메뉴 건너뛰기




Volumn 5, Issue 3, 2006, Pages 209-221

Histone acetylation in gene regulation

Author keywords

Acetylation; Cancer; Deacetylation; Gene expression; Nucleosomes

Indexed keywords

HISTONE; LYSINE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE;

EID: 33845198169     PISSN: 14739550     EISSN: 14774062     Source Type: Journal    
DOI: 10.1093/bfgp/ell028     Document Type: Review
Times cited : (194)

References (161)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K, Mader AW, Richmond RK, et al. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997;389:251-60.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3
  • 2
    • 0033850576 scopus 로고    scopus 로고
    • The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: Distribution in human fetal fibroblasts
    • Parseghian MH, Newcomb RL, Winokur ST, et al. The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: distribution in human fetal fibroblasts. Chromosome Res 2000;8:405-24.
    • (2000) Chromosome Res , vol.8 , pp. 405-424
    • Parseghian, M.H.1    Newcomb, R.L.2    Winokur, S.T.3
  • 3
    • 0034681115 scopus 로고    scopus 로고
    • Heterochromatic deposition of centromeric histone H3-like proteins
    • Henikoff S, Ahmad K, Platero JS, et al. Heterochromatic deposition of centromeric histone H3-like proteins. Proc Natl Acad Sci USA 2000;97:716-21.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 716-721
    • Henikoff, S.1    Ahmad, K.2    Platero, J.S.3
  • 4
    • 0032483564 scopus 로고    scopus 로고
    • Cse4p is a component of the core centromere of Saccharomyces cerevisiae
    • Meluh PB, Yang P, Glowczewski L, et al. Cse4p is a component of the core centromere of Saccharomyces cerevisiae. Cell 1998;94:607-13.
    • (1998) Cell , vol.94 , pp. 607-613
    • Meluh, P.B.1    Yang, P.2    Glowczewski, L.3
  • 5
    • 0033578004 scopus 로고    scopus 로고
    • Regions of variant histone His2AvD required for Drosophila development
    • Clarkson MJ, Wells JR, Gibson F, et al. Regions of variant histone His2AvD required for Drosophila development. Nature 1999;399:694-7.
    • (1999) Nature , vol.399 , pp. 694-697
    • Clarkson, M.J.1    Wells, J.R.2    Gibson, F.3
  • 6
    • 0034725587 scopus 로고    scopus 로고
    • Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster
    • Leach TJ, Mazzeo M, Chotkowski HL, et al. Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster. J Biol Chem 2000;275:23267-72.
    • (2000) J Biol Chem , vol.275 , pp. 23267-23272
    • Leach, T.J.1    Mazzeo, M.2    Chotkowski, H.L.3
  • 7
    • 0036532119 scopus 로고    scopus 로고
    • Breaking through to the other side: Silencers and barriers
    • Dhillon N, Kamakaka RT. Breaking through to the other side: Silencers and barriers. Curr Opin Genet Dev 2002;12: 188-92.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 188-192
    • Dhillon, N.1    Kamakaka, R.T.2
  • 8
    • 0035725036 scopus 로고    scopus 로고
    • H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions
    • Adam M, Robert F, Larochelle M, et al. H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions. Mol Cell Biol 2001; 21:6270-9.
    • (2001) Mol Cell Biol , vol.21 , pp. 6270-6279
    • Adam, M.1    Robert, F.2    Larochelle, M.3
  • 9
    • 30644459489 scopus 로고    scopus 로고
    • H2A.Z functions to regulate progression through the cell cycle
    • Dhillon N, Oki M, Szyjka SJ, et al. H2A.Z functions to regulate progression through the cell cycle. Mol Cell Biol 2006;26:489-501.
    • (2006) Mol Cell Biol , vol.26 , pp. 489-501
    • Dhillon, N.1    Oki, M.2    Szyjka, S.J.3
  • 10
    • 29144531244 scopus 로고    scopus 로고
    • Variant histone H2A.Z is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning
    • Guillemette B, Bataille AR, Gevry N, et al. Variant histone H2A.Z is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning. PLoS Biol 2005;3:2100-10.
    • (2005) PLoS Biol , vol.3 , pp. 2100-2110
    • Guillemette, B.1    Bataille, A.R.2    Gevry, N.3
  • 11
    • 26844489856 scopus 로고    scopus 로고
    • Genome-wide dynamics of HTZ1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss
    • Zhang H, Roberts DN, Cairns BR. Genome-wide dynamics of HTZ1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss. Cell 2005;123:219-231.
    • (2005) Cell , vol.123 , pp. 219-231
    • Zhang, H.1    Roberts, D.N.2    Cairns, B.R.3
  • 12
    • 26844511498 scopus 로고    scopus 로고
    • Histone variant H2A.Z marks the 5′ ends of both active and inactive genes in euchromatin
    • Raisner RM, Hartley PD, Meneghini MD, et al. Histone variant H2A.Z marks the 5′ ends of both active and inactive genes in euchromatin. Cell 2005;123:233-48.
    • (2005) Cell , vol.123 , pp. 233-248
    • Raisner, R.M.1    Hartley, P.D.2    Meneghini, M.D.3
  • 13
    • 29444454191 scopus 로고    scopus 로고
    • Preferential occupancy of histone variant H2A.Z at inactive promoters influences local histone modifications and chromatin remodeling
    • Li B, Pattenden SG, Lee D, et al. Preferential occupancy of histone variant H2A.Z at inactive promoters influences local histone modifications and chromatin remodeling. Proc Natl Acad Sci USA 2005;102:18385-90.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18385-18390
    • Li, B.1    Pattenden, S.G.2    Lee, D.3
  • 14
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000;403:41-5.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 15
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger SL. Histone modifications in transcriptional regulation. Curr Opin Genet Dev 2002;12:142-8.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 16
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner BM. Cellular memory and the histone code. Cell 2002;111:285-91.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 17
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle W, Wang Y, Allis CD. Binary switches and modification cassettes in histone biology and beyond. Nature 2003;425:475-9.
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 18
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell JE, Zhou J, Ranalli T, et al. Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 1996;84: 843-51.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3
  • 19
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of rna synthesis
    • Allfrey Vg, Faulkner R, Mirsky Ae. Acetylation and methylation of histones and their possible role in the regulation of rna synthesis. Proc Natl Acad Sci USA 1964;51: 786-94.
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, Vg.1    Faulkner, R.2    Mirsky, Ae.3
  • 20
    • 0035377556 scopus 로고    scopus 로고
    • Protein modules that manipulate histone tails for chromatin regulation
    • Marmorstein R. Protein modules that manipulate histone tails for chromatin regulation. Nat Rev Mol Cell Biol 2001;2: 422-32.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 422-432
    • Marmorstein, R.1
  • 21
  • 22
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg RD, Lorch Y. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell 1999;98:285-94.
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 23
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and bromodomain: A new partnership for signaling
    • Yang XJ. Lysine acetylation and bromodomain: A new partnership for signaling. Bioessays 2004;26:1076-87.
    • (2004) Bioessays , vol.26 , pp. 1076-1087
    • Yang, X.J.1
  • 24
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin C, Carlson JE, Zeng L, et al. Structure and ligand of a histone acetyltransferase bromodomain. Nature 1999; 399:491-6.
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3
  • 25
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • Hassan AH, Prochasson P, Neely KE, et al. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell 2002;111:369-79.
    • (2002) Cell , vol.111 , pp. 369-379
    • Hassan, A.H.1    Prochasson, P.2    Neely, K.E.3
  • 26
    • 10744233648 scopus 로고    scopus 로고
    • Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation
    • Mujtaba S, He Y, Zeng L, et al. Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. Mol Cell 2004;13:251-63.
    • (2004) Mol Cell , vol.13 , pp. 251-263
    • Mujtaba, S.1    He, Y.2    Zeng, L.3
  • 27
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAFII250 double bromodomain module
    • Jacobson RH, Ladurner AG, King DS, et al. Structure and function of a human TAFII250 double bromodomain module. Science 2000;288:1422-5.
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H.1    Ladurner, A.G.2    King, D.S.3
  • 28
    • 0034707037 scopus 로고    scopus 로고
    • Global histone acetylation and deacetylation in yeast
    • Vogelauer M, Wu J, Suka N, et al. Global histone acetylation and deacetylation in yeast. Nature 2000;408: 495-8.
    • (2000) Nature , vol.408 , pp. 495-498
    • Vogelauer, M.1    Wu, J.2    Suka, N.3
  • 29
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global histone acetylation patterns to gene expression
    • Kurdistani SK, Tavazoie S, Grunstein M. Mapping global histone acetylation patterns to gene expression. Cell 2004; 117:721-33.
    • (2004) Cell , vol.117 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 30
    • 17244368913 scopus 로고    scopus 로고
    • Genomic characterization reveals a simple histone H4 acetylation code
    • Dion MF, Altschuler SJ, Wu LF, et al. Genomic characterization reveals a simple histone H4 acetylation code. Proc Natl Acad Sci USA 2005;102:5501-6.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5501-5506
    • Dion, M.F.1    Altschuler, S.J.2    Wu, L.F.3
  • 31
    • 23944462969 scopus 로고    scopus 로고
    • Genome-wide map of nucleosome acetylation and methylation in yeast
    • Pokholok DK, Harbison CT, Levine S, et al. Genome-wide map of nucleosome acetylation and methylation in yeast. Cell 2005;122:517-27.
    • (2005) Cell , vol.122 , pp. 517-527
    • Pokholok, D.K.1    Harbison, C.T.2    Levine, S.3
  • 32
    • 23944443814 scopus 로고    scopus 로고
    • A new map for navigating the yeast epigenome
    • Schubeler D, Turner BM. A new map for navigating the yeast epigenome. Cell 2005;122:489-92.
    • (2005) Cell , vol.122 , pp. 489-492
    • Schubeler, D.1    Turner, B.M.2
  • 34
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson CL, Laniel MA. Histones and histone modifications. Curr Biol 2004;14:546-51.
    • (2004) Curr Biol , vol.14 , pp. 546-551
    • Peterson, C.L.1    Laniel, M.A.2
  • 35
    • 0030030611 scopus 로고    scopus 로고
    • Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5
    • Candau R, Moore PA, Wang L, et al. Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5. Mol Cell Biol 1996;16: 593-602.
    • (1996) Mol Cell Biol , vol.16 , pp. 593-602
    • Candau, R.1    Moore, P.A.2    Wang, L.3
  • 36
    • 0031678679 scopus 로고    scopus 로고
    • Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates
    • Xu W, Edmondson DG, Roth SY. Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates. Mol Cell Biol 1998;18:5659-69.
    • (1998) Mol Cell Biol , vol.18 , pp. 5659-5669
    • Xu, W.1    Edmondson, D.G.2    Roth, S.Y.3
  • 37
    • 0026783834 scopus 로고
    • Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription
    • Georgakopoulos T, Thireos G. Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J 1992;11:4145-52.
    • (1992) EMBO J , vol.11 , pp. 4145-4152
    • Georgakopoulos, T.1    Thireos, G.2
  • 38
    • 0028885077 scopus 로고
    • Identification of a gene encoding a yeast histone H4 acetyltransferase
    • Kleff S, Andrulis ED, Anderson CW, et al. Identification of a gene encoding a yeast histone H4 acetyltransferase. J Biol Chem 1995;270:24674-7.
    • (1995) J Biol Chem , vol.270 , pp. 24674-24677
    • Kleff, S.1    Andrulis, E.D.2    Anderson, C.W.3
  • 39
    • 0032526622 scopus 로고    scopus 로고
    • Cloning of Drosophila GCN5: Conserved futures among metazoan GCN5 funily members
    • Smith ER, Belote JM, Schiltz RL, et al. Cloning of Drosophila GCN5: conserved futures among metazoan GCN5 funily members. Nucleic Acids Res 1998; 26:2948-54.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2948-2954
    • Smith, E.R.1    Belote, J.M.2    Schiltz, R.L.3
  • 40
    • 0033571221 scopus 로고    scopus 로고
    • Cloning and analysis of a Toxoplasma gondii histone acetyltransferase: A novel chromatin remodelling factor in apicomplexan parasites
    • Hettmann C, Soldati D. Cloning and analysis of a Toxoplasma gondii histone acetyltransferase: A novel chromatin remodelling factor in apicomplexan parasites. Nucleic Acids Res 1999;27:4344-52.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4344-4352
    • Hettmann, C.1    Soldati, D.2
  • 41
    • 0031310741 scopus 로고    scopus 로고
    • Differential roles of p300 and PCAF acetylatransferases in muscle differentiation
    • Puri PL, Sartorelli V, Yang XJ, et al. Differential roles of p300 and PCAF acetylatransferases in muscle differentiation. Mol Cell 1997;1:35-45.
    • (1997) Mol Cell , vol.1 , pp. 35-45
    • Puri, P.L.1    Sartorelli, V.2    Yang, X.J.3
  • 42
    • 2642662483 scopus 로고    scopus 로고
    • The histone acetylase PCAF is a nuclear receptor coactivator
    • Blanco JC, Minucci S, Lu J, et al. The histone acetylase PCAF is a nuclear receptor coactivator. Genes Dev 1998;12: 1638-51.
    • (1998) Genes Dev , vol.12 , pp. 1638-1651
    • Blanco, J.C.1    Minucci, S.2    Lu, J.3
  • 43
    • 0032579292 scopus 로고    scopus 로고
    • Transcription factor-specif requirements for co-activators and their acetyltransferase function
    • Korzus E, Torchia J, Rose DW, et al. Transcription factor-specif requirements for co-activators and their acetyltransferase function. Science 1998;279:703-7.
    • (1998) Science , vol.279 , pp. 703-707
    • Korzus, E.1    Torchia, J.2    Rose, D.W.3
  • 44
    • 0032541637 scopus 로고    scopus 로고
    • Signal-specific co-activator domain requirements for Pit-1 activation
    • Xu L, Lavinsky RM, Dasen JS, et al. Signal-specific co-activator domain requirements for Pit-1 activation. Nature 1998;395:301-6.
    • (1998) Nature , vol.395 , pp. 301-306
    • Xu, L.1    Lavinsky, R.M.2    Dasen, J.S.3
  • 45
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister AJ, Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature 1996;384:641-3.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 46
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: Integrating signals with transcription factors and chromatin
    • Shikama N, Lyon J, La Thangue NB. The p300/CBP family: Integrating signals with transcription factors and chromatin. Trends Cell Biol 1997;6:230-6.
    • (1997) Trends Cell Biol , vol.6 , pp. 230-236
    • Shikama, N.1    Lyon, J.2    La Thangue, N.B.3
  • 47
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner DE, Berger SL. Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 2000;64: 435-59.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 48
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 2000;14:121-41.
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 49
    • 0030271392 scopus 로고    scopus 로고
    • The major cytoplasmic histone acetyltransferase in yeast: Links to chromatin replication and histone metabolism
    • Parthun MR, Widom J, Gottschling DE. The major cytoplasmic histone acetyltransferase in yeast: Links to chromatin replication and histone metabolism. Cell 1996; 87:85-94.
    • (1996) Cell , vol.87 , pp. 85-94
    • Parthun, M.R.1    Widom, J.2    Gottschling, D.E.3
  • 50
    • 0032524308 scopus 로고    scopus 로고
    • HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4
    • Ruiz-Garcia AB, Sendra R, Galiana M, et al. HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4. J Biol Chem 1998;273:12599-605.
    • (1998) J Biol Chem , vol.273 , pp. 12599-12605
    • Ruiz-Garcia, A.B.1    Sendra, R.2    Galiana, M.3
  • 51
    • 33646269070 scopus 로고    scopus 로고
    • Recruitment of the type B histone acetyltransferase Hat1p to chromatin is linked to DNA double-strand breaks
    • Qin S, Parthun MR. Recruitment of the type B histone acetyltransferase Hat1p to chromatin is linked to DNA double-strand breaks. Mol Cell Biol 2006;26: 3649-58.
    • (2006) Mol Cell Biol , vol.26 , pp. 3649-3658
    • Qin, S.1    Parthun, M.R.2
  • 52
    • 0033166761 scopus 로고    scopus 로고
    • A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme
    • Wittschieben B, Otero G, de Bizemont T, et al. A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme. Mol Cell 1999;4:123-8.
    • (1999) Mol Cell , vol.4 , pp. 123-128
    • Wittschieben, B.1    Otero, G.2    de Bizemont, T.3
  • 53
    • 0036809640 scopus 로고    scopus 로고
    • Transcriptional inhibition of genes with severe histone H3 hypoacetylation in the coding region
    • Kristjuhan A, Walker J, Suka N, et al. Transcriptional inhibition of genes with severe histone H3 hypoacetylation in the coding region. Mol Cell 2002;10:925-33.
    • (2002) Mol Cell , vol.10 , pp. 925-933
    • Kristjuhan, A.1    Walker, J.2    Suka, N.3
  • 54
    • 0032971711 scopus 로고    scopus 로고
    • Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation
    • Otero G, Fellows J, Li T, et al. Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Mol Cell 1999;3:109-18.
    • (1999) Mol Cell , vol.3 , pp. 109-118
    • Otero, G.1    Fellows, J.2    Li, T.3
  • 55
    • 9544220768 scopus 로고    scopus 로고
    • The translocation t(8;16) (p11;p13) of acute myeloid leukemia fuses a putative acetyltransferase to the CREB-binding protein
    • Borrow J, Stanton VP, Andersen JM, Jr, et al. The translocation t(8;16) (p11;p13) of acute myeloid leukemia fuses a putative acetyltransferase to the CREB-binding protein. Nat Genet 1996;14:33-41.
    • (1996) Nat Genet , vol.14 , pp. 33-41
    • Borrow, J.1    Stanton, V.P.2    Andersen Jr., J.M.3
  • 56
    • 0032080173 scopus 로고    scopus 로고
    • A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemias
    • Carapeti M, Aguiar RC, Goldman JM, et al. A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemias. Blood 1998; 91:3127-33.
    • (1998) Blood , vol.91 , pp. 3127-3133
    • Carapeti, M.1    Aguiar, R.C.2    Goldman, J.M.3
  • 57
    • 0032530267 scopus 로고    scopus 로고
    • Acute mixed lineage leukemia with an inv(8) (p11q13) resulting in fusion of the genes for MOZ and TIF2
    • Liang J, Prouty L, Williams BJ, et al. Acute mixed lineage leukemia with an inv(8) (p11q13) resulting in fusion of the genes for MOZ and TIF2. Blood 1998;92:2118-22.
    • (1998) Blood , vol.92 , pp. 2118-2122
    • Liang, J.1    Prouty, L.2    Williams, B.J.3
  • 58
    • 2342464348 scopus 로고    scopus 로고
    • Type MOZ/CBP (MYST3/CREBBP) is the most common chimeric transcript in acute myeloid leukemia with t(8;16) (p11;p13) translocation
    • Rozman M, Camos M, Colomer D, et al. Type MOZ/CBP (MYST3/CREBBP) is the most common chimeric transcript in acute myeloid leukemia with t(8;16) (p11;p13) translocation. Genes Chromosomes Cancer 2004;40:140-5.
    • (2004) Genes Chromosomes Cancer , vol.40 , pp. 140-145
    • Rozman, M.1    Camos, M.2    Colomer, D.3
  • 59
    • 33744956273 scopus 로고    scopus 로고
    • Co-activation of atrial natriuretic factor promoter by Tip60 and serum response factor
    • Apr 5, in press
    • Kim MS, Merlo X, Wilson C, et al. Co-activation of atrial natriuretic factor promoter by Tip60 and serum response factor. J Biol Cell 2006 Apr 5, in press.
    • (2006) J Biol Cell
    • Kim, M.S.1    Merlo, X.2    Wilson, C.3
  • 60
    • 2342599619 scopus 로고    scopus 로고
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
    • Yang XJ. The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases. Nucleic Acid Res 2004;32:959-76.
    • (2004) Nucleic Acid Res , vol.32 , pp. 959-976
    • Yang, X.J.1
  • 61
    • 10844233155 scopus 로고    scopus 로고
    • Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions
    • Kusch T, Florens L, Macdonald WH et al. Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions. Science 2004;306:2084-7.
    • (2004) Science , vol.306 , pp. 2084-2087
    • Kusch, T.1    Florens, L.2    Macdonald, W.H.3
  • 62
    • 0033215187 scopus 로고    scopus 로고
    • Identification of a human histone acetyltransferase related to monocyte leukemia zinc finger protein
    • Champagne N, Bertos NR, Pelletier N, et al. Identification of a human histone acetyltransferase related to monocyte leukemia zinc finger protein. J Biol Chem 1999;274: 28528-36.
    • (1999) J Biol Chem , vol.274 , pp. 28528-28536
    • Champagne, N.1    Bertos, N.R.2    Pelletier, N.3
  • 63
    • 0035805606 scopus 로고    scopus 로고
    • Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1
    • Burke TW, Cook JG, Nevins JR. Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1. J Biol Chem 2001;276:15397-408.
    • (2001) J Biol Chem , vol.276 , pp. 15397-15408
    • Burke, T.W.1    Cook, J.G.2    Nevins, J.R.3
  • 64
    • 0033551686 scopus 로고    scopus 로고
    • Histone acetyltransferase HBO1 interacs with ORC1 subunit of the human initiator protein
    • Iizuka M, Stillman B. Histone acetyltransferase HBO1 interacs with ORC1 subunit of the human initiator protein. J Biol Chem 1999;274:23027-34.
    • (1999) J Biol Chem , vol.274 , pp. 23027-23034
    • Iizuka, M.1    Stillman, B.2
  • 65
    • 0026645025 scopus 로고
    • Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains
    • Berger SL, Pina B, Silverman N, et al. Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains. Cell 1992;70: 251-65.
    • (1992) Cell , vol.70 , pp. 251-265
    • Berger, S.L.1    Pina, B.2    Silverman, N.3
  • 66
    • 0032567081 scopus 로고    scopus 로고
    • Dissecting the regulatory circuitry of a eukaryotic genome
    • Holstege FC, Jennings EG, Wyrick JJ, et al. Dissecting the regulatory circuitry of a eukaryotic genome. Cell 1998;95: 717-28.
    • (1998) Cell , vol.95 , pp. 717-728
    • Holstege, F.C.1    Jennings, E.G.2    Wyrick, J.J.3
  • 67
    • 0032101179 scopus 로고    scopus 로고
    • Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
    • Zhang W, Bone JR, Edmondson DG, et al. Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase. EMBO J 1998;17:3155-67.
    • (1998) EMBO J , vol.17 , pp. 3155-3167
    • Zhang, W.1    Bone, J.R.2    Edmondson, D.G.3
  • 68
    • 0034839973 scopus 로고    scopus 로고
    • Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin
    • Suka N, Suka Y, Carmen AA, et al. Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Mol Cell 2001;8:473-9.
    • (2001) Mol Cell , vol.8 , pp. 473-479
    • Suka, N.1    Suka, Y.2    Carmen, A.A.3
  • 69
    • 0030797349 scopus 로고    scopus 로고
    • Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt/Ada) complex
    • Grant PA, Duggan L, Cote J, et al. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev 1997;11:1640-50.
    • (1997) Genes Dev , vol.11 , pp. 1640-1650
    • Grant, P.A.1    Duggan, L.2    Cote, J.3
  • 70
    • 0033985079 scopus 로고    scopus 로고
    • The many HATs of transcription co-activators
    • Brown CE, Lechner T, Howe L, et al. The many HATs of transcription co-activators. Trends Biochem Sci 2000;25:15-9.
    • (2000) Trends Biochem Sci , vol.25 , pp. 15-19
    • Brown, C.E.1    Lechner, T.2    Howe, L.3
  • 71
    • 0032850594 scopus 로고    scopus 로고
    • The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae
    • Eberharter A, Sterner DE, Schieltz D, et al. The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae. Mol Cell Biol 1999;19:6621-31.
    • (1999) Mol Cell Biol , vol.19 , pp. 6621-6631
    • Eberharter, A.1    Sterner, D.E.2    Schieltz, D.3
  • 72
    • 0032480882 scopus 로고    scopus 로고
    • Transcription: A lesson in sharing?
    • Grant PA, Workman JL. Transcription: A lesson in sharing? Nature 1998;396:410-1.
    • (1998) Nature , vol.396 , pp. 410-411
    • Grant, P.A.1    Workman, J.L.2
  • 74
    • 0034724871 scopus 로고    scopus 로고
    • Steady-state levels of histone acetylation in Saccharomyces cereviasie
    • Waterborg JH. Steady-state levels of histone acetylation in Saccharomyces cereviasie. J Biol Chem 2000;275: 13007-11.
    • (2000) J Biol Chem , vol.275 , pp. 13007-13011
    • Waterborg, J.H.1
  • 75
    • 33644558031 scopus 로고    scopus 로고
    • A role for gcn5-mediated global histone acetylation in transcriptional regulation
    • Imoberdorf RM, Topalidou I, Strubin M. A role for gcn5-mediated global histone acetylation in transcriptional regulation. Mol Cell Biol 2006;26:1610-6.
    • (2006) Mol Cell Biol , vol.26 , pp. 1610-1616
    • Imoberdorf, R.M.1    Topalidou, I.2    Strubin, M.3
  • 76
    • 0035076210 scopus 로고    scopus 로고
    • Histone acetylation at promoters is differentially affected by specific activators and repressors
    • Deckert J, Struhl K. Histone acetylation at promoters is differentially affected by specific activators and repressors. Mol Cell 2001;21:2726-35.
    • (2001) Mol Cell , vol.21 , pp. 2726-2735
    • Deckert, J.1    Struhl, K.2
  • 77
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATF-related cofactor Tra1p
    • Allard S, Utley RT, Savard J, et al. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATF-related cofactor Tra1p. EMBO J 1999;18:5108-19.
    • (1999) EMBO J , vol.18 , pp. 5108-5119
    • Allard, S.1    Utley, R.T.2    Savard, J.3
  • 78
    • 0034515772 scopus 로고    scopus 로고
    • Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase
    • Reid JL, Iyer VR, Brown PO, et al. Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase. Mol Cell 2000;6: 1297-307.
    • (2000) Mol Cell , vol.6 , pp. 1297-1307
    • Reid, J.L.1    Iyer, V.R.2    Brown, P.O.3
  • 79
    • 33645224956 scopus 로고    scopus 로고
    • Genome-wide relationships between TAF1 and histone acetyltransferases in Saccharomyces cerevisiae
    • Durant M, Pugh BF. Genome-wide relationships between TAF1 and histone acetyltransferases in Saccharomyces cerevisiae. Mol Cell Biol 2006;26:2791-802.
    • (2006) Mol Cell Biol , vol.26 , pp. 2791-2802
    • Durant, M.1    Pugh, B.F.2
  • 80
    • 0030447943 scopus 로고    scopus 로고
    • The TAF(II)250 subunit of TAFIID has histone acetyltransferase activity
    • Mizzen CA, Yang XJ, Kobuko T, et al. The TAF(II)250 subunit of TAFIID has histone acetyltransferase activity. Cell 1996;87:1261-70.
    • (1996) Cell , vol.87 , pp. 1261-1270
    • Mizzen, C.A.1    Yang, X.J.2    Kobuko, T.3
  • 81
    • 0001262663 scopus 로고    scopus 로고
    • Redundant roles for the TFIID and SAGA complexes in global transcription
    • Lee TI, Causton HC, Holstege FC, et al. Redundant roles for the TFIID and SAGA complexes in global transcription. Nature 2000;405:701-4.
    • (2000) Nature , vol.405 , pp. 701-704
    • Lee, T.I.1    Causton, H.C.2    Holstege, F.C.3
  • 82
    • 18144368519 scopus 로고    scopus 로고
    • TAF1 histone acetyltransferase activity in Sp1 activation of the cyclin D1 promoter
    • Hilton TL, Li Y, Dunphy EL, et al. TAF1 histone acetyltransferase activity in Sp1 activation of the cyclin D1 promoter. Mol Cell Biol 2005;25:4321-32.
    • (2005) Mol Cell Biol , vol.25 , pp. 4321-4332
    • Hilton, T.L.1    Li, Y.2    Dunphy, E.L.3
  • 83
    • 0034656273 scopus 로고    scopus 로고
    • Bromodomain factor 1 corresponds to a missing piece of yeast TFIID
    • Matangkasombut O, Buratowski RM, Swilling NW, et al. Bromodomain factor 1 corresponds to a missing piece of yeast TFIID. Genes Dev 2000;14:951-62.
    • (2000) Genes Dev , vol.14 , pp. 951-962
    • Matangkasombut, O.1    Buratowski, R.M.2    Swilling, N.W.3
  • 84
    • 24744433805 scopus 로고    scopus 로고
    • Role of histone acetylation in the control of gene expression
    • Verdone L, Caserta M, Di Mauro E. Role of histone acetylation in the control of gene expression. Biochem Cell Biol 2005;83:344-53.
    • (2005) Biochem Cell Biol , vol.83 , pp. 344-353
    • Verdone, L.1    Caserta, M.2    Di Mauro, E.3
  • 85
    • 0037123767 scopus 로고    scopus 로고
    • Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases
    • Robyr D, Suka Y, Xenarios I, et al. Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases Cell 2002;109:437-46.
    • (2002) Cell , vol.109 , pp. 437-446
    • Robyr, D.1    Suka, Y.2    Xenarios, I.3
  • 86
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger CM, Schreiber SL. Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors. Chem Biol 2002;9:3-16.
    • (2002) Chem Biol , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 87
    • 33947511972 scopus 로고    scopus 로고
    • Targeting histone deacetylase in cancer therapy
    • Lin HY, Chen CS, Lin SP, et al. Targeting histone deacetylase in cancer therapy. Med Res Rev 2004;31;1-17.
    • (2004) Med Res Rev , vol.31 , pp. 1-17
    • Lin, H.Y.1    Chen, C.S.2    Lin, S.P.3
  • 88
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • Verdin E, Dequiedt F, Kasler HG. Class II histone deacetylases: versatile regulators. Trends Genet 2003;19: 286-93.
    • (2003) Trends Genet , vol.19 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 89
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai S, et al. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 2001; 107:137-48.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3
  • 90
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, Dessain SK, Ng Eaton E, et al. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 2001;107:149-59.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng Eaton, E.3
  • 91
    • 27544505676 scopus 로고    scopus 로고
    • Chromatin modifier enzymes, the histone code and cancer
    • Santos-Rosa H, Caldas C. Chromatin modifier enzymes, the histone code and cancer. Eur J Cancer 2005;41:2381-402.
    • (2005) Eur J Cancer , vol.41 , pp. 2381-2402
    • Santos-Rosa, H.1    Caldas, C.2
  • 92
    • 0035957097 scopus 로고    scopus 로고
    • Dynamics of histone acetylation in Saccharomyces cerevisiae
    • Waterborg JH. Dynamics of histone acetylation in Saccharomyces cerevisiae. Biochemistry 2001;40:2599-605.
    • (2001) Biochemistry , vol.40 , pp. 2599-2605
    • Waterborg, J.H.1
  • 93
    • 0037087576 scopus 로고    scopus 로고
    • Dynamics of global histone acetylation and deacetylation in vivo: Rapid restoration of normal histone acetylation status upon removal of activators and repressors
    • Katan-Khaykovich Y, Struhl K. Dynamics of global histone acetylation and deacetylation in vivo: Rapid restoration of normal histone acetylation status upon removal of activators and repressors Genes Dev 2002;16:743-52.
    • (2002) Genes Dev , vol.16 , pp. 743-752
    • Katan-Khaykovich, Y.1    Struhl, K.2
  • 94
    • 0029862602 scopus 로고    scopus 로고
    • Chromatin remodeling during saccharomyces cerevisiae ADH2 gene activation
    • Verdone L, Camilloni G, Di Mauro E, et al. Chromatin remodeling during saccharomyces cerevisiae ADH2 gene activation. Mol Cell Biol 1996;16:1978-88.
    • (1996) Mol Cell Biol , vol.16 , pp. 1978-1988
    • Verdone, L.1    Camilloni, G.2    Di Mauro, E.3
  • 95
    • 0036500258 scopus 로고    scopus 로고
    • Hyperacetylation of chromatin at the ADH2 promoter allows Adr1 to bind in repressed conditions
    • Verdone L, Wu J, van Riper K, et al. Hyperacetylation of chromatin at the ADH2 promoter allows Adr1 to bind in repressed conditions. EMBO J 2002;21:1101-11.
    • (2002) EMBO J , vol.21 , pp. 1101-1111
    • Verdone, L.1    Wu, J.2    van Riper, K.3
  • 96
    • 3042857554 scopus 로고    scopus 로고
    • Common chromatin architecture, common chromatin remodeling, and common transcription kinetics of Adr1-dependent genes in Saccharomyces cerevisiae
    • Agricola E, Verdone L, Xella B, et al. Common chromatin architecture, common chromatin remodeling, and common transcription kinetics of Adr1-dependent genes in Saccharomyces cerevisiae. Biochemisty 2004;43:8878-84.
    • (2004) Biochemisty , vol.43 , pp. 8878-8884
    • Agricola, E.1    Verdone, L.2    Xella, B.3
  • 97
    • 0020699979 scopus 로고
    • Hypomethylation distinguishes genes of some human cancers from their normal counterparts
    • Feinberg AP, Vogelstein B. Hypomethylation distinguishes genes of some human cancers from their normal counterparts. Nature 1983;301:89-92.
    • (1983) Nature , vol.301 , pp. 89-92
    • Feinberg, A.P.1    Vogelstein, B.2
  • 98
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones PA, Baylin SB. The fundamental role of epigenetic events in cancer. Nat Rev Genet 2002;3:415-28.
    • (2002) Nat Rev Genet , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 99
    • 0345357773 scopus 로고    scopus 로고
    • Gene silencing in cancer in association with promoter hypermethylation
    • Herman JG, Baylin SB. Gene silencing in cancer in association with promoter hypermethylation. N Engl J Med 2003;349:2042-54.
    • (2003) N Engl J Med , vol.349 , pp. 2042-2054
    • Herman, J.G.1    Baylin, S.B.2
  • 100
    • 1042278765 scopus 로고    scopus 로고
    • The history of cancer epigenetics
    • Feinberg AP, Tycko B. The history of cancer epigenetics. Nat Rev Cancer 2004;4:143-53.
    • (2004) Nat Rev Cancer , vol.4 , pp. 143-153
    • Feinberg, A.P.1    Tycko, B.2
  • 101
    • 13844320649 scopus 로고    scopus 로고
    • Aberrant DNA methylation as a cancer-inducing mechanism
    • Esteller M. Aberrant DNA methylation as a cancer-inducing mechanism. Annu Rev Pharmacol Toxicol 2005;45: 629-56.
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , pp. 629-656
    • Esteller, M.1
  • 102
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006;6:38-51.
    • (2006) Nat Rev Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 103
    • 0037115392 scopus 로고    scopus 로고
    • Dependence of histone modification and gene expression on DNA hypermethylation in cancer
    • Fahrner JA, Eguchi S, Herman JG, et al. Dependence of histone modification and gene expression on DNA hypermethylation in cancer Cancer. Res 2002;62:7213-8.
    • (2002) Cancer Res , vol.62 , pp. 7213-7218
    • Fahrner, J.A.1    Eguchi, S.2    Herman, J.G.3
  • 104
    • 0348134871 scopus 로고    scopus 로고
    • Methyl-CpG binding proteins identify novel sites of epigenetic inactivation in human cancer
    • Ballestar E, Paz MF, Valle L, et al. Methyl-CpG binding proteins identify novel sites of epigenetic inactivation in human cancer. EMBO J 2003;22:6335-45.
    • (2003) EMBO J , vol.22 , pp. 6335-6345
    • Ballestar, E.1    Paz, M.F.2    Valle, L.3
  • 105
    • 17444417521 scopus 로고    scopus 로고
    • Cancer epigenetics
    • Laird PW. Cancer epigenetics. Hum Mol Genet 2005;14: 65-76.
    • (2005) Hum Mol Genet , vol.14 , pp. 65-76
    • Laird, P.W.1
  • 106
    • 20144388146 scopus 로고    scopus 로고
    • Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
    • Fraga MF, Ballestar E, Villar-Garea A, et al. Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nat Genet 2005;37: 391-400.
    • (2005) Nat Genet , vol.37 , pp. 391-400
    • Fraga, M.F.1    Ballestar, E.2    Villar-Garea, A.3
  • 107
    • 21744457108 scopus 로고    scopus 로고
    • Global histone modification patterns predict risk of prostate cancer recurrence
    • Seligson DB, Horvath S, Shi T, et al. Global histone modification patterns predict risk of prostate cancer recurrence. Nature 2005;435:1262-6
    • (2005) Nature , vol.435 , pp. 1262-1266
    • Seligson, D.B.1    Horvath, S.2    Shi, T.3
  • 108
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: Past, present and future
    • Yoo CB, Jones PA. Epigenetic therapy of cancer: Past, present and future. Nat Rev Drug Discov 2006;5:37-50.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2
  • 109
    • 25844530426 scopus 로고    scopus 로고
    • Epigenetic changes in solid and hematopoietic tumors
    • Toyota M, Issa JP. Epigenetic changes in solid and hematopoietic tumors. Semin Oncol 2005;32:521-30.
    • (2005) Semin Oncol , vol.32 , pp. 521-530
    • Toyota, M.1    Issa, J.P.2
  • 110
    • 31444437920 scopus 로고    scopus 로고
    • Epigenetics provides a new generation of oncogenes and tumour-suppressor genes
    • Esteller M. Epigenetics provides a new generation of oncogenes and tumour-suppressor genes. Br J Cancer 2006; 94:179-83.
    • (2006) Br J Cancer , vol.94 , pp. 179-183
    • Esteller, M.1
  • 111
    • 1642358490 scopus 로고    scopus 로고
    • Linking the epigenetic 'language' of covalent histone modifications to cancer
    • Hake SB, Xiao A, Allis CD. Linking the epigenetic 'language' of covalent histone modifications to cancer. Br J Cancer 2004;90:761-9.
    • (2004) Br J Cancer , vol.90 , pp. 761-769
    • Hake, S.B.1    Xiao, A.2    Allis, C.D.3
  • 112
    • 15744370742 scopus 로고    scopus 로고
    • Curcumin-induced histone hypoacetylation: The role of reactive oxygen species
    • Kang J, Chen J, Shi Y, et al. Curcumin-induced histone hypoacetylation: the role of reactive oxygen species. Biochem Pharmacol 2005;69:1205-13.
    • (2005) Biochem Pharmacol , vol.69 , pp. 1205-1213
    • Kang, J.1    Chen, J.2    Shi, Y.3
  • 114
    • 19944385935 scopus 로고    scopus 로고
    • MOZ-TIF2, but not BCR-ABL, confers properties of leukemic stem cells to committed murine hematopoietic progenitors
    • Huntly BJ, Shigematsu H, Deguchi K, et al. MOZ-TIF2, but not BCR-ABL, confers properties of leukemic stem cells to committed murine hematopoietic progenitors Cancer Cell 2004;6:587-96.
    • (2004) Cancer Cell , vol.6 , pp. 587-596
    • Huntly, B.J.1    Shigematsu, H.2    Deguchi, K.3
  • 115
    • 2842572725 scopus 로고    scopus 로고
    • A further case of acute myelomonocytic leukemia with inv(8) chromosomal rearrangement and MOZ-NCOA2 gene fusion
    • Murati A, Adelaide J, Popovici C, et al. A further case of acute myelomonocytic leukemia with inv(8) chromosomal rearrangement and MOZ-NCOA2 gene fusion. Int J Mol Med 2003;12:423-8.
    • (2003) Int J Mol Med , vol.12 , pp. 423-428
    • Murati, A.1    Adelaide, J.2    Popovici, C.3
  • 116
    • 17644445419 scopus 로고    scopus 로고
    • Gene osage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300
    • Yao TP, Oh SP, Fuchs M, et al. Gene osage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300 Cell 1998;93:361-72.
    • (1998) Cell , vol.93 , pp. 361-372
    • Yao, T.P.1    Oh, S.P.2    Fuchs, M.3
  • 117
    • 0034141475 scopus 로고    scopus 로고
    • Gene dose-dependent control of hematopoiesis and hematologic tumor suppression by CBP
    • Kung AL, Rebel VI, Bronson RT, et al. Gene dose-dependent control of hematopoiesis and hematologic tumor suppression by CBP. Genes Dev 2000;14:272-7.
    • (2000) Genes Dev , vol.14 , pp. 272-277
    • Kung, A.L.1    Rebel, V.I.2    Bronson, R.T.3
  • 118
    • 4344578186 scopus 로고    scopus 로고
    • Disease-related potential of mutations in transcriptional cofactors CREB-binding protein and p300 in leukemias
    • Shigeno K, Yoshida H, Pan L, et al. Disease-related potential of mutations in transcriptional cofactors CREB-binding protein and p300 in leukemias. Cancer Lett 2004;213:11-20.
    • (2004) Cancer Lett , vol.213 , pp. 11-20
    • Shigeno, K.1    Yoshida, H.2    Pan, L.3
  • 119
    • 0034104047 scopus 로고    scopus 로고
    • Mutations truncating the EP300 acetylase in human cancers
    • Gayther SA, Batley SJ, Linger L, et al. Mutations truncating the EP300 acetylase in human cancers. Nat Genet 2000;24: 300-3.
    • (2000) Nat Genet , vol.24 , pp. 300-303
    • Gayther, S.A.1    Batley, S.J.2    Linger, L.3
  • 120
    • 0035339491 scopus 로고    scopus 로고
    • Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome
    • Murata T, Kurokawa R, Krones A, et al. Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome Hum Mol Genet 2001;10:1071-6.
    • (2001) Hum Mol Genet , vol.10 , pp. 1071-1076
    • Murata, T.1    Kurokawa, R.2    Krones, A.3
  • 121
    • 2942705826 scopus 로고    scopus 로고
    • Chromatin acetylation memory and LTP are impaired in CBP+/-mice: A model for the cognitive deficit in Rubinstein-Taybi syndrome and its amelioration
    • Alarcon JM, Malleret G, Touzani K, et al. Chromatin acetylation memory and LTP are impaired in CBP+/-mice: A model for the cognitive deficit in Rubinstein-Taybi syndrome and its amelioration Neuron. 2004;42: 947-59.
    • (2004) Neuron , vol.42 , pp. 947-959
    • Alarcon, J.M.1    Malleret, G.2    Touzani, K.3
  • 122
    • 2942731425 scopus 로고    scopus 로고
    • CBP histone acetyltransferase activity is a critical component of memory consolidation
    • Korzus E, Rosenfeld MG, Mayford M. CBP histone acetyltransferase activity is a critical component of memory consolidation. Neuron 2004;42:961-72.
    • (2004) Neuron , vol.42 , pp. 961-972
    • Korzus, E.1    Rosenfeld, M.G.2    Mayford, M.3
  • 124
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman RH, Smolik S. CBP/p300 in cell growth, transformation, and development. Genes Dev 2000;14: 1553-77.
    • (2000) Genes Dev , vol.14 , pp. 1553-1577
    • Goodman, R.H.1    Smolik, S.2
  • 125
    • 0034687687 scopus 로고    scopus 로고
    • Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP
    • Zhang Q, Yao H, Vo N, et al. Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP. Proc Natl Acad Sci USA 2000;97: 14323-8.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14323-14328
    • Zhang, Q.1    Yao, H.2    Vo, N.3
  • 126
    • 10044262126 scopus 로고    scopus 로고
    • The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60
    • Patel JH, Du Y, Ard PG, et al. The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60. Mol Cell Biol 2004;24:10826-34.
    • (2004) Mol Cell Biol , vol.24 , pp. 10826-10834
    • Patel, J.H.1    Du, Y.2    Ard, P.G.3
  • 127
    • 2942620920 scopus 로고    scopus 로고
    • E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1
    • Taubert S, Gorrini C, Frank SR, et al. E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1. Mol Cell Biol 2004;24:4546-56.
    • (2004) Mol Cell Biol , vol.24 , pp. 4546-4556
    • Taubert, S.1    Gorrini, C.2    Frank, S.R.3
  • 128
    • 0034254668 scopus 로고    scopus 로고
    • Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-erb. A yields a chromatin infrastructure-dependent transcriptional repression pathway
    • Urnov FD, Yee J, Sachs L, et al. Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-erb. A yields a chromatin infrastructure-dependent transcriptional repression pathway. EMBO J 2000;19:4074-90.
    • (2000) EMBO J , vol.19 , pp. 4074-4090
    • Urnov, F.D.1    Yee, J.2    Sachs, L.3
  • 129
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress WD, Seto E. Histone deacetylases, transcriptional control, and cancer. J Cell Physiol 2000;184:1-16.
    • (2000) J Cell Physiol , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 130
    • 0033109775 scopus 로고    scopus 로고
    • Retinoid receptors in health and disease: Co-regulators and the chromatin connection
    • Minucci S, Pelicci PG. Retinoid receptors in health and disease: co-regulators and the chromatin connection. Semin Cell Dev Biol 1999;10:215-25.
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 215-225
    • Minucci, S.1    Pelicci, P.G.2
  • 131
    • 0033638969 scopus 로고    scopus 로고
    • Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation
    • Minucci S, Maccarana M, Cioce M, et al. Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation. Mol Cell 2000;5: 811-20.
    • (2000) Mol Cell , vol.5 , pp. 811-820
    • Minucci, S.1    Maccarana, M.2    Cioce, M.3
  • 132
    • 0032949304 scopus 로고    scopus 로고
    • Molecular genetics of acute promyelocytic leukemia
    • Lin RJ, Egan DA, Evans RM. Molecular genetics of acute promyelocytic leukemia. Trends Genet 1999;15: 179-84.
    • (1999) Trends Genet , vol.15 , pp. 179-184
    • Lin, R.J.1    Egan, D.A.2    Evans, R.M.3
  • 133
    • 0033634946 scopus 로고    scopus 로고
    • Acquisition of oncogenic potential by RAR chimeras in acute promyelocytic leukemia through formation of homodimers
    • Lin RJ, Evans RM. Acquisition of oncogenic potential by RAR chimeras in acute promyelocytic leukemia through formation of homodimers. Mol Cell 2000;3:821-30.
    • (2000) Mol Cell , vol.3 , pp. 821-830
    • Lin, R.J.1    Evans, R.M.2
  • 134
    • 0035145329 scopus 로고    scopus 로고
    • Effects of the acute myeloid leukemia-associated fusion proteins on nuclear architecture
    • Faretta M, Di Croce L, Pelicci PG. Effects of the acute myeloid leukemia-associated fusion proteins on nuclear architecture. Semin Hematol 2001;38:42-53.
    • (2001) Semin Hematol , vol.38 , pp. 42-53
    • Faretta, M.1    Di Croce, L.2    Pelicci, P.G.3
  • 135
    • 0036040215 scopus 로고    scopus 로고
    • Chromatin modification, leukaemia and implications for therapy
    • Jones LK, Saba V. Chromatin modification, leukaemia and implications for therapy. Br J Haematol 2002;118:714-27.
    • (2002) Br J Haematol , vol.118 , pp. 714-727
    • Jones, L.K.1    Saba, V.2
  • 136
    • 0344845184 scopus 로고    scopus 로고
    • Targeting aberrant transcriptional repression in acute myeloid leukemia
    • Moe-Behrens GH Pandolfi PP. Targeting aberrant transcriptional repression in acute myeloid leukemia. Rev Clin Exp Hematol 2003;7:139-59.
    • (2003) Rev Clin Exp Hematol , vol.7 , pp. 139-159
    • Moe-Behrens, G.H.1    Pandolfi, P.P.2
  • 137
    • 1542268361 scopus 로고    scopus 로고
    • Mi-2/NuRD: Multiple complexes for many purposes
    • Bowen NJ, Fujita N, Kajita M, et al. Mi-2/NuRD: Multiple complexes for many purposes. Biochim Biophys Acta 2004;1677:52-7.
    • (2004) Biochim Biophys Acta , vol.1677 , pp. 52-57
    • Bowen, N.J.1    Fujita, N.2    Kajita, M.3
  • 138
    • 2442430362 scopus 로고    scopus 로고
    • Expression of the metastasis-associated MTA1 protein and its relationship to deacetylation of the histone H4 in esophageal squamous cell carcinomas
    • Toh Y, Ohga T, Endo K, et al. Expression of the metastasis-associated MTA1 protein and its relationship to deacetylation of the histone H4 in esophageal squamous cell carcinomas. Int J Cancer 2004; 110:362-7.
    • (2004) Int J Cancer , vol.110 , pp. 362-367
    • Toh, Y.1    Ohga, T.2    Endo, K.3
  • 139
    • 33645071569 scopus 로고    scopus 로고
    • Metastasis tumor antigen family proteins during breast cancer progression and metastasis in a reliable mouse model for human breast cancer
    • Zhang H, Stephens LC, Kumar R. Metastasis tumor antigen family proteins during breast cancer progression and metastasis in a reliable mouse model for human breast cancer. Clin Cancer Res 2006;12:1479-86.
    • (2006) Clin Cancer Res , vol.12 , pp. 1479-1486
    • Zhang, H.1    Stephens, L.C.2    Kumar, R.3
  • 140
    • 33645322383 scopus 로고    scopus 로고
    • Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1
    • Yoo YG, Kong G, Lee MO. Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1. EMBO J 2006; 23:1231-41.
    • (2006) EMBO J , vol.23 , pp. 1231-1241
    • Yoo, Y.G.1    Kong, G.2    Lee, M.O.3
  • 141
    • 2342603414 scopus 로고    scopus 로고
    • Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis
    • Zhu P, Martin E, Mengwasser J, et al. Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis. Cancer Cell 2004;3:455-63.
    • (2004) Cancer Cell , vol.3 , pp. 455-463
    • Zhu, P.1    Martin, E.2    Mengwasser, J.3
  • 142
    • 4944255743 scopus 로고    scopus 로고
    • Post-translational modification of p53 in tumorigenesis
    • Bode AM, Dong Z. Post-translational modification of p53 in tumorigenesis. Nat Rev Cancer 2004;4:793-805.
    • (2004) Nat Rev Cancer , vol.4 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 143
    • 12144287125 scopus 로고    scopus 로고
    • Impairment of p53 acetylation, stability and function by an oncogenic transcription factor
    • Insinga A, Monestiroli S, Ronzoni S, et al. Impairment of p53 acetylation, stability and function by an oncogenic transcription factor. EMBO J 2004;23:1144-54.
    • (2004) EMBO J , vol.23 , pp. 1144-1154
    • Insinga, A.1    Monestiroli, S.2    Ronzoni, S.3
  • 144
    • 16844362441 scopus 로고    scopus 로고
    • Histone deacetylation in epigenetics: An attractive target for anticancer therapy
    • Mai A, Massa S, Rotili D, et al. Histone deacetylation in epigenetics: an attractive target for anticancer therapy. Med Res Rev 2005;23:261-309.
    • (2005) Med Res Rev , vol.23 , pp. 261-309
    • Mai, A.1    Massa, S.2    Rotili, D.3
  • 145
    • 0842307061 scopus 로고    scopus 로고
    • Silencing of transgene transcription precedes methylation of promoter DNA and histone H3 lysine 9
    • Mutskov V, Felsenfeld G. Silencing of transgene transcription precedes methylation of promoter DNA and histone H3 lysine 9. EMBO J 2004;23:138-49.
    • (2004) EMBO J , vol.23 , pp. 138-149
    • Mutskov, V.1    Felsenfeld, G.2
  • 146
    • 20044390016 scopus 로고    scopus 로고
    • Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors
    • Ungerstedt JS, Sowa Y, Xu WS, et al. Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors. Proc Natl Acad Sci USA 2005;102: 673-8.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 673-678
    • Ungerstedt, J.S.1    Sowa, Y.2    Xu, W.S.3
  • 147
    • 0842277812 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1
    • Gui CY, Ngo L, Xu WS, et al. Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1. Proc Natl Acad Sci USA 2004;101:1241-6.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1241-1246
    • Gui, C.Y.1    Ngo, L.2    Xu, W.S.3
  • 148
    • 26444439216 scopus 로고    scopus 로고
    • Prospects: Histone deacetylase inhibitors
    • Dokmanovic M, Marks PA. Prospects: Histone deacetylase inhibitors. J Cell Biochem 2005;96:293-304.
    • (2005) J Cell Biochem , vol.96 , pp. 293-304
    • Dokmanovic, M.1    Marks, P.A.2
  • 149
    • 18644365597 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors differentially stabilize acetylated p53 and induce cell cycle arrest or apoptosis in prostate cancer cells
    • Roy S, Packman K, Jeffrey R, et al. Histone deacetylase inhibitors differentially stabilize acetylated p53 and induce cell cycle arrest or apoptosis in prostate cancer cells. Cell Death Differ 2005;12:482-91.
    • (2005) Cell Death Differ , vol.12 , pp. 482-491
    • Roy, S.1    Packman, K.2    Jeffrey, R.3
  • 150
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo J, Su F, Chen D, et al. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 2000;408: 377-81.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3
  • 151
    • 16344376556 scopus 로고    scopus 로고
    • Ku70 acetylation mediates neuroblastoma cell death induced by histone deacetylase inhibitors
    • Subramanian C, Opipari AW, Jr, Bian X, et al. Ku70 acetylation mediates neuroblastoma cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci USA 2005; 102:4842-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4842-4847
    • Subramanian, C.1    Opipari Jr., A.W.2    Bian, X.3
  • 152
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem 2005;280:26729-34.
    • (2005) J Biol Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3
  • 153
    • 27144475816 scopus 로고    scopus 로고
    • Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors
    • Bradbury CA, Khanim FL, Hayden R, et al. Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors. Leukemia 2005;19: 1751-9.
    • (2005) Leukemia , vol.19 , pp. 1751-1759
    • Bradbury, C.A.1    Khanim, F.L.2    Hayden, R.3
  • 154
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells
    • Marks PA, Richon VM, Rifkind RA. Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. J Natl Cancer Inst 2000;92: 1210-6.
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 155
    • 0034765511 scopus 로고    scopus 로고
    • Histone deacetylases inhibitors as new cancer drugs
    • Marks PA, Richon VM, Breswlow R. Histone deacetylases inhibitors as new cancer drugs. Curr Opin Oncol 2001; 13:1-13.
    • (2001) Curr Opin Oncol , vol.13 , pp. 1-13
    • Marks, P.A.1    Richon, V.M.2    Breswlow, R.3
  • 157
    • 0036176617 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer treatment
    • Vigushin DM, Coombes RC. Histone deacetylase inhibitors in cancer treatment. Anticancer Drugs 2002;13: 1-13.
    • (2002) Anticancer Drugs , vol.13 , pp. 1-13
    • Vigushin, D.M.1    Coombes, R.C.2
  • 158
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron EE, Bachman KE, Myohanen S, et al. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat Genet 1999; 21:103-7.
    • (1999) Nat Genet , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3
  • 159
    • 10944243759 scopus 로고    scopus 로고
    • Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/non histone proteins and histone acetyltransferase-dependent chromatin transcription
    • Balasubramanyam K, Varier RA, Altaf M, et al. Curcumin, a novel p300/ CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/non histone proteins and histone acetyltransferase-dependent chromatin transcription. J Biol Chem 2004;279: 51163-71.
    • (2004) J Biol Chem , vol.279 , pp. 51163-51171
    • Balasubramanyam, K.1    Varier, R.A.2    Altaf, M.3
  • 160
    • 30044446136 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) down-regulates expression of cell proliferation and antiapoptotic and metastatic gene products through suppression of Ikappa B alpha kinase and Akt activation
    • Aggarwal S, Ichikawa H, Takada Y, et al. Curcumin (diferuloylmethane) down-regulates expression of cell proliferation and antiapoptotic and metastatic gene products through suppression of Ikappa B alpha kinase and Akt activation. Mol Pharmacol 2006;69:195-206.
    • (2006) Mol Pharmacol , vol.69 , pp. 195-206
    • Aggarwal, S.1    Ichikawa, H.2    Takada, Y.3
  • 161
    • 29244457579 scopus 로고    scopus 로고
    • A blueprint for Human Epigenome Project: The AACR Human Epigenome Workshop
    • Jones PA, Martienssen R. A blueprint for Human Epigenome Project: The AACR Human Epigenome Workshop. Cancer Res 2005;24:11241-6.
    • (2005) Cancer Res , vol.24 , pp. 11241-11246
    • Jones, P.A.1    Martienssen, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.