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Volumn 68, Issue , 2004, Pages 93-122

Nuclear Receptor Recruitment of Histone-Modifying Enzymes to Target Gene Promoters

Author keywords

[No Author keywords available]

Indexed keywords

CELL RECEPTOR; HISTONE; NUCLEAR PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; TRANSFERASE;

EID: 3242892659     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0083-6729(04)68003-4     Document Type: Article
Times cited : (44)

References (140)
  • 1
    • 85047671736 scopus 로고    scopus 로고
    • The SANT domain: A putative DNA-binding domain in the SWI⧸SNF and ADA complexes, the transcriptional corepressor NCoR, and TFIIIB
    • R Aasland A.F Stewart T Gibson The SANT domain: A putative DNA-binding domain in the SWI⧸SNF and ADA complexes, the transcriptional corepressor NCoR, and TFIIIB Trends Biochem. Sci. 21 1996 87 88
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 87-88
    • Aasland, R1    Stewart, A.F2    Gibson, T3
  • 3
    • 0033681250 scopus 로고    scopus 로고
    • Ordered recruitment of chromatin-modifying and general transcription factors to the IFN-beta promoter
    • T Agalioti S Lomvardas B Parekh J Yie T Maniatis D Thanos Ordered recruitment of chromatin-modifying and general transcription factors to the IFN-beta promoter Cell 103 2000 667 678
    • (2000) Cell , vol.103 , pp. 667-678
    • Agalioti, T1    Lomvardas, S2    Parekh, B3    Yie, J4    Maniatis, T5    Thanos, D6
  • 4
    • 0030959244 scopus 로고    scopus 로고
    • Role for NCoR and histone deacetylase in Sin3-mediated transcriptional repression
    • L Alland R Muhle H Hou Jr. J Potes L Chin N Schreiber-Agus R.A DePinho Role for NCoR and histone deacetylase in Sin3-mediated transcriptional repression Nature 387 1997 49 55
    • (1997) Nature , vol.387 , pp. 49-55
    • Alland, L1    Muhle, R2    Hou, H3    Potes, J4    Chin, L5    Schreiber-Agus, N6    DePinho, R.A7
  • 5
    • 0035815105 scopus 로고    scopus 로고
    • Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites
    • J.D Anderson P.T Lowary J Widom Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites J. Mol. Biol. 307 2001 977 985
    • (2001) J. Mol. Biol. , vol.307 , pp. 977-985
    • Anderson, J.D1    Lowary, P.T2    Widom, J3
  • 7
    • 0042626227 scopus 로고    scopus 로고
    • A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling
    • M Ariyoshi J.W Schwabe A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling Genes Dev. 17 2003 1909 1920
    • (2003) Genes Dev. , vol.17 , pp. 1909-1920
    • Ariyoshi, M1    Schwabe, J.W2
  • 8
    • 0030480969 scopus 로고    scopus 로고
    • The CBP coactivator is a histone acetyltransferase
    • A.J Bannister T Kouzarides The CBP coactivator is a histone acetyltransferase Nature 384 1996 641 643
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J1    Kouzarides, T2
  • 9
    • 0041589541 scopus 로고    scopus 로고
    • Nuclear receptors: A rendezvous for chromatin remodeling factors
    • B Belandia M.G Parker Nuclear receptors: A rendezvous for chromatin remodeling factors Cell 114 2003 277 280
    • (2003) Cell , vol.114 , pp. 277-280
    • Belandia, B1    Parker, M.G2
  • 10
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • S.L Berger Histone modifications in transcriptional regulation Curr. Opin. Genet. Dev. 12 2002 142 148
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 142-148
    • Berger, S.L1
  • 11
    • 0034935019 scopus 로고    scopus 로고
    • Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling
    • R.N Bhattacharjee G.C Banks K.W Trotter H.L Lee T.K Archer Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling Mol. Cell. Biol. 21 2001 5417 5425
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5417-5425
    • Bhattacharjee, R.N1    Banks, G.C2    Trotter, K.W3    Lee, H.L4    Archer, T.K5
  • 12
    • 0032833981 scopus 로고    scopus 로고
    • Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, Huntingtin
    • J.M Boutell P Thomas J.W Neal V.J Weston J Duce P.S Harper A.L Jones Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, Huntingtin Hum. Mol. Genet. 8 1999 1647 1655
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1647-1655
    • Boutell, J.M1    Thomas, P2    Neal, J.W3    Weston, V.J4    Duce, J5    Harper, P.S6    Jones, A.L7
  • 13
  • 15
    • 0034731452 scopus 로고    scopus 로고
    • Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300
    • D Chen S.M Huang M.R Stallcup Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300 J. Biol. Chem. 275 2000 40810 40816
    • (2000) J. Biol. Chem. , vol.275 , pp. 40810-40816
    • Chen, D1    Huang, S.M2    Stallcup, M.R3
  • 17
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P⧸CAF and CBP⧸p300
    • H Chen R.J Lin R.L Schiltz D Chakravarti A Nash L Nagy M.L Privalsky Y Nakatani R.M Evans Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P⧸CAF and CBP⧸p300 Cell 90 1997 569 580
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H1    Lin, R.J2    Schiltz, R.L3    Chakravarti, D4    Nash, A5    Nagy, L6    Privalsky, M.L7    Nakatani, Y8    Evans, R.M9
  • 18
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • H Chen R.J Lin W Xie D Wilpitz R.M Evans Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase Cell 98 1999 675 686
    • (1999) Cell , vol.98 , pp. 675-686
    • Chen, H1    Lin, R.J2    Xie, W3    Wilpitz, D4    Evans, R.M5
  • 19
    • 0033630453 scopus 로고    scopus 로고
    • Steroid⧸nuclear receptor coactivators
    • J.D Chen Steroid⧸nuclear receptor coactivators Vitam. Horm. 58 2000 391 448
    • (2000) Vitam. Horm. , vol.58 , pp. 391-448
    • Chen, J.D1
  • 20
    • 0029097233 scopus 로고
    • A transcriptional corepressor that interacts with nuclear hormone receptors
    • J.D Chen R.M Evans A transcriptional corepressor that interacts with nuclear hormone receptors Nature 377 1995 454 457
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D1    Evans, R.M2
  • 21
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • P Cheung C.D Allis P Sassone-Corsi Signaling to chromatin through histone modifications Cell 103 2000 263 271
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P1    Allis, C.D2    Sassone-Corsi, P3
  • 22
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • P Cheung K.G Tanner W.L Cheung P Sassone-Corsi J.M Denu C.D Allis Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation Mol. Cell 5 2000 905 915
    • (2000) Mol. Cell , vol.5 , pp. 905-915
    • Cheung, P1    Tanner, K.G2    Cheung, W.L3    Sassone-Corsi, P4    Denu, J.M5    Allis, C.D6
  • 23
    • 0036190459 scopus 로고    scopus 로고
    • CtBP, an unconventional transcriptional corepressor in development and oncogenesis
    • G Chinnadurai CtBP, an unconventional transcriptional corepressor in development and oncogenesis Mol. Cell 9 2002 213 224
    • (2002) Mol. Cell , vol.9 , pp. 213-224
    • Chinnadurai, G1
  • 24
    • 0036671407 scopus 로고    scopus 로고
    • Ordered recruitment: Gene-specific mechanism of transcription activation
    • M.P Cosma Ordered recruitment: Gene-specific mechanism of transcription activation Mol. Cell 10 2002 227 236
    • (2002) Mol. Cell , vol.10 , pp. 227-236
    • Cosma, M.P1
  • 25
    • 0037164736 scopus 로고    scopus 로고
    • Cross-talk between CARM1 methylation and CBP acetylation on histone H3
    • S Daujat U.M Bauer V Shah B Turner S Berger T Kouzarides Cross-talk between CARM1 methylation and CBP acetylation on histone H3 Curr. Biol. 12 2002 2090 2097
    • (2002) Curr. Biol. , vol.12 , pp. 2090-2097
    • Daujat, S1    Bauer, U.M2    Shah, V3    Turner, B4    Berger, S5    Kouzarides, T6
  • 26
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • C Dhalluin J.E Carlson L Zeng C He A.K Aggarwal M.M Zhou Structure and ligand of a histone acetyltransferase bromodomain Nature 399 1999 491 496
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C1    Carlson, J.E2    Zeng, L3    He, C4    Aggarwal, A.K5    Zhou, M.M6
  • 27
    • 0033636323 scopus 로고    scopus 로고
    • ATP-driven chromatin remodeling activity and histone acetyltransferases act sequentially during transactivation by RAR⧸RXR in vitro
    • F.J Dilworth C Fromental-Ramain K Yamamoto P Chambon ATP-driven chromatin remodeling activity and histone acetyltransferases act sequentially during transactivation by RAR⧸RXR in vitro Mol. Cell 6 2000 1049 1058
    • (2000) Mol. Cell , vol.6 , pp. 1049-1058
    • Dilworth, F.J1    Fromental-Ramain, C2    Yamamoto, K3    Chambon, P4
  • 28
    • 0036218774 scopus 로고    scopus 로고
    • The amino terminus of the human AR is target for corepressor action and antihormone agonism
    • H Dotzlaw U Moehren S Mink A.C Cato J.A Iniguez Lluhi A Baniahmad The amino terminus of the human AR is target for corepressor action and antihormone agonism Mol. Endocrinol. 16 2002 661 673
    • (2002) Mol. Endocrinol. , vol.16 , pp. 661-673
    • Dotzlaw, H1    Moehren, U2    Mink, S3    Cato, A.C4    Iniguez Lluhi, J.A5    Baniahmad, A6
  • 29
    • 0030003051 scopus 로고    scopus 로고
    • Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4
    • D.G Edmondson M.M Smith S.Y Roth Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4 Genes Dev. 10 1996 1247 1259
    • (1996) Genes Dev. , vol.10 , pp. 1247-1259
    • Edmondson, D.G1    Smith, M.M2    Roth, S.Y3
  • 30
    • 0037417752 scopus 로고    scopus 로고
    • Effects of retinoid ligands on RIP140: Molecular interaction with retinoid receptors and biological activity
    • M Farooqui P.J Franco J Thompson H Kagechika R.A Chandraratna L Banaszak L.N Wei Effects of retinoid ligands on RIP140: Molecular interaction with retinoid receptors and biological activity Biochemistry 42 2003 971 979
    • (2003) Biochemistry , vol.42 , pp. 971-979
    • Farooqui, M1    Franco, P.J2    Thompson, J3    Kagechika, H4    Chandraratna, R.A5    Banaszak, L6    Wei, L.N7
  • 31
    • 0037248643 scopus 로고    scopus 로고
    • Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms
    • I Fernandes Y Bastien T Wai K Nygard R Lin O Cormier H.S Lee F Eng N.R Bertos N Pelletier Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms Mol. Cell 11 2003 139 150
    • (2003) Mol. Cell , vol.11 , pp. 139-150
    • Fernandes, I1    Bastien, Y2    Wai, T3    Nygard, K4    Lin, R5    Cormier, O6    Lee, H.S7    Eng, F8    Bertos, N.R9    Pelletier, N10
  • 32
    • 0036161439 scopus 로고    scopus 로고
    • Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT⧸NCoR
    • W Fischle F Dequiedt M.J Hendzel M.G Guenther M.A Lazar W Voelter E Verdin Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT⧸NCoR Mol. Cell 9 2002 45 57
    • (2002) Mol. Cell , vol.9 , pp. 45-57
    • Fischle, W1    Dequiedt, F2    Hendzel, M.J3    Guenther, M.G4    Lazar, M.A5    Voelter, W6    Verdin, E7
  • 33
    • 0036383067 scopus 로고    scopus 로고
    • Chromatin remodeling, histone modifications, and DNA methylation—How does it all fit together?
    • T.M Geiman K.D Robertson Chromatin remodeling, histone modifications, and DNA methylation—How does it all fit together? J. Cell. Biochem. 87 2002 117 125
    • (2002) J. Cell. Biochem. , vol.87 , pp. 117-125
    • Geiman, T.M1    Robertson, K.D2
  • 34
    • 0037216704 scopus 로고    scopus 로고
    • Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins
    • Y.H Goo Y.C Sohn D.H Kim S.W Kim M.J Kang D.J Jung E Kwak N.A Barlev S.L Berger V.T Chow Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins Mol. Cell. Biol. 23 2003 140 149
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 140-149
    • Goo, Y.H1    Sohn, Y.C2    Kim, D.H3    Kim, S.W4    Kang, M.J5    Jung, D.J6    Kwak, E7    Barlev, N.A8    Berger, S.L9    Chow, V.T10
  • 35
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • C.K Glass M.G Rosenfeld The coregulator exchange in transcriptional functions of nuclear receptors Genes Dev. 14 2000 121 141
    • (2000) Genes Dev. , vol.14 , pp. 121-141
    • Glass, C.K1    Rosenfeld, M.G2
  • 36
    • 0034234237 scopus 로고    scopus 로고
    • CBP⧸p300 in cell growth, transformation, and development
    • R.H Goodman S Smolik CBP⧸p300 in cell growth, transformation, and development Genes Dev. 14 2000 1553 1577
    • (2000) Genes Dev. , vol.14 , pp. 1553-1577
    • Goodman, R.H1    Smolik, S2
  • 37
    • 0035724413 scopus 로고    scopus 로고
    • The SMRT and NCoR corepressors are activating cofactors for histone deacetylase 3
    • M.G Guenther O Barak M.A Lazar The SMRT and NCoR corepressors are activating cofactors for histone deacetylase 3 Mol. Cell. Biol. 21 2001 6091 6101
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6091-6101
    • Guenther, M.G1    Barak, O2    Lazar, M.A3
  • 38
    • 0034192756 scopus 로고    scopus 로고
    • A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness
    • M.G Guenther W.S Lane W Fischle E Verdin M.A Lazar R Shiekhattar A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness Genes Dev. 14 2000 1048 1057
    • (2000) Genes Dev. , vol.14 , pp. 1048-1057
    • Guenther, M.G1    Lane, W.S2    Fischle, W3    Verdin, E4    Lazar, M.A5    Shiekhattar, R6
  • 39
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions
    • J.C Hansen Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions Annu. Rev. Biophys. Biomol. Struct. 31 2002 361 392
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 361-392
    • Hansen, J.C1
  • 40
    • 0035937419 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes stabilize SWI⧸SNF binding to promoter nucleosomes
    • A.H Hassan K.E Neely J.L Workman Histone acetyltransferase complexes stabilize SWI⧸SNF binding to promoter nucleosomes Cell 104 2001 817 827
    • (2001) Cell , vol.104 , pp. 817-827
    • Hassan, A.H1    Neely, K.E2    Workman, J.L3
  • 41
    • 0038380293 scopus 로고    scopus 로고
    • Chromatin remodeling by nuclear receptors
    • P.B Hebbar T.K Archer Chromatin remodeling by nuclear receptors Chromosoma 111 2003 495 504
    • (2003) Chromosoma , vol.111 , pp. 495-504
    • Hebbar, P.B1    Archer, T.K2
  • 43
    • 0030847164 scopus 로고    scopus 로고
    • SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF–RARalpha oncoproteins associated with acute promyelocytic leukemia
    • S.H Hong G David C.W Wong A Dejean M.L Privalsky SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF–RARalpha oncoproteins associated with acute promyelocytic leukemia Proc. Natl. Acad. Sci. USA 94 1997 9028 9033
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9028-9033
    • Hong, S.H1    David, G2    Wong, C.W3    Dejean, A4    Privalsky, M.L5
  • 45
    • 0037072601 scopus 로고    scopus 로고
    • Molecular biology. Chromatin higher order folding—Wrapping up transcription
    • P.J Horn C.L Peterson Molecular biology. Chromatin higher order folding—Wrapping up transcription Science 297 2002 1824 1827
    • (2002) Science , vol.297 , pp. 1824-1827
    • Horn, P.J1    Peterson, C.L2
  • 46
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3-specific acetyltransferases are essential for cell cycle progression
    • L Howe D Auston P Grant S John R.G Cook J.L Workman L Pillus Histone H3-specific acetyltransferases are essential for cell cycle progression Genes Dev. 15 2001 3144 3154
    • (2001) Genes Dev. , vol.15 , pp. 3144-3154
    • Howe, L1    Auston, D2    Grant, P3    John, S4    Cook, R.G5    Workman, J.L6    Pillus, L7
  • 47
    • 0033523917 scopus 로고    scopus 로고
    • The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors
    • X Hu M.A Lazar The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors Nature 402 1999 93 96
    • (1999) Nature , vol.402 , pp. 93-96
    • Hu, X1    Lazar, M.A2
  • 48
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • E.Y Huang J Zhang E.A Miska M.G Guenther T Kouzarides M.A Lazar 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.Y1    Zhang, J2    Miska, E.A3    Guenther, M.G4    Kouzarides, T5    Lazar, M.A6
  • 49
    • 0038112654 scopus 로고    scopus 로고
    • The role of the androgen receptor in prostate cancer
    • H Huang D.J Tindall The role of the androgen receptor in prostate cancer Crit. Rev. Eukaryot. Gene Expr. 12 2002 193 207
    • (2002) Crit. Rev. Eukaryot. Gene Expr. , vol.12 , pp. 193-207
    • Huang, H1    Tindall, D.J2
  • 50
    • 0035318741 scopus 로고    scopus 로고
    • The TRAP⧸SMCC⧸Mediator complex and thyroid hormone receptor function
    • M Ito R.G Roeder The TRAP⧸SMCC⧸Mediator complex and thyroid hormone receptor function Trends Endocrinol. Metab. 12 2001 127 134
    • (2001) Trends Endocrinol. Metab. , vol.12 , pp. 127-134
    • Ito, M1    Roeder, R.G2
  • 51
    • 0242335773 scopus 로고    scopus 로고
    • Molecular action of the estrogen receptor and hormone dependency in breast cancer
    • H Iwase Molecular action of the estrogen receptor and hormone dependency in breast cancer Breast Cancer 10 2003 89 96
    • (2003) Breast Cancer , vol.10 , pp. 89-96
    • Iwase, H1
  • 52
    • 0030998328 scopus 로고    scopus 로고
    • The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7⧸SPA and the corepressors NCoR or SMRT
    • T.A Jackson J.K Richer D.L Bain G.S Takimoto L Tung K.B Horwitz The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7⧸SPA and the corepressors NCoR or SMRT Mol. Endocrinol. 11 1997 693 705
    • (1997) Mol. Endocrinol. , vol.11 , pp. 693-705
    • Jackson, T.A1    Richer, J.K2    Bain, D.L3    Takimoto, G.S4    Tung, L5    Horwitz, K.B6
  • 53
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAFII250 double bromodomain module
    • R.H Jacobson A.G Ladurner D.S King R Tjian Structure and function of a human TAFII250 double bromodomain module Science 288 2000 1422 1425
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H1    Ladurner, A.G2    King, D.S3    Tjian, R4
  • 54
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • T Jenuwein C.D Allis Translating the histone code Science 293 2001 1074 1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T1    Allis, C.D2
  • 55
    • 0033964661 scopus 로고    scopus 로고
    • Mammalian chromodomain proteins: Their role in genome organisation and expression
    • D.O Jones I.G Cowell P.B Singh Mammalian chromodomain proteins: Their role in genome organisation and expression Bioessays 22 2000 124 137
    • (2000) Bioessays , vol.22 , pp. 124-137
    • Jones, D.O1    Cowell, I.G2    Singh, P.B3
  • 57
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • H.Y Kao M Downes P Ordentlich R.M Evans 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.Y1    Downes, M2    Ordentlich, P3    Evans, R.M4
  • 59
    • 0032540755 scopus 로고    scopus 로고
    • How do histone acetyltransferases select lysine residues in core histones?
    • A Kimura M Horikoshi How do histone acetyltransferases select lysine residues in core histones? FEBS Lett. 431 1998 131 133
    • (1998) FEBS Lett. , vol.431 , pp. 131-133
    • Kimura, A1    Horikoshi, M2
  • 60
    • 0033568312 scopus 로고    scopus 로고
    • ATP-dependent remodeling and acetylation as regulators of chromatin fluidity
    • R.E Kingston G.J Narlikar ATP-dependent remodeling and acetylation as regulators of chromatin fluidity Genes Dev. 13 1999 2339 2352
    • (1999) Genes Dev. , vol.13 , pp. 2339-2352
    • Kingston, R.E1    Narlikar, G.J2
  • 61
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities
    • S.S Koh D Chen Y.H Lee M.R Stallcup Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities J. Biol. Chem. 276 2001 1089 1098
    • (2001) J. Biol. Chem. , vol.276 , pp. 1089-1098
    • Koh, S.S1    Chen, D2    Lee, Y.H3    Stallcup, M.R4
  • 63
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • T Kouzarides Histone methylation in transcriptional control Curr. Opin. Genet. Dev. 12 2002 198 209
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T1
  • 64
    • 0033499866 scopus 로고    scopus 로고
    • Biochemical analysis of distinct activation functions in p300 that enhance transcription initiation with chromatin templates
    • W.L Kraus E.T Manning J.T Kadonaga Biochemical analysis of distinct activation functions in p300 that enhance transcription initiation with chromatin templates Mol. Cell. Biol. 19 1999 8123 8135
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8123-8135
    • Kraus, W.L1    Manning, E.T2    Kadonaga, J.T3
  • 65
    • 0036094275 scopus 로고    scopus 로고
    • Nuclear receptor-dependent transcription with chromatin. Is it all about enzymes?
    • W.L Kraus J Wong Nuclear receptor-dependent transcription with chromatin. Is it all about enzymes? Eur. J. Biochem. 269 2002 2275 2283
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2275-2283
    • Kraus, W.L1    Wong, J2
  • 66
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • M.H Kuo C.D Allis Roles of histone acetyltransferases and deacetylases in gene regulation Bioessays 20 1998 615 626
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H1    Allis, C.D2
  • 67
    • 0031451570 scopus 로고    scopus 로고
    • Evolution of the nuclear receptor superfamily: Early diversification from an ancestral orphan receptor
    • V Laudet Evolution of the nuclear receptor superfamily: Early diversification from an ancestral orphan receptor J. Mol. Endocrinol. 19 1997 207 226
    • (1997) J. Mol. Endocrinol. , vol.19 , pp. 207-226
    • Laudet, V1
  • 68
    • 0031741654 scopus 로고    scopus 로고
    • Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2
    • C.H Lee C Chinpaisal L.N Wei Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2 Mol. Cell. Biol. 18 1998 6745 6755
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6745-6755
    • Lee, C.H1    Chinpaisal, C2    Wei, L.N3
  • 69
    • 0032473501 scopus 로고    scopus 로고
    • Prolonged glucocorticoid exposure dephosphorylates histone H1 and inactivates the MMTV promoter
    • H.L Lee T.K Archer Prolonged glucocorticoid exposure dephosphorylates histone H1 and inactivates the MMTV promoter EMBO J. 17 1998 1454 1466
    • (1998) EMBO J. , vol.17 , pp. 1454-1466
    • Lee, H.L1    Archer, T.K2
  • 70
    • 0036093624 scopus 로고    scopus 로고
    • Synergy among nuclear receptor coactivators: Selective requirement for protein methyltransferase and acetyltransferase activities
    • Y.H Lee S.S Koh X Zhang X Cheng M.R Stallcup Synergy among nuclear receptor coactivators: Selective requirement for protein methyltransferase and acetyltransferase activities Mol. Cell. Biol. 22 2002 3621 3632
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3621-3632
    • Lee, Y.H1    Koh, S.S2    Zhang, X3    Cheng, X4    Stallcup, M.R5
  • 71
    • 0036311564 scopus 로고    scopus 로고
    • Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor
    • J Li Q Lin H.G Yoon Z.Q Huang B.D Strahl C.D Allis J Wong Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor Mol. Cell. Biol. 22 2002 5688 5697
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5688-5697
    • Li, J1    Lin, Q2    Yoon, H.G3    Huang, Z.Q4    Strahl, B.D5    Allis, C.D6    Wong, J7
  • 72
    • 0034663815 scopus 로고    scopus 로고
    • Both corepressor proteins SMRT and NCoR exist in large protein complexes containing HDAC3
    • J Li J Wang Z Nawaz J.M Liu J Qin J Wong Both corepressor proteins SMRT and NCoR exist in large protein complexes containing HDAC3 EMBO J. 19 2000 4342 4350
    • (2000) EMBO J. , vol.19 , pp. 4342-4350
    • Li, J1    Wang, J2    Nawaz, Z3    Liu, J.M4    Qin, J5    Wong, J6
  • 74
    • 0037559902 scopus 로고    scopus 로고
    • Split ends is a tissue⧸promoter specific regulator of Wingless signaling
    • H.V Lin D.B Doroquez S Cho F Chen I Rebay K.M Cadigan Split ends is a tissue⧸promoter specific regulator of Wingless signaling Development 130 2003 3125 3135
    • (2003) Development , vol.130 , pp. 3125-3135
    • Lin, H.V1    Doroquez, D.B2    Cho, S3    Chen, F4    Rebay, I5    Cadigan, K.M6
  • 75
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukemia
    • R.J Lin L Nagy S Inoue W Shao W.H Miller Jr. R.M Evans Role of the histone deacetylase complex in acute promyelocytic leukemia Nature 391 1998 811 814
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J1    Nagy, L2    Inoue, S3    Shao, W4    Miller, W.H5    Evans, R.M6
  • 76
    • 0035969097 scopus 로고    scopus 로고
    • Transcriptional regulation in acute promyelocytic leukemia
    • R.J Lin T Sternsdorf M Tini R.M Evans Transcriptional regulation in acute promyelocytic leukemia Oncogene 20 2001 7204 7215
    • (2001) Oncogene , vol.20 , pp. 7204-7215
    • Lin, R.J1    Sternsdorf, T2    Tini, M3    Evans, R.M4
  • 77
    • 0035940497 scopus 로고    scopus 로고
    • Sequential recruitment of steroid receptor coactivator-1 (SRC-1) and p300 enhances progesterone receptor-dependent initiation and reinitiation of transcription from chromatin
    • Z Liu J Wong S.Y Tsai M.J Tsai B.W O'Malley Sequential recruitment of steroid receptor coactivator-1 (SRC-1) and p300 enhances progesterone receptor-dependent initiation and reinitiation of transcription from chromatin Proc. Natl. Acad. Sci. USA 98 2001 12426 12431
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12426-12431
    • Liu, Z1    Wong, J2    Tsai, S.Y3    Tsai, M.J4    O'Malley, B.W5
  • 78
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • W.S Lo R.C Trievel J.R Rojas L Duggan J.Y Hsu C.D Allis R Marmorstein S.L Berger Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14 Mol. Cell 5 2000 917 926
    • (2000) Mol. Cell , vol.5 , pp. 917-926
    • Lo, W.S1    Trievel, R.C2    Rojas, J.R3    Duggan, L4    Hsu, J.Y5    Allis, C.D6    Marmorstein, R7    Berger, S.L8
  • 79
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8Å resolution
    • K Luger A.W Mader R.K Richmond D.F Sargent T.J Richmond Crystal structure of the nucleosome core particle at 2.8Å resolution Nature 389 1997 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K1    Mader, A.W2    Richmond, R.K3    Sargent, D.F4    Richmond, T.J5
  • 81
    • 0025872683 scopus 로고
    • Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors
    • L.C Mahadevan A.C Willis M.J Barratt Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors Cell 65 1991 775 783
    • (1991) Cell , vol.65 , pp. 775-783
    • Mahadevan, L.C1    Willis, A.C2    Barratt, M.J3
  • 82
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • D.J Mangelsdorf R.M Evans The RXR heterodimers and orphan receptors Cell 83 1995 841 850
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J1    Evans, R.M2
  • 83
    • 0035012326 scopus 로고    scopus 로고
    • p300 forms a stable, template-committed complex with chromatin: Role for the bromodomain
    • E.T Manning T Ikehara T Ito J.T Kadonaga W.L Kraus p300 forms a stable, template-committed complex with chromatin: Role for the bromodomain Mol. Cell. Biol. 21 2001 3876 3887
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3876-3887
    • Manning, E.T1    Ikehara, T2    Ito, T3    Kadonaga, J.T4    Kraus, W.L5
  • 84
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Cellular and molecular biology
    • N.J McKenna R.B Lanz B.W O'Malley Nuclear receptor coregulators: Cellular and molecular biology Endocr. Rev. 20 1999 321 344
    • (1999) Endocr. Rev. , vol.20 , pp. 321-344
    • McKenna, N.J1    Lanz, R.B2    O'Malley, B.W3
  • 85
    • 0033997967 scopus 로고    scopus 로고
    • The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein
    • A.M Melnick J.J Westendorf A Polinger G.W Carlile S Arai H.J Ball B Lutterbach S.W Hiebert J.D Licht The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein Mol. Cell. Biol. 20 2000 2075 2086
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2075-2086
    • Melnick, A.M1    Westendorf, J.J2    Polinger, A3    Carlile, G.W4    Arai, S5    Ball, H.J6    Lutterbach, B7    Hiebert, S.W8    Licht, J.D9
  • 87
    • 0035831040 scopus 로고    scopus 로고
    • Arginine methylation of STAT1 modulates IFNalpha⧸beta-induced transcription
    • K.A Mowen J Tang W Zhu B.T Schurter K Shuai H.R Herschman M David Arginine methylation of STAT1 modulates IFNalpha⧸beta-induced transcription Cell 104 2001 731 741
    • (2001) Cell , vol.104 , pp. 731-741
    • Mowen, K.A1    Tang, J2    Zhu, W3    Schurter, B.T4    Shuai, K5    Herschman, H.R6    David, M7
  • 88
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • L Nagy H.Y Kao D Chakravarti R.J Lin C.A Hassig D.E Ayer S.L Schreiber R.M Evans Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase Cell 89 1997 373 380
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L1    Kao, H.Y2    Chakravarti, D3    Lin, R.J4    Hassig, C.A5    Ayer, D.E6    Schreiber, S.L7    Evans, R.M8
  • 89
    • 0035803483 scopus 로고    scopus 로고
    • Functional interaction of STAT5 and nuclear receptor corepressor SMRT: Implications in negative regulation of STAT5-dependent transcription
    • H Nakajima P.K Brindle M Handa J.N Ihle Functional interaction of STAT5 and nuclear receptor corepressor SMRT: Implications in negative regulation of STAT5-dependent transcription EMBO J. 20 2001 6836 6844
    • (2001) EMBO J. , vol.20 , pp. 6836-6844
    • Nakajima, H1    Brindle, P.K2    Handa, M3    Ihle, J.N4
  • 90
    • 0037083757 scopus 로고    scopus 로고
    • SET9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • K Nishioka S Chuikov K Sarma H Erdjument-Bromage C.D Allis P Tempst D Reinberg SET9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation Genes Dev. 16 2002 479 489
    • (2002) Genes Dev. , vol.16 , pp. 479-489
    • Nishioka, K1    Chuikov, S2    Sarma, K3    Erdjument-Bromage, H4    Allis, C.D5    Tempst, P6    Reinberg, D7
  • 91
    • 0033557497 scopus 로고    scopus 로고
    • Ski is a component of the histone deacetylase complex required for transcriptional repression by Mad and thyroid hormone receptor
    • T Nomura M.M Khan S.C Kaul H.D Dong R Wadhwa C Colmenares I Kohno S Ishii Ski is a component of the histone deacetylase complex required for transcriptional repression by Mad and thyroid hormone receptor Genes Dev. 13 1999 412 423
    • (1999) Genes Dev. , vol.13 , pp. 412-423
    • Nomura, T1    Khan, M.M2    Kaul, S.C3    Dong, H.D4    Wadhwa, R5    Colmenares, C6    Kohno, I7    Ishii, S8
  • 92
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • V.V Ogryzko R.L Schiltz V Russanova B.H Howard Y Nakatani The transcriptional coactivators p300 and CBP are histone acetyltransferases Cell 87 1996 953 959
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V1    Schiltz, R.L2    Russanova, V3    Howard, B.H4    Nakatani, Y5
  • 94
    • 0034026193 scopus 로고    scopus 로고
    • Promoter targeting and chromatin remodeling by the SWI⧸SNF complex
    • C.L Peterson J.L Workman Promoter targeting and chromatin remodeling by the SWI⧸SNF complex Curr. Opin. Genet. Dev. 10 2000 187 192
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 187-192
    • Peterson, C.L1    Workman, J.L2
  • 95
    • 0034669165 scopus 로고    scopus 로고
    • Chromosomal localization links the SIN3–RPD3 complex to the regulation of chromatin condensation, histone acetylation, and gene expression
    • L.A Pile D.A Wassarman Chromosomal localization links the SIN3–RPD3 complex to the regulation of chromatin condensation, histone acetylation, and gene expression EMBO J. 19 2000 6131 6140
    • (2000) EMBO J. , vol.19 , pp. 6131-6140
    • Pile, L.A1    Wassarman, D.A2
  • 96
    • 0031416394 scopus 로고    scopus 로고
    • Histone H1 and chromatin higher-order structure
    • V Ramakrishnan Histone H1 and chromatin higher-order structure Crit. Rev. Eukaryot. Gene Expr. 7 1997 215 230
    • (1997) Crit. Rev. Eukaryot. Gene Expr. , vol.7 , pp. 215-230
    • Ramakrishnan, V1
  • 98
    • 0035265922 scopus 로고    scopus 로고
    • A transient histone hyperacetylation signal marks nucleosomes for remodeling at the PHO8 promoter in vivo
    • H Reinke P.D Gregory W Horz A transient histone hyperacetylation signal marks nucleosomes for remodeling at the PHO8 promoter in vivo Mol. Cell 7 2001 529 538
    • (2001) Mol. Cell , vol.7 , pp. 529-538
    • Reinke, H1    Gregory, P.D2    Horz, W3
  • 101
    • 0029657787 scopus 로고    scopus 로고
    • Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors
    • S Sande M.L Privalsky Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors Mol. Endocrinol. 10 1996 813 825
    • (1996) Mol. Endocrinol. , vol.10 , pp. 813-825
    • Sande, S1    Privalsky, M.L2
  • 104
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Y Shang X Hu J DiRenzo M.A Lazar M Brown Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription Cell 103 2000 843 852
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y1    Hu, X2    DiRenzo, J3    Lazar, M.A4    Brown, M5
  • 105
    • 0037062460 scopus 로고    scopus 로고
    • Ordered recruitment of histone acetyltransferases and the TRAP⧸Mediator complex to thyroid hormone-responsive promoters in vivo
    • D Sharma J.D Fondell 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 7939
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7934-7939
    • Sharma, D1    Fondell, J.D2
  • 106
    • 0035339146 scopus 로고    scopus 로고
    • Sharp, an inducible cofactor that integrates nuclear receptor repression and activation
    • Y Shi M Downes W Xie H.Y Kao P Ordentlich C.C Tsai M Hon R.M Evans Sharp, an inducible cofactor that integrates nuclear receptor repression and activation Genes Dev. 15 2001 1140 1151
    • (2001) Genes Dev. , vol.15 , pp. 1140-1151
    • Shi, Y1    Downes, M2    Xie, W3    Kao, H.Y4    Ordentlich, P5    Tsai, C.C6    Hon, M7    Evans, R.M8
  • 107
    • 0033053181 scopus 로고    scopus 로고
    • The nuclear receptor superfamily has undergone extensive proliferation and diversification in nematodes
    • A.E Sluder S.W Mathews D Hough V.P Yin C.V Maina The nuclear receptor superfamily has undergone extensive proliferation and diversification in nematodes Genome Res. 9 1999 103 120
    • (1999) Genome Res. , vol.9 , pp. 103-120
    • Sluder, A.E1    Mathews, S.W2    Hough, D3    Yin, V.P4    Maina, C.V5
  • 109
    • 0035962649 scopus 로고    scopus 로고
    • Role of protein methylation in chromatin remodeling and transcriptional regulation
    • M.R Stallcup Role of protein methylation in chromatin remodeling and transcriptional regulation Oncogene 20 2001 3014 3020
    • (2001) Oncogene , vol.20 , pp. 3014-3020
    • Stallcup, M.R1
  • 110
    • 0043178993 scopus 로고    scopus 로고
    • A mutant form of MeCP2 protein associated with human Rett syndrome cannot be displaced from methylated DNA by notch in Xenopus embryos
    • I Stancheva A.L Collins I.B van den Veyver H Zoghbi R.R Meehan A mutant form of MeCP2 protein associated with human Rett syndrome cannot be displaced from methylated DNA by notch in Xenopus embryos Mol. Cell 12 2003 425 435
    • (2003) Mol. Cell , vol.12 , pp. 425-435
    • Stancheva, I1    Collins, A.L2    van den Veyver, I.B3    Zoghbi, H4    Meehan, R.R5
  • 111
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • D.E Sterner S.L Berger Acetylation of histones and transcription-related factors Microbiol. Mol. Biol. Rev. 64 2000 435 459
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E1    Berger, S.L2
  • 112
    • 0033592999 scopus 로고    scopus 로고
    • Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena
    • B.D Strahl R Ohba R.G Cook C.D Allis Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena Proc. Natl. Acad. Sci. USA 96 1999 14967 14972
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14967-14972
    • Strahl, B.D1    Ohba, R2    Cook, R.G3    Allis, C.D4
  • 113
    • 0037195877 scopus 로고    scopus 로고
    • Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function
    • C Teyssier D Chen M.R Stallcup Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function J. Biol. Chem. 277 2002 46066 46072
    • (2002) J. Biol. Chem. , vol.277 , pp. 46066-46072
    • Teyssier, C1    Chen, D2    Stallcup, M.R3
  • 114
    • 0033151772 scopus 로고    scopus 로고
    • Histone H1: Location and role
    • J.O Thomas Histone H1: Location and role Curr. Opin. Cell. Biol. 11 1999 312 317
    • (1999) Curr. Opin. Cell. Biol. , vol.11 , pp. 312-317
    • Thomas, J.O1
  • 115
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3⧸HMG-14 kinase
    • S Thomson A.L Clayton C.A Hazzalin S Rose M.J Barratt L.C Mahadevan The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3⧸HMG-14 kinase EMBO J. 18 1999 4779 4793
    • (1999) EMBO J. , vol.18 , pp. 4779-4793
    • Thomson, S1    Clayton, A.L2    Hazzalin, C.A3    Rose, S4    Barratt, M.J5    Mahadevan, L.C6
  • 117
    • 0029588203 scopus 로고
    • From embryogenesis to metamorphosis: The regulation and function of Drosophila nuclear receptor superfamily members
    • C.S Thummel From embryogenesis to metamorphosis: The regulation and function of Drosophila nuclear receptor superfamily members Cell 83 1995 871 877
    • (1995) Cell , vol.83 , pp. 871-877
    • Thummel, C.S1
  • 120
    • 0033180592 scopus 로고    scopus 로고
    • SMRTER, a Drosophila nuclear receptor coregulator, reveals that EcR-mediated repression is critical for development
    • C.C Tsai H.Y Kao T.P Yao M McKeown R.M Evans SMRTER, a Drosophila nuclear receptor coregulator, reveals that EcR-mediated repression is critical for development Mol. Cell 4 1999 175 186
    • (1999) Mol. Cell , vol.4 , pp. 175-186
    • Tsai, C.C1    Kao, H.Y2    Yao, T.P3    McKeown, M4    Evans, R.M5
  • 121
    • 0029349023 scopus 로고
    • Histone acetylation in chromatin and chromosomes
    • B.M Turner L.P O'Neill Histone acetylation in chromatin and chromosomes Semin. Cell. Biol. 6 1995 229 236
    • (1995) Semin. Cell. Biol. , vol.6 , pp. 229-236
    • Turner, B.M1    O'Neill, L.P2
  • 122
    • 0035134963 scopus 로고    scopus 로고
    • A necessary good: Nuclear hormone receptors and their chromatin templates
    • F.D Urnov A.P Wolffe 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.D1    Wolffe, A.P2
  • 123
    • 0035724042 scopus 로고    scopus 로고
    • Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP
    • N Vo C Fjeld R.H Goodman Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP Mol. Cell. Biol. 21 2001 6181 6188
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6181-6188
    • Vo, N1    Fjeld, C2    Goodman, R.H3
  • 124
    • 0032518944 scopus 로고    scopus 로고
    • The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways
    • J.J Voegel M.J Heine M Tini V Vivat P Chambon H Gronemeyer The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways EMBO J. 17 1998 507 519
    • (1998) EMBO J. , vol.17 , pp. 507-519
    • Voegel, J.J1    Heine, M.J2    Tini, M3    Vivat, V4    Chambon, P5    Gronemeyer, H6
  • 126
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3 lysine 4-specific methyltransferase
    • H Wang R Cao L Xia H Erdjument-Bromage C Borchers P Tempst Y Zhang Purification and functional characterization of a histone H3 lysine 4-specific methyltransferase Mol. Cell. 8 2001 1207 1217
    • (2001) Mol. Cell. , vol.8 , pp. 1207-1217
    • Wang, H1    Cao, R2    Xia, L3    Erdjument-Bromage, H4    Borchers, C5    Tempst, P6    Zhang, Y7
  • 128
    • 0035844255 scopus 로고    scopus 로고
    • Ligand-dependent formation of retinoid receptors, receptor-interacting protein 140 (RIP140), and histone deacetylase complex is mediated by a novel receptor-interacting motif of RIP140
    • L.N Wei M Farooqui X Hu Ligand-dependent formation of retinoid receptors, receptor-interacting protein 140 (RIP140), and histone deacetylase complex is mediated by a novel receptor-interacting motif of RIP140 J. Biol. Chem. 276 2001 16107 16112
    • (2001) J. Biol. Chem. , vol.276 , pp. 16107-16112
    • Wei, L.N1    Farooqui, M2    Hu, X3
  • 129
    • 0034731401 scopus 로고    scopus 로고
    • Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing
    • L.N Wei X Hu D Chandra E Seto M Farooqui Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing J. Biol. Chem. 275 2000 40782 40787
    • (2000) J. Biol. Chem. , vol.275 , pp. 40782-40787
    • Wei, L.N1    Hu, X2    Chandra, D3    Seto, E4    Farooqui, M5
  • 130
    • 0031104747 scopus 로고    scopus 로고
    • What do linker histones do in chromatin?
    • A.P Wolffe S Khochbin S Dimitrov What do linker histones do in chromatin? Bioessays 19 1997 249 255
    • (1997) Bioessays , vol.19 , pp. 249-255
    • Wolffe, A.P1    Khochbin, S2    Dimitrov, S3
  • 131
    • 0037828418 scopus 로고    scopus 로고
    • Thyroid hormone action: Insight from transgenic mouse models
    • F.E Wondisford Thyroid hormone action: Insight from transgenic mouse models J. Investig. Med. 51 2003 215 220
    • (2003) J. Investig. Med. , vol.51 , pp. 215-220
    • Wondisford, F.E1
  • 132
    • 0042334873 scopus 로고    scopus 로고
    • Review of the in vivo functions of the p160 steroid receptor coactivator family
    • J Xu Q Li Review of the in vivo functions of the p160 steroid receptor coactivator family Mol. Endocrinol. 17 2003 1681 1692
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1681-1692
    • Xu, J1    Li, Q2
  • 134
    • 0029665857 scopus 로고    scopus 로고
    • A p300⧸CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • X.J Yang V.V Ogryzko J Nishikawa B.H Howard Y Nakatani A p300⧸CBP-associated factor that competes with the adenoviral oncoprotein E1A Nature 382 1996 319 324
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J1    Ogryzko, V.V2    Nishikawa, J3    Howard, B.H4    Nakatani, Y5
  • 135
    • 0141638426 scopus 로고    scopus 로고
    • NCoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso
    • H.G Yoon D.W Chan A.B Reynolds J Qin J Wong NCoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso Mol. Cell. 12 2003 723 734
    • (2003) Mol. Cell. , vol.12 , pp. 723-734
    • Yoon, H.G1    Chan, D.W2    Reynolds, A.B3    Qin, J4    Wong, J5
  • 136
    • 0037925529 scopus 로고    scopus 로고
    • A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation
    • J Yu Y Li T Ishizuka M.G Guenther M.A Lazar A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation EMBO J. 22 2003 3403 3410
    • (2003) EMBO J. , vol.22 , pp. 3403-3410
    • Yu, J1    Li, Y2    Ishizuka, T3    Guenther, M.G4    Lazar, M.A5
  • 137
    • 0035969115 scopus 로고    scopus 로고
    • Translocations of the RARalpha gene in acute promyelocytic leukemia
    • A Zelent F Guidez A Melnick S Waxman J.D Licht Translocations of the RARalpha gene in acute promyelocytic leukemia Oncogene 20 2001 7186 7203
    • (2001) Oncogene , vol.20 , pp. 7186-7203
    • Zelent, A1    Guidez, F2    Melnick, A3    Waxman, S4    Licht, J.D5
  • 138
    • 0036211850 scopus 로고    scopus 로고
    • The NCoR–HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2
    • J Zhang M Kalkum B.T Chait R.G Roeder The NCoR–HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2 Mol. Cell 9 2002 611 623
    • (2002) Mol. Cell , vol.9 , pp. 611-623
    • Zhang, J1    Kalkum, M2    Chait, B.T3    Roeder, R.G4
  • 139
    • 0032230289 scopus 로고    scopus 로고
    • A nuclear receptor corepressor modulates transcriptional activity of antagonist-occupied steroid hormone receptor
    • X Zhang M Jeyakumar S Petukhov M.K Bagchi A nuclear receptor corepressor modulates transcriptional activity of antagonist-occupied steroid hormone receptor Mol. Endocrinol. 12 1998 513 524
    • (1998) Mol. Endocrinol. , vol.12 , pp. 513-524
    • Zhang, X1    Jeyakumar, M2    Petukhov, S3    Bagchi, M.K4
  • 140
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • X Zhang L Zhou X Cheng Crystal structure of the conserved core of protein arginine methyltransferase PRMT3 EMBO J. 19 2000 3509 3519
    • (2000) EMBO J. , vol.19 , pp. 3509-3519
    • Zhang, X1    Zhou, L2    Cheng, X3


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