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Volumn 83, Issue 3, 2005, Pages 344-353

Role of histone acetylation in the control of gene expression

Author keywords

Gene expression; HATs; HDACs; Nucleosome; Transcription

Indexed keywords

ACETYLATION; DNA SEQUENCES; ENZYMES; HISTOLOGY; PROTEINS;

EID: 24744433805     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o05-041     Document Type: Review
Times cited : (278)

References (115)
  • 1
    • 0036850346 scopus 로고    scopus 로고
    • Deciphering the transcriptional histone acetylation code for a human gene
    • Agalioti, T., Chen, G., and Thanos, D. 2002. Deciphering the transcriptional histone acetylation code for a human gene. Cell, 111: 381-392.
    • (2002) Cell , vol.111 , pp. 381-392
    • Agalioti, T.1    Chen, G.2    Thanos, D.3
  • 2
    • 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., Di Mauro, E., and Caserta, M. 2004. Common chromatin architecture, common chromatin remodeling, and common transcription kinetics of Adr1-dependent genes in Saccharomyces cerevisiae. Biochemistry, 43: 8878-8884.
    • (2004) Biochemistry , vol.43 , pp. 8878-8884
    • Agricola, E.1    Verdone, L.2    Xella, B.3    Di Mauro, E.4    Caserta, M.5
  • 3
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p
    • Allard, S., Utley, R.T., Savard, J., Clarke, A., Grant, P., Brandl, CJ. et al. 1999. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J. 18: 5108-5119.
    • (1999) EMBO J. , vol.18 , pp. 5108-5119
    • Allard, S.1    Utley, R.T.2    Savard, J.3    Clarke, A.4    Grant, P.5    Brandl, C.J.6
  • 4
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V., Faulkner, R.M., and Mirsky, A.E. 1964. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 51: 786-794.
    • (1964) Proc. Natl. Acad. Sci. U.S.A. , vol.51 , pp. 786-794
    • Allfrey, V.1    Faulkner, R.M.2    Mirsky, A.E.3
  • 5
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A.J., and Kouzarides, T. 1996. The CBP co-activator is a histone acetyltransferase. Nature (London), 384: 641-643.
    • (1996) Nature (London) , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 6
    • 0031913215 scopus 로고    scopus 로고
    • Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by ku/DNA-PKcs complex
    • Barlev, N.A., Poltoratsky, V., Owen-Hughes, T., Ying, C., Liu, L., Carter, T. et al. 1998. Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by ku/DNA-PKcs complex. Mol. Cell. Biol. 18: 1349-1358.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1349-1358
    • Barlev, N.A.1    Poltoratsky, V.2    Owen-Hughes, T.3    Ying, C.4    Liu, L.5    Carter, T.6
  • 7
  • 8
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger, S.L. 2002. Histone modifications in transcriptional regulation. Curr. Opin. Genetics Dev. 12: 142-148.
    • (2002) Curr. Opin. Genetics Dev. , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 10
    • 2642662483 scopus 로고    scopus 로고
    • The histone acetylase PCAF is a nuclear receptor coactivator
    • Blanco, J.C., Minucci, S., Lu, J., Yang, X.J., Walker, K.K., Chen, H. et al. 1998. The histone acetylase PCAF is a nuclear receptor coactivator. Genes Dev. 12: 1638-1651.
    • (1998) Genes Dev. , vol.12 , pp. 1638-1651
    • Blanco, J.C.1    Minucci, S.2    Lu, J.3    Yang, X.J.4    Walker, K.K.5    Chen, H.6
  • 11
    • 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, V.P., Andersen, J.M., Jr., Becher, R., Behm, F.G., Chaganti, R.S. et al. 1996. The translocation t(8;16) (p11;p13) of acute myeloid leukemia fuses a putative acetyltransferase to the CREB-binding protein. Nat. Genet. 14: 33-41.
    • (1996) Nat. Genet. , vol.14 , pp. 33-41
    • Borrow, J.1    Stanton, V.P.2    Andersen Jr., J.M.3    Becher, R.4    Behm, F.G.5    Chaganti, R.S.6
  • 12
    • 0038284360 scopus 로고    scopus 로고
    • Yeast enhancer of polycomb defines global Esal-dependent acetylation of chromatin
    • Boudreault, A.A., Cronier, D., Selleck, W., Lacoste, N., Utley, R.T., Allard, S. et al. 2003. Yeast enhancer of polycomb defines global Esal-dependent acetylation of chromatin. Genes Dev. 17: 1415-1428.
    • (2003) Genes Dev. , vol.17 , pp. 1415-1428
    • Boudreault, A.A.1    Cronier, D.2    Selleck, W.3    Lacoste, N.4    Utley, R.T.5    Allard, S.6
  • 13
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell, J.E., Zhou, J., Ranalli, T., Kobayashi, R., Edmondson, D.G., Roth, S.Y., and Allis, C.D. 1996. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell, 84: 843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 14
    • 0035805606 scopus 로고    scopus 로고
    • Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1
    • Burke, T.W., Cook, J.G., and Nevins, J.R. 2001. Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1. J. Biol. Chem. 276: 15397-15408.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15397-15408
    • Burke, T.W.1    Cook, J.G.2    Nevins, J.R.3
  • 15
    • 0030030611 scopus 로고    scopus 로고
    • Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5
    • Candau, R., Moore, P.A., Wang, L., Barlev, N., Ying, C.Y., Rosen, C.A., and Berger, S.L. 1996. Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5. Mol. Cell. Biol. 16: 593-602.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 593-602
    • Candau, R.1    Moore, P.A.2    Wang, L.3    Barlev, N.4    Ying, C.Y.5    Rosen, C.A.6    Berger, S.L.7
  • 16
    • 0032080173 scopus 로고    scopus 로고
    • A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemias
    • Carapeti, M., Aguiar, R.C., Goldman, J.M., and Cross, N.C. 1998. A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemias. Blood, 91: 3127-3133.
    • (1998) Blood , vol.91 , pp. 3127-3133
    • Carapeti, M.1    Aguiar, R.C.2    Goldman, J.M.3    Cross, N.C.4
  • 17
    • 0038204415 scopus 로고    scopus 로고
    • The diverse functions of histone acetyltransferase complexes
    • Carrozza, M., Utley, R.T., Workman, J.L., and Côté, J. 2003. The diverse functions of histone acetyltransferase complexes. Trends Genet. 19: 321-329.
    • (2003) Trends Genet. , vol.19 , pp. 321-329
    • Carrozza, M.1    Utley, R.T.2    Workman, J.L.3    Côté, J.4
  • 18
    • 0033215187 scopus 로고    scopus 로고
    • Identification of a human histone acetyltransferase related to monocyte leukemia zinc finger protein
    • Champagne, N., Bertos, N.R., Pelletier, N., Wang, A.H., Vezmar, M., Yang, Y. et al. 1999. Identification of a human histone acetyltransferase related to monocyte leukemia zinc finger protein. J. Biol. Chem. 274: 28528-28536.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28528-28536
    • Champagne, N.1    Bertos, N.R.2    Pelletier, N.3    Wang, A.H.4    Vezmar, M.5    Yang, Y.6
  • 19
    • 0035807044 scopus 로고    scopus 로고
    • Distinct site specificity of two pea histone deacetylase complexes
    • Clemente, S., Franco, L., and Lopez-Rodas G. 2001. Distinct site specificity of two pea histone deacetylase complexes. Biochemistry, 40: 10671-10676.
    • (2001) Biochemistry , vol.40 , pp. 10671-10676
    • Clemente, S.1    Franco, L.2    Lopez-Rodas, G.3
  • 20
    • 0025122175 scopus 로고
    • On the biological role of histone acetylation
    • Csordas, A. 1990. On the biological role of histone acetylation. Biochem. J. 265: 23-28.
    • (1990) Biochem. J. , vol.265 , pp. 23-28
    • Csordas, A.1
  • 21
    • 0035076210 scopus 로고    scopus 로고
    • Histone acetylation at promoters is differentially affected by specific activators and repressers
    • Deckert, J., and Strahl, K. 2001. Histone acetylation at promoters is differentially affected by specific activators and repressers. Mol. Cell. Biol. 21: 2726-2735.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2726-2735
    • Deckert, J.1    Strahl, K.2
  • 22
    • 1642580754 scopus 로고    scopus 로고
    • The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes
    • de Nadal, E., Zapater, M., Alepuz, P.M., Sumoy, L., Mas, G., and Posas, F. 2004. The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes. Nature (London), 427: 370-374.
    • (2004) Nature (London) , vol.427 , pp. 370-374
    • De Nadal, E.1    Zapater, M.2    Alepuz, P.M.3    Sumoy, L.4    Mas, G.5    Posas, F.6
  • 23
    • 0036510384 scopus 로고    scopus 로고
    • In vivo changes of nucleosome positioning in the pretranscription state
    • Di Mauro, E., Verdone, L., Chiappini, B., and Caserta, M. 2002. In vivo changes of nucleosome positioning in the pretranscription state. J. Biol. Chem. 277: 7002-7009.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7002-7009
    • Di Mauro, E.1    Verdone, L.2    Chiappini, B.3    Caserta, M.4
  • 24
    • 0036211013 scopus 로고    scopus 로고
    • Histone acetylation: A switch between repressive and permissive chromatin
    • Eberharter, A., and Becker, P.B. 2002. Histone acetylation: a switch between repressive and permissive chromatin. EMBO Rep. 3: 224-229
    • (2002) EMBO Rep. , vol.3 , pp. 224-229
    • Eberharter, A.1    Becker, P.B.2
  • 25
    • 4444320809 scopus 로고    scopus 로고
    • MAP kinases as structural adaptors and enzymatic activators in transcription complexes
    • Edmunds, J.W., and Mahadevan, L.C. 2004. MAP kinases as structural adaptors and enzymatic activators in transcription complexes. J. Cell Sci. 117: 3715-3723.
    • (2004) J. Cell Sci. , vol.117 , pp. 3715-3723
    • Edmunds, J.W.1    Mahadevan, L.C.2
  • 26
    • 1042278765 scopus 로고    scopus 로고
    • The history of cancer epigenetics
    • Feinberg, A.P., and Tycko, B. 2004. The history of cancer epigenetics. Nature (London), 4: 143-153.
    • (2004) Nature (London) , vol.4 , pp. 143-153
    • Feinberg, A.P.1    Tycko, B.2
  • 28
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle, W., Wang, Y., and Allis, C.D. 20036. Binary switches and modification cassettes in histone biology and beyond. Nature (London), 425: 475-479.
    • (2003) Nature (London) , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 29
    • 0029046603 scopus 로고
    • Modulation of chromatin folding by histone acetylation
    • Garcia-Ramirez, M., Rocchini, C., and Ausio, J. 1995. Modulation of chromatin folding by histone acetylation. J. Biol. Chem. 270: 17923-17928.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17923-17928
    • Garcia-Ramirez, M.1    Rocchini, C.2    Ausio, J.3
  • 30
    • 0842263749 scopus 로고    scopus 로고
    • Roles of SWI/SNF and HATs throuhgout the dynamic transcription of a yeast glucose-repressible gene
    • Geng, F., and Laurent, B.C. 2004. Roles of SWI/SNF and HATs throuhgout the dynamic transcription of a yeast glucose-repressible gene. EMBO J. 23: 127-137.
    • (2004) EMBO J. , vol.23 , pp. 127-137
    • Geng, F.1    Laurent, B.C.2
  • 31
    • 0026783834 scopus 로고
    • Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription
    • Georgakopoulos, T., and Thireos, G. 1992. Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J. 11: 4145-152.
    • (1992) EMBO J. , vol.11 , pp. 4145-4152
    • Georgakopoulos, T.1    Thireos, G.2
  • 32
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass, C.K., and Rosenfeld, M.G. 2000. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 14: 121-141.
    • (2000) Genes Dev. , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 33
    • 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, P.A., Duggan, L., Cote, J., Roberts, S.M., Brownell, I.E., Candau, R. et al. 1997. Yeast GCN5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev. 11: 1640-1650.
    • (1997) Genes Dev. , vol.11 , pp. 1640-1650
    • Grant, P.A.1    Duggan, L.2    Cote, J.3    Roberts, S.M.4    Brownell, I.E.5    Candau, R.6
  • 34
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. 1997. Histone acetylation in chromatin structure and transcription. Nature (London), 389: 349-352.
    • (1997) Nature (London) , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 35
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms and functions
    • Hansen, J.C. 2002. Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms and functions. Annu. Rev. Biophys. Biomol. Struct. 31: 361-369.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 361-369
    • Hansen, J.C.1
  • 36
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • Hassan, A.H., Prochasson, P., Neely, K.E., Galasinski, S.C., Chandy, M., Carrozza, M.J., and Workman, J.L. 2002. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell, 111: 369-379.
    • (2002) Cell , vol.111 , pp. 369-379
    • Hassan, A.H.1    Prochasson, P.2    Neely, K.E.3    Galasinski, S.C.4    Chandy, M.5    Carrozza, M.J.6    Workman, J.L.7
  • 37
    • 0033571221 scopus 로고    scopus 로고
    • Cloning and analysis of Toxolasma gondii histone acetyltransferase: A novel chromatin remodelling factor in Apicomplexan parasites
    • Hettmann, C., and Soldati, D. 1999. Cloning and analysis of Toxolasma gondii histone acetyltransferase: a novel chromatin remodelling factor in Apicomplexan parasites. Nucleic Acids Res. 27: 4344-4352.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4344-4352
    • Hettmann, C.1    Soldati, D.2
  • 38
    • 0032744688 scopus 로고    scopus 로고
    • TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinary and contains a histone-specific acetyltransferase activity
    • Hsieh, Y.J., Kundu, T.K., Wang, Z., Kovelman, R., and Roeder, R.G. 1999. TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinary and contains a histone-specific acetyltransferase activity. Mol. Cell. Biol. 19: 7697-7704.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7697-7704
    • Hsieh, Y.J.1    Kundu, T.K.2    Wang, Z.3    Kovelman, R.4    Roeder, R.G.5
  • 39
    • 0034387879 scopus 로고    scopus 로고
    • Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
    • Hudson, B.P., Martinez-Yamout, M.A., Dyson, H.J., and Wright, P.E. 2000. Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J. Mol. Biol. 304: 355-370.
    • (2000) J. Mol. Biol. , vol.304 , pp. 355-370
    • Hudson, B.P.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 41
    • 1542285166 scopus 로고    scopus 로고
    • A genome-wide housekeeping role for TFIID and a highly regulated stress-related role for SAGA in Saccharomyces cerevisiae
    • Huisinga, K.L., and Pugh, B.F. 2004. A genome-wide housekeeping role for TFIID and a highly regulated stress-related role for SAGA in Saccharomyces cerevisiae. Mol. Cell 13: 573-585.
    • (2004) Mol. Cell , vol.13 , pp. 573-585
    • Huisinga, K.L.1    Pugh, B.F.2
  • 42
    • 0033551686 scopus 로고    scopus 로고
    • Histone acetyltransferase HBO1 interacts with ORC1 subunit of the human initiator protein
    • Iizuka, M., and Stillman B. 1999. Histone acetyltransferase HBO1 interacts with ORC1 subunit of the human initiator protein. J. Biol. Chem. 274: 23027-23034.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23027-23034
    • Iizuka, M.1    Stillman, B.2
  • 43
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • Ikura, T., Ogryzko, V.V., Grigoriev, M., Groisman, R., Wang, J., Horikoshi, M. et al. 2000. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell, 102: 463-473
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1    Ogryzko, V.V.2    Grigoriev, M.3    Groisman, R.4    Wang, J.5    Horikoshi, M.6
  • 44
    • 0031865050 scopus 로고    scopus 로고
    • Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo
    • Kadosh, D., and Struhl, K. 1998. Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo. Mol. Cell. Biol. 18: 5121-5127.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5121-5127
    • Kadosh, D.1    Struhl, K.2
  • 45
    • 1442285891 scopus 로고    scopus 로고
    • Loss of CBP causes T cell lymphomagenesis in synergy with p27Kip1 insuficiency
    • Kang-Decker, N., Tong, C., Boussouar, F., Baker, D.J., Xu, W., Leontovich, A.A. et al. 2004. Loss of CBP causes T cell lymphomagenesis in synergy with p27Kip1 insuficiency. Cancer Cell, 5: 177-189.
    • (2004) Cancer Cell , vol.5 , pp. 177-189
    • Kang-Decker, N.1    Tong, C.2    Boussouar, F.3    Baker, D.J.4    Xu, W.5    Leontovich, A.A.6
  • 46
    • 1642564551 scopus 로고    scopus 로고
    • Selective recognition of acetylated histones by bromodomain proteins visualized in living cells
    • Kanno, T., Kanno, Y., Siegel, R.M., Jang, M.K., Lenardo, M.J., and Ozato, K. 2004. Selective recognition of acetylated histones by bromodomain proteins visualized in living cells. Mol. Cell 13: 33-43.
    • (2004) Mol. Cell , vol.13 , pp. 33-43
    • Kanno, T.1    Kanno, Y.2    Siegel, R.M.3    Jang, M.K.4    Lenardo, M.J.5    Ozato, K.6
  • 47
    • 0033568312 scopus 로고    scopus 로고
    • ATP-dependent remodeling and acetylation as regulators of chromatin fluidity
    • Kingston, R.E., and Narlikar, G.J. 1999. ATP-dependent remodeling and acetylation as regulators of chromatin fluidity. Genes Dev. 13: 2339-2352.
    • (1999) Genes Dev. , vol.13 , pp. 2339-2352
    • Kingston, R.E.1    Narlikar, G.J.2
  • 48
    • 0028885077 scopus 로고
    • Identification of a gene encoding a yeast histone H4 acetyltransferase
    • Kleff, S., Andrulis, E.D., Anderson, C.W., and Sternglanz, R. 1995. Identification of a gene encoding a yeast histone H4 acetyltransferase. J. Biol. Chem. 270: 24674-24677.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24674-24677
    • Kleff, S.1    Andrulis, E.D.2    Anderson, C.W.3    Sternglanz, R.4
  • 49
    • 0033602995 scopus 로고    scopus 로고
    • Different types of maize histone deacetylases are distinguished by a highly complex substrate and site specificity
    • Kolle, D., Brosch, G., Lechner, T., Pipal, A., Helliger, W., Taplick, J., and Loidl, G. 1999. Different types of maize histone deacetylases are distinguished by a highly complex substrate and site specificity. Biochemistry, 38: 6769-6773.
    • (1999) Biochemistry , vol.38 , pp. 6769-6773
    • Kolle, D.1    Brosch, G.2    Lechner, T.3    Pipal, A.4    Helliger, W.5    Taplick, J.6    Loidl, G.7
  • 50
    • 0032579292 scopus 로고    scopus 로고
    • Transcription factor-specific requirements for coactivators and their acetyltransferase functions
    • Korzus, E., Torchia, J., Rose, D.W., Xu, L., Kurokawa, R., McInerney, E.M. et al. 1998. Transcription factor-specific requirements for coactivators and their acetyltransferase functions. Science (Wash.), 279: 703-707.
    • (1998) Science (Wash.) , vol.279 , pp. 703-707
    • Korzus, E.1    Torchia, J.2    Rose, D.W.3    Xu, L.4    Kurokawa, R.5    McInerney, E.M.6
  • 51
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides, T. 2000. Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19: 1176-1179.
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 52
    • 0036809640 scopus 로고    scopus 로고
    • Transcriptional inhibition of genes with severe histone H3 hypoacetylation in the coding region
    • Kristjuhan, A., Walker, J., Suka, N., Grunstein, M., Roberts, D., Cairns, B.R., and Svejstrup, J.Q. 2002. Transcriptional inhibition of genes with severe histone H3 hypoacetylation in the coding region. Mol. Cell 10: 925-933.
    • (2002) Mol. Cell , vol.10 , pp. 925-933
    • Kristjuhan, A.1    Walker, J.2    Suka, N.3    Grunstein, M.4    Roberts, D.5    Cairns, B.R.6    Svejstrup, J.Q.7
  • 53
    • 0032907345 scopus 로고    scopus 로고
    • Human TFIIIC relieves chromatin-mediated repression of RNA polymerase III transcription and contains an intrinsic histone acetyltransferase activity
    • Kundu, T.K., Wang, Z., and Roeder, R.G. 1999. Human TFIIIC relieves chromatin-mediated repression of RNA polymerase III transcription and contains an intrinsic histone acetyltransferase activity. Mol. Cell. Biol. 19: 1605-1615.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1605-1615
    • Kundu, T.K.1    Wang, Z.2    Roeder, R.G.3
  • 56
    • 0036649756 scopus 로고    scopus 로고
    • Genome-wide binding map of the histone deacetylase Rpd3 in yeast
    • Kurdistani, S.K., Robyr, D., Tavazoie, S., and Grunstein, M. 2002. Genome-wide binding map of the histone deacetylase Rpd3 in yeast. Nat. Genet. 31: 248-254.
    • (2002) Nat. Genet. , vol.31 , pp. 248-254
    • Kurdistani, S.K.1    Robyr, D.2    Tavazoie, S.3    Grunstein, M.4
  • 57
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global histone acetylation patterns to gene expression
    • Kurdistani, S.K., Tavazoie, S., and Grunstein, M. 2004. Mapping global histone acetylation patterns to gene expression. Cell, 117: 721-733.
    • (2004) Cell , vol.117 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 58
    • 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, B.J., Dayton, M.A., and Blanchard, K.L. 1998. Acute mixed lineage leukemia with an inv(8)(p11q13) resulting in fusion of the genes for MOZ and TIF2. Blood, 92: 2118-2122.
    • (1998) Blood , vol.92 , pp. 2118-2122
    • Liang, J.1    Prouty, L.2    Williams, B.J.3    Dayton, M.A.4    Blanchard, K.L.5
  • 59
    • 0038820074 scopus 로고    scopus 로고
    • Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation
    • Liu, X., Tesfai, J., Evrard, Y.A., Dent, S.Y., and Martinez, E. 2003. c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation. J. Biol. Chem. 278: 20405-20412.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20405-20412
    • Liu, X.1    Tesfai, J.2    Evrard, Y.A.3    Dent, S.Y.4    Martinez, E.5
  • 60
    • 0035929147 scopus 로고    scopus 로고
    • Nucleosome sliding via TBP DNA binding in vivo
    • Lomvardas, S., and Thanos, D. 2001. Nucleosome sliding via TBP DNA binding in vivo. Cell, 106: 685-696.
    • (2001) Cell , vol.106 , pp. 685-696
    • Lomvardas, S.1    Thanos, D.2
  • 61
    • 0035012326 scopus 로고    scopus 로고
    • P300 forms a stable, template-committed complex with chromatin: Role for the bromodomain
    • Manning, E.T., Ikehara, T., Ito, T., Kadonaga, J.T., and Kraus, W.L. 2001. P300 forms a stable, template-committed complex with chromatin: role for the bromodomain. Mol. Cell. Biol. 21: 3876-3887.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3876-3887
    • Manning, E.T.1    Ikehara, T.2    Ito, T.3    Kadonaga, J.T.4    Kraus, W.L.5
  • 63
  • 64
    • 0034812915 scopus 로고    scopus 로고
    • Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo
    • Martinez, E., Palhan, V.B., Tjernberg, A., Lymar, E.S., Gamper, A.M., Kundu, T.K. et al. 2001. Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. Mol. Cell. Biol. 21: 6782-6795.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6782-6795
    • Martinez, E.1    Palhan, V.B.2    Tjernberg, A.3    Lymar, E.S.4    Gamper, A.M.5    Kundu, T.K.6
  • 65
    • 3042801306 scopus 로고    scopus 로고
    • Precise nucleosome positioning and the TATA box dictate requirements for the histone H4 tail and the bromodomain factor Bdf1
    • Martinez-Campa, C., Politis, P., Moreau, J.-L., Kent, N., Goodall, J., Mellor, J., and Goding, C.R. 2004. Precise nucleosome positioning and the TATA box dictate requirements for the histone H4 tail and the bromodomain factor Bdf1. Mol. Cell, 15: 69-81.
    • (2004) Mol. Cell , vol.15 , pp. 69-81
    • Martinez-Campa, C.1    Politis, P.2    Moreau, J.-L.3    Kent, N.4    Goodall, J.5    Mellor, J.6    Goding, C.R.7
  • 67
    • 0032493894 scopus 로고    scopus 로고
    • The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins
    • McMahon, S.B., Van Buskirk, H.A., Dugan, K.A., Copeland, T.D., and Cole, M.D. 1998. The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins. Cell, 94: 363-374.
    • (1998) Cell , vol.94 , pp. 363-374
    • McMahon, S.B.1    Van Buskirk, H.A.2    Dugan, K.A.3    Copeland, T.D.4    Cole, M.D.5
  • 68
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Métivier, R., Penot, G., Hübner, M.R., Reid, G., Brand, H., Kos, M., and Gannon, F. 2003. Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell, 115: 751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Métivier, R.1    Penot, G.2    Hübner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 69
    • 20844451181 scopus 로고    scopus 로고
    • Transcriptional complexes engaged by apo-estrogen receptor-α isoforms have divergent outcomes
    • Métivier, R., Penot, G., Carmouche, R.P., Hübner, M.R., Reid, G., Denger, S. et al. 2004. Transcriptional complexes engaged by apo-estrogen receptor-α isoforms have divergent outcomes. EMBO J. 23: 3653-3666.
    • (2004) EMBO J. , vol.23 , pp. 3653-3666
    • Métivier, R.1    Penot, G.2    Carmouche, R.P.3    Hübner, M.R.4    Reid, G.5    Denger, S.6
  • 70
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand, J., Zambetti, G.P., Olson, D.C., George, D., and Levine, A.J. 1992. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell, 69: 1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 71
    • 0042567276 scopus 로고    scopus 로고
    • Inhibition of MMTV transcription by HADC inhibitors occurs independent of changes in chromatin remodelling and histone acetylation
    • Mulholland, N.M., Soeth, E., and Smith, C.L. 2003. Inhibition of MMTV transcription by HADC inhibitors occurs independent of changes in chromatin remodelling and histone acetylation. Oncogene, 22: 4807-4818.
    • (2003) Oncogene , vol.22 , pp. 4807-4818
    • Mulholland, N.M.1    Soeth, E.2    Smith, C.L.3
  • 72
    • 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., Tatsumi, K., Ishii, M., Taki, T. et al. 2001. Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome. Hum. Mol. Genet. 10: 1071-1076.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1071-1076
    • Murata, T.1    Kurokawa, R.2    Krones, A.3    Tatsumi, K.4    Ishii, M.5    Taki, T.6
  • 73
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • Ng, H.H., Xu, R.M., Zhang, Y., and Struhl, K. 2002. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. J. Biol. Chem. 277: 34655-34657.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 74
    • 3342979659 scopus 로고    scopus 로고
    • Recruitment of the NuA4 complex poises the PHO5 promoter for chormatin remodeling and activation
    • Nourani, A., Utley, R.T., Allard, S., and Côté, J. 2004. Recruitment of the NuA4 complex poises the PHO5 promoter for chormatin remodeling and activation. EMBO J. 23: 2597-2607.
    • (2004) EMBO J. , vol.23 , pp. 2597-2607
    • Nourani, A.1    Utley, R.T.2    Allard, S.3    Côté, J.4
  • 76
    • 0034161329 scopus 로고    scopus 로고
    • Mapping chromosomal proteins in vivo by formaldehyde-crosslinked- chromatin immunoprecipitation
    • Orlando, V. 2000. Mapping chromosomal proteins in vivo by formaldehyde-crosslinked-chromatin immunoprecipitation. Trends Biochem. Sci. 25: 99-104.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 99-104
    • Orlando, V.1
  • 77
    • 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., De Bizemont, T., Dirac, A.M., Gustafsson, C.M. et al. 1999. Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Mol. Cell, 3: 109-118.
    • (1999) Mol. Cell , vol.3 , pp. 109-118
    • Otero, G.1    Fellows, J.2    Li, T.3    De Bizemont, T.4    Dirac, A.M.5    Gustafsson, C.M.6
  • 78
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodimain of histone acetyltransferase Gcn5p
    • Owen, D.J., Ornaghi, P., Yang, J.C., Lowe, N., Evans, P.R., Ballario, P. et al. 2000. The structural basis for the recognition of acetylated histone H4 by the bromodimain of histone acetyltransferase Gcn5p. EMBO J. 19: 6141-6149.
    • (2000) EMBO J. , vol.19 , pp. 6141-6149
    • Owen, D.J.1    Ornaghi, P.2    Yang, J.C.3    Lowe, N.4    Evans, P.R.5    Ballario, P.6
  • 79
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson, C.L., and Laniel, M.-A. 2004. Histones and histone modifications. Curr. Biol. 14: 546-551.
    • (2004) Curr. Biol. , vol.14 , pp. 546-551
    • Peterson, C.L.1    Laniel, M.-A.2
  • 80
    • 0029022770 scopus 로고
    • Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP
    • Petrij, F., Giles, R.H., Dauwerse, N., Saris, J.J., Hennekam, R.C., Masuno, M. et al. 1995. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature (London), 376: 348-351.
    • (1995) Nature (London) , vol.376 , pp. 348-351
    • Petrij, F.1    Giles, R.H.2    Dauwerse, N.3    Saris, J.J.4    Hennekam, R.C.5    Masuno, M.6
  • 81
    • 0031310741 scopus 로고    scopus 로고
    • Differential roles of p300 and PCAF acetyltransferases in muscle differentiation
    • Puri, P.L., Sartorelli, V., Yang, X.J., Hamamori, Y., Ogryzko, V.V., Howard, B.H. et al. 1997. Differential roles of p300 and PCAF acetyltransferases in muscle differentiation. Mol. Cell, 1: 35-45.
    • (1997) Mol. Cell , vol.1 , pp. 35-45
    • Puri, P.L.1    Sartorelli, V.2    Yang, X.J.3    Hamamori, Y.4    Ogryzko, V.V.5    Howard, B.H.6
  • 82
    • 0036286677 scopus 로고    scopus 로고
    • Human estrogen receptor-alpha: Regulation by synthesis, modification and degradation
    • Reid, G., Denger, S., Kos, M., and Gannon. F. 2002. Human estrogen receptor-alpha: regulation by synthesis, modification and degradation. Cell Mol. Life Sci. 59: 821-831.
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 821-831
    • Reid, G.1    Denger, S.2    Kos, M.3    Gannon, F.4
  • 83
    • 0038094502 scopus 로고    scopus 로고
    • Histones are first hyperacetylated and then lose contact with the activated PHO5 promoter
    • Reinke, H., and Hörz, W. 2003. Histones are first hyperacetylated and then lose contact with the activated PHO5 promoter. Mol. Cell 11: 1599-1607.
    • (2003) Mol. Cell , vol.11 , pp. 1599-1607
    • Reinke, H.1    Hörz, W.2
  • 84
    • 0037123767 scopus 로고    scopus 로고
    • Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases
    • Robyr, D., Suka, Y., Xenarios, I., Kurdistani, S.K., Wang, A., Suka, N., and Grunstein, M. 2002. Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell, 109: 437-446.
    • (2002) Cell , vol.109 , pp. 437-446
    • Robyr, D.1    Suka, Y.2    Xenarios, I.3    Kurdistani, S.K.4    Wang, A.5    Suka, N.6    Grunstein, M.7
  • 85
    • 2342464348 scopus 로고    scopus 로고
    • Type I 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., Villamor, N., Esteve, J., Costa, D. et al. 2004. Type I MOZ/CBP (MYST3/CREBBP) is the most common chimeric transcript in acute myeloid leukemia with t(8;16)(p11;p13) translocation. Genes Chromosomes Cancer, 40: 140-145.
    • (2004) Genes Chromosomes Cancer , vol.40 , pp. 140-145
    • Rozman, M.1    Camos, M.2    Colomer, D.3    Villamor, N.4    Esteve, J.5    Costa, D.6
  • 86
    • 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, A.B., Sendra, R., Galiana, M., Pamblanco, M., Perez-Ortin, I.E., and Tordela, V. 1998. HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4. J. Biol. Chem. 273: 12599-12605.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12599-12605
    • Ruiz-Garcia, A.B.1    Sendra, R.2    Galiana, M.3    Pamblanco, M.4    Perez-Ortin, I.E.5    Tordela, V.6
  • 87
    • 2642570305 scopus 로고    scopus 로고
    • The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote
    • Schübeler, D., MacAlpine, D.M., Scalzo, D., Wirbelauer, C., Kooperberg, C., van Leeuwen, F. et al. 2004. The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes Dev. 18: 1263-1271.
    • (2004) Genes Dev. , vol.18 , pp. 1263-1271
    • Schübeler, D.1    MacAlpine, D.M.2    Scalzo, D.3    Wirbelauer, C.4    Kooperberg, C.5    Van Leeuwen, F.6
  • 88
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang, Y., Hu, X., Di Renzo, J., Lazar, and Brown, M. 2000. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell, 103: 843-852.
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    Di Renzo, J.3    Lazar4    Brown, M.5
  • 89
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: Integrating signals with transcription factors and chromatin
    • Shikama, N., Lyon, J., and La Thangue, N.B. 1997. The p300/CBP family: integrating signals with transcription factors and chromatin. Trends Cell Biol. 7: 230-236.
    • (1997) Trends Cell Biol. , vol.7 , pp. 230-236
    • Shikama, N.1    Lyon, J.2    La Thangue, N.B.3
  • 91
    • 7644241815 scopus 로고    scopus 로고
    • ORC, MCM, and hyperacetylation at the Kaposi's sarcoma-associated herpesvirus latent replication origin
    • Stedman, W., Deng, Z., Lu, F., and Lieberman, P.M. 2004. ORC, MCM, and hyperacetylation at the Kaposi's sarcoma-associated herpesvirus latent replication origin. J. Virol. 78: 12566-12575.
    • (2004) J. Virol. , vol.78 , pp. 12566-12575
    • Stedman, W.1    Deng, Z.2    Lu, F.3    Lieberman, P.M.4
  • 92
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner, D.E., and Berger, S.L. 2000. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64: 435-459.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 93
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D., and Allis, C.D. 2000. The language of covalent histone modifications. Nature (London), 403: 41-45.
    • (2000) Nature (London) , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 94
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl, K. 1998. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 12: 599-606.
    • (1998) Genes Dev. , vol.12 , pp. 599-606
    • Struhl, K.1
  • 95
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun, Z.W., and Allis, C.D. 2002. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature (London), 418: 104-108.
    • (2002) Nature (London) , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 96
    • 0032814843 scopus 로고    scopus 로고
    • A general requirement for the Sin3-Rpd3 histone deacetylase complex in regulating silencing in Saccharomyces cerevisiae
    • Sun, Z.W., and Hampsey, M. 1999. A general requirement for the Sin3-Rpd3 histone deacetylase complex in regulating silencing in Saccharomyces cerevisiae. Genetics, 152: 921-932.
    • (1999) Genetics , vol.152 , pp. 921-932
    • Sun, Z.W.1    Hampsey, M.2
  • 97
    • 0034704815 scopus 로고    scopus 로고
    • The Gcn5 bromodomain co-ordinates nucleosome remodeling
    • Syntichaki, P., Topalidou, I., and Thireos, G. 2000. The Gcn5 bromodomain co-ordinates nucleosome remodeling. Nature (London), 404: 414-417.
    • (2000) Nature (London) , vol.404 , pp. 414-417
    • Syntichaki, P.1    Topalidou, I.2    Thireos, G.3
  • 99
    • 0025779831 scopus 로고
    • Histone acetylation and the control of gene expression
    • Turner, B.M. 1991. Histone acetylation and the control of gene expression. J. Cell Sci. 99: 13-20.
    • (1991) J. Cell Sci. , vol.99 , pp. 13-20
    • Turner, B.M.1
  • 100
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner, B.M. 2002. Cellular memory and the histone code. Cell, 111: 285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 102
    • 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., Kacherovsky, N., Vogelauer, M., Young, E.T. et al. 2002. Hyperacetylation of chromatin at the ADH2 promoter allows Adr1 to bind in repressed conditions. EMBO J. 21: 1101-1111.
    • (2002) EMBO J. , vol.21 , pp. 1101-1111
    • Verdone, L.1    Wu, J.2    Van Riper, K.3    Kacherovsky, N.4    Vogelauer, M.5    Young, E.T.6
  • 103
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase
    • Verreault, A., Kaufman, P.D., Kobayashi, R., and Stillman, B. 1998. Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. Curr. Biol. 8: 96-108.
    • (1998) Curr. Biol. , vol.8 , pp. 96-108
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 104
    • 0031036154 scopus 로고    scopus 로고
    • Histone acetyltransferase activity is conserved between yeast and human GCN5 and required for complementation of growth and transcriptional activation
    • Wang, L., Mizzen, C., Ying, C., Candau, R., Barlev, N., Brownell, J. et al. 1997. Histone acetyltransferase activity is conserved between yeast and human GCN5 and required for complementation of growth and transcriptional activation. Mol. Cell. Biol. 17: 519-527.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 519-527
    • Wang, L.1    Mizzen, C.2    Ying, C.3    Candau, R.4    Barlev, N.5    Brownell, J.6
  • 105
    • 0035918170 scopus 로고    scopus 로고
    • Effects of histone acetylation on the solubility and folding of the chromatin fiber
    • Wang, X., He, C., Moore, S.C., and Ausio, J. 2001. Effects of histone acetylation on the solubility and folding of the chromatin fiber. J. Biol. Chem. 276: 12764-12768.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12764-12768
    • Wang, X.1    He, C.2    Moore, S.C.3    Ausio, J.4
  • 106
    • 0035957097 scopus 로고    scopus 로고
    • Dynamics of histone acetylation in Saccharomyces cerevisiae
    • Waterborg, J.H. 2001. Dynamics of histone acetylation in Saccharomyces cerevisiae. Biochemistry, 40: 2599-2605.
    • (2001) Biochemistry , vol.40 , pp. 2599-2605
    • Waterborg, J.H.1
  • 107
    • 0032516156 scopus 로고    scopus 로고
    • Function of TAFII-containing complex without TBP in transcription by RNA polymerase II
    • Wieczorek, E., Brand, M., Jacq, X., and Tora, L. 1998. Function of TAFII-containing complex without TBP in transcription by RNA polymerase II. Nature (London), 393: 187-191.
    • (1998) Nature (London) , vol.393 , pp. 187-191
    • Wieczorek, E.1    Brand, M.2    Jacq, X.3    Tora, L.4
  • 108
    • 0033166761 scopus 로고    scopus 로고
    • A novel histone acetylatransferase is an integral subunit of elongating RNA polymerase II holoenzyme
    • Wittschieben, B., Otero, G., de Bizemont, T., Fellows, J., Erdjument-Bromage, H., Ohba, R. et al. 1999. A novel histone acetylatransferase is an integral subunit of elongating RNA polymerase II holoenzyme. Mol. Cell, 4: 123-128.
    • (1999) Mol. Cell , vol.4 , pp. 123-128
    • Wittschieben, B.1    Otero, G.2    De Bizemont, T.3    Fellows, J.4    Erdjument-Bromage, H.5    Ohba, R.6
  • 109
    • 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 D.G., and Roth, S.Y. 1998a. Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates. Mol. Cell. Biol. 18: 5659-5669.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5659-5669
    • Xu, W.1    Edmondson, D.G.2    Roth, S.Y.3
  • 111
    • 0030712311 scopus 로고    scopus 로고
    • Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60
    • Yamamoto, T., and Horikoshi M. 1997. Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60. J. Biol. Chem 272: 30595-30598.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30595-30598
    • Yamamoto, T.1    Horikoshi, M.2
  • 112
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: A new partnership for signalling
    • Yang, X.-J. 2004. Lysine acetylation and the bromodomain: a new partnership for signalling. BioEssays, 26: 1076-1087.
    • (2004) BioEssays , vol.26 , pp. 1076-1087
    • Yang, X.-J.1
  • 113
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral E1A oncoprotein
    • Yang, X.J., Ogryzko, V.V., Nishikawa, J., Howard, B.H., and Nakatani Y. 1996. A p300/CBP-associated factor that competes with the adenoviral E1A oncoprotein. Nature (London), 382: 319-324.
    • (1996) Nature (London) , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 114
    • 17644445419 scopus 로고    scopus 로고
    • Gene dosage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300
    • Yao, P.T., Oh, S.P., Fuchs, M., Zhou, N.D., Ch'ng L.E., Newsome, D. et al. 1998. Gene dosage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300. Cell, 93: 361-372.
    • (1998) Cell , vol.93 , pp. 361-372
    • Yao, P.T.1    Oh, S.P.2    Fuchs, M.3    Zhou, N.D.4    Ch'ng, L.E.5    Newsome, D.6
  • 115
    • 0032192502 scopus 로고    scopus 로고
    • Characterization of a human homologue of the Saccharomyces cerevisiae transcription factor spt3 (SUPT3H)
    • Yu, J., Madison, J.M., Mundlos, S., Winston, F., and Olsen, B.R. 1998. Characterization of a human homologue of the Saccharomyces cerevisiae transcription factor spt3 (SUPT3H). Genomics, 53: 90-96.
    • (1998) Genomics , vol.53 , pp. 90-96
    • Yu, J.1    Madison, J.M.2    Mundlos, S.3    Winston, F.4    Olsen, B.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.