeger H., Griesenbeck J., Strattan J.S., and Kornberg R.D. Nucleosomes unfold completely at a transcriptionally active promoter. Mol Cell 11 (2003) 1587 98
    • (2003) Mol Cell , vol.11 , pp. 1587
    • Boeger, H.1    Griesenbeck, J.2    Strattan, J.S.3    Kornberg, R.D.4
  • 155
    • 0038094502 scopus 로고    scopus 로고
    • Histones are first hyperacetylated and then lose contact with the activated PHO5 promoter
    • 607
    • Reinke H., and Horz W. Histones are first hyperacetylated and then lose contact with the activated PHO5 promoter. Mol Cell 11 (2003) 1599 607
    • (2003) Mol Cell , vol.11 , pp. 1599
    • Reinke, H.1    Horz, W.2
  • 157
    • 57449095143 scopus 로고    scopus 로고
    • Identifying positioned nucleosomes with epigenetic marks in human from ChIP-Seq
    • Zhang Y., Shin H., Song J.S., Lei Y., and Liu X.S. Identifying positioned nucleosomes with epigenetic marks in human from ChIP-Seq. BMC Genomics 9 (2008) 537
    • (2008) BMC Genomics , vol.9 , pp. 537
    • Zhang, Y.1    Shin, H.2    Song, J.S.3    Lei, Y.4    Liu, X.S.5
  • 158
    • 39749145198 scopus 로고    scopus 로고
    • Dynamic regulation of nucleosome positioning in the human genome
    • 98
    • Schones D.E., Cui K., Cuddapah S., Roh T.Y., Barski A., Wang Z., et al. Dynamic regulation of nucleosome positioning in the human genome. Cell 132 (2008) 887 98
    • (2008) Cell , vol.132 , pp. 887
    • Schones, D.E.1    Cui, K.2    Cuddapah, S.3    Roh, T.Y.4    Barski, A.5    Wang, Z.6
  • 159
    • 39449088572 scopus 로고    scopus 로고
    • Genome-wide approaches to studying chromatin modifications
    • 91
    • Schones D.E., and Zhao K. Genome-wide approaches to studying chromatin modifications. Nat Rev Genet 9 (2008) 179 91
    • (2008) Nat Rev Genet , vol.9 , pp. 179
    • Schones, D.E.1    Zhao, K.2
  • 160
    • 0032933431 scopus 로고    scopus 로고
    • Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily
    • 94
    • Dressel U., Thormeyer D., Altincicek B., Paululat A., Eggert M., Schneider S., et al. Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily. Mol Cell Biol 19 (1999) 3383 94
    • (1999) Mol Cell Biol , vol.19 , pp. 3383
    • Dressel, U.1    Thormeyer, D.2    Altincicek, B.3    Paululat, A.4    Eggert, M.5    Schneider, S.6
  • 161
    • 34248162451 scopus 로고    scopus 로고
    • The nucleosome assembly activity of NAP1 is enhanced by Alien
    • 68
    • Eckey M., Hong W., Papaioannou M., and Baniahmad A. The nucleosome assembly activity of NAP1 is enhanced by Alien. Mol Cell Biol 27 (2007) 3557 68
    • (2007) Mol Cell Biol , vol.27 , pp. 3557
    • Eckey, M.1    Hong, W.2    Papaioannou, M.3    Baniahmad, A.4
  • 162
    • 0033568312 scopus 로고    scopus 로고
    • ATP-dependent remodeling and acetylation as regulators of chromatin fluidity
    • 52
    • Kingston R.E., and Narlikar G.J. ATP-dependent remodeling and acetylation as regulators of chromatin fluidity. Genes Dev 13 (1999) 2339 52
    • (1999) Genes Dev , vol.13 , pp. 2339
    • Kingston, R.E.1    Narlikar, G.J.2
  • 163
    • 33745790132 scopus 로고    scopus 로고
    • Chromatin remodelling: the industrial revolution of DNA around histones
    • 47
    • Saha A., Wittmeyer J., and Cairns B.R. Chromatin remodelling: the industrial revolution of DNA around histones. Nat Rev Mol Cell Biol 7 (2006) 437 47
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 437
    • Saha, A.1    Wittmeyer, J.2    Cairns, B.R.3
  • 164
    • 4444289406 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodelling: factors and functions
    • 11
    • Eberharter A., and Becker P.B. ATP-dependent nucleosome remodelling: factors and functions. J Cell Sci 117 (2004) 3707 11
    • (2004) J Cell Sci , vol.117 , pp. 3707
    • Eberharter, A.1    Becker, P.B.2
  • 165
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • 73
    • Becker P.B., and Horz W. ATP-dependent nucleosome remodeling. Annu Rev Biochem 71 (2002) 247 73
    • (2002) Annu Rev Biochem , vol.71 , pp. 247
    • Becker, P.B.1    Horz, W.2
  • 166
    • 0034131012 scopus 로고    scopus 로고
    • Recruitment of chromatin remodeling machines
    • 85
    • Peterson C.L., and Logie C. Recruitment of chromatin remodeling machines. J Cell Biochem 78 (2000) 179 85
    • (2000) J Cell Biochem , vol.78 , pp. 179
    • Peterson, C.L.1    Logie, C.2
  • 167
    • 0021715020 scopus 로고
    • Genes affecting the regulation of SUC2 gene expression by glucose repression in Saccharomyces cerevisiae
    • 58
    • Neigeborn L., and Carlson M. Genes affecting the regulation of SUC2 gene expression by glucose repression in Saccharomyces cerevisiae. Genetics 108 (1984) 845 58
    • (1984) Genetics , vol.108 , pp. 845
    • Neigeborn, L.1    Carlson, M.2
  • 168
    • 0021659727 scopus 로고
    • Five SWI genes are required for expression of the HO gene in yeast
    • 68
    • Stern M., Jensen R., and Herskowitz I. Five SWI genes are required for expression of the HO gene in yeast. J Mol Biol 178 (1984) 853 68
    • (1984) J Mol Biol , vol.178 , pp. 853
    • Stern, M.1    Jensen, R.2    Herskowitz, I.3
  • 169
    • 0026584855 scopus 로고
    • Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription
    • 83
    • Peterson C.L., and Herskowitz I. Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription. Cell 68 (1992) 573 83
    • (1992) Cell , vol.68 , pp. 573
    • Peterson, C.L.1    Herskowitz, I.2
  • 170
    • 0028987268 scopus 로고
    • The SWI-SNF complex: a chromatin remodeling machine?
    • 6
    • Peterson C.L., and Tamkun J.W. The SWI-SNF complex: a chromatin remodeling machine?. Trends Biochem Sci 20 (1995) 143 6
    • (1995) Trends Biochem Sci , vol.20 , pp. 143
    • Peterson, C.L.1    Tamkun, J.W.2
  • 171
    • 0037380161 scopus 로고    scopus 로고
    • Recent advances in understanding chromatin remodeling by Swi/Snf complexes
    • 42
    • Martens J.A., and Winston F. Recent advances in understanding chromatin remodeling by Swi/Snf complexes. Curr Opin Genet Dev 13 (2003) 136 42
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 136
    • Martens, J.A.1    Winston, F.2
  • 172
    • 0030971868 scopus 로고    scopus 로고
    • Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix
    • 74
    • Reyes J.C., Muchardt C., and Yaniv M. Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix. J Cell Biol 137 (1997) 263 74
    • (1997) J Cell Biol , vol.137 , pp. 263
    • Reyes, J.C.1    Muchardt, C.2    Yaniv, M.3
  • 173
    • 36549078554 scopus 로고    scopus 로고
    • Dynamics of coactivator recruitment and chromatin modifications during nuclear receptor mediated transcription
    • Aoyagi S., and Archer T.K. Dynamics of coactivator recruitment and chromatin modifications during nuclear receptor mediated transcription. Mol Cell Endocrinol 280 (2008) 1-5
    • (2008) Mol Cell Endocrinol , vol.280 , pp. 1-5
    • Aoyagi, S.1    Archer, T.K.2
  • 174
    • 0038380293 scopus 로고    scopus 로고
    • Chromatin remodeling by nuclear receptors
    • Hebbar P.B., and Archer T.K. Chromatin remodeling by nuclear receptors. Chromosoma 111 (2003) 495-504
    • (2003) Chromosoma , vol.111 , pp. 495-504
    • Hebbar, P.B.1    Archer, T.K.2
  • 175
    • 33847131992 scopus 로고    scopus 로고
    • Nuclear receptors and chromatin remodeling machinery
    • 7
    • Trotter K.W., and Archer T.K. Nuclear receptors and chromatin remodeling machinery. Mol Cell Endocrinol 265-266 (2007) 162 7
    • (2007) Mol Cell Endocrinol , vol.265-266 , pp. 162
    • Trotter, K.W.1    Archer, T.K.2
  • 176
    • 0027434083 scopus 로고
    • A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor
    • 90
    • Muchardt C., and Yaniv M. A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. EMBO J 12 (1993) 4279 90
    • (1993) EMBO J , vol.12 , pp. 4279
    • Muchardt, C.1    Yaniv, M.2
  • 177
    • 3142596494 scopus 로고    scopus 로고
    • Transcriptional activation by nuclear receptors
    • Acevedo M.L., and Kraus W.L. Transcriptional activation by nuclear receptors. Essays Biochem 40 (2004) 73-88
    • (2004) Essays Biochem , vol.40 , pp. 73-88
    • Acevedo, M.L.1    Kraus, W.L.2
  • 178
    • 0026506720 scopus 로고
    • Transcription factor loading on the MMTV promoter: a bimodal mechanism for promoter activation
    • 6
    • Archer T.K., Lefebvre P., Wolford R.G., and Hager G.L. Transcription factor loading on the MMTV promoter: a bimodal mechanism for promoter activation. Science 255 (1992) 1573 6
    • (1992) Science , vol.255 , pp. 1573
    • Archer, T.K.1    Lefebvre, P.2    Wolford, R.G.3    Hager, G.L.4
  • 179
    • 0030812908 scopus 로고    scopus 로고
    • Transcription factor access to chromatin
    • 63
    • Beato M., and Eisfeld K. Transcription factor access to chromatin. Nucleic Acids Res 25 (1997) 3559 63
    • (1997) Nucleic Acids Res , vol.25 , pp. 3559
    • Beato, M.1    Eisfeld, K.2
  • 180
    • 0343632400 scopus 로고    scopus 로고
    • Ligand-dependent interaction between the estrogen receptor and the human homologues of SWI2/SNF2
    • Ichinose H., Garnier J.M., Chambon P., and Losson R. Ligand-dependent interaction between the estrogen receptor and the human homologues of SWI2/SNF2. Gene 188 (1997) 95-100
    • (1997) Gene , vol.188 , pp. 95-100
    • Ichinose, H.1    Garnier, J.M.2    Chambon, P.3    Losson, R.4
  • 181
    • 1842609849 scopus 로고    scopus 로고
    • Reconstitution of glucocorticoid receptor-dependent transcription in vivo
    • 58
    • Trotter K.W., and Archer T.K. Reconstitution of glucocorticoid receptor-dependent transcription in vivo. Mol Cell Biol 24 (2004) 3347 58
    • (2004) Mol Cell Biol , vol.24 , pp. 3347
    • Trotter, K.W.1    Archer, T.K.2
  • 182
    • 0041589541 scopus 로고    scopus 로고
    • Nuclear receptors: a rendezvous for chromatin remodeling factors
    • 80
    • Belandia B., and Parker M.G. Nuclear receptors: a rendezvous for chromatin remodeling factors. Cell 114 (2003) 277 80
    • (2003) Cell , vol.114 , pp. 277
    • Belandia, B.1    Parker, M.G.2
  • 183
    • 0028239595 scopus 로고
    • Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor
    • 20
    • Chiba H., Muramatsu M., Nomoto A., and Kato H. Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor. Nucleic Acids Res 22 (1994) 1815 20
    • (1994) Nucleic Acids Res , vol.22 , pp. 1815
    • Chiba, H.1    Muramatsu, M.2    Nomoto, A.3    Kato, H.4
  • 184
    • 0038046628 scopus 로고    scopus 로고
    • The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome
    • 17
    • Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., et al. The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome. Cell 113 (2003) 905 17
    • (2003) Cell , vol.113 , pp. 905
    • Kitagawa, H.1    Fujiki, R.2    Yoshimura, K.3    Mezaki, Y.4    Uematsu, Y.5    Matsui, D.6
  • 186
    • 0031444148 scopus 로고    scopus 로고
    • ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
    • 55
    • Ito T., Bulger M., Pazin M.J., Kobayashi R., and Kadonaga J.T. ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. Cell 90 (1997) 145 55
    • (1997) Cell , vol.90 , pp. 145
    • Ito, T.1    Bulger, M.2    Pazin, M.J.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 187
    • 0030839857 scopus 로고    scopus 로고
    • Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II
    • Varga-Weisz P.D., Wilm M., Bonte E., Dumas K., Mann M., and Becker P.B. Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II. Nature 388 (1997) 598-602
    • (1997) Nature , vol.388 , pp. 598-602
    • Varga-Weisz, P.D.1    Wilm, M.2    Bonte, E.3    Dumas, K.4    Mann, M.5    Becker, P.B.6
  • 188
    • 0033965391 scopus 로고    scopus 로고
    • A family of chromatin remodeling factors related to Williams syndrome transcription factor
    • 43
    • Bochar D.A., Savard J., Wang W., Lafleur D.W., Moore P., Cote J., et al. A family of chromatin remodeling factors related to Williams syndrome transcription factor. Proc Natl Acad Sci USA 97 (2000) 1038 43
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1038
    • Bochar, D.A.1    Savard, J.2    Wang, W.3    Lafleur, D.W.4    Moore, P.5    Cote, J.6
  • 189
    • 0942290537 scopus 로고    scopus 로고
    • Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo
    • 83
    • Fyodorov D.V., Blower M.D., Karpen G.H., and Kadonaga J.T. Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo. Genes Dev 18 (2004) 170 83
    • (2004) Genes Dev , vol.18 , pp. 170
    • Fyodorov, D.V.1    Blower, M.D.2    Karpen, G.H.3    Kadonaga, J.T.4
  • 190
    • 0034721670 scopus 로고    scopus 로고
    • The Isw2 chromatin remodeling complex represses early meiotic genes upon recruitment by Ume6p
    • 33
    • Goldmark J.P., Fazzio T.G., Estep P.W., Church G.M., and Tsukiyama T. The Isw2 chromatin remodeling complex represses early meiotic genes upon recruitment by Ume6p. Cell 103 (2000) 423 33
    • (2000) Cell , vol.103 , pp. 423
    • Goldmark, J.P.1    Fazzio, T.G.2    Estep, P.W.3    Church, G.M.4    Tsukiyama, T.5
  • 191
    • 0345276461 scopus 로고    scopus 로고
    • Chromatin remodeling in vivo: evidence for a nucleosome sliding mechanism
    • 40
    • Fazzio T.G., and Tsukiyama T. Chromatin remodeling in vivo: evidence for a nucleosome sliding mechanism. Mol Cell 12 (2003) 1333 40
    • (2003) Mol Cell , vol.12 , pp. 1333
    • Fazzio, T.G.1    Tsukiyama, T.2
  • 192
    • 0038771223 scopus 로고    scopus 로고
    • Regulated displacement of TBP from the PHO8 promoter in vivo requires Cbf1 and the Isw1 chromatin remodeling complex
    • 20
    • Moreau J.L., Lee M., Mahachi N., Vary J., Mellor J., Tsukiyama T., et al. Regulated displacement of TBP from the PHO8 promoter in vivo requires Cbf1 and the Isw1 chromatin remodeling complex. Mol Cell 11 (2003) 1609 20
    • (2003) Mol Cell , vol.11 , pp. 1609
    • Moreau, J.L.1    Lee, M.2    Mahachi, N.3    Vary, J.4    Mellor, J.5    Tsukiyama, T.6
  • 193
    • 33745847547 scopus 로고    scopus 로고
    • Antagonistic forces that position nucleosomes in vivo
    • 40
    • Whitehouse I., and Tsukiyama T. Antagonistic forces that position nucleosomes in vivo. Nat Struct Mol Biol 13 (2006) 633 40
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 633
    • Whitehouse, I.1    Tsukiyama, T.2
  • 194
    • 0344198601 scopus 로고    scopus 로고
    • The ISWI ATPase Snf2h is required for early mouse development
    • 102
    • Stopka T., and Skoultchi A.I. The ISWI ATPase Snf2h is required for early mouse development. Proc Natl Acad Sci USA 100 (2003) 14097 102
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14097
    • Stopka, T.1    Skoultchi, A.I.2
  • 195
    • 53649109937 scopus 로고    scopus 로고
    • The chromatin remodelers ISWI and ACF1 directly repress Wingless transcriptional targets
    • Liu Y.I., Chang M.V., Li H.E., Barolo S., Chang J.L., Blauwkamp T.A., et al. The chromatin remodelers ISWI and ACF1 directly repress Wingless transcriptional targets. Dev Biol 323 (2008) 41-52
    • (2008) Dev Biol , vol.323 , pp. 41-52
    • Liu, Y.I.1    Chang, M.V.2    Li, H.E.3    Barolo, S.4    Chang, J.L.5    Blauwkamp, T.A.6
  • 196
    • 0033166365 scopus 로고    scopus 로고
    • Two-step synergism between the progesterone receptor and the DNA-binding domain of nuclear factor 1 on MMTV minichromosomes
    • Di Croce L., Koop R., Venditti P., Westphal H.M., Nightingale K.P., Corona D.F., et al. Two-step synergism between the progesterone receptor and the DNA-binding domain of nuclear factor 1 on MMTV minichromosomes. Mol Cell 4 (1999) 45-54
    • (1999) Mol Cell , vol.4 , pp. 45-54
    • Di Croce, L.1    Koop, R.2    Venditti, P.3    Westphal, H.M.4    Nightingale, K.P.5    Corona, D.F.6
  • 197
    • 27644580861 scopus 로고    scopus 로고
    • The Drosophila nucleosome remodeling factor NURF is required for Ecdysteroid signaling and metamorphosis
    • 5
    • Badenhorst P., Xiao H., Cherbas L., Kwon S.Y., Voas M., Rebay I., et al. The Drosophila nucleosome remodeling factor NURF is required for Ecdysteroid signaling and metamorphosis. Genes Dev 19 (2005) 2540 5
    • (2005) Genes Dev , vol.19 , pp. 2540
    • Badenhorst, P.1    Xiao, H.2    Cherbas, L.3    Kwon, S.Y.4    Voas, M.5    Rebay, I.6
  • 198
    • 0035898615 scopus 로고    scopus 로고
    • Acf1, the largest subunit of CHRAC, regulates ISWI-induced nucleosome remodelling
    • 8
    • Eberharter A., Ferrari S., Langst G., Straub T., Imhof A., Varga-Weisz P., et al. Acf1, the largest subunit of CHRAC, regulates ISWI-induced nucleosome remodelling. EMBO J 20 (2001) 3781 8
    • (2001) EMBO J , vol.20 , pp. 3781
    • Eberharter, A.1    Ferrari, S.2    Langst, G.3    Straub, T.4    Imhof, A.5    Varga-Weisz, P.6
  • 199
    • 8144224380 scopus 로고    scopus 로고
    • ACF1 improves the effectiveness of nucleosome mobilization by ISWI through PHD-histone contacts
    • 39
    • Eberharter A., Vetter I., Ferreira R., and Becker P.B. ACF1 improves the effectiveness of nucleosome mobilization by ISWI through PHD-histone contacts. EMBO J 23 (2004) 4029 39
    • (2004) EMBO J , vol.23 , pp. 4029
    • Eberharter, A.1    Vetter, I.2    Ferreira, R.3    Becker, P.B.4
  • 200
    • 0036899341 scopus 로고    scopus 로고
    • An ACF1-ISWI chromatin-remodeling complex is required for DNA replication through heterochromatin
    • 32
    • Collins N., Poot R.A., Kukimoto I., Garcia-Jimenez C., Dellaire G., and Varga-Weisz P.D. An ACF1-ISWI chromatin-remodeling complex is required for DNA replication through heterochromatin. Nat Genet 32 (2002) 627 32
    • (2002) Nat Genet , vol.32 , pp. 627
    • Collins, N.1    Poot, R.A.2    Kukimoto, I.3    Garcia-Jimenez, C.4    Dellaire, G.5    Varga-Weisz, P.D.6
  • 201
    • 23244448558 scopus 로고    scopus 로고
    • The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing
    • 8
    • Zhou Y., and Grummt I. The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing. Curr Biol 15 (2005) 1434 8
    • (2005) Curr Biol , vol.15 , pp. 1434
    • Zhou, Y.1    Grummt, I.2
  • 202
    • 0037009366 scopus 로고    scopus 로고
    • The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription
    • 40
    • Zhou Y., Santoro R., and Grummt I. The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription. EMBO J 21 (2002) 4632 40
    • (2002) EMBO J , vol.21 , pp. 4632
    • Zhou, Y.1    Santoro, R.2    Grummt, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.