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Volumn 64, Issue 2, 2000, Pages 435-459

Acetylation of histones and transcription-related factors

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CELL NUCLEUS RECEPTOR; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; ERYTHROID KRUPPEL LIKE FACTOR; HISTONE; HISTONE ACETYLTRANSFERASE; PROTEIN P53; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR E2F; TRANSCRIPTION FACTOR GATA 1;

EID: 0034051227     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.64.2.435-459.2000     Document Type: Review
Times cited : (1478)

References (288)
  • 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., R. T. Utley, J. Savard, A. Clarke, P. Grant, C. J. Brandi, L. Pillus, J. L. Workman, and J. Côté. 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    Brandi, C.J.6    Pillus, L.7    Workman, J.L.8    Côté, J.9
  • 4
    • 0022365083 scopus 로고
    • Deposition-related histone acetylation in micronuclei of conjugating Tetrahymena
    • Allis, C. D., L. G. Chicoine, R. Richman, and I. G. Schulman. 1985. Deposition-related histone acetylation in micronuclei of conjugating Tetrahymena. Proc. Natl. Acad. Sci. USA 82:8048-8052.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8048-8052
    • Allis, C.D.1    Chicoine, L.G.2    Richman, R.3    Schulman, I.G.4
  • 5
    • 0033579559 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily
    • Angus-Hill, M. L., R. N. Dutnall, S. T. Tafrov, R. Sternglanz, and V. Ramakrishnan. 1999. Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily. J. Mol. Biol. 294:1311-1325.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1311-1325
    • Angus-Hill, M.L.1    Dutnall, R.N.2    Tafrov, S.T.3    Sternglanz, R.4    Ramakrishnan, V.5
  • 7
    • 0025900189 scopus 로고
    • Modifiers of position effect are shared between telomeric and silent mating-type loci in S. Cerevisiae
    • Aparicio, O. M., B. L. Billington, and D. E. Gottschling. 1991. Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae. Cell 66:1279-1287.
    • (1991) Cell , vol.66 , pp. 1279-1287
    • Aparicio, O.M.1    Billington, B.L.2    Gottschling, D.E.3
  • 8
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A. J., and T. Kouzarides. 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
  • 9
    • 0034177669 scopus 로고    scopus 로고
    • Acetylation of importin-α nuclear import factors by CBP/p300
    • Bannister, A. J., E. A. Miska, D. Görlich, and T. Kouzarides. 2000. Acetylation of importin-α 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    Görlich, D.3    Kouzarides, T.4
  • 10
    • 0029096813 scopus 로고
    • Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein
    • Barlev, N. A., R. Candau, L. Wang, P. Darpino, N. Silverman, and S. L. Berger. 1995. Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein. J. Biol. Chem. 270:19337-19344.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19337-19344
    • Barlev, N.A.1    Candau, R.2    Wang, L.3    Darpino, P.4    Silverman, N.5    Berger, S.L.6
  • 11
    • 0031913215 scopus 로고    scopus 로고
    • Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku/DNA-PKcs complex
    • Barlev, N. A., V. Poltoratsky, T. Owen-Hughes, C. Ying, L. Liu, T. Carter, J. L. Workman, and S. L. Berger. 1998. Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the 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    Workman, J.L.7    Berger, S.L.8
  • 12
    • 0027744166 scopus 로고
    • Yeast origin recognition complex functions in transcription silencing and DNA replication
    • Bell, S. P., R. Kobayashi, and B. Stillman. 1993. Yeast origin recognition complex functions in transcription silencing and DNA replication. Science 262:1844-1849.
    • (1993) Science , vol.262 , pp. 1844-1849
    • Bell, S.P.1    Kobayashi, R.2    Stillman, B.3
  • 13
    • 0026607331 scopus 로고
    • ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex
    • Bell, S. P., and B. Stillman. 1992. ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex. Nature 357:128-134.
    • (1992) Nature , vol.357 , pp. 128-134
    • Bell, S.P.1    Stillman, B.2
  • 14
    • 0033373603 scopus 로고    scopus 로고
    • Interplay between chromatin modifying and remodeling complexes in transcriptional regulation
    • Belotserkovskaya, R., and S. L. Berger. 1999. Interplay between chromatin modifying and remodeling complexes in transcriptional regulation. Crit. Rev. Eukaryot. Gene Expression 9:221-230.
    • (1999) Crit. Rev. Eukaryot. Gene Expression , vol.9 , pp. 221-230
    • Belotserkovskaya, R.1    Berger, S.L.2
  • 15
    • 0033957403 scopus 로고    scopus 로고
    • Inhibition of TATA-binding protein function by SAGA subunits Spt3 and Spt8 at Gcn4-activated promoters
    • Belotserkovskaya, R., D. E. Sterner, M. Deng, M. H. Sayre, P. M. Lieberman, and S. L. Berger. 2000. Inhibition of TATA-binding protein function by SAGA subunits Spt3 and Spt8 at Gcn4-activated promoters. Mol. Cell. Biol. 20:634-647.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 634-647
    • Belotserkovskaya, R.1    Sterner, D.E.2    Deng, M.3    Sayre, M.H.4    Lieberman, P.M.5    Berger, S.L.6
  • 16
    • 0032544559 scopus 로고    scopus 로고
    • Activation of integrated provirus requires histone acetyltransferase. p300 and P/CAF are coactivators for HIV-1 tat
    • Benkirane, M., R. F. Chun, H. Xiao, V. V. Ogryzko, B. H. Howard, Y. Nakatani, and K. T. Jeang. 1998. Activation of integrated provirus requires histone acetyltransferase. p300 and P/CAF are coactivators for HIV-1 Tat. J. Biol. Chem. 273:24898-24905.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24898-24905
    • Benkirane, M.1    Chun, R.F.2    Xiao, H.3    Ogryzko, V.V.4    Howard, B.H.5    Nakatani, Y.6    Jeang, K.T.7
  • 17
    • 0026645025 scopus 로고
    • Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains
    • Berger, S. L., B. Piña, N. Silverman, G. A. Marcus, J. Agapite, J. L. Regier, S. J. Triezenberg, and L. Guarente. 1992. Genetic isolation of ADA2: a potential transcriptional adaptor required for function of certain acidic activation domains. Cell 70:251-265.
    • (1992) Cell , vol.70 , pp. 251-265
    • Berger, S.L.1    Piña, B.2    Silverman, N.3    Marcus, G.A.4    Agapite, J.5    Regier, J.L.6    Triezenberg, S.J.7    Guarente, L.8
  • 18
    • 0024322804 scopus 로고
    • Tat trans-activates the human immunodeficiency virus through a nascent RNA target
    • Berkhout, B., R. H. Silverman, and K. T. Jeang. 1989. Tat trans-activates the human immunodeficiency virus through a nascent RNA target. Cell 59: 273-282.
    • (1989) Cell , vol.59 , pp. 273-282
    • Berkhout, B.1    Silverman, R.H.2    Jeang, K.T.3
  • 19
    • 0033561043 scopus 로고    scopus 로고
    • Continuous and widespread roles for the Swi-Snf complex in transcription
    • Biggar, S. R., and G. R. Crabtree. 1999. Continuous and widespread roles for the Swi-Snf complex in transcription. EMBO J. 18:2254-2264.
    • (1999) EMBO J. , vol.18 , pp. 2254-2264
    • Biggar, S.R.1    Crabtree, G.R.2
  • 22
    • 0028009294 scopus 로고
    • Acetylated histone H4 on the male X chromosome is associated with dosage compensation in Drosophila
    • Bone, J. R., J. Lavender, R. Richman, M. J. Palmer, B. M. Turner, and M. I. Kuroda. 1994. Acetylated histone H4 on the male X chromosome is associated with dosage compensation in Drosophila. Genes Dev. 8:96-104.
    • (1994) Genes Dev. , vol.8 , pp. 96-104
    • Bone, J.R.1    Lavender, J.2    Richman, R.3    Palmer, M.J.4    Turner, B.M.5    Kuroda, M.I.6
  • 24
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • Boyes, J., P. Byfield, Y. Nakatani, and V. Ogryzko. 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
  • 25
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury, E. M. 1992. Reversible histone modifications and the chromosome cell cycle. Bioessays 14:9-16.
    • (1992) Bioessays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 27
    • 0033603317 scopus 로고    scopus 로고
    • II-containing complex subunits suggests a role in nucleosome acetylation and signal transduction
    • II-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. J. Biol. Chem. 274: 18285-18289.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18285-18289
    • Brand, M.1    Yamamoto, K.2    Staub, A.3    Tora, L.4
  • 28
    • 0027192267 scopus 로고
    • Transcriptional silencing in yeast is associated with reduced nucleosome acetylation
    • Braunstein, M., A. B. Rose, S. G. Holmes, C. D. Allis, and J. R. Broach. 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
  • 29
    • 0029049102 scopus 로고
    • An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei
    • Brownell, J. E., and C. D. Allis. 1995. An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei. Proc. Natl. Acad. Sci. USA 92:6364-6368.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6364-6368
    • Brownell, J.E.1    Allis, C.D.2
  • 30
    • 0029925512 scopus 로고    scopus 로고
    • Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation
    • Brownell, J. E., and C. D. Allis. 1996. Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation. Curr. Opin. Genet. Dev. 6:176-184.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 176-184
    • Brownell, J.E.1    Allis, C.D.2
  • 31
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A transcriptional co-activator linking gene expression to histone acetylation
    • Brownell, J. E., J. Zhou, T. Ranalli, R. Kobayashi, D. G. Edmondson, S. Y. Roth, and C. D. Allis. 1996. Tetrahymena histone acetyltransferase A: a transcriptional co-activator linking gene expression to histone acetylation. 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
  • 32
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor IID (TFIID)
    • Burley, S. K., and R. G. Roeder. 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
  • 33
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin, M., and R. Reeves. 1996. High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nucleic Acids Res. Mol. Biol. 54:35-100.
    • (1996) Prog. Nucleic Acids Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 34
    • 0029348071 scopus 로고
    • The HMG-14/-17 chromosomal protein family: Architectural elements that enhance transcription from chromatin templates
    • Bustin, M., L. Trieschmann, and Y. V. Postnikov. 1995. The HMG-14/-17 chromosomal protein family: architectural elements that enhance transcription from chromatin templates. Semin. Cell Biol. 6:247-255.
    • (1995) Semin. Cell Biol. , vol.6 , pp. 247-255
    • Bustin, M.1    Trieschmann, L.2    Postnikov, Y.V.3
  • 35
    • 0029932309 scopus 로고    scopus 로고
    • Structural and functional analysis of yeast putative adaptors: Evidence for an adaptor complex in vivo
    • Candau, R., and S. L. Berger. 1996. Structural and functional analysis of yeast putative adaptors: evidence for an adaptor complex in vivo. J. Biol. Chem. 271:5237-5345.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5237-5345
    • Candau, R.1    Berger, S.L.2
  • 36
    • 0030030611 scopus 로고    scopus 로고
    • Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5
    • Candau, R., P. A. Moore, L. Wang, N. Barlev, C. Y. Ying, C. A. Rosen, and S. L. Berger. 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
  • 37
    • 0031031755 scopus 로고    scopus 로고
    • Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo
    • Candau, R., J. Zhou, C. D. Allis, and S. L. Berger. 1997. Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo. EMBO J. 16:555-565.
    • (1997) EMBO J. , vol.16 , pp. 555-565
    • Candau, R.1    Zhou, J.2    Allis, C.D.3    Berger, S.L.4
  • 38
    • 0032080173 scopus 로고    scopus 로고
    • A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia
    • Carapeti, M., R. C. Aguiar, J. M. Goldman, and N. C. Cross. 1998. A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia. 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
  • 39
    • 0032498230 scopus 로고    scopus 로고
    • The enhanceosome and transcriptional synergy
    • Carey, M. 1998. The enhanceosome and transcriptional synergy. Cell 92:5-8.
    • (1998) Cell , vol.92 , pp. 5-8
    • Carey, M.1
  • 40
    • 0033524942 scopus 로고    scopus 로고
    • A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity
    • Chakravarti, D., V. Ogryzko, H. Y. Kao, A. Nash, H. Chen, Y. Nakatani, and R. M. Evans. 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    Evans, R.M.7
  • 41
    • 0033215187 scopus 로고    scopus 로고
    • Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein
    • Champagne, N., N. R. Bertos, N. Pelletier, A. H. Wang, M. Vezmar, Y. Yang, H. H. Heng, and X. J. Yang. 1999. Identification of a human histone acetyltransferase related to monocytic 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    Heng, H.H.7    Yang, X.J.8
  • 42
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with PCAF and CBP/p300
    • Chen, H., R. J. Lin, R. L. Schiltz, D. Chakravarti, A. Nash, L. Nagy, M. L. Privalsky, Y. Nakatani, and R. M. Evans. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with PCAF and CBP/p300. Cell 90:569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 43
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of acetylase
    • Chen, H., R. J. Lin, W. Xie, D. Wilpitz, and R. M. Evans. 1999. Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of 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
  • 44
    • 0029906977 scopus 로고    scopus 로고
    • Erythroid krüppel-like factor (EKLF) contains a multifunctional transcriptional activation domain important for inter- and intramolecular interactions
    • Chen, X., and J. J. Bieker. 1996. Erythroid Krüppel-like factor (EKLF) contains a multifunctional transcriptional activation domain important for inter- and intramolecular interactions. EMBO J. 15:5888-5896.
    • (1996) EMBO J. , vol.15 , pp. 5888-5896
    • Chen, X.1    Bieker, J.J.2
  • 45
    • 0022650761 scopus 로고
    • Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena: Evidence for functionally distinct H4 acetylation sites
    • Chicoine, L. G., I. G. Schulman, R. Richman, R. G. Cook, and C. D. Allis. 1986. Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena: evidence for functionally distinct H4 acetylation sites. J. Biol. Chem. 261:1071-1076.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1071-1076
    • Chicoine, L.G.1    Schulman, I.G.2    Richman, R.3    Cook, R.G.4    Allis, C.D.5
  • 47
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • Clarke, A. S., J. E. Lowell, S. J. Jacobson, and L. Pillus. 1999. Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol. Cell. Biol. 19:2515-2526.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2515-2526
    • Clarke, A.S.1    Lowell, J.E.2    Jacobson, S.J.3    Pillus, L.4
  • 48
    • 0033168714 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
    • Clements, A., J. R. Rojas, R. C. Trievel, L. Wang, S. L. Berger, and R. Marmorstein. 1999. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. EMBO J. 18:3521-3532.
    • (1999) EMBO J. , vol.18 , pp. 3521-3532
    • Clements, A.1    Rojas, J.R.2    Trievel, R.C.3    Wang, L.4    Berger, S.L.5    Marmorstein, R.6
  • 49
    • 0031283286 scopus 로고    scopus 로고
    • TCF/LEF factor earn their wings
    • Clevers, H., and M. van de Wetering. 1997. TCF/LEF factor earn their wings. Trends Genet. 13:485-489.
    • (1997) Trends Genet. , vol.13 , pp. 485-489
    • Clevers, H.1    Van De Wetering, M.2
  • 50
    • 0033529253 scopus 로고    scopus 로고
    • Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein
    • Creaven, M., F. Hans, V. Mutskov, E. Col, C. Caron, S. Dimitrov, and S. Khochbin. 1999. Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein. Tat. Biochemistry 38:8826-8830.
    • (1999) Tat. Biochemistry , vol.38 , pp. 8826-8830
    • Creaven, M.1    Hans, F.2    Mutskov, V.3    Col, E.4    Caron, C.5    Dimitrov, S.6    Khochbin, S.7
  • 51
    • 0026676799 scopus 로고
    • Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain
    • Crippa, M. P., P. J. Alfonso, and M. Bustin. 1992. Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain. J. Mol. Biol. 228:442-449.
    • (1992) J. Mol. Biol. , vol.228 , pp. 442-449
    • Crippa, M.P.1    Alfonso, P.J.2    Bustin, M.3
  • 53
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin, C., J. E. Carlson, L. Zeng, C. He, A. K. Aggarwal, and M. M. Zhou. 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.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5    Zhou, M.M.6
  • 55
    • 0027932770 scopus 로고
    • SPT10 and SPT21 are required for transcription of particular histone genes in Saccharomyces cerevisiae
    • Dollard, C., S. L. Ricupero-Hovasse, G. Natsoulis, J. D. Boeke, and F. Winston. 1994. SPT10 and SPT21 are required for transcription of particular histone genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 14:5223-5228.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5223-5228
    • Dollard, C.1    Ricupero-Hovasse, S.L.2    Natsoulis, G.3    Boeke, J.D.4    Winston, F.5
  • 56
    • 0028936440 scopus 로고
    • Role of erythroid Krüppel-like factor in human gamma- to beta-globin gene switching
    • Donze, D., T. M. Townes, and J. J. Bieker. 1995. Role of erythroid Krüppel-like factor in human gamma- to beta-globin gene switching. J. Biol. Chem. 270:1955-1959.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1955-1959
    • Donze, D.1    Townes, T.M.2    Bieker, J.J.3
  • 57
    • 0032710459 scopus 로고    scopus 로고
    • The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo
    • Dudley, A. M., C. Rougeulle, and F. Winston. 1999. The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo. Genes Dev. 13:2940-2945.
    • (1999) Genes Dev. , vol.13 , pp. 2940-2945
    • Dudley, A.M.1    Rougeulle, C.2    Winston, F.3
  • 59
    • 0032555689 scopus 로고    scopus 로고
    • Structure of the histone acetyltransferase Hat1: A paradigm for the GCN5-related N-acetyltransferase superfamily
    • Dutnall, R. N., S. T. Tafrov, R. Sternglanz, and V. Ramakrishnan. 1998. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 94:427-438.
    • (1998) Cell , vol.94 , pp. 427-438
    • Dutnall, R.N.1    Tafrov, S.T.2    Sternglanz, R.3    Ramakrishnan, V.4
  • 60
    • 0031467141 scopus 로고    scopus 로고
    • Initiation of DNA replication in eukaryotic cells
    • Dutta, A., and S. P. Bell. 1997. Initiation of DNA replication in eukaryotic cells. Annu. Rev. Cell Dev. Biol. 13:293-332.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 293-332
    • Dutta, A.1    Bell, S.P.2
  • 61
    • 0032941717 scopus 로고    scopus 로고
    • Regulation of LEF-1/TCF transcription factors by Wnt and other signals
    • Eastman, Q., and R. Grosschedl. 1999. Regulation of LEF-1/TCF transcription factors by Wnt and other signals. Curr. Opin. Cell. Biol. 11:233-240.
    • (1999) Curr. Opin. Cell. Biol. , vol.11 , pp. 233-240
    • Eastman, Q.1    Grosschedl, R.2
  • 62
    • 0031710891 scopus 로고    scopus 로고
    • Identification and analysis of yeast nucleosomal histone acetyltransferase complexes
    • Eberharter, A., S. John, P. A. Grant, R. T. Utley, and J. L. Workman. 1998. Identification and analysis of yeast nucleosomal histone acetyltransferase complexes. Methods (Orlando) 15:315-321.
    • (1998) Methods (Orlando) , vol.15 , pp. 315-321
    • Eberharter, A.1    John, S.2    Grant, P.A.3    Utley, R.T.4    Workman, J.L.5
  • 64
    • 0030939235 scopus 로고    scopus 로고
    • The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function
    • Ehrenhofer-Murray, A. E., D. H. Rivier, and J. Rine. 1997. The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function. Genetics 145:923-934.
    • (1997) Genetics , vol.145 , pp. 923-934
    • Ehrenhofer-Murray, A.E.1    Rivier, D.H.2    Rine, J.3
  • 65
    • 0026764896 scopus 로고
    • SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae
    • Eisenmann, D. M., K. M. Arndt, S. L. Ricupero, J. W. Rooney, and F. Winston. 1992. SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae. Genes Dev. 6:1319-1331.
    • (1992) Genes Dev. , vol.6 , pp. 1319-1331
    • Eisenmann, D.M.1    Arndt, K.M.2    Ricupero, S.L.3    Rooney, J.W.4    Winston, F.5
  • 66
    • 0028233352 scopus 로고
    • The saccharomyces cerevisiae SPT8 gene encodes a very acidic protein that is functionally related to SPT3 and TATA-binding protein
    • Eisenmann, D. M., C. Chapon, S. M. Roberts, C. Dollard, and F. Winston. 1994. The Saccharomyces cerevisiae SPT8 gene encodes a very acidic protein that is functionally related to SPT3 and TATA-binding protein. Genetics 137:647-657.
    • (1994) Genetics , vol.137 , pp. 647-657
    • Eisenmann, D.M.1    Chapon, C.2    Roberts, S.M.3    Dollard, C.4    Winston, F.5
  • 67
    • 0345184762 scopus 로고
    • An erythrocyte-specific DNA-binding factor recognizes a regulatory sequence common to all chicken globin genes
    • Evans, T., M. Reitman, and G. Felsenfeld. 1988. An erythrocyte-specific DNA-binding factor recognizes a regulatory sequence common to all chicken globin genes. Proc. Natl. Acad. Sci. USA 85:5976-5980.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5976-5980
    • Evans, T.1    Reitman, M.2    Felsenfeld, G.3
  • 68
    • 0029619641 scopus 로고
    • Reversal of intrinsic DNA bends in the IFN-β gene enhancer by transcription factors and the architectural protein HMG I(Y)
    • Falvo, J. V., D. Thanos, and T. Maniatis. 1995. Reversal of intrinsic DNA bends in the IFN-β gene enhancer by transcription factors and the architectural protein HMG I(Y). Cell 83:1101-1111.
    • (1995) Cell , vol.83 , pp. 1101-1111
    • Falvo, J.V.1    Thanos, D.2    Maniatis, T.3
  • 69
    • 0028858566 scopus 로고
    • Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms
    • Fletcher, T. M., and J. C. Hansen. 1995. Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms. J. Biol. Chem. 270:25359-25362.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25359-25362
    • Fletcher, T.M.1    Hansen, J.C.2
  • 71
    • 0027787870 scopus 로고
    • Origin recognition complex (ORC) in transcriptional silencing and DNA replication in S. Cerevisiae
    • Foss, M., F. J. McNally, P. Laurenson, and J. Rine. 1993. Origin recognition complex (ORC) in transcriptional silencing and DNA replication in S. cerevisiae. Science 262:1838-1844.
    • (1993) Science , vol.262 , pp. 1838-1844
    • Foss, M.1    McNally, F.J.2    Laurenson, P.3    Rine, J.4
  • 72
    • 1842367918 scopus 로고    scopus 로고
    • The origin recognition complex, SIR1, and the S phase requirement for silencing
    • Fox, C. A., A. E. Ehrenhofer-Murray, S. Loo, and J. Rine. 1997. The origin recognition complex, SIR1, and the S phase requirement for silencing. Science 276:1547-1551.
    • (1997) Science , vol.276 , pp. 1547-1551
    • Fox, C.A.1    Ehrenhofer-Murray, A.E.2    Loo, S.3    Rine, J.4
  • 73
    • 0028897908 scopus 로고
    • The origin recognition complex has essential functions in transcriptional silencing and chromosomal replication
    • Fox, C. A., S. Loo, A. Dillin, and J. Rine. 1995. The origin recognition complex has essential functions in transcriptional silencing and chromosomal replication. Genes Dev. 9:911-924.
    • (1995) Genes Dev. , vol.9 , pp. 911-924
    • Fox, C.A.1    Loo, S.2    Dillin, A.3    Rine, J.4
  • 74
    • 0033166348 scopus 로고    scopus 로고
    • The roX1 and roX2 RNAs are essential components of the compensasome, which mediates dosage compensation in Drosophila
    • Franke, A., and B. S. Baker. 1999. The roX1 and roX2 RNAs are essential components of the compensasome, which mediates dosage compensation in Drosophila. Mol. Cell 4:117-122.
    • (1999) Mol. Cell , vol.4 , pp. 117-122
    • Franke, A.1    Baker, B.S.2
  • 75
    • 0028796702 scopus 로고
    • The Saccharomyces cerevisiae SPT7 gene encodes a very acidic protein important for transcription in vivo
    • Gansheroff, L. J., C. Dullard, P. Tan, and F. Winston. 1995. The Saccharomyces cerevisiae SPT7 gene encodes a very acidic protein important for transcription in vivo. Genetics 139:523-536.
    • (1995) Genetics , vol.139 , pp. 523-536
    • Gansheroff, L.J.1    Dullard, C.2    P, T.3    Winston, F.4
  • 76
    • 0019321889 scopus 로고
    • Comparative studies of histone acetylation in nucleosomes, nuclei, and intact cells: Evidence for special factors which modify acetylase action
    • Garcea, R. L., and B. M. Alberts. 1980. Comparative studies of histone acetylation in nucleosomes, nuclei, and intact cells: evidence for special factors which modify acetylase action. J. Biol. Chem. 255:11454-11463.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11454-11463
    • Garcea, R.L.1    Alberts, B.M.2
  • 77
    • 0029843541 scopus 로고    scopus 로고
    • Activator-dependent transcription by mammalian RNA polymerase II: In vitro reconstitution with general transcription factors and cofactors
    • Ge, H., E. Martinez, C. M. Chiang, and R. G. Roeder. 1996. Activator-dependent transcription by mammalian RNA polymerase II: in vitro reconstitution with general transcription factors and cofactors. Methods Enzymol. 274:57-71.
    • (1996) Methods Enzymol. , vol.274 , pp. 57-71
    • Ge, H.1    Martinez, E.2    Chiang, C.M.3    Roeder, R.G.4
  • 78
    • 0028962230 scopus 로고
    • Genetic evidence for the interaction of the yeast transcriptional co-activator proteins GCN5 and ADA2
    • Georgakopoulos, T., N. Gounalaki, and G. Thireos. 1995. Genetic evidence for the interaction of the yeast transcriptional co-activator proteins GCN5 and ADA2. Mol. Gen. Genet. 246:723-728.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 723-728
    • Georgakopoulos, T.1    Gounalaki, N.2    Thireos, G.3
  • 79
    • 0026783834 scopus 로고
    • Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription
    • Georgakopoulos, T., and G. Thireos. 1992. Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J. 11:4145-4152.
    • (1992) EMBO J. , vol.11 , pp. 4145-4152
    • Georgakopoulos, T.1    Thireos, G.2
  • 81
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia, A. J., and M. B. Kastan. 1998. The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev. 12:2973-2983.
    • (1998) Genes Dev. , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 82
    • 0032076229 scopus 로고    scopus 로고
    • Conjunction dysfunction: CBP/p300 in human disease
    • Giles, R. H., D. J. Peters, and M. H. Breuning. 1998. Conjunction dysfunction: CBP/p300 in human disease. Trends Genet. 14:178-183.
    • (1998) Trends Genet. , vol.14 , pp. 178-183
    • Giles, R.H.1    Peters, D.J.2    Breuning, M.H.3
  • 83
    • 0032829090 scopus 로고    scopus 로고
    • p300 and CBP: Partners for life and death
    • Giordano, A., and M. L. Avantaggiati. 1999. p300 and CBP: partners for life and death. J. Cell. Physiol. 181:218-230.
    • (1999) J. Cell. Physiol. , vol.181 , pp. 218-230
    • Giordano, A.1    Avantaggiati, A.M.L.2
  • 84
    • 0028883875 scopus 로고
    • The amino-terminal tails of the core histones and the translational position of the TATA box determine TBP/TFIIA association with nucleosomal DNA
    • Godde, J. S., Y. Nakatani, and A. P. Wolffe. 1995. The amino-terminal tails of the core histones and the translational position of the TATA box determine TBP/TFIIA association with nucleosomal DNA. Nucleic Acids Res. 23:4557-4564.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4557-4564
    • Godde, J.S.1    Nakatani, Y.2    Wolffe, A.P.3
  • 85
    • 0029980043 scopus 로고    scopus 로고
    • p53 in growth control and neoplasia
    • Gottlieb, T. M., and M. Oren. 1996. p53 in growth control and neoplasia. Biochim. Biophys. Acta 1287:77-102.
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 77-102
    • Gottlieb, T.M.1    Oren, M.2
  • 89
    • 0032254147 scopus 로고    scopus 로고
    • The ATM-related cofactor Tra1 is a component of the purified SAGA complex
    • Grant, P. A., D. Schieltz, M. G. Pray-Grant, J. R. Yates III, and J. L. Workman. 1998. The ATM-related cofactor Tra1 is a component of the purified SAGA complex. Mol. Cell 2:863-867.
    • (1998) Mol. Cell , vol.2 , pp. 863-867
    • Grant, P.A.1    Schieltz, D.2    Pray-Grant, M.G.3    Yates J.R. III4    Workman, J.L.5
  • 90
    • 0032080848 scopus 로고    scopus 로고
    • The SAGA unfolds: Convergence of transcription regulators in chromatin-modifying complexes
    • Grant, P. A., D. E. Sterner, L. J. Duggan, J. L. Workman, and S. L. Berger. 1998. The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes. Trends Cell Biol. 8:193-197.
    • (1998) Trends Cell Biol. , vol.8 , pp. 193-197
    • Grant, P.A.1    Sterner, D.E.2    Duggan, L.J.3    Workman, J.L.4    Berger, S.L.5
  • 91
    • 0032015582 scopus 로고    scopus 로고
    • Absence of Gcn5 HAT activity defines a novel state in the opening of chromatin at the PHO5 promoter in yeast
    • Gregory, P. D., A. Schmid, M. Zavari, L. Liu, S. L. Berger, and W. Hörz. 1998. Absence of Gcn5 HAT activity defines a novel state in the opening of chromatin at the PHO5 promoter in yeast. Mol. Cell 1:495-505.
    • (1998) Mol. Cell , vol.1 , pp. 495-505
    • Gregory, P.D.1    Schmid, A.2    Zavari, M.3    Liu, L.4    Berger, S.L.5    Hörz, W.6
  • 92
    • 0033571273 scopus 로고    scopus 로고
    • Chromatin remodelling at the PHO8 promoter requires SWI-SNF and SAGA at a step subsequent to activator binding
    • Gregory, P. D., A. Schmid, M. Zavari, M. Münsterkötter, and W. Hörz. 1999. Chromatin remodelling at the PHO8 promoter requires SWI-SNF and SAGA at a step subsequent to activator binding. EMBO J. 18:6407-6414.
    • (1999) EMBO J. , vol.18 , pp. 6407-6414
    • Gregory, P.D.1    Schmid, A.2    Zavari, M.3    Münsterkötter, M.4    Hörz, W.5
  • 93
    • 0025224576 scopus 로고
    • Nucleosomes: Regulators of transcription
    • Grunstein, M. 1990. Nucleosomes: regulators of transcription. Trends Genet. 6:395-400.
    • (1990) Trends Genet. , vol.6 , pp. 395-400
    • Grunstein, M.1
  • 94
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W., and R. Roeder. 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.2
  • 95
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • Gu, W., X. L. Shi, and R. G. Roeder. 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
  • 96
    • 0029034451 scopus 로고
    • MyoD-induced expression of p21 inhibits cyclin-dependent kinase activity upon myocyte terminal differentiation
    • Guo, K., J. Wang, V. Andres, R. C. Smith, and K. Walsh. 1995. MyoD-induced expression of p21 inhibits cyclin-dependent kinase activity upon myocyte terminal differentiation. Mol. Cell. Biol. 15:3823-3829.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3823-3829
    • Guo, K.1    Wang, J.2    Andres, V.3    Smith, R.C.4    Walsh, K.5
  • 98
    • 0033525094 scopus 로고    scopus 로고
    • Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A
    • Hamamori, Y., V. Sartorelli, V. Ogryzko, P. L. Puri, H. Y. Wu, J. Y. Wang, Y. Nakatani, and L. Kodes. 1999. Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein 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    Nakatani, Y.7    Kodes, L.8
  • 99
    • 0031840672 scopus 로고    scopus 로고
    • Molecular genetics of the RNA polymerase II general transcriptional machinery
    • Hampsey, M. 1998. Molecular genetics of the RNA polymerase II general transcriptional machinery. Microbiol. Mol. Biol. Rev. 62:465-503.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 465-503
    • Hampsey, M.1
  • 101
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes, T. R., A. W. Thorne, and C. Crane-Robinson. 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
  • 102
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery, D. M., E. Kalkhoven, S. Hoare, and M. G. Parker. 1997. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 103
    • 0032933141 scopus 로고    scopus 로고
    • Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes
    • Herrera, J. E., K. Sakaguchi, M. Bergel, L. Trieschmann, Y. Nakatani, and M. Bustin. 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
  • 104
    • 0033571221 scopus 로고    scopus 로고
    • Cloning and analysis of a Toxoplasma gondii histone acetyltransferase: A novel chromatin remodelling factor in Apicomplexan parasites
    • Hettmann, C., and D. Soldati. 1999. Cloning and analysis of a Toxoplasma 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
  • 105
    • 0030891858 scopus 로고    scopus 로고
    • mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila
    • Hilfiker, A., D. Hilfiker-Kleiner, A. Pannuti, and J. C. Lucchesi. 1997. mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila. EMBO J. 16:2054-2060.
    • (1997) EMBO J. , vol.16 , pp. 2054-2060
    • Hilfiker, A.1    Hilfiker-Kleiner, D.2    Pannuti, A.3    Lucchesi, J.C.4
  • 108
    • 0030949836 scopus 로고    scopus 로고
    • GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors
    • Hong, H., K. Kohli, M. J. Garabedian, and M. R. Stallcup. 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell. Biol. 17:2735-2744.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2735-2744
    • Hong, H.1    Kohli, K.2    Garabedian, M.J.3    Stallcup, M.R.4
  • 109
    • 0027525970 scopus 로고
    • Studies of the DNA binding properties of histone H4 amino terminus: Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA
    • Hong, L., G. P. Schroth, H. R. Matthews, P. Yau, and E. M. Bradbury. 1993. Studies of the DNA binding properties of histone H4 amino terminus: thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA. J. Biol. Chem. 268:305-314.
    • (1993) J. Biol. Chem. , vol.268 , pp. 305-314
    • Hong, L.1    Schroth, G.P.2    Matthews, H.R.3    Yau, P.4    Bradbury, E.M.5
  • 110
    • 0030977168 scopus 로고    scopus 로고
    • ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3
    • Horiuchi, J., N. Silverman, B. Piña, G. A. Marcus, and L. Guarente. 1997. ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3. Mol. Cell. Biol. 17:3220-3228.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3220-3228
    • Horiuchi, J.1    Silverman, N.2    Piña, B.3    Marcus, G.A.4    Guarente, L.5
  • 111
    • 0028876860 scopus 로고
    • ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex
    • Horiuchi, J., N. Silverman, G. A. Marcus, and L. Guarente. 1995. ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex. Mol. Cell. Biol. 15:1203-1209.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1203-1209
    • Horiuchi, J.1    Silverman, N.2    Marcus, G.A.3    Guarente, L.4
  • 112
    • 0031690395 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 1 Tat with the transcriptional coactivators p300 and CREB binding protein
    • Hottiger, M. O., and G. J. Nabel. 1998. Interaction of human immunodeficiency virus type 1 Tat with the transcriptional coactivators p300 and CREB binding protein. J. Virol. 72:8252-8256.
    • (1998) J. Virol. , vol.72 , pp. 8252-8256
    • Hottiger, M.O.1    Nabel, G.J.2
  • 113
    • 0032744688 scopus 로고    scopus 로고
    • The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity
    • Hsieh, Y. J., T. K. Kundu, Z. Wang, R. Kovelman, and R. G. Roeder. 1999. The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery 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
  • 114
    • 0032910957 scopus 로고    scopus 로고
    • CREB-binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites
    • Hung, H. L., J. Lau, A. Y. Kim, M. J. Weiss, and G. A. Blobel. 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
    • Hung, H.L.1    Lau, J.2    Kim, A.Y.3    Weiss, M.J.4    Blobel, G.A.5
  • 115
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp, T. R., D. W. Meek, C. A. Midgley, and D. P. Lane. 1992. Regulation of the specific DNA binding function of p53. Cell 71:875-886.
    • (1992) Cell , vol.71 , pp. 875-886
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 116
    • 0033551686 scopus 로고    scopus 로고
    • Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein
    • Iizuka, M., and B. Stillman. 1999. Histone acetyltransferase HBO1 interacts with the 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
  • 117
    • 0032909655 scopus 로고    scopus 로고
    • Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes
    • Ikeda, K., D. J. Steger, A. Eberharter, and J. L. Workman. 1999. Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes. Mol. Cell. Biol. 19:855-863.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 855-863
    • Ikeda, K.1    Steger, D.J.2    Eberharter, A.3    Workman, J.L.4
  • 118
    • 0032470510 scopus 로고    scopus 로고
    • Energy-dependent chromatin remodelers: Complex complexes and their components
    • Imbalzano, A. N. 1998. Energy-dependent chromatin remodelers: complex complexes and their components. Crit. Rev. Eukaryot. Gene Expression 8: 225-255.
    • (1998) Crit. Rev. Eukaryot. Gene Expression , vol.8 , pp. 225-255
    • Imbalzano, A.N.1
  • 119
    • 0028068714 scopus 로고
    • Facilitated binding of TATA-binding protein to nucleosomal DNA
    • Imbalzano, A. N., H. Kwon, M. R. Green, and R. E. Kingston. 1994. Facilitated binding of TATA-binding protein to nucleosomal DNA. Nature 370:481-485.
    • (1994) Nature , vol.370 , pp. 481-485
    • Imbalzano, A.N.1    Kwon, H.2    Green, M.R.3    Kingston, R.E.4
  • 120
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • Imhof, A., X. J. Yang, V. V. Ogryzko, Y. Nakatani, A. P. Wolffe, and H. Ge. 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
  • 122
    • 0030774549 scopus 로고    scopus 로고
    • Taking a new TAK on tat transactivation
    • Jones, K. A. 1997. Taking a new TAK on tat transactivation. Genes Dev. 11: 2593-2599.
    • (1997) Genes Dev. , vol.11 , pp. 2593-2599
    • Jones, K.A.1
  • 124
    • 0029961534 scopus 로고    scopus 로고
    • Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 tat transactivator
    • Kamine, J., B. Elangovan, T. Subramanian, D, Coleman, and G. Chinnadurai. 1996. Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. Virology 216:357-366.
    • (1996) Virology , vol.216 , pp. 357-366
    • Kamine, J.1    Elangovan, B.2    Subramanian, T.3    Coleman, D.4    Chinnadurai, G.5
  • 125
    • 0029565873 scopus 로고
    • Equality for X chromosomes
    • Kelley, R. L., and M. I. Kuroda. 1995. Equality for X chromosomes. Science 270:1607-1610.
    • (1995) Science , vol.270 , pp. 1607-1610
    • Kelley, R.L.1    Kuroda, M.I.2
  • 126
    • 0033588309 scopus 로고    scopus 로고
    • Epigenetic spreading of the Drosophila dosage compensation complex from roX RNA genes into flanking chromatin
    • Kelley, R. L., V. H. Meller, P. R. Gordadze, G. Roman, R. L. Davis, and M. I. Kuroda. 1999. Epigenetic spreading of the Drosophila dosage compensation complex from roX RNA genes into flanking chromatin. Cell 98: 513-522.
    • (1999) Cell , vol.98 , pp. 513-522
    • Kelley, R.L.1    Meller, V.H.2    Gordadze, P.R.3    Roman, G.4    Davis, R.L.5    Kuroda, M.I.6
  • 127
    • 0029063585 scopus 로고
    • Expression of msl-2 causes assembly of dosage compensation regulators on the X chromosomes and female lethality in Drosophila
    • Kelley, R. L., I. Solovyeva, L. M. Lyman, R. Richman, V. Solovyev, and M. I. Kuroda. 1995. Expression of msl-2 causes assembly of dosage compensation regulators on the X chromosomes and female lethality in Drosophila. Cell 81:867-877.
    • (1995) Cell , vol.81 , pp. 867-877
    • Kelley, R.L.1    Solovyeva, I.2    Lyman, L.M.3    Richman, R.4    Solovyev, V.5    Kuroda, M.I.6
  • 129
    • 0032467640 scopus 로고    scopus 로고
    • Tip60 acetylates six lysines of a specific class in core histones in vitro
    • Kimura, A., and M. Horikoshi. 1998. Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells 3:789-800.
    • (1998) Genes Cells , vol.3 , pp. 789-800
    • Kimura, A.1    Horikoshi, M.2
  • 130
    • 0029917840 scopus 로고    scopus 로고
    • Repression and activation by multiprotein complexes that alter chromatin structure
    • Kingston, R. E., C. A. Bunker, and A. N. Imbalzano. 1996. Repression and activation by multiprotein complexes that alter chromatin structure. Genes Dev. 10:905-920.
    • (1996) Genes Dev. , vol.10 , pp. 905-920
    • Kingston, R.E.1    Bunker, C.A.2    Imbalzano, A.N.3
  • 131
    • 0028885077 scopus 로고
    • Identification of a gene encoding a yeast histone H4 acetyltransferase
    • Kleff, S., E. D. Andrulis, C. W. Anderson, and R. Sternglanz. 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
  • 132
    • 0029972806 scopus 로고    scopus 로고
    • p53: Puzzle and paradigm
    • Ko, L. J., and C. Prives. 1996. p53: puzzle and paradigm. Genes Dev. 10: 1054-1072.
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 133
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg, R. D., and Y. Lorch. 1999. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell 98:285-294.
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 135
    • 0025836057 scopus 로고
    • A negative regulator of HO transcription, SIN1 (SPT2), is a nonspecific DNA-binding protein related to HMG1
    • Kruger, W., and I. Herskowitz. 1991. A negative regulator of HO transcription, SIN1 (SPT2), is a nonspecific DNA-binding protein related to HMG1. Mol. Cell. Biol. 11:4135-4146.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4135-4146
    • Kruger, W.1    Herskowitz, I.2
  • 137
    • 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., Z. Wang, and R. G. Roeder. 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
  • 138
    • 0032030906 scopus 로고    scopus 로고
    • Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo
    • Kuo, M.-H., J. Zhou, P. Jambeck, M. E. A. Churchill, and C. D. Allis. 1998. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo. Genes Dev. 12:627-639.
    • (1998) Genes Dev. , vol.12 , pp. 627-639
    • Kuo, M.-H.1    Zhou, J.2    Jambeck, P.3    Churchill, M.E.A.4    Allis, C.D.5
  • 139
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo, M.-H., and C. D. Allis. 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
  • 140
    • 0029835806 scopus 로고    scopus 로고
    • GCN5p, a yeast nuclear histone acetyltransferase, acetylates specific lysines in histone H3 and H4 that differ from deposition-related acetylation sites
    • Kuo, M.-H., J. E. Brownell, R. E. Sobel, T. A. Ranalli, R. G. Cook, D. G. Edmonson, S. Y. Roth, and C. D. Allis. 1996. GCN5p, a yeast nuclear histone acetyltransferase, acetylates specific lysines in histone H3 and H4 that differ from deposition-related acetylation sites. Nature 383:269-272.
    • (1996) Nature , vol.383 , pp. 269-272
    • Kuo, M.-H.1    Brownell, J.E.2    Sobel, R.E.3    Ranalli, T.A.4    Cook, R.G.5    Edmonson, D.G.6    Roth, S.Y.7    Allis, C.D.8
  • 141
    • 0021022011 scopus 로고
    • Transcription of class III genes: Formation of preinitiation complexes
    • Lassar, A. B., P. L. Martin, and R. G. Roeder. 1983. Transcription of class III genes: formation of preinitiation complexes. Science 222:740-748.
    • (1983) Science , vol.222 , pp. 740-748
    • Lassar, A.B.1    Martin, P.L.2    Roeder, R.G.3
  • 142
    • 0028292621 scopus 로고
    • DP and E2F proteins: Components of a heterodimeric transcription factor implicated in cell cycle control
    • La Thangue, N. B. 1994. DP and E2F proteins: components of a heterodimeric transcription factor implicated in cell cycle control. Curr. Opin. Cell Biol. 6:443-450.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 443-450
    • La Thangue, N.B.1
  • 143
    • 0034615669 scopus 로고    scopus 로고
    • The SRC family of nuclear receptor coactivators
    • Leo, C., and J. D. Chen. 2000. The SRC family of nuclear receptor coactivators. Gene 245:1-11.
    • (2000) Gene , vol.245 , pp. 1-11
    • Leo, C.1    Chen, J.D.2
  • 144
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A. J. 1997. p53, the cellular gatekeeper for growth and division. Cell 88:323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 145
    • 0021993649 scopus 로고
    • Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine
    • L'Hernault, S. W., and J. L. Rosenbaum. 1985. Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine. Biochemistry 24:473-478.
    • (1985) Biochemistry , vol.24 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 146
    • 0030872716 scopus 로고    scopus 로고
    • RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2
    • Li, H., P. J. Gomes, and J. D. Chen. 1997. RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc. Natl. Acad. Sci. USA 94:8479-8484.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8479-8484
    • Li, H.1    Gomes, P.J.2    Chen, J.D.3
  • 147
    • 0028826925 scopus 로고
    • Yeast global transcriptional regulators Sin4 and Rgr1 are components of mediator complex/RNA polymerase II holoenzyme
    • Li, Y., S. Bjorklund, Y. W. Jiang, Y. J. Kim, W. S. Lane, D. J. Stillman, and R. D. Kornberg. 1995. Yeast global transcriptional regulators Sin4 and Rgr1 are components of mediator complex/RNA polymerase II holoenzyme. Proc. Natl. Acad. Sci. USA 92:10864-10868.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10864-10868
    • Li, Y.1    Bjorklund, S.2    Jiang, Y.W.3    Kim, Y.J.4    Lane, W.S.5    Stillman, D.J.6    Kornberg, R.D.7
  • 148
    • 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., L. Prouty, B. J. Williams, M. A. Dayton, and K. L. Blanchard. 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
  • 150
    • 0033168497 scopus 로고    scopus 로고
    • Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A
    • Lin, Y., C. M. Fletcher, J. Zhou, C. D. Allis, and G. Wagner. 1999. Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A. Nature 400:86-89.
    • (1999) Nature , vol.400 , pp. 86-89
    • Lin, Y.1    Fletcher, C.M.2    Zhou, J.3    Allis, C.D.4    Wagner, G.5
  • 153
    • 0028608018 scopus 로고
    • Histone acetylation: Facts and questions
    • Loidl, P. 1994. Histone acetylation: facts and questions. Chromosoma 103: 441-449.
    • (1994) Chromosoma , vol.103 , pp. 441-449
    • Loidl, P.1
  • 154
    • 0032055416 scopus 로고    scopus 로고
    • Dosage compensation in flies and worms: The ups and downs of X-chromosome regulation
    • Lucchesi, J. C. 1998. Dosage compensation in flies and worms: the ups and downs of X-chromosome regulation. Curr. Opin. Genet. Dev. 8:179-184.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 179-184
    • Lucchesi, J.C.1
  • 155
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., A. W. Mader, R. K. Richmond, D. F. Sargent, and T. J. Richmond. 1997. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 156
  • 157
    • 0029984931 scopus 로고    scopus 로고
    • ADA5/ SPT20 links the ADA and SPT genes, which are involved in yeast transcription
    • Marcus, G. A., J. Horiuchi, N. Silverman, and L. Guarente. 1996. ADA5/ SPT20 links the ADA and SPT genes, which are involved in yeast transcription. Mol. Cell. Biol. 16:3197-3205.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3197-3205
    • Marcus, G.A.1    Horiuchi, J.2    Silverman, N.3    Guarente, L.4
  • 158
    • 0027948984 scopus 로고
    • Functional similarity and physical association between GCN5 and ADA2: Putative transcriptional adaptors
    • Marcus, G. A., N. Silverman, S. L. Berger, J. Horiuchi, and L. Guarente. 1994. Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors. EMBO J. 13:4807-4815.
    • (1994) EMBO J. , vol.13 , pp. 4807-4815
    • Marcus, G.A.1    Silverman, N.2    Berger, S.L.3    Horiuchi, J.4    Guarente, L.5
  • 159
    • 0019176523 scopus 로고
    • Nucleosome cores have two specific binding sites for nonhistone chromosomal proteins HMG 14 and HMG 17
    • Mardian, J. K., A. E. Paton, G. J. Bunick, and D. E. Olins. 1980. Nucleosome cores have two specific binding sites for nonhistone chromosomal proteins HMG 14 and HMG 17. Science 209:1534-1536.
    • (1980) Science , vol.209 , pp. 1534-1536
    • Mardian, J.K.1    Paton, A.E.2    Bunick, G.J.3    Olins, D.E.4
  • 160
    • 0024560650 scopus 로고
    • Increased gamma-globin expression in a nondeletion HPFH mediated by an erythroid-specific DNA-binding factor
    • Martin, D. I., S. F. Tsai, and S. H. Orkin. 1989. Increased gamma-globin expression in a nondeletion HPFH mediated by an erythroid-specific DNA-binding factor. Nature 338:435-438.
    • (1989) Nature , vol.338 , pp. 435-438
    • Martin, D.I.1    Tsai, S.F.2    Orkin, S.H.3
  • 161
  • 164
    • 0032506242 scopus 로고    scopus 로고
    • HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter
    • Marzio, G., M. Tyagi, M. I. Gutierrez, and M. Giacca. 1998. HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter. Proc. Natl. Acad. Sci. USA 95:13519-13524.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13519-13524
    • Marzio, G.1    Tyagi, M.2    Gutierrez, M.I.3    Giacca, M.4
  • 165
    • 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., H. A. Van Buskirk, K. A. Dugan, T. D. Copeland, and M. D. Cole. 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
  • 166
    • 0034695501 scopus 로고    scopus 로고
    • A role for histone acetylation in the developmental regulation of V(D)J recombination
    • McMurry, M. T., and M. S. Krangel. 2000. A role for histone acetylation in the developmental regulation of V(D)J recombination. Science 287:495-498.
    • (2000) Science , vol.287 , pp. 495-498
    • McMurry, M.T.1    Krangel, M.S.2
  • 167
    • 0028455516 scopus 로고
    • Post-translational modification of p53
    • Meek, D. W. 1994. Post-translational modification of p53. Semin. Cancer Biol. 5:203-210.
    • (1994) Semin. Cancer Biol. , vol.5 , pp. 203-210
    • Meek, D.W.1
  • 168
    • 0025647724 scopus 로고
    • Recombinant yeast TFIID, a general transcription factor, mediates activation by the gene-specific factor USF in a chromatin assembly assay
    • Meisterernst, M., M. Horikoshi, and R. G. Roeder. 1990. Recombinant yeast TFIID, a general transcription factor, mediates activation by the gene-specific factor USF in a chromatin assembly assay. Proc. Natl. Acad. Sci. USA 87:9153-9157.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9153-9157
    • Meisterernst, M.1    Horikoshi, M.2    Roeder, R.G.3
  • 169
    • 0033953362 scopus 로고    scopus 로고
    • Dosage compensation: Making 1X equal 2X
    • Meller, V. H. 2000. Dosage compensation: making 1X equal 2X. Trends Cell Biol. 10:54-59.
    • (2000) Trends Cell Biol. , vol.10 , pp. 54-59
    • Meller, V.H.1
  • 170
    • 0034628634 scopus 로고    scopus 로고
    • Ordered assembly of roX RNAs into MSL complexes on the dosage-compensated X chromosome in Drosophila
    • Meller, V. H., P. R. Gordadze, Y. Park, X. Chu, C. Stuckenholz, R. L. Kelley, and M. I. Kuroda. 2000. Ordered assembly of roX RNAs into MSL complexes on the dosage-compensated X chromosome in Drosophila. Curr. Biol. 10:136-143.
    • (2000) Curr. Biol. , vol.10 , pp. 136-143
    • Meller, V.H.1    Gordadze, P.R.2    Park, Y.3    Chu, X.4    Stuckenholz, C.5    Kelley, R.L.6    Kuroda, M.I.7
  • 171
    • 0031604766 scopus 로고    scopus 로고
    • Recruitment of CBP/p300 by the IFN-β enhanceosome is required for synergistic activation of transcription
    • Merika, M., A. J. Williams, G. Chen, T. Collins, and D. Thanos. 1998. Recruitment of CBP/p300 by the IFN-β enhanceosome is required for synergistic activation of transcription. Mol. Cell. 1:277-287.
    • (1998) Mol. Cell. , vol.1 , pp. 277-287
    • Merika, M.1    Williams, A.J.2    Chen, G.3    Collins, T.4    Thanos, D.5
  • 172
    • 0027211845 scopus 로고
    • A novel, erythroid cell-specific murine transcription factor that binds to the CACCC element and is related to the Krüppel family of nuclear proteins
    • Miller, I. J., and J. J. Bieker. 1993. A novel, erythroid cell-specific murine transcription factor that binds to the CACCC element and is related to the Krüppel family of nuclear proteins. Mol. Cell. Biol. 13:2776-2786.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2776-2786
    • Miller, I.J.1    Bieker, J.J.2
  • 175
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome
    • Munshi, N., M. Merika, J. Yie, K. Senger, G. Chen, and D. Thanos. 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
  • 176
    • 0026321729 scopus 로고
    • The products of the SPT10 and SPT21 genes of Saccharomyces cerevisiae increase the amplitude of transcriptional regulation at a large number of unlinked loci
    • Natsoulis, G., C. Dollard, F. Winston, and J. D. Boeke. 1991. The products of the SPT10 and SPT21 genes of Saccharomyces cerevisiae increase the amplitude of transcriptional regulation at a large number of unlinked loci. New Biol. 3:1249-1259.
    • (1991) New Biol. , vol.3 , pp. 1249-1259
    • Natsoulis, G.1    Dollard, C.2    Winston, F.3    Boeke, J.D.4
  • 177
    • 0028047615 scopus 로고
    • The SPT10 and SPT21 genes of Saccharomyces cerevisiae
    • Natsoulis, G., F. Winston, and J. D. Boeke. 1994. The SPT10 and SPT21 genes of Saccharomyces cerevisiae. Genetics 136:93-105.
    • (1994) Genetics , vol.136 , pp. 93-105
    • Natsoulis, G.1    Winston, F.2    Boeke, J.D.3
  • 178
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • Neuwald, A. F., and D. Landsman. 1997. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22:154-155.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 179
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core particle linking number change
    • Norton, V. G., B. S. Imai, P. Yau, and E. M. Bradbury. 1989. Histone acetylation reduces nucleosome core particle linking number change. Cell 57:449-457.
    • (1989) Cell , vol.57 , pp. 449-457
    • Norton, V.G.1    Imai, B.S.2    Yau, P.3    Bradbury, E.M.4
  • 180
    • 0034646349 scopus 로고    scopus 로고
    • II250 modulate expression of distinct subsets of mammalian genes
    • II250 modulate expression of distinct subsets of mammalian genes. Proc. Natl. Acad. Sci. USA 97:2456-2461.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2456-2461
    • O'Brien, T.1    Tjian, R.2
  • 182
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V. V., R. L. Schlitz, V. Russanova, B. H. Howard, and Y. Nakatani. 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    Schlitz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 184
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Oñate, S. A., S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354-1357.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Oñate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3    O'Malley, B.W.4
  • 185
    • 0033582943 scopus 로고    scopus 로고
    • The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4
    • Ornaghi, P., P. Ballario, A. M. Lena, A. Gonzalez, and P. Filetici. 1999. The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4. J. Mol. Biol. 287:1-7.
    • (1999) J. Mol. Biol. , vol.287 , pp. 1-7
    • Ornaghi, P.1    Ballario, P.2    Lena, A.M.3    Gonzalez, A.4    Filetici, P.5
  • 187
    • 0028966257 scopus 로고
    • Experimental analysis of chromatin function in transcription control
    • Owen-Hughes, T., and J. L. Workman. 1994. Experimental analysis of chromatin function in transcription control. Crit. Rev. Eukarot. Gene Expression 4:403-441.
    • (1994) Crit. Rev. Eukarot. Gene Expression , vol.4 , pp. 403-441
    • Owen-Hughes, T.1    Workman, J.L.2
  • 188
    • 0030722744 scopus 로고    scopus 로고
    • Association of the origin recognition complex with heterochromatin and HP1 in higher eukaryotcs
    • Pak, D. T., M. Pflumm, I. Chesnokov, D. W. Huang, R. Kellum, J. Marr, P. Romanowski, and M. R. Botchan. 1997. Association of the origin recognition complex with heterochromatin and HP1 in higher eukaryotcs. Cell 91: 311-323.
    • (1997) Cell , vol.91 , pp. 311-323
    • Pak, D.T.1    Pflumm, M.2    Chesnokov, I.3    Huang, D.W.4    Kellum, R.5    Marr, J.6    Romanowski, P.7    Botchan, M.R.8
  • 189
    • 0030271392 scopus 로고    scopus 로고
    • The major cytoplasmic histone acetyltransferase in yeast: Links to chromatin replication and histone metabolism
    • Parthun, M. R., J. Widom, and D. E. Gottschling. 1996. The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism. Cell 87:85-94.
    • (1996) Cell , vol.87 , pp. 85-94
    • Parthun, M.R.1    Widom, J.2    Gottschling, D.E.3
  • 190
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin, M., and J. Kadonaga. 1997. What's up and down with histone deacetylation and transcription? Cell 89:325-328.
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.1    Kadonaga, J.2
  • 192
    • 0022399572 scopus 로고
    • Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms
    • Piperno, G., and M. T. Fuller. 1985. Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms. J. Cell Biol. 101:2085-2094.
    • (1985) J. Cell Biol. , vol.101 , pp. 2085-2094
    • Piperno, G.1    Fuller, M.T.2
  • 193
    • 0030881740 scopus 로고    scopus 로고
    • Role for ADA/GCN5 products in antagonizing chromatin-mediated transcriptional repression
    • Pollard, K. J., and C. L. Peterson. 1997. Role for ADA/GCN5 products in antagonizing chromatin-mediated transcriptional repression. Mol. Cell. Biol. 17:6212-6222.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6212-6222
    • Pollard, K.J.1    Peterson, C.L.2
  • 198
    • 0029741343 scopus 로고    scopus 로고
    • Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases
    • Reifsnyder, C., J. Lowell, A. Clarke, and L. Pillus. 1996. Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases. Nat. Genet. 14:42-49.
    • (1996) Nat. Genet. , vol.14 , pp. 42-49
    • Reifsnyder, C.1    Lowell, J.2    Clarke, A.3    Pillus, L.4
  • 199
    • 0030876429 scopus 로고    scopus 로고
    • Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf/Swi and Srb/mediator complexes
    • Roberts, S. M., and F. Winston. 1997. Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf/Swi and Srb/mediator complexes. Genetics 147:451-465.
    • (1997) Genetics , vol.147 , pp. 451-465
    • Roberts, S.M.1    Winston, F.2
  • 200
    • 0029897489 scopus 로고    scopus 로고
    • SPT20/ADA5 encodes a novel protein functionally related to the TATA-binding protein and important for transcription in saccharomyces cerevisiae
    • Roberts, S. M., and F. Winston. 1996. SPT20/ADA5 encodes a novel protein functionally related to the TATA-binding protein and important for transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:3206-3213.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3206-3213
    • Roberts, S.M.1    Winston, F.2
  • 202
    • 0030271391 scopus 로고    scopus 로고
    • Histone acetylation and chromatin assembly: A single escort, multiple dances?
    • Roth, S. Y., and C. D. Allis. 1996. Histone acetylation and chromatin assembly: a single escort, multiple dances? Cell 87:5-8.
    • (1996) Cell , vol.87 , pp. 5-8
    • Roth, S.Y.1    Allis, C.D.2
  • 203
    • 0016723918 scopus 로고
    • Processing of newly synthesized histone molecules
    • Ruiz-Carrillo, A., L. J. Wangh, and V. G. Allfrey. 1975. Processing of newly synthesized histone molecules. Science 190:117-128.
    • (1975) Science , vol.190 , pp. 117-128
    • Ruiz-Carrillo, A.1    Wangh, L.J.2    Allfrey, V.G.3
  • 204
    • 0032524308 scopus 로고    scopus 로고
    • HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4
    • Ruiz-García, A. B., R. Sendra, M. Galiana, M. Pamblanco, J. E. Perez-Ortin, and V. Tordera. 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-García, A.B.1    Sendra, R.2    Galiana, M.3    Pamblanco, M.4    Perez-Ortin, J.E.5    Tordera, V.6
  • 205
    • 0031056461 scopus 로고    scopus 로고
    • Gcn5p is involved in the acetylation of histone H3 in nucleosomes
    • Ruiz-García, A. B., R. Sendra, M. Pamblanco, and V. Tordera. 1997. Gcn5p is involved in the acetylation of histone H3 in nucleosomes. FEBS Lett. 403: 186-190.
    • (1997) FEBS Lett. , vol.403 , pp. 186-190
    • Ruiz-García, A.B.1    Sendra, R.2    Pamblanco, M.3    Tordera, V.4
  • 207
    • 0031052033 scopus 로고    scopus 로고
    • Identification of native complexes containing the yeast coactivator/repressor proteins NGG1/ ADA3 and ADA2
    • Saleh, A., V. Lang, R. Cook, and C. J. Brandi. 1997. Identification of native complexes containing the yeast coactivator/repressor proteins NGG1/ ADA3 and ADA2. J. Biol. Chem. 272:5571-5578.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5571-5578
    • Saleh, A.1    Lang, V.2    Cook, R.3    Brandi, C.J.4
  • 209
    • 0019322514 scopus 로고
    • The interaction of high mobility proteins HMG14 and 17 with nucleosomes
    • Sandeen, G., W. I. Wood, and G. Felsenfeld. 1980. The interaction of high mobility proteins HMG14 and 17 with nucleosomes. Nucleic Acids Res. 8: 3757-3778.
    • (1980) Nucleic Acids Res. , vol.8 , pp. 3757-3778
    • Sandeen, G.1    Wood, W.I.2    Felsenfeld, G.3
  • 211
    • 0033556404 scopus 로고    scopus 로고
    • Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates
    • Schiltz, R. L., C. A. Mizzen, A. Vassilev, R. G. Cook, C. D. Allis, and Y. Nakatani. 1999. Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates. J. Biol. Chem. 274:1189-1192.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1189-1192
    • Schiltz, R.L.1    Mizzen, C.A.2    Vassilev, A.3    Cook, R.G.4    Allis, C.D.5    Nakatani, Y.6
  • 212
    • 0023608861 scopus 로고
    • Posttranslational modification and microtubule stability
    • Schulze, E., D. J. Asai, J. C. Bulinski, and M. Kirschner. 1987. Posttranslational modification and microtubule stability. J. Cell Biol. 105:2167-2177.
    • (1987) J. Cell Biol. , vol.105 , pp. 2167-2177
    • Schulze, E.1    Asai, D.J.2    Bulinski, J.C.3    Kirschner, M.4
  • 213
    • 0030880936 scopus 로고    scopus 로고
    • CREB-binding protein and p300/CBP-associated factor are transcriptional coactivators of the p53 tumor suppressor protein
    • Scolnick, D. M., N. H. Chehab, E. S. Stavridi, M. C. Lien, L. Caruso, E. Moran, S. L. Berger, and T. D. Halazonetis. 1997. CREB-binding protein and p300/CBP-associated factor are transcriptional coactivators of the p53 tumor suppressor protein. Cancer Res. 57:3693-3696.
    • (1997) Cancer Res. , vol.57 , pp. 3693-3696
    • Scolnick, D.M.1    Chehab, N.H.2    Stavridi, E.S.3    Lien, M.C.4    Caruso, L.5    Moran, E.6    Berger, S.L.7    Halazonetis, T.D.8
  • 214
    • 0034602829 scopus 로고    scopus 로고
    • MSL1 plays a central role in assembly of the MSL complex, essential for dosage compensation in drosophila
    • Scott, M. J., L. L. Pan, S. B. Cleland, A. L. Knox, and J. Heinrich. 2000. MSL1 plays a central role in assembly of the MSL complex, essential for dosage compensation in Drosophila. EMBO J. 19:144-155.
    • (2000) EMBO J. , vol.19 , pp. 144-155
    • Scott, M.J.1    Pan, L.L.2    Cleland, S.B.3    Knox, A.L.4    Heinrich, J.5
  • 215
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: Integrating signals with transcription factors and chromatin
    • Shikama, N., J. Lyon, and N. B. La Thangue. 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
  • 217
    • 0028104786 scopus 로고
    • Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription
    • Silverman, N., J. Agapite, and L. Guarente. 1994. Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription. Proc. Natl. Acad. Sci. USA 91:11665-11668.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11665-11668
    • Silverman, N.1    Agapite, J.2    Guarente, L.3
  • 218
    • 0029786690 scopus 로고    scopus 로고
    • CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription
    • Smith, C. L., S. A. Onate, M. J. Tsai, and B. W. O'Malley. 1996. CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription. Proc. Natl. Acad. Sci. USA 93:8884-8888.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8884-8888
    • Smith, C.L.1    Onate, S.A.2    Tsai, M.J.3    O'Malley, B.W.4
  • 221
    • 0033988212 scopus 로고    scopus 로고
    • The Drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation
    • Smith, E. R., A. Pannuti, W. Gu, A. Steurnagel, R. G. Cook, C. D. Allis, and J. C. Lucchesi. 2000. The Drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation. Mol. Cell. Biol. 20:312-318.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 312-318
    • Smith, E.R.1    Pannuti, A.2    Gu, W.3    Steurnagel, A.4    Cook, R.G.5    Allis, C.D.6    Lucchesi, J.C.7
  • 222
    • 0028847955 scopus 로고
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4
    • Sobel, R. E., R. G. Cook, C. A. Perry, A. T. Annunziato, and C. D. Allis. 1995. Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4. Proc. Natl. Acad. Sci. USA 92:1237-1241.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1237-1241
    • Sobel, R.E.1    Cook, R.G.2    Perry, C.A.3    Annunziato, A.T.4    Allis, C.D.5
  • 223
    • 0029655780 scopus 로고    scopus 로고
    • SSN genes that affect transcriptional repression in Saccharomyces cerevisiae encode SIN4, ROX3, and SRB proteins associated with RNA polymerase II
    • Song, W., I. Treich, N. Qian, S. Kuchin, and M. Carlson. 1996. SSN genes that affect transcriptional repression in Saccharomyces cerevisiae encode SIN4, ROX3, and SRB proteins associated with RNA polymerase II. Mol. Cell. Biol. 16:115-120.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 115-120
    • Song, W.1    Treich, I.2    Qian, N.3    Kuchin, S.4    Carlson, M.5
  • 225
    • 0030297734 scopus 로고    scopus 로고
    • Remodeling chromatin structures for transcription: What happens to the histones?
    • Steger, D. J., and J. L. Workman. 1996. Remodeling chromatin structures for transcription: what happens to the histones? BioEssays 18:875-884.
    • (1996) BioEssays , vol.18 , pp. 875-884
    • Steger, D.J.1    Workman, J.L.2
  • 226
    • 0023666071 scopus 로고
    • Activation of the yeast HO gene by release from multiple negative controls
    • Sternberg, P. W., M. J. Stern, I. Clark, and I. Herskowitz. 1987. Activation of the yeast HO gene by release from multiple negative controls. Cell 48: 567-577.
    • (1987) Cell , vol.48 , pp. 567-577
    • Sternberg, P.W.1    Stern, M.J.2    Clark, I.3    Herskowitz, I.4
  • 227
    • 0032911635 scopus 로고    scopus 로고
    • Functional organization of the yeast SAGA complex: Distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction
    • Sterner, D. E., P. A. Grant, S. M. Roberts, L. J. Duggan, R. Belotserkovskaya, L. A. Pacella, F. Winston, J. L. Workman, and S. L. Berger. 1999. Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction. Mol. Cell. Biol. 19:86-98.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 86-98
    • Sterner, D.E.1    Grant, P.A.2    Roberts, S.M.3    Duggan, L.J.4    Belotserkovskaya, R.5    Pacella, L.A.6    Winston, F.7    Workman, J.L.8    Berger, S.L.9
  • 228
    • 0019877270 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins: Identification of the sites of acetylation in high mobility group proteins 14 and 17
    • Sterner, R., G. Vidali, and V. G. Allfrey. 1981. Studies of acetylation and deacetylation in high mobility group proteins: identification of the sites of acetylation in high mobility group proteins 14 and 17. J. Biol. Chem. 256: 8892-8895.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8892-8895
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 229
    • 0018801554 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins: Identification of the sites of acetylation in HMG-1
    • Sterner, R., G. Vidali, and V. G. Allfrey. 1979. Studies of acetylation and deacetylation in high mobility group proteins: identification of the sites of acetylation in HMG-1. J. Biol. Chem. 254:11577-11583.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11577-11583
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 230
    • 0018265525 scopus 로고
    • Postsynthetic modification of high mobility group proteins: Evidence that high mobility group proteins are acetylated
    • Sterner, R., G. Vidali, R. L. Heinrikson, and V. G. Allfrey. 1978. Postsynthetic modification of high mobility group proteins: evidence that high mobility group proteins are acetylated. J. Biol. Chem. 253:7601-7604.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7601-7604
    • Sterner, R.1    Vidali, G.2    Heinrikson, R.L.3    Allfrey, V.G.4
  • 231
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D., and C. D. Allis. 2000. The language of covalent histone modifications. Nature 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 232
    • 0032503940 scopus 로고    scopus 로고
    • The TAFs in the HAT
    • Struhl, K., and Z. Moqtaderi. 1998. The TAFs in the HAT. Cell 94:1-4.
    • (1998) Cell , vol.94 , pp. 1-4
    • Struhl, K.1    Moqtaderi, Z.2
  • 233
    • 0033151812 scopus 로고    scopus 로고
    • The nucleosome remodeling complex, Snf/Swi, is required for the maintenance of transcription in vivo and is partially redundant with the histone acetyltransferase, Gcn5
    • Sudarsanam, P., Y. Cao, L. Wu, B. C. Laurent, and F. Winston. 1999. The nucleosome remodeling complex, Snf/Swi, is required for the maintenance of transcription in vivo and is partially redundant with the histone acetyltransferase, Gcn5. EMBO J. 18:3101-3106.
    • (1999) EMBO J. , vol.18 , pp. 3101-3106
    • Sudarsanam, P.1    Cao, Y.2    Wu, L.3    Laurent, B.C.4    Winston, F.5
  • 234
    • 0033590107 scopus 로고    scopus 로고
    • Sas3 is a histone acetyltransferase and requires a zinc finger motif
    • Takechi, S., and T. Nakayama. 1999. Sas3 is a histone acetyltransferase and requires a zinc finger motif. Biochem. Biophys. Res. Commun. 266:405-410.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 405-410
    • Takechi, S.1    Nakayama, T.2
  • 235
    • 0030786270 scopus 로고    scopus 로고
    • TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivatorr-1
    • Takeshita, A., G. R. Cardona, N. Koibuchi, C. S. Suen, and W. W. Chin. 1997. TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivatorr-1. J. Biol. Chem. 272:27629-27634.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27629-27634
    • Takeshita, A.1    Cardona, G.R.2    Koibuchi, N.3    Suen, C.S.4    Chin, W.W.5
  • 236
    • 0030967030 scopus 로고    scopus 로고
    • The t(11;16)(q23; p13) translocation in myelodysplastic syndrome fuses the MLL gene to the CBP gene
    • Taki, T., M. Sako, M. Tsuchida, and Y. Hayashi. 1997. The t(11;16)(q23; p13) translocation in myelodysplastic syndrome fuses the MLL gene to the CBP gene. Blood 89:3945-3950.
    • (1997) Blood , vol.89 , pp. 3945-3950
    • Taki, T.1    Sako, M.2    Tsuchida, M.3    Hayashi, Y.4
  • 237
    • 0026580006 scopus 로고
    • Brahma: A regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/SWI2
    • Tamkun, J. W., R. Deuring, M. P. Scott, M. Kissinger, A. M. Pattatucci, T. C. Kaufman, and J. A. Kennison. 1992. brahma: a regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/SWI2. Cell 68:561-572.
    • (1992) Cell , vol.68 , pp. 561-572
    • Tamkun, J.W.1    Deuring, R.2    Scott, M.P.3    Kissinger, M.4    Pattatucci, A.M.5    Kaufman, T.C.6    Kennison, J.A.7
  • 238
    • 0033603555 scopus 로고    scopus 로고
    • Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
    • Tanner, K. G., R. C. Trievel, M. H. Kuo, R. M. Howard, S. L. Berger, C. D. Allis, R. Marmorstein, and J. M. Denu. 1999. Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator. J. Biol. Chem. 274:18157-18160.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18157-18160
    • Tanner, K.G.1    Trievel, R.C.2    Kuo, M.H.3    Howard, R.M.4    Berger, S.L.5    Allis, C.D.6    Marmorstein, R.7    Denu, J.M.8
  • 239
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcription regulator Rpd3p
    • Taunton, J., C. A. Hassig, and S. L. Schreiber. 1996. A mammalian histone deacetylase related to the yeast transcription regulator Rpd3p. Science 272: 408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 240
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L., and I. B. Zhulin. 1999. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 241
    • 0029617947 scopus 로고
    • Virus induction of human IFN-β gene expression requires the assembly of an enhanceosome
    • Thanos, D., and T. Maniatis. 1995. Virus induction of human IFN-β 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
  • 242
    • 0029278720 scopus 로고
    • Myb: An old oncoprotein with new roles
    • Thompson, M. A., and R. G. Ramsay. 1995. Myb: an old oncoprotein with new roles. Bioessays 17:341-350.
    • (1995) Bioessays , vol.17 , pp. 341-350
    • Thompson, M.A.1    Ramsay, R.G.2
  • 244
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
    • Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. K. Glass, and M. G. Rosenfeld. 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677-684.
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1    Rose, D.W.2    Inostroza, J.3    Kamei, Y.4    Westin, S.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 246
    • 0029922959 scopus 로고    scopus 로고
    • Role of interactions between the origin recognition complex and SIR1 in transcriptional silencing
    • Triolo, T., and R. Sternglanz. 1996. Role of interactions between the origin recognition complex and SIR1 in transcriptional silencing. Nature 381:251-253.
    • (1996) Nature , vol.381 , pp. 251-253
    • Triolo, T.1    Sternglanz, A.R.2
  • 247
    • 0032484010 scopus 로고    scopus 로고
    • Gcn5p, a transcription-related histone acetyltransferase, acetylates nucleosomes and folded nucleosomal arrays in the absence of other protein subunits
    • Tse, C., E. I. Georgieva, A. B. Ruiz-García, R. Sendra, and J. C. Hansen. 1998. Gcn5p, a transcription-related histone acetyltransferase, acetylates nucleosomes and folded nucleosomal arrays in the absence of other protein subunits. J. Biol. Chem. 273:32388-32392.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32388-32392
    • Tse, C.1    Georgieva, E.I.2    Ruiz-García, A.B.3    Sendra, R.4    Hansen, J.C.5
  • 248
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner, B. M. 1993. Decoding the nucleosome. Cell 75:5-8.
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 249
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner, B. M., A. J. Birley, and J. Lavender. 1992. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 69:375-384.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 252
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone-binding subunit of the human hat1 acetyltransferase
    • Verreault, A., P. D. Kaufman, R. Kobayashi, and B. Stillman. 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
  • 253
    • 0030272047 scopus 로고    scopus 로고
    • Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
    • Verreault, A., P. D. Kaufman, R. Kobayashi, and B. Stillman. 1996. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 87:95-104.
    • (1996) Cell , vol.87 , pp. 95-104
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 254
    • 0030249382 scopus 로고    scopus 로고
    • TAFs mediate transcriptional activation and promoter selectivity
    • Verrijzer, C., and R. Tjian. 1996. TAFs mediate transcriptional activation and promoter selectivity. Trends Biochem. Sci. 21:338-342.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 338-342
    • Verrijzer, C.1    Tjian, R.2
  • 255
    • 0032518944 scopus 로고    scopus 로고
    • The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways
    • Voegel, J. J., M. J. Heine, M. Tini, V. Vivat, P. Chambon, and H. Gronemeyer. 1998. The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J. 17:507-519.
    • (1998) EMBO J. , vol.17 , pp. 507-519
    • Voegel, J.J.1    Heine, M.J.2    Tini, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6
  • 256
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel, J. J., M. J. Heine, C. Zechel, P. Chambon, and H. Gronemeyer. 1996. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:3667-3675.
    • (1996) EMBO J. , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 257
    • 0024080427 scopus 로고
    • The human beta-globin gene 3′ enhancer contains multiple binding sites for an erythroid-specific protein
    • Wall, L., E. deBoer, and F. Grosveld. 1988. The human beta-globin gene 3′ enhancer contains multiple binding sites for an erythroid-specific protein. Genes Dev. 2:1089-1100.
    • (1988) Genes Dev. , vol.2 , pp. 1089-1100
    • Wall, L.1    DeBoer, E.2    Grosveld, F.3
  • 258
    • 0032793296 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes can mediate transcriptional activation by the major glucocorticoid receptor activation domain
    • Wallberg, A. E., K. E. Neely, J. A. Gustafsson, J. L. Workman, A. P. Wright, and P. A. Grant. 1999. Histone acetyltransferase complexes can mediate transcriptional activation by the major glucocorticoid receptor activation domain. Mol. Cell. Biol. 19:5952-5959.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5952-5959
    • Wallberg, A.E.1    Neely, K.E.2    Gustafsson, J.A.3    Workman, J.L.4    Wright, A.P.5    Grant, P.A.6
  • 259
    • 0032189630 scopus 로고    scopus 로고
    • Drosophila CBP represses the transcription factor TCF to antagonize Wingless signalling
    • Waltzer, L., and M. Bienz. 1998. Drosophila CBP represses the transcription factor TCF to antagonize Wingless signalling. Nature 395:521-525.
    • (1998) Nature , vol.395 , pp. 521-525
    • Waltzer, L.1    Bienz, M.2
  • 260
    • 0032031606 scopus 로고    scopus 로고
    • Critical residues for histone acetylation by GCN5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo
    • Wang, L., L. Liu, and S. L. Berger. 1998. Critical residues for histone acetylation by GCN5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo. Genes Dev. 12:640-653.
    • (1998) Genes Dev. , vol.12 , pp. 640-653
    • Wang, L.1    Liu, L.2    Berger, S.L.3
  • 261
    • 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., C. Mizzen, C. Ying, R. Candau, N. Barlev, J. Brownell, C. D. Allis, and S. Berger. 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    Allis, C.D.7    Berger, S.8
  • 262
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei, P., M. E. Garber, S. M. Fang, W. H. Fischer, and K. A. Jones. 1998. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 92:451-462.
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.M.3    Fischer, W.H.4    Jones, K.A.5
  • 264
    • 0029043782 scopus 로고
    • Mechanism of active transcriptional repression by the retinoblastoma protein
    • Weintraub, S. J., K. N. Chow, R. X. Luo, S. H. Zhang, S. He, and D. C. Dean. 1995. Mechanism of active transcriptional repression by the retinoblastoma protein. Nature 375:812-815.
    • (1995) Nature , vol.375 , pp. 812-815
    • Weintraub, S.J.1    Chow, K.N.2    Luo, R.X.3    Zhang, S.H.4    He, S.5    Dean, D.C.6
  • 267
    • 0033551391 scopus 로고    scopus 로고
    • Reassessing the role of C-MYB in tumorigenesis
    • Weston, K. 1999. Reassessing the role of C-MYB in tumorigenesis. Oncogene 18:3034-3038.
    • (1999) Oncogene , vol.18 , pp. 3034-3038
    • Weston, K.1
  • 268
    • 0023426588 scopus 로고
    • The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus
    • Whiteway, M., R. Freedman, S. Van Arsdell, J. W. Szostak, and J. Thorner. 1987. The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus. Mol. Cell. Biol. 7:3713-3722.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3713-3722
    • Whiteway, M.1    Freedman, R.2    Van Arsdell, S.3    Szostak, J.W.4    Thorner, J.5
  • 269
    • 0032516156 scopus 로고    scopus 로고
    • II-containing complex without TBP in transcription by RNA polymerase II
    • II-containing complex without TBP in transcription by RNA polymerase II. Nature 393:187-191.
    • (1998) Nature , vol.393 , pp. 187-191
    • Wieczorek, E.1    Brand, M.2    Jacq, X.3    Tora, L.4
  • 271
    • 0000112508 scopus 로고
    • Analysis of SPT genes: A genetic approach toward analysis of TFIID, histones, and other transcription factors of yeast
    • S. L. McKnight and K. R. Yamamoto (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Winston, F. 1992. Analysis of SPT genes: a genetic approach toward analysis of TFIID, histones, and other transcription factors of yeast, p. 1271-1293. In S. L. McKnight and K. R. Yamamoto (ed.), Transcriptional regulation. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) Transcriptional Regulation , pp. 1271-1293
    • Winston, F.1
  • 272
    • 17444386662 scopus 로고    scopus 로고
    • The bromodomain: A chromatin-targeting module?
    • Winston, F., and C. D. Allis. 1999. The bromodomain: a chromatin-targeting module? Nat. Struct. Biol. 6:601-604.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 601-604
    • Winston, F.1    Allis, C.D.2
  • 274
    • 0032555691 scopus 로고    scopus 로고
    • Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase
    • Wolf, E., A. Vassilev, Y. Makino, A. Sali, Y. Nakatani, and S. K. Burley. 1998. Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase. Cell 94:439-449.
    • (1998) Cell , vol.94 , pp. 439-449
    • Wolf, E.1    Vassilev, A.2    Makino, Y.3    Sali, A.4    Nakatani, Y.5    Burley, S.K.6
  • 276
    • 85047674124 scopus 로고
    • High-mobility group and other nonhistone substrates for nuclear histone N-acetyltransferase
    • Wong, L. C., D. J. Sharpe, and S. S. Wong. 1991. High-mobility group and other nonhistone substrates for nuclear histone N-acetyltransferase. Biochem. Genet. 29:461-475.
    • (1991) Biochem. Genet. , vol.29 , pp. 461-475
    • Wong, L.C.1    Sharpe, D.J.2    Wong, S.S.3
  • 277
    • 0023661185 scopus 로고
    • Binding of transcription factor TFIID to the major late promoter during in vitro nucleosome assembly potentiates subsequent initiation by RNA polymerase II
    • Workman, J. L., and R. G. Roeder. 1987. Binding of transcription factor TFIID to the major late promoter during in vitro nucleosome assembly potentiates subsequent initiation by RNA polymerase II. Cell 51:613-622.
    • (1987) Cell , vol.51 , pp. 613-622
    • Workman, J.L.1    Roeder, R.G.2
  • 280
    • 0031678679 scopus 로고    scopus 로고
    • Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates
    • Xu, W., D. G. Edmondson, and S. Y. Roth. 1998. 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
  • 281
    • 0030712311 scopus 로고    scopus 로고
    • Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60
    • Yamamoto, T., and M. Horikoshi. 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
  • 282
    • 0027143707 scopus 로고
    • Isolation and characterization of the SUD1 gene, which encodes a global repressor of core promoter activity in Saccharomyces cerevisiae
    • Yamashita, I. 1993. Isolation and characterization of the SUD1 gene, which encodes a global repressor of core promoter activity in Saccharomyces cerevisiae. Mol. Gen. Genet. 241:616-626.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 616-626
    • Yamashita, I.1
  • 283
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral E1A oncoprotein
    • Yang, X.-J., V. V. Ogryzko, J. Nishikawa, B. H. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral E1A oncoprotein. 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
  • 284
    • 0029773871 scopus 로고    scopus 로고
    • The nuclear hormone receptor coactivator SRC-1 is a specific target of p300
    • Yao, T. P., G. Ku, N. Zhou, R. Scully, and D. M. Livingston. 1996. The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc. Natl. Acad. Sci. USA 93:10626-10631.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10626-10631
    • Yao, T.P.1    Ku, G.2    Zhou, N.3    Scully, R.4    Livingston, D.M.5
  • 285
    • 0032192502 scopus 로고    scopus 로고
    • Characterization of a human homologue of the Saccharomyces cerevisiae transcription factor Spt3 (SUPT3H)
    • Yu, J., J. M. Madison, S. Mundlos, F. Winston, and B. R. Olsen. 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
  • 286
    • 0034116142 scopus 로고    scopus 로고
    • Architectural transcription factors and the SAGA complex function in parallel pathways to activate transcription
    • Yu, Y., P. Eriksson, and D. J. Stillman. 2000. Architectural transcription factors and the SAGA complex function in parallel pathways to activate transcription. Mol. Cell. Biol. 20:2350-2357.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2350-2357
    • Yu, Y.1    Eriksson, P.2    Stillman, D.J.3
  • 287
    • 0032544123 scopus 로고    scopus 로고
    • Acetylation and modulation of crythroid Krüppel-like factor (EKLF) activity by interaction with histone acetyltransferases
    • Zhang, W., and J. J. Bicker. 1998. Acetylation and modulation of crythroid Krüppel-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    Bicker, J.J.2


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