메뉴 건너뛰기




Volumn 26, Issue 10, 2004, Pages 1076-1087

Lysine acetylation and the bromodomain: A new partnership for signaling

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; GENERAL CONTROL NON DEREPRESSIBLE 5 PROTEIN; HISTONE; HISTONE ACETYLTRANSFERASE PCAF; LYSINE; MYOD PROTEIN; PROTEIN; PROTEIN 14 3 3; PROTEIN C MYB; PROTEIN P53; PROTEIN SH2; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR TAF1; UNCLASSIFIED DRUG;

EID: 7044250740     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20104     Document Type: Review
Times cited : (316)

References (140)
  • 1
    • 0014430407 scopus 로고
    • Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones
    • Vidali G, Gershey E, Allfrey VG. 1968. Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones. J Biol Chem 243:6361-6366.
    • (1968) J Biol Chem , vol.243 , pp. 6361-6366
    • Vidali, G.1    Gershey, E.2    Allfrey, V.G.3
  • 2
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides T. 2000. Acetylation: a regulatory modification to rival phosphorylation? EMBO J 19:1176-1179.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 3
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner DE, Berger SL. 2000. Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64:435-459.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 4
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: An acetyl-lysine binding domain
    • Zeng L, Zhou MM. 2002. Bromodomain: an acetyl-lysine binding domain. FEBS Lett 513:124-128.
    • (2002) FEBS Lett , vol.513 , pp. 124-128
    • Zeng, L.1    Zhou, M.M.2
  • 6
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger CM, Schreiber SL. 2002. Deacetylase enzymes: biological functions and the use of small-molecule inhibitors. Chem Biol 9:3-16.
    • (2002) Chem Biol , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 7
    • 0018801554 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1
    • Sterner R, Vidali G, Allfrey VG. 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
  • 8
    • 0034646638 scopus 로고    scopus 로고
    • Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes
    • Bergel M, Herrera JE, Thatcher BJ, Prymakowska-Bosak M, Vassilev A, et al. 2000. Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes. J Biol Chem 275:11514-11520.
    • (2000) J Biol Chem , vol.275 , pp. 11514-11520
    • Bergel, M.1    Herrera, J.E.2    Thatcher, B.J.3    Prymakowska-Bosak, M.4    Vassilev, A.5
  • 9
    • 0032933141 scopus 로고    scopus 로고
    • Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes
    • Herrera JE, Sakaguchi K, Bergel M, Trieschmann L, Nakatani Y, et al. 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
  • 12
    • 0347624645 scopus 로고    scopus 로고
    • Growth inhibition by the mammalian SWI-SNF subunit Brm is regulated by acetylation
    • Bourachot B, Yaniv M, Muchardt C. 2003. Growth inhibition by the mammalian SWI-SNF subunit Brm is regulated by acetylation. EMBO J 22:6505-6515.
    • (2003) EMBO J , vol.22 , pp. 6505-6515
    • Bourachot, B.1    Yaniv, M.2    Muchardt, C.3
  • 13
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • Chen H, Lin RJ, Xie W, Wilpitz D, Evans RM. 1999. Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 98:675-686.
    • (1999) Cell , vol.98 , pp. 675-686
    • Chen, H.1    Lin, R.J.2    Xie, W.3    Wilpitz, D.4    Evans, R.M.5
  • 14
    • 0033767150 scopus 로고    scopus 로고
    • Acetylation by PCAF enhances CIITA nuclear accumulation and transactivation of major histocompatibility complex class II genes
    • Spilanakis C, Papamatheakis J, Kretsovali A. 2000. Acetylation by PCAF enhances CIITA nuclear accumulation and transactivation of major histocompatibility complex class II genes. Mol Cell Biol 20:8489-8498.
    • (2000) Mol Cell Biol , vol.20 , pp. 8489-8498
    • Spilanakis, C.1    Papamatheakis, J.2    Kretsovali, A.3
  • 15
    • 11144353713 scopus 로고    scopus 로고
    • Acetylation of beta-catenin by p300 regulates beta-catenin-Tcf4 interaction
    • Levy L, Wei Y, Labalette C, Wu Y, Renard CA, et al. 2004. Acetylation of beta-catenin by p300 regulates beta-catenin-Tcf4 interaction. Mol Cell Biol 24:3404-3414.
    • (2004) Mol Cell Biol , vol.24 , pp. 3404-3414
    • Levy, L.1    Wei, Y.2    Labalette, C.3    Wu, Y.4    Renard, C.A.5
  • 17
    • 0035724042 scopus 로고    scopus 로고
    • Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP
    • Vo N, Fjeld C, Goodman RH. 2001. Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP. Mol Cell Biol 21:6181-6188.
    • (2001) Mol Cell Biol , vol.21 , pp. 6181-6188
    • Vo, N.1    Fjeld, C.2    Goodman, R.H.3
  • 18
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • Imhof A, Yang X-J, Ogryzko VV, Nakatani Y, Wolffe AP, et al. 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
  • 19
    • 0035907267 scopus 로고    scopus 로고
    • p300-mediated acetylation of human transcriptional coactivator PC4 is inhibited by phosphorylation
    • Kumar BR, Swaminathan V, Banerjee S, Kundu TK. 2001. p300-mediated acetylation of human transcriptional coactivator PC4 is inhibited by phosphorylation. J Biol Chem 276:16804-16809.
    • (2001) J Biol Chem , vol.276 , pp. 16804-16809
    • Kumar, B.R.1    Swaminathan, V.2    Banerjee, S.3    Kundu, T.K.4
  • 20
    • 0042358902 scopus 로고    scopus 로고
    • Transcription factor IIB acetylates itself to regulate transcription
    • Choi CH, Hiromura M, Usheva A. 2003. Transcription factor IIB acetylates itself to regulate transcription. Nature 424:965-969.
    • (2003) Nature , vol.424 , pp. 965-969
    • Choi, C.H.1    Hiromura, M.2    Usheva, A.3
  • 21
    • 0035868764 scopus 로고    scopus 로고
    • Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription
    • Muth V, Nadaud S, Grummt I, Voit R. 2001. Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. EMBO J 20:1353-1362.
    • (2001) EMBO J , vol.20 , pp. 1353-1362
    • Muth, V.1    Nadaud, S.2    Grummt, I.3    Voit, R.4
  • 22
    • 0035097884 scopus 로고    scopus 로고
    • MCM3AP, a novel acetyltransferase that acetylates replication protein MCM3
    • Takei Y, Swietlik M, Tanoue A, Tsujimoto G, Kouzarides T, et al. 2001. MCM3AP, a novel acetyltransferase that acetylates replication protein MCM3. EMBO Rep 2:119-123.
    • (2001) EMBO Rep , vol.2 , pp. 119-123
    • Takei, Y.1    Swietlik, M.2    Tanoue, A.3    Tsujimoto, G.4    Kouzarides, T.5
  • 23
    • 2442431498 scopus 로고    scopus 로고
    • The post-translational modifications of proliferating cell nuclear antigen (PCNA): Acetylation, not phosphorylation, plays an important role in the regulation of its function
    • Naryzhny SN, Lee H. 2004. The post-translational modifications of proliferating cell nuclear antigen (PCNA): acetylation, not phosphorylation, plays an important role in the regulation of its function. J Biol Chem 279:20194-20199.
    • (2004) J Biol Chem , vol.279 , pp. 20194-20199
    • Naryzhny, S.N.1    Lee, H.2
  • 24
    • 0034969453 scopus 로고    scopus 로고
    • Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300
    • Hasan S, Stucki M, Hassa PO, Imhof R, Gehrig P, et al. 2001. Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300. Mol Cell 7:1221-1231.
    • (2001) Mol Cell , vol.7 , pp. 1221-1231
    • Hasan, S.1    Stucki, M.2    Hassa, P.O.3    Imhof, R.4    Gehrig, P.5
  • 25
    • 0036184090 scopus 로고    scopus 로고
    • Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription
    • Tini M, Benecke A, Um SJ, Torchia J, Evans RM, et al. 2002. Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. Mol Cell 9:265-277.
    • (2002) Mol Cell , vol.9 , pp. 265-277
    • Tini, M.1    Benecke, A.2    Um, S.J.3    Torchia, J.4    Evans, R.M.5
  • 26
    • 0037185024 scopus 로고    scopus 로고
    • DNA damage-induced translocation of the Werner helicase is regulated by acetylation
    • Blander G, Zalle N, Daniely Y, Taplick J, Gray MD, et al. 2002. DNA damage-induced translocation of the Werner helicase is regulated by acetylation. J Biol Chem 277:50934-50940.
    • (2002) J Biol Chem , vol.277 , pp. 50934-50940
    • Blander, G.1    Zalle, N.2    Daniely, Y.3    Taplick, J.4    Gray, M.D.5
  • 27
    • 0037133040 scopus 로고    scopus 로고
    • Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion
    • Ivanov D, Schleiffer A, Eisenhaber F, Mechtler K, Haering CH, et al. 2002. Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion. Curr Biol 12:323-328.
    • (2002) Curr Biol , vol.12 , pp. 323-328
    • Ivanov, D.1    Schleiffer, A.2    Eisenhaber, F.3    Mechtler, K.4    Haering, C.H.5
  • 28
    • 0344663967 scopus 로고    scopus 로고
    • Two putative acetyltransferases, san and deco, are required for establishing sister chromatid cohesion in Drosophila
    • Williams BC, Garrett-Engele CM, Li Z, Williams EV, Rosenman ED, et al. 2003. Two putative acetyltransferases, san and deco, are required for establishing sister chromatid cohesion in Drosophila. Curr Biol 13:2025-2036.
    • (2003) Curr Biol , vol.13 , pp. 2025-2036
    • Williams, B.C.1    Garrett-Engele, C.M.2    Li, Z.3    Williams, E.V.4    Rosenman, E.D.5
  • 29
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetylation and ubiquitination
    • Gronroos E, Hellman U, Heldin CH, Ericsson J. 2002. Control of Smad7 stability by competition between acetylation and ubiquitination. Mol Cell 10:483-493.
    • (2002) Mol Cell , vol.10 , pp. 483-493
    • Gronroos, E.1    Hellman, U.2    Heldin, C.H.3    Ericsson, J.4
  • 31
    • 12144286529 scopus 로고    scopus 로고
    • Acetylation of the C Terminus of Ku70 by CBP and PCAF Controls Bax-Mediated Apoptosis
    • Cohen HY, Lavu S, Bitterman KJ, Hekking B, Imahiyerobo TA, et al. 2004. Acetylation of the C Terminus of Ku70 by CBP and PCAF Controls Bax-Mediated Apoptosis. Mol Cell 13:627-638.
    • (2004) Mol Cell , vol.13 , pp. 627-638
    • Cohen, H.Y.1    Lavu, S.2    Bitterman, K.J.3    Hekking, B.4    Imahiyerobo, T.A.5
  • 32
    • 0034177669 scopus 로고    scopus 로고
    • Acetylation of importin-alpha nuclear import factors by CBP/p300
    • Bannister AJ, Miska EA, Gorlich D, Kouzarides T. 2000. Acetylation of importin-alpha nuclear import factors by CBP/p300. Curr Biol 10:467-470.
    • (2000) Curr Biol , vol.10 , pp. 467-470
    • Bannister, A.J.1    Miska, E.A.2    Gorlich, D.3    Kouzarides, T.4
  • 33
    • 0034687687 scopus 로고    scopus 로고
    • Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP
    • Zhang Q, Yao H, Vo N, Goodman RH. 2000. Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP. Proc Natl Acad Sci USA 97:14323-14328.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14323-14328
    • Zhang, Q.1    Yao, H.2    Vo, N.3    Goodman, R.H.4
  • 34
    • 0037064068 scopus 로고    scopus 로고
    • Acetylation of the adenovirus-transforming protein E1A determines nuclear localization by disrupting association with importin-alpha
    • Madison DL, Yaciuk P, Kwok RP, Lundblad JR. 2002. Acetylation of the adenovirus-transforming protein E1A determines nuclear localization by disrupting association with importin-alpha. J Biol Chem 277:38755-38763.
    • (2002) J Biol Chem , vol.277 , pp. 38755-38763
    • Madison, D.L.1    Yaciuk, P.2    Kwok, R.P.3    Lundblad, J.R.4
  • 35
    • 0036840610 scopus 로고    scopus 로고
    • Stimulation of DNA replication from the polyomavirus origin by PCAF and GCN5 acetyltransferases: Acetylation of large T antigen
    • Xie AY, Bermudez VP, Folk WR. 2002. Stimulation of DNA replication from the polyomavirus origin by PCAF and GCN5 acetyltransferases: acetylation of large T antigen. Mol Cell Biol 22:7907-7918.
    • (2002) Mol Cell Biol , vol.22 , pp. 7907-7918
    • Xie, A.Y.1    Bermudez, V.P.2    Folk, W.R.3
  • 36
    • 0033230613 scopus 로고    scopus 로고
    • HIV-1 tat transcriptional activity is regulated by acetylation
    • Kiernan RE, Vanhulle C, Schiltz L, Adam E, Xiao H, et al. 1999. HIV-1 tat transcriptional activity is regulated by acetylation. EMBO J 18:6106-6118.
    • (1999) EMBO J , vol.18 , pp. 6106-6118
    • Kiernan, R.E.1    Vanhulle, C.2    Schiltz, L.3    Adam, E.4    Xiao, H.5
  • 37
    • 0033576557 scopus 로고    scopus 로고
    • Acetylation of the HIV-1 Tat protein by p300 is important for its transcriptional activity
    • Ott M, Schnolzer M, Garnica J, Fischle W, Emiliani S, et al. 1999. Acetylation of the HIV-1 Tat protein by p300 is important for its transcriptional activity. Curr Biol 9:1489-1492.
    • (1999) Curr Biol , vol.9 , pp. 1489-1492
    • Ott, M.1    Schnolzer, M.2    Garnica, J.3    Fischle, W.4    Emiliani, S.5
  • 38
    • 0037704925 scopus 로고    scopus 로고
    • A novel Arabidopsis acetyltransferase interacts with the geminivirus movement protein NSP
    • McGarry RC, Barron YD, Carvalho MF, Hill JE, Gold D, et al. 2003. A novel Arabidopsis acetyltransferase interacts with the geminivirus movement protein NSP. Plant Cell 15:1605-1618.
    • (2003) Plant Cell , vol.15 , pp. 1605-1618
    • McGarry, R.C.1    Barron, Y.D.2    Carvalho, M.F.3    Hill, J.E.4    Gold, D.5
  • 39
    • 84983719289 scopus 로고    scopus 로고
    • The small delta antigen of hepatitis delta virus is an acetylated protein and acetylation of lysine 72 may influence its cellular localization and viral RNA synthesis
    • Mu JJ, Tsay YG, Juan LJ, Fu TF, Huang WH, et al. 2004. The small delta antigen of hepatitis delta virus is an acetylated protein and acetylation of lysine 72 may influence its cellular localization and viral RNA synthesis. Virology 319:60-70.
    • (2004) Virology , vol.319 , pp. 60-70
    • Mu, J.J.1    Tsay, Y.G.2    Juan, L.J.3    Fu, T.F.4    Huang, W.H.5
  • 40
    • 0037023326 scopus 로고    scopus 로고
    • The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation
    • Bell SD, Botting CH, Wardleworth BN, Jackson SP, White MF. 2002. The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation. Science 296:148-151.
    • (2002) Science , vol.296 , pp. 148-151
    • Bell, S.D.1    Botting, C.H.2    Wardleworth, B.N.3    Jackson, S.P.4    White, M.F.5
  • 41
    • 0032574810 scopus 로고    scopus 로고
    • Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY
    • Ramakrishnan R, Schuster M, Bourret RB. 1998. Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY. Proc Natl Acad Sci USA 95:4918-4923.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4918-4923
    • Ramakrishnan, R.1    Schuster, M.2    Bourret, R.B.3
  • 42
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • Starai VJ, Celic I, Cole RN, Boeke JD, Escalante-Semerena JC. 2002. Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298:2390-2392.
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 43
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. 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
  • 44
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner BM. 2000. Histone acetylation and an epigenetic code. Bioessays 22:836-845.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 45
    • 0037072601 scopus 로고    scopus 로고
    • Chromatin higher order folding-wrapping up transcription
    • Horn PJ, Peterson CL. 2002. Chromatin higher order folding-wrapping up transcription. Science 297:1824-1827.
    • (2002) Science , vol.297 , pp. 1824-1827
    • Horn, P.J.1    Peterson, C.L.2
  • 46
    • 0038204415 scopus 로고    scopus 로고
    • The diverse functions of histone acetyltransferase complexes
    • Carrozza MJ, Utley RT, Workman JL, Cote J. 2003. The diverse functions of histone acetyltransferase complexes. Trends Genet 19:321-329.
    • (2003) Trends Genet , vol.19 , pp. 321-329
    • Carrozza, M.J.1    Utley, R.T.2    Workman, J.L.3    Cote, J.4
  • 47
    • 0037111879 scopus 로고    scopus 로고
    • Requirement of Hos2 histone deacetylase for gene activity in yeast
    • Wang A, Kurdistani SK, Grunstein M. 2002. Requirement of Hos2 histone deacetylase for gene activity in yeast. Science 298:1412-1414.
    • (2002) Science , vol.298 , pp. 1412-1414
    • Wang, A.1    Kurdistani, S.K.2    Grunstein, M.3
  • 48
    • 1642580754 scopus 로고    scopus 로고
    • The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes
    • De Nadal E, Zapater M, Alepuz PM, Sumoy L, Mas G, et al. 2004. The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes. Nature 427:370-374.
    • (2004) Nature , vol.427 , pp. 370-374
    • De Nadal, E.1    Zapater, M.2    Alepuz, P.M.3    Sumoy, L.4    Mas, G.5
  • 49
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG. 1997. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90:595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 50
    • 0032530486 scopus 로고    scopus 로고
    • DNA damage activates p53 through a phosphorylation-acetylation cascade
    • Sakaguchi K, Herrera JE, Saito S, Miki T, Bustin M, et al. 1998. DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev 12:2831-2841.
    • (1998) Genes Dev , vol.12 , pp. 2831-2841
    • Sakaguchi, K.1    Herrera, J.E.2    Saito, S.3    Miki, T.4    Bustin, M.5
  • 51
    • 0032906633 scopus 로고    scopus 로고
    • p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage
    • Liu L, Scolnick DM, Trievel RC, Zhang HB, Marmorstein R, et al. 1999. p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Mol Cell Biol 19:1202-1909.
    • (1999) Mol Cell Biol , vol.19 , pp. 1202-1909
    • Liu, L.1    Scolnick, D.M.2    Trievel, R.C.3    Zhang, H.B.4    Marmorstein, R.5
  • 52
    • 18244408596 scopus 로고    scopus 로고
    • DNA damage-dependent acetylation of p73 dictates the selective activation of apoptotic target genes
    • Costanzo A, Merlo P, Pediconi N, Fulco M, Sartorelli V, et al. 2002. DNA damage-dependent acetylation of p73 dictates the selective activation of apoptotic target genes. Mol Cell 9:175-186.
    • (2002) Mol Cell , vol.9 , pp. 175-186
    • Costanzo, A.1    Merlo, P.2    Pediconi, N.3    Fulco, M.4    Sartorelli, V.5
  • 53
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB
    • Chen LF, Mu Y, Greene WC. 2002. Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J 21:6539-6548.
    • (2002) EMBO J , vol.21 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 54
    • 0037462725 scopus 로고    scopus 로고
    • Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65
    • Kiernan R, Bres V, Ng RW, Coudart MP, El Messaoudi S, et al. 2003. Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65. J Biol Chem 278:2758-2766.
    • (2003) J Biol Chem , vol.278 , pp. 2758-2766
    • Kiernan, R.1    Bres, V.2    Ng, R.W.3    Coudart, M.P.4    El Messaoudi, S.5
  • 55
    • 0038813706 scopus 로고    scopus 로고
    • Up-regulation of p300 binding and p50 acetylation in tumor necrosis factor-alpha-induced cyclooxygenase-2 promoter activation
    • Deng WG, Zhu Y, Wu KK. 2003. Up-regulation of p300 binding and p50 acetylation in tumor necrosis factor-alpha-induced cyclooxygenase-2 promoter activation. J Biol Chem 278:4770-4777.
    • (2003) J Biol Chem , vol.278 , pp. 4770-4777
    • Deng, W.G.1    Zhu, Y.2    Wu, K.K.3
  • 56
    • 0035900679 scopus 로고    scopus 로고
    • Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene
    • Shankaranarayanan P, Chaitidis P, Kuhn H, Nigam S. 2001. Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene. J Biol Chem 276:42753-42760.
    • (2001) J Biol Chem , vol.276 , pp. 42753-42760
    • Shankaranarayanan, P.1    Chaitidis, P.2    Kuhn, H.3    Nigam, S.4
  • 57
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome
    • Munshi N, Merika M, Yie J, Senger K, Chen G, et al. 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
  • 58
    • 0033636744 scopus 로고    scopus 로고
    • Competitive recruitment of CBP and Rb-HDAC regulates UBF acetylation and ribosomal transcription
    • Pelletier G, Stefanovsky VY, Faubladier M, Hirschler-Laszkiewicz I, Savard J, et al. 2000. Competitive recruitment of CBP and Rb-HDAC regulates UBF acetylation and ribosomal transcription. Mol Cell 6:1059-1066.
    • (2000) Mol Cell , vol.6 , pp. 1059-1066
    • Pelletier, G.1    Stefanovsky, V.Y.2    Faubladier, M.3    Hirschler-Laszkiewicz, I.4    Savard, J.5
  • 59
    • 0032189630 scopus 로고    scopus 로고
    • Drosophila CBP represses the transcription factor TCF to antagonize Wingless signalling
    • Waltzer L, Bienz M. 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
  • 60
    • 0037444225 scopus 로고    scopus 로고
    • Acetylation regulates subcellular localization of the Wnt signaling nuclear effector POP-1
    • Gay F, Calvo D, Lo MC, Ceron J, Maduro M, et al. 2003. Acetylation regulates subcellular localization of the Wnt signaling nuclear effector POP-1. Genes Dev 17:717-722.
    • (2003) Genes Dev , vol.17 , pp. 717-722
    • Gay, F.1    Calvo, D.2    Lo, M.C.3    Ceron, J.4    Maduro, M.5
  • 61
    • 0032476596 scopus 로고    scopus 로고
    • Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo
    • Li Q, Herrler M, Landsberger N, Kaludov N, Ogryzko VV, et al. 1998. Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo. EMBO J 17:6300-6315.
    • (1998) EMBO J , vol.17 , pp. 6300-6315
    • Li, Q.1    Herrler, M.2    Landsberger, N.3    Kaludov, N.4    Ogryzko, V.V.5
  • 62
    • 0033231604 scopus 로고    scopus 로고
    • Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program
    • Sartorelli V, Puri PL, Hamamori Y, Ogryzko V, Chung G, et al. 1999. Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program. Mol Cell 4:725-734.
    • (1999) Mol Cell , vol.4 , pp. 725-734
    • Sartorelli, V.1    Puri, P.L.2    Hamamori, Y.3    Ogryzko, V.4    Chung, G.5
  • 64
    • 0034671643 scopus 로고    scopus 로고
    • P/CAF-mediated acetylation regulates the function of the basic helix-loop-helix transcription factor TAL1/SCL
    • Huang S, Qiu Y, Shi Y, Xu Z, Brandt SJ. 2000. P/CAF-mediated acetylation regulates the function of the basic helix-loop-helix transcription factor TAL1/SCL. EMBO J 19:6792-6803.
    • (2000) EMBO J , vol.19 , pp. 6792-6803
    • Huang, S.1    Qiu, Y.2    Shi, Y.3    Xu, Z.4    Brandt, S.J.5
  • 65
    • 0037462721 scopus 로고    scopus 로고
    • Regulation of E2A activities by histone acetyltransferases in B lymphocyte development
    • Bradney C, Hjelmeland M, Komatsu Y, Yoshida M, Yao TP, et al. 2003. Regulation of E2A activities by histone acetyltransferases in B lymphocyte development. J Biol Chem 278:2370-2376.
    • (2003) J Biol Chem , vol.278 , pp. 2370-2376
    • Bradney, C.1    Hjelmeland, M.2    Komatsu, Y.3    Yoshida, M.4    Yao, T.P.5
  • 66
    • 1642297146 scopus 로고    scopus 로고
    • Acetylation of the BETA2 transcription factor by PCAF is important in insulin gene expression
    • in press
    • Qiu Y, Guo M, Huang S, Stein RW. 2003. Acetylation of the BETA2 transcription factor by PCAF is important in insulin gene expression. J Biol Chem in press.
    • (2003) J Biol Chem
    • Qiu, Y.1    Guo, M.2    Huang, S.3    Stein, R.W.4
  • 67
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation
    • Jeong JW, Bae MK, Ahn MY, Kim SH, Sohn TK, et al. 2003. Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation. Cell 111:709-720.
    • (2003) Cell , vol.111 , pp. 709-720
    • Jeong, J.W.1    Bae, M.K.2    Ahn, M.Y.3    Kim, S.H.4    Sohn, T.K.5
  • 68
    • 0037507270 scopus 로고    scopus 로고
    • Acetylation of cAMP-responsive element-binding protein (CREB) by CREB-binding protein enhances CREB-dependent transcription
    • Lu Q, Hutchins AE, Doyle CM, Lundblad JR, Kwok RP. 2003. Acetylation of cAMP-responsive element-binding protein (CREB) by CREB-binding protein enhances CREB-dependent transcription. J Biol Chem 278: 15727-15734.
    • (2003) J Biol Chem , vol.278 , pp. 15727-15734
    • Lu, Q.1    Hutchins, A.E.2    Doyle, C.M.3    Lundblad, J.R.4    Kwok, R.P.5
  • 69
    • 0035503278 scopus 로고    scopus 로고
    • A specific lysine in c-Jun is required for transcriptional repression by E1A and is acetylated by p300
    • Vries RG, Prudenziati M, Zwartjes C, Verlaan M, Kalkhoven E, et al. 2001. A specific lysine in c-Jun is required for transcriptional repression by E1A and is acetylated by p300. EMBO J 20:6095-6103.
    • (2001) EMBO J , vol.20 , pp. 6095-6103
    • Vries, R.G.1    Prudenziati, M.2    Zwartjes, C.3    Verlaan, M.4    Kalkhoven, E.5
  • 70
    • 0037450634 scopus 로고    scopus 로고
    • STAT5-induced Id-1 transcription involves recruitment of HDAC1 and deacetylation of C/EBPbeta
    • Xu M, Nie L, Kim SH, Sun XH. 2003. STAT5-induced Id-1 transcription involves recruitment of HDAC1 and deacetylation of C/EBPbeta. EMBO J 22:893-904.
    • (2003) EMBO J , vol.22 , pp. 893-904
    • Xu, M.1    Nie, L.2    Kim, S.H.3    Sun, X.H.4
  • 71
    • 0035815647 scopus 로고    scopus 로고
    • Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation
    • Hung HL, Kim AY, Hong W, Rakowski C, Blobel GA. 2001. Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation. J Biol Chem 276:10715-10721.
    • (2001) J Biol Chem , vol.276 , pp. 10715-10721
    • Hung, H.L.1    Kim, A.Y.2    Hong, W.3    Rakowski, C.4    Blobel, G.A.5
  • 73
    • 0034646630 scopus 로고    scopus 로고
    • E2F family members are differentially regulated by reversible acetylation
    • Marzio G, Wagener C, Gutierrez MI, Cartwright P, Helin K, et al. 2000. E2F family members are differentially regulated by reversible acetylation. J Biol Chem 275:10887-10892.
    • (2000) J Biol Chem , vol.275 , pp. 10887-10892
    • Marzio, G.1    Wagener, C.2    Gutierrez, M.I.3    Cartwright, P.4    Helin, K.5
  • 74
    • 0037378516 scopus 로고    scopus 로고
    • Coactivator-dependent acetylation stabilizes members of the SREBP family of transcription factors
    • Giandomenico V, Simonsson M, Gronroos E, Ericsson J. 2003. Coactivator-dependent acetylation stabilizes members of the SREBP family of transcription factors. Mol Cell Biol 23:2587-2599.
    • (2003) Mol Cell Biol , vol.23 , pp. 2587-2599
    • Giandomenico, V.1    Simonsson, M.2    Gronroos, E.3    Ericsson, J.4
  • 75
    • 0034688345 scopus 로고    scopus 로고
    • c-Myb acetylation at the carboxyl-terminal conserved domain by transcriptional co-activator p300
    • Tomita A, Towatari M, Tsuzuki S, Hayakawa F, Kosugi H, et al. 2000. c-Myb acetylation at the carboxyl-terminal conserved domain by transcriptional co-activator p300. Oncogene 19:444-451.
    • (2000) Oncogene , vol.19 , pp. 444-451
    • Tomita, A.1    Towatari, M.2    Tsuzuki, S.3    Hayakawa, F.4    Kosugi, H.5
  • 76
    • 0035793593 scopus 로고    scopus 로고
    • Increased affinity of c-Myb for CREB-binding protein (CBP) after CBP-induced acetylation
    • Sano Y, Ishii S. 2001. Increased affinity of c-Myb for CREB-binding protein (CBP) after CBP-induced acetylation. J Biol Chem 276:3674-3682.
    • (2001) J Biol Chem , vol.276 , pp. 3674-3682
    • Sano, Y.1    Ishii, S.2
  • 77
    • 0038491558 scopus 로고    scopus 로고
    • Interferon regulatory factor-2 regulates cell growth through its acetylation
    • Masumi A, Yamakawa Y, Fukazawa H, Ozato K, Komuro K. 2003. Interferon regulatory factor-2 regulates cell growth through its acetylation. J Biol Chem 278:25401-25407.
    • (2003) J Biol Chem , vol.278 , pp. 25401-25407
    • Masumi, A.1    Yamakawa, Y.2    Fukazawa, H.3    Ozato, K.4    Komuro, K.5
  • 78
    • 0347298773 scopus 로고    scopus 로고
    • Acetylation of interferon regulatory factor-7 by p300/CREB-binding protein (CBP)-associated factor (PCAF) impairs its DNA binding
    • Caillaud A, Prakash A, Smith E, Masumi A, Hovanessian AG, et al. 2002. Acetylation of interferon regulatory factor-7 by p300/CREB-binding protein (CBP)-associated factor (PCAF) impairs its DNA binding. J Biol Chem 277:49417-49421.
    • (2002) J Biol Chem , vol.277 , pp. 49417-49421
    • Caillaud, A.1    Prakash, A.2    Smith, E.3    Masumi, A.4    Hovanessian, A.G.5
  • 80
  • 81
    • 0032544123 scopus 로고    scopus 로고
    • Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases
    • Zhang W, Bieker JJ. 1998. Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc Natl Acad Sci USA 95:9855-9860.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9855-9860
    • Zhang, W.1    Bieker, J.J.2
  • 82
    • 0034905085 scopus 로고    scopus 로고
    • Regulation of transcription factor YY1 by acetylation and deacetylation
    • Yao YL, Yang WM, Seto E. 2001. Regulation of transcription factor YY1 by acetylation and deacetylation. Mol Cell Biol 21:5979-5991.
    • (2001) Mol Cell Biol , vol.21 , pp. 5979-5991
    • Yao, Y.L.1    Yang, W.M.2    Seto, E.3
  • 83
    • 0038399824 scopus 로고    scopus 로고
    • Functional interplay between CBP and PCAF in acetylation and regulation of transcription factor KLF13 activity
    • Song CZ, Keller K, Chen Y, Stamatoyannopoulos G. 2003. Functional interplay between CBP and PCAF in acetylation and regulation of transcription factor KLF13 activity. J Mol Biol 329:207-215.
    • (2003) J Mol Biol , vol.329 , pp. 207-215
    • Song, C.Z.1    Keller, K.2    Chen, Y.3    Stamatoyannopoulos, G.4
  • 84
    • 0035976892 scopus 로고    scopus 로고
    • Interaction of EVI1 with CBP and P/CAF results in reversible acetylation of EVI1 and in colocalization in nuclear speckles
    • Chakraborty S, Senyuk V, Sitailo S, Chi Y, Nucifora G. 2001. Interaction of EVI1 with CBP and P/CAF results in reversible acetylation of EVI1 and in colocalization in nuclear speckles. J Biol Chem 276:44936-44943.
    • (2001) J Biol Chem , vol.276 , pp. 44936-44943
    • Chakraborty, S.1    Senyuk, V.2    Sitailo, S.3    Chi, Y.4    Nucifora, G.5
  • 86
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • Boyes J, Byfield P, Nakatani Y, Ogryzko V. 1998. Regulation of activity of the transcription factor GATA-1 by acetylation. Nature 396:594-598.
    • (1998) Nature , vol.396 , pp. 594-598
    • Boyes, J.1    Byfield, P.2    Nakatani, Y.3    Ogryzko, V.4
  • 87
    • 0032910957 scopus 로고    scopus 로고
    • CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites
    • Hung HL, Lau J, Kim AY, Weiss MJ, Blobel GA. 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
  • 88
    • 0034282480 scopus 로고    scopus 로고
    • Acetylation of GATA-3 affects T-cell survival and homing to secondary lymphoid organs
    • Yamagata T, Mitani K, Oda H, Suzuki T, Honda H, et al. 2000. Acetylation of GATA-3 affects T-cell survival and homing to secondary lymphoid organs. EMBO J 19:4676-4687.
    • (2000) EMBO J , vol.19 , pp. 4676-4687
    • Yamagata, T.1    Mitani, K.2    Oda, H.3    Suzuki, T.4    Honda, H.5
  • 89
    • 0036898253 scopus 로고    scopus 로고
    • Acetylation inactivates the transcriptional repressor BCL6
    • Bereshchenko OR, Gu W, Dalla-Favera R. 2002. Acetylation inactivates the transcriptional repressor BCL6. Nat Genet 32:606-613
    • (2002) Nat Genet , vol.32 , pp. 606-613
    • Bereshchenko, O.R.1    Gu, W.2    Dalla-Favera, R.3
  • 90
    • 0037135566 scopus 로고    scopus 로고
    • Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor
    • Gaughan L, Logan IR, Cook S, Neal DE, Robson CN. 2002. Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor. J Bio Chem 277: 25904-25913.
    • (2002) J Bio Chem , vol.277 , pp. 25904-25913
    • Gaughan, L.1    Logan, I.R.2    Cook, S.3    Neal, D.E.4    Robson, C.N.5
  • 91
    • 0242637385 scopus 로고    scopus 로고
    • Acetylation of androgen receptor enhances coactivator binding and promotes prostate cancer cell growth
    • Fu M, Rao M, Wang C, Sakamaki T, Wang J, et al. 2003. Acetylation of androgen receptor enhances coactivator binding and promotes prostate cancer cell growth. Mol Cell Biol 23:8563-8575.
    • (2003) Mol Cell Biol , vol.23 , pp. 8563-8575
    • Fu, M.1    Rao, M.2    Wang, C.3    Sakamaki, T.4    Wang, J.5
  • 92
    • 0242637101 scopus 로고    scopus 로고
    • Direct acetylation of the estrogen receptor alpha hinge region by p300 regulates transactivation and hormone sensitivity
    • Wang C, Fu M, Angeletti RH, Siconolfi-Baez L, Reutens AT, et al. 2001. Direct acetylation of the estrogen receptor alpha hinge region by p300 regulates transactivation and hormone sensitivity. J Biol Chem 276: 18375-18383.
    • (2001) J Biol Chem , vol.276 , pp. 18375-18383
    • Wang, C.1    Fu, M.2    Angeletti, R.H.3    Siconolfi-Baez, L.4    Reutens, A.T.5
  • 93
    • 0033636892 scopus 로고    scopus 로고
    • Acetylation regulates transcription factor activity at multiple levels
    • Soutoglou E, Katrakili N, Talianidis I. 2000. Acetylation regulates transcription factor activity at multiple levels. Mol Cell 5:745-751.
    • (2000) Mol Cell , vol.5 , pp. 745-751
    • Soutoglou, E.1    Katrakili, N.2    Talianidis, I.3
  • 94
    • 0035813148 scopus 로고    scopus 로고
    • Acetylation of steroidogenic factor 1 protein regulates its transcriptional activity and recruits the coactivator GCN5
    • Jacob AL, Lund J, Martinez P, Hedin L. 2001. Acetylation of steroidogenic factor 1 protein regulates its transcriptional activity and recruits the coactivator GCN5. J Biol Chem 276:37659-37664.
    • (2001) J Biol Chem , vol.276 , pp. 37659-37664
    • Jacob, A.L.1    Lund, J.2    Martinez, P.3    Hedin, L.4
  • 95
    • 0042971584 scopus 로고    scopus 로고
    • Acetylation-mediated transcriptional activation of the ETS protein ER81 by p300, P/CAF, and HER2/Neu
    • Goel A, Janknecht R. 2003. Acetylation-mediated transcriptional activation of the ETS protein ER81 by p300, P/CAF, and HER2/Neu. Mol Cell Biol 23:6243-6254.
    • (2003) Mol Cell Biol , vol.23 , pp. 6243-6254
    • Goel, A.1    Janknecht, R.2
  • 96
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, Sweeney LB, Sturgill JF, Chua KF, Greer PL, et al. 2004. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 303:2011-2015.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3    Chua, K.F.4    Greer, P.L.5
  • 97
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • Motta MC, Divecha N, Lemieux M, Kamel C, Chen D, et al. 2004. Mammalian SIRT1 Represses Forkhead Transcription Factors. Cell 116: 551-563.
    • (2004) Cell , vol.116 , pp. 551-563
    • Motta, M.C.1    Divecha, N.2    Lemieux, M.3    Kamel, C.4    Chen, D.5
  • 98
    • 2342445654 scopus 로고    scopus 로고
    • Negative regulation of forkhead transcription factor AFX (Foxo4) by CBP-induced acetylation
    • Fukuoka M, Daitoku H, Hatta M, Matsuzaki H, Umemura S, et al. 2003. Negative regulation of forkhead transcription factor AFX (Foxo4) by CBP-induced acetylation. Int J Mol Med 12:503-508.
    • (2003) Int J Mol Med , vol.12 , pp. 503-508
    • Fukuoka, M.1    Daitoku, H.2    Hatta, M.3    Matsuzaki, H.4    Umemura, S.5
  • 99
    • 2442500635 scopus 로고    scopus 로고
    • AML1 is functionally regulated through p300-mediated acetylation on specific lysine residues
    • Yamaguchi Y, Imai Y, Izutsu K, Asai T, Ichikawa M, et al. 2004. AML1 is functionally regulated through p300-mediated acetylation on specific lysine residues. J Biol Chem 279:15630-15638.
    • (2004) J Biol Chem , vol.279 , pp. 15630-15638
    • Yamaguchi, Y.1    Imai, Y.2    Izutsu, K.3    Asai, T.4    Ichikawa, M.5
  • 100
    • 0242552509 scopus 로고    scopus 로고
    • The proline repeat domain of p53 binds directly to the transcriptional coactivator p300 and allosterically controls DNA-dependent acetylation of p53
    • Dornan D, Shimizu H, Burch L, Smith AJ, Hupp TR. 2003. The proline repeat domain of p53 binds directly to the transcriptional coactivator p300 and allosterically controls DNA-dependent acetylation of p53. Mol Cell Biol 23:8846-8861.
    • (2003) Mol Cell Biol , vol.23 , pp. 8846-8861
    • Dornan, D.1    Shimizu, H.2    Burch, L.3    Smith, A.J.4    Hupp, T.R.5
  • 101
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks CL, Gu W. 2003. Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr Opin Cell Biol 15:164-171.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 102
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • Fulco M, Schiltz RL, Iezzi S, King MT, Zhao P, et al. 2003. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell 12:51-62.
    • (2003) Mol Cell , vol.12 , pp. 51-62
    • Fulco, M.1    Schiltz, R.L.2    Iezzi, S.3    King, M.T.4    Zhao, P.5
  • 103
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. 2003. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11:437-444.
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 104
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella E, Anderson CW. 2001. Post-translational modifications and activation of p53 by genotoxic stresses. Eur J Biochem 268:2764-2772.
    • (2001) Eur J Biochem , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 105
    • 2342599619 scopus 로고    scopus 로고
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
    • Yang XJ. 2004. The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases. Nucleic Acids Res 32:959-976.
    • (2004) Nucleic Acids Res , vol.32 , pp. 959-976
    • Yang, X.J.1
  • 106
    • 0035966316 scopus 로고    scopus 로고
    • Why is p53 acetylated?
    • Prives C, Manley JL. 2001. Why is p53 acetylated? Cell 107:815-818.
    • (2001) Cell , vol.107 , pp. 815-818
    • Prives, C.1    Manley, J.L.2
  • 107
    • 0026608175 scopus 로고
    • The bromodomain: A conserved sequence found in human, Drosophila and yeast proteins
    • Haynes SR, Dollard C, Winston F, Beck S, Trowsdale J, et al. 1992. The bromodomain: a conserved sequence found in human, Drosophila and yeast proteins. Nucleic Acids Res 20:2603.
    • (1992) Nucleic Acids Res , vol.20 , pp. 2603
    • Haynes, S.R.1    Dollard, C.2    Winston, F.3    Beck, S.4    Trowsdale, J.5
  • 109
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, et al. 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
  • 110
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAFII250 double bromodomain module
    • Jacobson RH, Ladurner AG, King DS, Tjian R. 2000. Structure and function of a human TAFII250 double bromodomain module. Science 288:1422-1425.
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H.1    Ladurner, A.G.2    King, D.S.3    Tjian, R.4
  • 111
    • 0034387879 scopus 로고    scopus 로고
    • Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
    • Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE. 2000. Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J Mol Biol 304:355-370.
    • (2000) J Mol Biol , vol.304 , pp. 355-370
    • Hudson, B.P.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 112
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p
    • Owen DJ, Ornaghi P, Yang JC, Lowe N, Evans PR, et al. 2000. The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p. EMBO J 19:6141-6149.
    • (2000) EMBO J , vol.19 , pp. 6141-6149
    • Owen, D.J.1    Ornaghi, P.2    Yang, J.C.3    Lowe, N.4    Evans, P.R.5
  • 113
    • 0036206045 scopus 로고    scopus 로고
    • Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain
    • Mujtaba S, He Y, Zeng L, Farooq A, Carlson JE, et al. 2002. Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain. Mol Cell 9:575-586.
    • (2002) Mol Cell , vol.9 , pp. 575-586
    • Mujtaba, S.1    He, Y.2    Zeng, L.3    Farooq, A.4    Carlson, J.E.5
  • 114
    • 10744233648 scopus 로고    scopus 로고
    • Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation
    • Mujtaba S, He Y, Zeng L, Yan S, Plotnikova O, et al. 2004. Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. Mol Cell 13:251-263.
    • (2004) Mol Cell , vol.13 , pp. 251-263
    • Mujtaba, S.1    He, Y.2    Zeng, L.3    Yan, S.4    Plotnikova, O.5
  • 115
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • Hassan AH, Prochasson P, Neely KE, Galasinski SC, Chandy M, et al. 2002. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell 111:369-379.
    • (2002) Cell , vol.111 , pp. 369-379
    • Hassan, A.H.1    Prochasson, P.2    Neely, K.E.3    Galasinski, S.C.4    Chandy, M.5
  • 116
    • 0035814925 scopus 로고    scopus 로고
    • Chromatin remodeling enzymes: Who's on first?
    • Fry CJ, Peterson CL. 2001. Chromatin remodeling enzymes: who's on first? Curr Biol 11:R185-R197.
    • (2001) Curr Biol , vol.11
    • Fry, C.J.1    Peterson, C.L.2
  • 117
    • 0030447612 scopus 로고    scopus 로고
    • RSC, an essential, abundant chromatin-remodeling complex
    • Cairns BR, Lorch Y, Li Y, Zhang M, Lacomis L, et al. 1996. RSC, an essential, abundant chromatin-remodeling complex. Cell 83:1249-1260.
    • (1996) Cell , vol.83 , pp. 1249-1260
    • Cairns, B.R.1    Lorch, Y.2    Li, Y.3    Zhang, M.4    Lacomis, L.5
  • 118
    • 0033231625 scopus 로고    scopus 로고
    • Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains
    • Cairns BR, Schlichter A, Erdjument-Bromage H, Tempst P, Kornberg RD, et al. 1999. Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains. Mol Cell 4:715-723.
    • (1999) Mol Cell , vol.4 , pp. 715-723
    • Cairns, B.R.1    Schlichter, A.2    Erdjument-Bromage, H.3    Tempst, P.4    Kornberg, R.D.5
  • 119
    • 1942535223 scopus 로고    scopus 로고
    • Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14
    • Kasten M, Szerlong H, Erdjument-Bromage H, Tempst P, Werner M, et al. 2004. Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14. EMBO J 23:1348-1359.
    • (2004) EMBO J , vol.23 , pp. 1348-1359
    • Kasten, M.1    Szerlong, H.2    Erdjument-Bromage, H.3    Tempst, P.4    Werner, M.5
  • 120
    • 0034700134 scopus 로고    scopus 로고
    • The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes
    • Xue Y, Canman JC, Lee CS, Nie Z, Yang D, et al. 2000. The human SWI/ SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes. Proc Natl Acad Sci USA 97:13015-13020.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13015-13020
    • Xue, Y.1    Canman, J.C.2    Lee, C.S.3    Nie, Z.4    Yang, D.5
  • 121
    • 0036056999 scopus 로고    scopus 로고
    • The in vivo functions of ATP-dependent chromatin-remodelling factors
    • Tsukiyama T. 2002. The in vivo functions of ATP-dependent chromatin-remodelling factors. Rev Mol Cell Biol 3:422-429.
    • (2002) Rev Mol Cell Biol , vol.3 , pp. 422-429
    • Tsukiyama, T.1
  • 122
    • 0344198456 scopus 로고    scopus 로고
    • Chromatin remodeling by ATP-dependent molecular machines
    • Lusser A, Kadonaga JT. 2003. Chromatin remodeling by ATP-dependent molecular machines. Bioessays 25:1192-1200.
    • (2003) Bioessays , vol.25 , pp. 1192-1200
    • Lusser, A.1    Kadonaga, J.T.2
  • 124
    • 0036091456 scopus 로고    scopus 로고
    • Growth and early postimplantation defects in mice deficient for the bromodomain-containing protein Brd4
    • Houzelstein D, Bullock SL, Lynch DE, Grigorieva EF, Wilson VA, et al. 2002. Growth and early postimplantation defects in mice deficient for the bromodomain-containing protein Brd4. Mol Cell Biol 22:3794-3802.
    • (2002) Mol Cell Biol , vol.22 , pp. 3794-3802
    • Houzelstein, D.1    Bullock, S.L.2    Lynch, D.E.3    Grigorieva, E.F.4    Wilson, V.A.5
  • 125
    • 0037291695 scopus 로고    scopus 로고
    • Different sensitivities of bromodomain factors 1 and 2 to histone H4 acetylation
    • Matangkasombut O, Buratowski S. 2003. Different sensitivities of bromodomain factors 1 and 2 to histone H4 acetylation. Mol Cell 11: 353-363.
    • (2003) Mol Cell , vol.11 , pp. 353-363
    • Matangkasombut, O.1    Buratowski, S.2
  • 126
    • 0037291760 scopus 로고    scopus 로고
    • Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries
    • Ladurner AG, Inouye C, Jain R, Tjian R. 2003. Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries. Mol Cell 11:365-376.
    • (2003) Mol Cell , vol.11 , pp. 365-376
    • Ladurner, A.G.1    Inouye, C.2    Jain, R.3    Tjian, R.4
  • 127
    • 1642564551 scopus 로고    scopus 로고
    • Selective recognition of acetylated histones by bromodomain proteins visualized in living cells
    • Kanno T, Kanno Y, Siegel RM, Jang MK, Lenardo MJ, et al. 2004. Selective recognition of acetylated histones by bromodomain proteins visualized in living cells. Mol Cell 13:33-43.
    • (2004) Mol Cell , vol.13 , pp. 33-43
    • Kanno, T.1    Kanno, Y.2    Siegel, R.M.3    Jang, M.K.4    Lenardo, M.J.5
  • 128
    • 0041806599 scopus 로고    scopus 로고
    • The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis
    • Dey A, Chitsaz F, Abbasi A, Misteli T, Ozato K. 2003. The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis. Proc Natl Acad Sci USA 100:8758-8763.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8758-8763
    • Dey, A.1    Chitsaz, F.2    Abbasi, A.3    Misteli, T.4    Ozato, K.5
  • 129
    • 0042090936 scopus 로고    scopus 로고
    • Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein
    • Pivot-Pajot C, Caron C, Govin J, Vion A, Rousseaux S, et al. 2003. Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein. Mol Cell Biol 23:5354-5365.
    • (2003) Mol Cell Biol , vol.23 , pp. 5354-5365
    • Pivot-Pajot, C.1    Caron, C.2    Govin, J.3    Vion, A.4    Rousseaux, S.5
  • 130
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of co-activators/histone acetyltransferases
    • Barlev NA, Liu L, Chehab NH, Mansfield K, Harris KG, et al. 2001. Acetylation of p53 activates transcription through recruitment of co-activators/histone acetyltransferases. Mol Cell 8:1243-1254.
    • (2001) Mol Cell , vol.8 , pp. 1243-1254
    • Barlev, N.A.1    Liu, L.2    Chehab, N.H.3    Mansfield, K.4    Harris, K.G.5
  • 131
    • 0034934713 scopus 로고    scopus 로고
    • Interaction between acetylated MyoD and the bromodomain of CBP and/ or p300
    • Polesskaya A, Naguibneva I, Duquet A, Bengal E, Robin P, et al. 2001. Interaction between acetylated MyoD and the bromodomain of CBP and/ or p300. Mol Cell Biol 21:5312-5320.
    • (2001) Mol Cell Biol , vol.21 , pp. 5312-5320
    • Polesskaya, A.1    Naguibneva, I.2    Duquet, A.3    Bengal, E.4    Robin, P.5
  • 132
    • 0037013851 scopus 로고    scopus 로고
    • Transcriptional synergy between Tat and PCAF is dependent on the binding of acetylated Tat to the PCAF bromodomain
    • Dorr A, Kiermer V, Pedal A, Rackwitz HR, Henklein P, et al. 2002. Transcriptional synergy between Tat and PCAF is dependent on the binding of acetylated Tat to the PCAF bromodomain. EMBO J 21:2715-2723.
    • (2002) EMBO J , vol.21 , pp. 2715-2723
    • Dorr, A.1    Kiermer, V.2    Pedal, A.3    Rackwitz, H.R.4    Henklein, P.5
  • 133
    • 12244271066 scopus 로고    scopus 로고
    • Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF
    • Bres V, Tagami H, Peloponese JM, Loret E, Jeang KT, et al. 2002. Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF. EMBO J 21:6811-6819.
    • (2002) EMBO J , vol.21 , pp. 6811-6819
    • Bres, V.1    Tagami, H.2    Peloponese, J.M.3    Loret, E.4    Jeang, K.T.5
  • 134
    • 0035012326 scopus 로고    scopus 로고
    • p300 forms a stable, template-committed complex with chromatin: Role for the bromodomain
    • Manning ET, Ikehara T, Ito T, Kadonaga JT, Kraus WL. 2001. p300 forms a stable, template-committed complex with chromatin: role for the bromodomain. Mol Cell Biol 21:3876-3887.
    • (2001) Mol Cell Biol , vol.21 , pp. 3876-3887
    • Manning, E.T.1    Ikehara, T.2    Ito, T.3    Kadonaga, J.T.4    Kraus, W.L.5
  • 135
    • 0031913215 scopus 로고    scopus 로고
    • Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex
    • Barlev NA, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, et al. 1998. Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex. Mol Cell Biol 18:1349-1358.
    • (1998) Mol Cell Biol , vol.18 , pp. 1349-1358
    • Barlev, N.A.1    Poltoratsky, V.2    Owen-Hughes, T.3    Ying, C.4    Liu, L.5
  • 136
    • 0037184916 scopus 로고    scopus 로고
    • The bromodomain mediates transcriptional intermediary factor 1alpha-nucleosome interactions
    • Remboutsika E, Yamamoto K, Harbers M, Schmutz M. 2002. The bromodomain mediates transcriptional intermediary factor 1alpha-nucleosome interactions. J Biol Chem 277:50318-50325.
    • (2002) J Biol Chem , vol.277 , pp. 50318-50325
    • Remboutsika, E.1    Yamamoto, K.2    Harbers, M.3    Schmutz, M.4
  • 137
    • 0034212582 scopus 로고    scopus 로고
    • Involvement of 14-3-3 proteins in nuclear localization of telomerase
    • Seimiya H, Sawada H, Muramatsu Y, Shimizu M, Ohko K, et al. 2000. Involvement of 14-3-3 proteins in nuclear localization of telomerase. EMBO J 19:2652-2661.
    • (2000) EMBO J , vol.19 , pp. 2652-2661
    • Seimiya, H.1    Sawada, H.2    Muramatsu, Y.3    Shimizu, M.4    Ohko, K.5
  • 138
    • 0042203565 scopus 로고    scopus 로고
    • SH2 and PTB domains in tyrosine kinase signaling
    • Schlessinger J, Lemmon MA. 2003. SH2 and PTB domains in tyrosine kinase signaling. Sci STKE:RE12.
    • (2003) Sci STKE
    • Schlessinger, J.1    Lemmon, M.A.2
  • 140
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson T, Nash P. 2003. Assembly of cell regulatory systems through protein interaction domains. Science 300:445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.