메뉴 건너뛰기




Volumn 57, Issue 8-9, 2000, Pages 1184-1192

Regulation of gene expression by transcription factor acetylation

Author keywords

Acetylation; Acetyltransferase; Chromatin; Gene expression; Histones; Transcription factors

Indexed keywords

TRANSCRIPTION FACTOR;

EID: 0033837634     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00000758     Document Type: Review
Times cited : (132)

References (59)
  • 1
    • 0018267877 scopus 로고
    • The histone core complex: An octamer assembled by two sets of protein-protein interactions
    • 1 Eickbush T. H. and Moudrianakis E. N. (1978) The histone core complex: an octamer assembled by two sets of protein-protein interactions. Biochemistry 17: 4955-4964
    • (1978) Biochemistry , vol.17 , pp. 4955-4964
    • Eickbush, T.H.1    Moudrianakis, E.N.2
  • 2
    • 0033080794 scopus 로고    scopus 로고
    • Chromatin disruption and modification
    • 2 Wolffe A. P. and Hayes J. J. (1999) Chromatin disruption and modification. Nucleic Acids Res. 27: 711-720
    • (1999) Nucleic Acids Res. , vol.27 , pp. 711-720
    • Wolffe, A.P.1    Hayes, J.J.2
  • 3
    • 78651162036 scopus 로고
    • Acetylation and methylation of histories and their possible role in the regulation of RNA synthesis
    • 3 Allfrey V. G., Faulkner R. and Mirsky A. E. (1964) Acetylation and methylation of histories and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. USA 51: 786-794
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 4
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • 4 Hebbes T. R., Thorne A. W. and Crane Robinson C. (1988) A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 7: 1395-1402
    • (1988) EMBO J. , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane Robinson, C.3
  • 5
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • 5 Pazin M. J. and Kadonaga J. T. (1997) What's up and down with histone deacetylation and transcription? Cell 89: 325-328
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 6
    • 0027192267 scopus 로고
    • Transcriptional silencing in yeast is associated with reduced nucleosome acetylation
    • 6 Braunstein M., Rose A. B., Holmes S. G., Allis C. D. and Broach J. R. (1993) Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev. 7: 592-604
    • (1993) Genes Dev. , vol.7 , pp. 592-604
    • Braunstein, M.1    Rose, A.B.2    Holmes, S.G.3    Allis, C.D.4    Broach, J.R.5
  • 7
    • 0032101179 scopus 로고    scopus 로고
    • Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
    • 7 Zhang W., Bone J. R., Edmondson D. G., Turner B. M. and Roth S. Y. (1998) Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase. EMBO J. 17: 3155-3167
    • (1998) EMBO J. , vol.17 , pp. 3155-3167
    • Zhang, W.1    Bone, J.R.2    Edmondson, D.G.3    Turner, B.M.4    Roth, S.Y.5
  • 8
    • 0029123092 scopus 로고
    • Histone H4 and the maintenance of genome integrity
    • 8 Megee P. C., Morgan B. A. and Smith M. M. (1995) Histone H4 and the maintenance of genome integrity. Genes Dev. 9: 1716-1727
    • (1995) Genes Dev. , vol.9 , pp. 1716-1727
    • Megee, P.C.1    Morgan, B.A.2    Smith, M.M.3
  • 9
    • 0025736044 scopus 로고
    • Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
    • 9 Durrin L. K., Mann R. K., Kayne P. S. and Grunstein M. (1991) Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell 65: 1023-1031
    • (1991) Cell , vol.65 , pp. 1023-1031
    • Durrin, L.K.1    Mann, R.K.2    Kayne, P.S.3    Grunstein, M.4
  • 10
    • 1842411320 scopus 로고    scopus 로고
    • X-ray structure of the nucleosome core particle at 2.8 Å resolution
    • 10 Luger K., Maeder A. W., Richmond R. K., Sargent D. F. and Richmond T. J. (1997) X-ray structure of the nucleosome core particle at 2.8 Å resolution. Nature 389: 251-259
    • (1997) Nature , vol.389 , pp. 251-259
    • Luger, K.1    Maeder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 11
    • 0017403915 scopus 로고
    • Chromatin core particle unfolding induced by tryptic cleavage of histones
    • 11 Lilley D. M. and Tatchell K. (1977) Chromatin core particle unfolding induced by tryptic cleavage of histones. Nucleic Acids Res. 4: 2039-2055
    • (1977) Nucleic Acids Res. , vol.4 , pp. 2039-2055
    • Lilley, D.M.1    Tatchell, K.2
  • 12
    • 0020131558 scopus 로고
    • Participation of core histone 'tails' in the stabilization of the chromatin solenoid
    • 12 Allan J., Harborne N., Rau D. C. and Gould H. (1982) Participation of core histone 'tails' in the stabilization of the chromatin solenoid. J. Cell Biol. 93: 285-297
    • (1982) J. Cell Biol. , vol.93 , pp. 285-297
    • Allan, J.1    Harborne, N.2    Rau, D.C.3    Gould, H.4
  • 13
    • 0029805633 scopus 로고    scopus 로고
    • The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast
    • 13 De Rubertis F., Kadosh D., Henchoz S., Pauli D., Reuter G., Struhl K. et al. (1996) The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast. Nature 384: 589-591
    • (1996) Nature , vol.384 , pp. 589-591
    • De Rubertis, F.1    Kadosh, D.2    Henchoz, S.3    Pauli, D.4    Reuter, G.5    Struhl, K.6
  • 14
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • 14 Brownell J. E., Zhou J., Ranalli T., Kobayashi R., Edmondson D. G., Roth S. Y. et al. (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
  • 15
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • 15 Bannister A. J. and Kouzarides T. (1996) The CBP co-activator is a histone acetyltransferase. Nature 384: 641-643
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 16
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • 16 Ogryzko V. V., Schiltz R. L., Russanova V., Howard B. H. and Nakatani Y. (1996) The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87: 953-959
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 17
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • 17 Kouzarides T. (1999) Histone acetylases and deacetylases in cell proliferation. Curr. Opin. Genet. Dev. 9: 40-48
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 19
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein EIA
    • 19 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 oncoprotein EIA. Nature 382: 319-324
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 20
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor IID (TFIID)
    • 20 Burley S. K. and Roeder R. G. (1996) Biochemistry and structural biology of transcription factor IID (TFIID). Annu. Rev. Biochem. 65: 769-799
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 769-799
    • Burley, S.K.1    Roeder, R.G.2
  • 22
    • 0033166761 scopus 로고    scopus 로고
    • A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme
    • Erdjument-22
    • 22 Wittschieben B. O., Otero, G., de Bizemont, T., Fellows, J., Erdjument-22. Bromage, H., Ohba, R., et al. (1999) A novel histone acetyltransferase 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.O.1    Otero, G.2    De Bizemont, T.3    Fellows, J.4    Bromage, H.5    Ohba, R.6
  • 23
    • 0032504104 scopus 로고    scopus 로고
    • A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation
    • 23 Grant P. A., Schieltz, D., Pray Grant, M. G., Steger, D. J., Reese, J. C., Yates, J. R. III., et al. (1998) A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation. Cell 94: 45-53
    • (1998) Cell , vol.94 , pp. 45-53
    • Grant, P.A.1    Schieltz, D.2    Pray Grant, M.G.3    Steger, D.J.4    Reese, J.C.5    Yates J.R. III6
  • 25
    • 0032503940 scopus 로고    scopus 로고
    • The TAFs in the HAT
    • 25 Struhl K. and Moqtaderi Z. (1998) The TAFs in the HAT. Cell 94: 1-4
    • (1998) Cell , vol.94 , pp. 1-4
    • Struhl, K.1    Moqtaderi, Z.2
  • 26
    • 0032814140 scopus 로고    scopus 로고
    • Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins
    • 26 Bustin M. (1999) Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins. Mol. Cell Biol. 19: 5237-5246
    • (1999) Mol. Cell Biol. , vol.19 , pp. 5237-5246
    • Bustin, M.1
  • 27
    • 0029617947 scopus 로고
    • Virus induction of human IFN beta gene expression requires the assembly of an enhanceosome
    • 27 Thanos D. and Maniatis T. (1995) Virus induction of human IFN beta gene expression requires the assembly of an enhanceosome. Cell 83: 1091-1100
    • (1995) Cell , vol.83 , pp. 1091-1100
    • Thanos, D.1    Maniatis, T.2
  • 28
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome
    • 28 Munshi N., Merika M., Yie J., Senger K., Chen G. and Thanos D. (1998) Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. Mol. Cell 2: 457-467
    • (1998) Mol. Cell , vol.2 , pp. 457-467
    • Munshi, N.1    Merika, M.2    Yie, J.3    Senger, K.4    Chen, G.5    Thanos, D.6
  • 29
    • 0032971444 scopus 로고    scopus 로고
    • Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFN-beta promoter
    • 29 Parekh B. S. and Maniatis T. (1999) Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFN-beta promoter. Mol. Cell 3: 125-129
    • (1999) Mol. Cell , vol.3 , pp. 125-129
    • Parekh, B.S.1    Maniatis, T.2
  • 30
    • 0032933141 scopus 로고    scopus 로고
    • Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes
    • 30 Herrera J. E., Sakaguchi K., Bergel M., Trieschmann L., Nakatani Y. and Bustin M. (1999) Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes. Mol. Cell Biol. 19: 3466-3473
    • (1999) Mol. Cell Biol. , vol.19 , pp. 3466-3473
    • Herrera, J.E.1    Sakaguchi, K.2    Bergel, M.3    Trieschmann, L.4    Nakatani, Y.5    Bustin, M.6
  • 31
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • 31 Imhof A., Yang X. J., Ogryzko V. V., Nakatani Y., Wolffe A. P. and Ge H. (1997) Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 7: 689-692
    • (1997) Curr. Biol. , vol.7 , pp. 689-692
    • Imhof, A.1    Yang, X.J.2    Ogryzko, V.V.3    Nakatani, Y.4    Wolffe, A.P.5    Ge, H.6
  • 32
    • 0025988495 scopus 로고
    • Activation of gene transcription by regulatory factors is potentiated by a novel activity
    • 32 Meisterernst M., Roy A. L., Lieu H. M. and Roeder R. G. (1991) Activation of gene transcription by regulatory factors is potentiated by a novel activity. Cell 66: 981-993
    • (1991) Cell , vol.66 , pp. 981-993
    • Meisterernst, M.1    Roy, A.L.2    Lieu, H.M.3    Roeder, R.G.4
  • 33
    • 0027284478 scopus 로고
    • Unique TATA-binding protein-containing complexes and cofactors involved in transcription by RNA polymerases II and III
    • 33 Chiang C. M., Ge H., Wang Z., Hoffmann A. and Roeder R. G. (1993) Unique TATA-binding protein-containing complexes and cofactors involved in transcription by RNA polymerases II and III. EMBO J. 12: 2749-2762
    • (1993) EMBO J. , vol.12 , pp. 2749-2762
    • Chiang, C.M.1    Ge, H.2    Wang, Z.3    Hoffmann, A.4    Roeder, R.G.5
  • 34
    • 0024280897 scopus 로고
    • O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation
    • 34 Jackson S. P. and Tjian R. (1988) O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation. Cell 55: 125-133
    • (1988) Cell , vol.55 , pp. 125-133
    • Jackson, S.P.1    Tjian, R.2
  • 35
    • 0033027346 scopus 로고    scopus 로고
    • Covalent and noncovalent modifiers of the p53 protein
    • 35 Jayaraman L. and Prives C. (1999) Covalent and noncovalent modifiers of the p53 protein. Cell. Mol. Life Sci. 55: 76-87
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 76-87
    • Jayaraman, L.1    Prives, C.2
  • 36
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • 36 Gu W. and Roeder R. G. (1997) Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90: 595-606
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 37
    • 0032530486 scopus 로고    scopus 로고
    • DNA damage activates p53 through a phosphorylation-acetylation cascade
    • 37 Sakaguchi K., Herrera J. E., Saito S., Miki T., Bustin M., Vassilev A. et al. (1998) DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev. 12: 2831-2841
    • (1998) Genes Dev. , vol.12 , pp. 2831-2841
    • Sakaguchi, K.1    Herrera, J.E.2    Saito, S.3    Miki, T.4    Bustin, M.5    Vassilev, A.6
  • 38
    • 0032906633 scopus 로고    scopus 로고
    • p53 Sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage
    • 38 Liu L., Scolnick D. M., Trievel R. C., Zhang H. B., Marmorstein R., Halazonetis T. D. et al. (1999) p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Mol. Cell Biol. 19: 1202-1209
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1202-1209
    • Liu, L.1    Scolnick, D.M.2    Trievel, R.C.3    Zhang, H.B.4    Marmorstein, R.5    Halazonetis, T.D.6
  • 39
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • 39 Gu W., Shi X. L. and Roeder R. G. (1997) Synergistic activation of transcription by CBP and p53. Nature 387: 819-823
    • (1997) Nature , vol.387 , pp. 819-823
    • Gu, W.1    Shi, X.L.2    Roeder, R.G.3
  • 40
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • 40 Boyes J., Byfield P., Nakatani Y. and Ogryzko V. (1998) Regulation of activity of the transcription factor GATA-1 by acetylation. Nature 396: 594-598
    • (1998) Nature , vol.396 , pp. 594-598
    • Boyes, J.1    Byfield, P.2    Nakatani, Y.3    Ogryzko, V.4
  • 41
    • 0032544123 scopus 로고    scopus 로고
    • Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases
    • 41 Zhang W. and Bieker J. J. (1998) Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc. Natl. Acad. Sci. USA 95: 9855-9860
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9855-9860
    • Zhang, W.1    Bieker, J.J.2
  • 42
    • 0032910957 scopus 로고    scopus 로고
    • CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites
    • 42 Huang H. L., Lau J., Kim A. Y., Weiss M. J. and Blobel G. A. (1999) CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites. Mol. Cell Biol. 19: 3496-3505
    • (1999) Mol. Cell Biol. , vol.19 , pp. 3496-3505
    • Huang, H.L.1    Lau, J.2    Kim, A.Y.3    Weiss, M.J.4    Blobel, G.A.5
  • 43
    • 0033231604 scopus 로고    scopus 로고
    • Acetylation of MyoD directed by PCAF is necessary for the exectution of the muscle program
    • 43 Sartorelli V., Puri P. L., Hamamori Y., Ogryzko V., Chung G., Nakatani Y. et al. (1999) Acetylation of MyoD directed by PCAF is necessary for the exectution of the muscle program. Mol. Cell 4: 725-734
    • (1999) Mol. Cell , vol.4 , pp. 725-734
    • Sartorelli, V.1    Puri, P.L.2    Hamamori, Y.3    Ogryzko, V.4    Chung, G.5    Nakatani, Y.6
  • 45
    • 0032189630 scopus 로고    scopus 로고
    • Drosophilia CBP represses the transcription factor TCF to antagonize Wingless signalling
    • 44 Walzer L. and Bienz M. (1998) Drosophilia CBP represses the transcription factor TCF to antagonize Wingless signalling. Nature 395: 521-525
    • (1998) Nature , vol.395 , pp. 521-525
    • Walzer, L.1    Bienz, M.2
  • 46
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • 45 Chen H., Lin R. J., Xie W., Wilpitz, D. and Evans R. M. (1999) Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 98: 675-686
    • (1999) Cell , vol.98 , pp. 675-686
    • Chen, H.1    Lin, R.J.2    Xie, W.3    Wilpitz, D.4    Evans, R.M.5
  • 47
    • 0030870910 scopus 로고    scopus 로고
    • The histone acetyltransferase activity of human GCN5 and PCAF is stabilized by coenzymes
    • 46 Herrera J. E., Bergel M., Yang X. J., Nakatani Y. and Bustin M. (1997) The histone acetyltransferase activity of human GCN5 and PCAF is stabilized by coenzymes. J. Biol. Chem. 272: 27253-27258
    • (1997) J. Biol. Chem. , vol.272 , pp. 27253-27258
    • Herrera, J.E.1    Bergel, M.2    Yang, X.J.3    Nakatani, Y.4    Bustin, M.5
  • 48
    • 0033524942 scopus 로고    scopus 로고
    • A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity
    • 47 Chakravarti D., Ogryzko V., Kao H. Y., Nash A., Chen H., Nakatani Y. et al. (1999) A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity. Cell 96: 393-403
    • (1999) Cell , vol.96 , pp. 393-403
    • Chakravarti, D.1    Ogryzko, V.2    Kao, H.Y.3    Nash, A.4    Chen, H.5    Nakatani, Y.6
  • 49
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • 48 Kuo M. H. and Allis C. D. (1998) Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20: 615-626
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 50
    • 0033517354 scopus 로고    scopus 로고
    • Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide
    • 49 Rojas J.R., Trievel R.C., Zhou J., Mo Y., Li X., Berger S.L. et al. (1999) Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Nature 401: 93-98
    • (1999) Nature , vol.401 , pp. 93-98
    • Rojas, J.R.1    Trievel, R.C.2    Zhou, J.3    Mo, Y.4    Li, X.5    Berger, S.L.6
  • 51
    • 0034177669 scopus 로고    scopus 로고
    • Acetylation of the importin-α family of nuclear import factors by CBP/p300
    • 50 Bannister A. J., Miska E. A., Gorlich D. and Kouzarides T. (2000) Acetylation of the importin-α family of nuclear import factors by CBP/p300. Curr. Biol. 10: 467-470
    • (2000) Curr. Biol. , vol.10 , pp. 467-470
    • Bannister, A.J.1    Miska, E.A.2    Gorlich, D.3    Kouzarides, T.4
  • 52
    • 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
    • 51 Grant P. A., Duggan L., Cote J., Roberts S. M., Brownell J. 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, J.E.5    Candau, R.6
  • 53
    • 0032483380 scopus 로고    scopus 로고
    • CBP: A signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV
    • 52 Chawla S., Hardingham G. E., Quinn D. R. and Bading H. (1998) CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV. Science 281: 1505-1509
    • (1998) Science , vol.281 , pp. 1505-1509
    • Chawla, S.1    Hardingham, G.E.2    Quinn, D.R.3    Bading, H.4
  • 54
    • 0029010417 scopus 로고
    • Phosphorylation of the adenovirus E1A-associated 300 kDa protein in response to retinoic acid and E1A during the differentiation of F9 cells
    • 53 Kitabayashi I., Eckner R., Arany Z., Chiu R., Gachelin G., Livingston D. M. et al. (1995) Phosphorylation of the adenovirus E1A-associated 300 kDa protein in response to retinoic acid and E1A during the differentiation of F9 cells. EMBO J. 14: 3496-3509
    • (1995) EMBO J. , vol.14 , pp. 3496-3509
    • Kitabayashi, I.1    Eckner, R.2    Arany, Z.3    Chiu, R.4    Gachelin, G.5    Livingston, D.M.6
  • 55
    • 0031913215 scopus 로고    scopus 로고
    • Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex
    • 54 Barlev N. A., Poltoratsky, V., Owen Hughes, T., Ying, C., Liu, L., Workman, J. L., et al. (1998) Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase 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    Workman, J.L.6
  • 56
    • 0032511884 scopus 로고    scopus 로고
    • Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A
    • 55 Ait-Si-Ali S., Ramirez S., Barre F. X., Dkhissi F., Magnaghi-Jaulin L., Girault J. A. et al. (1998) Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A. Nature 396: 184-186
    • (1998) Nature , vol.396 , pp. 184-186
    • Ait-Si-Ali, S.1    Ramirez, S.2    Barre, F.X.3    Dkhissi, F.4    Magnaghi-Jaulin, L.5    Girault, J.A.6
  • 58
    • 0033525094 scopus 로고    scopus 로고
    • Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oneoprotein E1A
    • 57 Hamamori Y., Sartorelli V., Ogryzko V., Puri P. L., Wu H. Y., Wang J. Y. et al. (1999) Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oneoprotein E1A. Cell 96: 405-413
    • (1999) Cell , vol.96 , pp. 405-413
    • Hamamori, Y.1    Sartorelli, V.2    Ogryzko, V.3    Puri, P.L.4    Wu, H.Y.5    Wang, J.Y.6
  • 59
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • 58 Dhalluin C., Carlson J. F., Zeng L., He C., Aggarwal A. K. and Zhou M. M. (1999) Structure and ligand of a histone acetyltransferase bromodomain. Nature 399: 491-496
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.F.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5    Zhou, M.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.