메뉴 건너뛰기




Volumn 34, Issue 11, 2009, Pages 571-578

Biochemical pathways that regulate acetyltransferase and deacetylase activity in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 2; ACYLTRANSFERASE; CYCLIN DEPENDENT KINASE 2; CYCLIN E; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE PCAF; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE INHIBITOR; HYDROLASE; PROTEIN MDM2; PROTEIN P53; SIRTUIN 1; VORINOSTAT;

EID: 70350350917     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2009.06.010     Document Type: Review
Times cited : (42)

References (77)
  • 1
    • 66249105703 scopus 로고    scopus 로고
    • ATP-citrate lyase links cellular metabolism to histone acetylation
    • Wellen K.E., et al. ATP-citrate lyase links cellular metabolism to histone acetylation. Science 324 (2009) 1076-1080
    • (2009) Science , vol.324 , pp. 1076-1080
    • Wellen, K.E.1
  • 2
    • 0242439348 scopus 로고    scopus 로고
    • Regulating histone acetyltransferases and deacetylases
    • Legube G., and Trouche D. Regulating histone acetyltransferases and deacetylases. EMBO Rep. 4 (2003) 944-947
    • (2003) EMBO Rep. , vol.4 , pp. 944-947
    • Legube, G.1    Trouche, D.2
  • 3
    • 33845668682 scopus 로고    scopus 로고
    • To die or not to die: a HAT trick
    • Tyteca S., et al. To die or not to die: a HAT trick. Mol. Cell 24 (2006) 807-808
    • (2006) Mol. Cell , vol.24 , pp. 807-808
    • Tyteca, S.1
  • 4
    • 36048958965 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: overview and perspectives
    • Dokmanovic M., et al. Histone deacetylase inhibitors: overview and perspectives. Mol. Cancer. Res. 5 (2007) 981-989
    • (2007) Mol. Cancer. Res. , vol.5 , pp. 981-989
    • Dokmanovic, M.1
  • 5
    • 38949206260 scopus 로고    scopus 로고
    • Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response
    • Cheng Z., et al. Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response. Oncogene 27 (2008) 931-941
    • (2008) Oncogene , vol.27 , pp. 931-941
    • Cheng, Z.1
  • 6
    • 0034916613 scopus 로고    scopus 로고
    • p300/CBP proteins: HATs for transcriptional bridges and scaffolds
    • Chan H.M., and La Thangue N.B. p300/CBP proteins: HATs for transcriptional bridges and scaffolds. J. Cell Sci. 114 (2001) 2363-2373
    • (2001) J. Cell Sci. , vol.114 , pp. 2363-2373
    • Chan, H.M.1    La Thangue, N.B.2
  • 7
    • 0000631273 scopus 로고    scopus 로고
    • The signal-dependent coactivator CBP is a nuclear target for pp90RSK
    • Nakajima T., et al. The signal-dependent coactivator CBP is a nuclear target for pp90RSK. Cell 86 (1996) 465-474
    • (1996) Cell , vol.86 , pp. 465-474
    • Nakajima, T.1
  • 8
    • 0032484204 scopus 로고    scopus 로고
    • Nerve growth factor up-regulates the transcriptional activity of CBP through activation of the p42/p44(MAPK) cascade
    • Liu Y.Z., et al. Nerve growth factor up-regulates the transcriptional activity of CBP through activation of the p42/p44(MAPK) cascade. J. Biol. Chem. 273 (1998) 32400-32407
    • (1998) J. Biol. Chem. , vol.273 , pp. 32400-32407
    • Liu, Y.Z.1
  • 9
    • 0032483380 scopus 로고    scopus 로고
    • CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV
    • Chawla S., et al. CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV. Science 281 (1998) 1505-1509
    • (1998) Science , vol.281 , pp. 1505-1509
    • Chawla, S.1
  • 10
    • 0032511884 scopus 로고    scopus 로고
    • Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A
    • Ait-Si-Ali S., et al. Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A. Nature 396 (1998) 184-186
    • (1998) Nature , vol.396 , pp. 184-186
    • Ait-Si-Ali, S.1
  • 11
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko V.V., et al. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87 (1996) 953-959
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1
  • 12
    • 0036208002 scopus 로고    scopus 로고
    • Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes
    • Martens J.H., et al. Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes. Mol. Cell Biol. 22 (2002) 2598-2606
    • (2002) Mol. Cell Biol. , vol.22 , pp. 2598-2606
    • Martens, J.H.1
  • 13
    • 0033525094 scopus 로고    scopus 로고
    • Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A
    • Hamamori Y., et al. Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A. Cell 96 (1999) 405-413
    • (1999) Cell , vol.96 , pp. 405-413
    • Hamamori, Y.1
  • 14
    • 1842420646 scopus 로고    scopus 로고
    • Regulation of the p300 HAT domain via a novel activation loop
    • Thompson P.R., et al. Regulation of the p300 HAT domain via a novel activation loop. Nat. Struct. Mol. Biol. 11 (2004) 308-315
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 308-315
    • Thompson, P.R.1
  • 15
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis J.M., and Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81 (2001) 807-869
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 16
    • 34047229996 scopus 로고    scopus 로고
    • The diverse biological roles of MYST histone acetyltransferase family proteins
    • Thomas T., and Voss A.K. The diverse biological roles of MYST histone acetyltransferase family proteins. Cell Cycle 6 (2007) 696-704
    • (2007) Cell Cycle , vol.6 , pp. 696-704
    • Thomas, T.1    Voss, A.K.2
  • 17
    • 33846026402 scopus 로고    scopus 로고
    • Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation
    • Karanam B., et al. Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation. J. Biol. Chem. 281 (2006) 40292-40301
    • (2006) J. Biol. Chem. , vol.281 , pp. 40292-40301
    • Karanam, B.1
  • 18
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim S.C., et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol. Cell 23 (2006) 607-618
    • (2006) Mol. Cell , vol.23 , pp. 607-618
    • Kim, S.C.1
  • 19
    • 0033529253 scopus 로고    scopus 로고
    • Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein
    • Creaven M., et al. Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein. Tat. Biochemistry 38 (1999) 8826-8830
    • (1999) Tat. Biochemistry , vol.38 , pp. 8826-8830
    • Creaven, M.1
  • 20
    • 10044262126 scopus 로고    scopus 로고
    • The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60
    • Patel J.H., et al. The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60. Mol. Cell Biol. 24 (2004) 10826-10834
    • (2004) Mol. Cell Biol. , vol.24 , pp. 10826-10834
    • Patel, J.H.1
  • 21
    • 0033912223 scopus 로고    scopus 로고
    • Adenovirus E1B 55-kilodalton oncoprotein inhibits p53 acetylation by PCAF
    • Liu Y., et al. Adenovirus E1B 55-kilodalton oncoprotein inhibits p53 acetylation by PCAF. Mol. Cell Biol. 20 (2000) 5540-5553
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5540-5553
    • Liu, Y.1
  • 22
    • 0033529845 scopus 로고    scopus 로고
    • Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator
    • Trievel R.C., et al. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8931-8936
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8931-8936
    • Trievel, R.C.1
  • 23
    • 0036830560 scopus 로고    scopus 로고
    • The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate
    • Yan Y., et al. The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate. Nat. Struct. Biol. 9 (2002) 862-869
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 862-869
    • Yan, Y.1
  • 24
    • 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 Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22 (1997) 154-155
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 25
    • 0030973238 scopus 로고    scopus 로고
    • Binding and modulation of p53 by p300/CBP coactivators
    • Lill N.L., et al. Binding and modulation of p53 by p300/CBP coactivators. Nature 387 (1997) 823-827
    • (1997) Nature , vol.387 , pp. 823-827
    • Lill, N.L.1
  • 26
    • 33748415010 scopus 로고    scopus 로고
    • A mechanism for coordinating chromatin modification and preinitiation complex assembly
    • Black J.C., et al. A mechanism for coordinating chromatin modification and preinitiation complex assembly. Mol. Cell 23 (2006) 809-818
    • (2006) Mol. Cell , vol.23 , pp. 809-818
    • Black, J.C.1
  • 27
    • 0034069878 scopus 로고    scopus 로고
    • A novel transcriptional repression domain mediates p21(WAF1/CIP1) induction of p300 transactivation
    • Snowden A.W., et al. A novel transcriptional repression domain mediates p21(WAF1/CIP1) induction of p300 transactivation. Mol. Cell Biol. 20 (2000) 2676-2686
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2676-2686
    • Snowden, A.W.1
  • 28
    • 0037961625 scopus 로고    scopus 로고
    • P300 transcriptional repression is mediated by SUMO modification
    • Girdwood D., et al. P300 transcriptional repression is mediated by SUMO modification. Mol. Cell 11 (2003) 1043-1054
    • (2003) Mol. Cell , vol.11 , pp. 1043-1054
    • Girdwood, D.1
  • 29
    • 15444377466 scopus 로고    scopus 로고
    • SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1
    • Bouras T., et al. SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1. J. Biol. Chem. 280 (2005) 10264-10276
    • (2005) J. Biol. Chem. , vol.280 , pp. 10264-10276
    • Bouras, T.1
  • 30
    • 0019132555 scopus 로고
    • Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid hormones
    • McKnight G.S., et al. Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid hormones. Cell 22 (1980) 469-477
    • (1980) Cell , vol.22 , pp. 469-477
    • McKnight, G.S.1
  • 31
    • 0030569556 scopus 로고    scopus 로고
    • Direct inhibition of the expression of cyclin D1 gene by sodium butyrate
    • Lallemand F., et al. Direct inhibition of the expression of cyclin D1 gene by sodium butyrate. Biochem. Biophys. Res. Commun. 229 (1996) 163-169
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 163-169
    • Lallemand, F.1
  • 32
    • 0025297904 scopus 로고
    • Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate
    • Bresnick E.H., et al. Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 3977-3981
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 3977-3981
    • Bresnick, E.H.1
  • 33
    • 0042567276 scopus 로고    scopus 로고
    • Inhibition of MMTV transcription by HDAC inhibitors occurs independent of changes in chromatin remodeling and increased histone acetylation
    • Mulholland N.M., et al. Inhibition of MMTV transcription by HDAC inhibitors occurs independent of changes in chromatin remodeling and increased histone acetylation. Oncogene 22 (2003) 4807-4818
    • (2003) Oncogene , vol.22 , pp. 4807-4818
    • Mulholland, N.M.1
  • 34
    • 33744510851 scopus 로고    scopus 로고
    • HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription
    • Qiu Y., et al. HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription. Mol. Cell 22 (2006) 669-679
    • (2006) Mol. Cell , vol.22 , pp. 669-679
    • Qiu, Y.1
  • 35
    • 0013537360 scopus 로고    scopus 로고
    • Dynamic behavior of transcription factors on a natural promoter in living cells
    • Becker M., et al. Dynamic behavior of transcription factors on a natural promoter in living cells. EMBO Rep. 3 (2002) 1188-1194
    • (2002) EMBO Rep. , vol.3 , pp. 1188-1194
    • Becker, M.1
  • 36
    • 23744495968 scopus 로고    scopus 로고
    • Multiple mechanisms induce transcriptional silencing of a subset of genes, including oestrogen receptor alpha, in response to deacetylase inhibition by valproic acid and trichostatin A
    • Reid G., et al. Multiple mechanisms induce transcriptional silencing of a subset of genes, including oestrogen receptor alpha, in response to deacetylase inhibition by valproic acid and trichostatin A. Oncogene 24 (2005) 4894-4907
    • (2005) Oncogene , vol.24 , pp. 4894-4907
    • Reid, G.1
  • 37
    • 26244448867 scopus 로고    scopus 로고
    • Individual histone deacetylases in Drosophila modulate transcription of distinct genes
    • Cho Y., et al. Individual histone deacetylases in Drosophila modulate transcription of distinct genes. Genomics 86 (2005) 606-617
    • (2005) Genomics , vol.86 , pp. 606-617
    • Cho, Y.1
  • 38
    • 12844280515 scopus 로고    scopus 로고
    • Transcript profiling in Arabidopsis reveals complex responses to global inhibition of DNA methylation and histone deacetylation
    • Chang S., and Pikaard C.S. Transcript profiling in Arabidopsis reveals complex responses to global inhibition of DNA methylation and histone deacetylation. J. Biol. Chem. 280 (2005) 796-804
    • (2005) J. Biol. Chem. , vol.280 , pp. 796-804
    • Chang, S.1    Pikaard, C.S.2
  • 39
    • 34249664888 scopus 로고    scopus 로고
    • SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes
    • Berdeaux R., et al. SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes. Nat. Med. 13 (2007) 597-603
    • (2007) Nat. Med. , vol.13 , pp. 597-603
    • Berdeaux, R.1
  • 40
    • 55749103407 scopus 로고    scopus 로고
    • The HDAC inhibitor 4b ameliorates the disease phenotype and transcriptional abnormalities in Huntington's disease transgenic mice
    • Thomas E.A., et al. The HDAC inhibitor 4b ameliorates the disease phenotype and transcriptional abnormalities in Huntington's disease transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 15564-15569
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15564-15569
    • Thomas, E.A.1
  • 41
    • 58149267462 scopus 로고    scopus 로고
    • Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau
    • Green K.N., et al. Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau. J. Neurosci. 28 (2008) 11500-11510
    • (2008) J. Neurosci. , vol.28 , pp. 11500-11510
    • Green, K.N.1
  • 42
    • 65349193781 scopus 로고    scopus 로고
    • A limited group of class I histone deacetylases acts to repress human immunodeficiency virus type 1 expression
    • Keedy K.S., et al. A limited group of class I histone deacetylases acts to repress human immunodeficiency virus type 1 expression. J. Virol. 83 (2009) 4749-4756
    • (2009) J. Virol. , vol.83 , pp. 4749-4756
    • Keedy, K.S.1
  • 43
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p
    • Allard S., et al. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J. 18 (1999) 5108-5119
    • (1999) EMBO J. , vol.18 , pp. 5108-5119
    • Allard, S.1
  • 44
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • Clarke A.S., et al. Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol. Cell. Biol. 19 (1999) 2515-2526
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2515-2526
    • Clarke, A.S.1
  • 45
    • 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., et al. Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. Virology 216 (1996) 357-366
    • (1996) Virology , vol.216 , pp. 357-366
    • Kamine, J.1
  • 46
    • 0030712311 scopus 로고    scopus 로고
    • Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60
    • Yamamoto T., and Horikoshi M. Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60. J. Biol. Chem. 272 (1997) 30595-30598
    • (1997) J. Biol. Chem. , vol.272 , pp. 30595-30598
    • Yamamoto, T.1    Horikoshi, M.2
  • 47
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • Ikura T., et al. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102 (2000) 463-473
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1
  • 48
    • 33747882071 scopus 로고    scopus 로고
    • Tip60 in DNA damage response and growth control: many tricks in one HAT
    • Squatrito M., et al. Tip60 in DNA damage response and growth control: many tricks in one HAT. Trends Cell Biol. 16 (2006) 433-442
    • (2006) Trends Cell Biol. , vol.16 , pp. 433-442
    • Squatrito, M.1
  • 49
    • 24944516931 scopus 로고    scopus 로고
    • A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM
    • Sun Y., et al. A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 13182-13187
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13182-13187
    • Sun, Y.1
  • 50
    • 20344365811 scopus 로고    scopus 로고
    • Involvement of human MOF in ATM function
    • Gupta A., et al. Involvement of human MOF in ATM function. Mol. Cell Biol. 25 (2005) 5292-5305
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5292-5305
    • Gupta, A.1
  • 51
    • 10844233155 scopus 로고    scopus 로고
    • Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions
    • Kusch T., et al. Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions. Science 306 (2004) 2084-2087
    • (2004) Science , vol.306 , pp. 2084-2087
    • Kusch, T.1
  • 52
    • 7244253057 scopus 로고    scopus 로고
    • Role of the histone acetyl transferase Tip60 in the p53 pathway
    • Legube G., et al. Role of the histone acetyl transferase Tip60 in the p53 pathway. J. Biol. Chem. 279 (2004) 44825-44833
    • (2004) J. Biol. Chem. , vol.279 , pp. 44825-44833
    • Legube, G.1
  • 53
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-binding domain regulates apoptosis induction
    • Sykes S.M., et al. Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol. Cell 24 (2006) 841-851
    • (2006) Mol. Cell , vol.24 , pp. 841-851
    • Sykes, S.M.1
  • 54
    • 33845668241 scopus 로고    scopus 로고
    • Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis
    • Tang Y., et al. Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol. Cell 24 (2006) 827-839
    • (2006) Mol. Cell , vol.24 , pp. 827-839
    • Tang, Y.1
  • 55
    • 0037007236 scopus 로고    scopus 로고
    • Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation
    • Legube G., et al. Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation. EMBO J. 21 (2002) 1704-1712
    • (2002) EMBO J. , vol.21 , pp. 1704-1712
    • Legube, G.1
  • 56
    • 47749095009 scopus 로고    scopus 로고
    • Regulation of TIP60 by ATF2 modulates ATM activation
    • Bhoumik A., et al. Regulation of TIP60 by ATF2 modulates ATM activation. J. Biol. Chem. 283 (2008) 17605-17614
    • (2008) J. Biol. Chem. , vol.283 , pp. 17605-17614
    • Bhoumik, A.1
  • 57
    • 0038576279 scopus 로고    scopus 로고
    • Tip60 acetyltransferase activity is controlled by phosphorylation
    • Lemercier C., et al. Tip60 acetyltransferase activity is controlled by phosphorylation. J. Biol. Chem. 278 (2003) 4713-4718
    • (2003) J. Biol. Chem. , vol.278 , pp. 4713-4718
    • Lemercier, C.1
  • 58
    • 17244378084 scopus 로고    scopus 로고
    • Transcriptional regulation of a metastasis suppressor gene by Tip60 and beta-catenin complexes
    • Kim J.H., et al. Transcriptional regulation of a metastasis suppressor gene by Tip60 and beta-catenin complexes. Nature 434 (2005) 921-926
    • (2005) Nature , vol.434 , pp. 921-926
    • Kim, J.H.1
  • 59
    • 34548312368 scopus 로고    scopus 로고
    • Tip60 is a haplo-insufficient tumour suppressor required for an oncogene-induced DNA damage response
    • Gorrini C., et al. Tip60 is a haplo-insufficient tumour suppressor required for an oncogene-induced DNA damage response. Nature 448 (2007) 1063-1067
    • (2007) Nature , vol.448 , pp. 1063-1067
    • Gorrini, C.1
  • 60
    • 58149202185 scopus 로고    scopus 로고
    • Phosphorylation regulates SIRT1 function
    • Sasaki T., et al. Phosphorylation regulates SIRT1 function. PLoS ONE 3 (2008) e4020
    • (2008) PLoS ONE , vol.3
    • Sasaki, T.1
  • 61
    • 35748962613 scopus 로고    scopus 로고
    • SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • Yang Y., et al. SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat. Cell Biol. 9 (2007) 1253-1262
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1253-1262
    • Yang, Y.1
  • 62
    • 0041353442 scopus 로고    scopus 로고
    • MDM2-ARF complex regulates p53 sumoylation
    • Chen L., and Chen J. MDM2-ARF complex regulates p53 sumoylation. Oncogene 22 (2003) 5348-5357
    • (2003) Oncogene , vol.22 , pp. 5348-5357
    • Chen, L.1    Chen, J.2
  • 63
    • 61549117795 scopus 로고    scopus 로고
    • Targeted therapies in solid tumours: pinpointing the tumour's Achilles heel
    • Kornek G., and Selzer E. Targeted therapies in solid tumours: pinpointing the tumour's Achilles heel. Curr. Pharm. Des. 15 (2009) 207-242
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 207-242
    • Kornek, G.1    Selzer, E.2
  • 64
    • 65649102301 scopus 로고    scopus 로고
    • First-line therapy for chronic myeloid leukemia: Past, present, and future
    • Pavlovsky C., et al. First-line therapy for chronic myeloid leukemia: Past, present, and future. Am. J. Hematol. (2009)
    • (2009) Am. J. Hematol.
    • Pavlovsky, C.1
  • 65
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W., and Roeder R.G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90 (1997) 595-606
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 66
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • Boyes J., et al. Regulation of activity of the transcription factor GATA-1 by acetylation. Nature 396 (1998) 594-598
    • (1998) Nature , vol.396 , pp. 594-598
    • Boyes, J.1
  • 67
    • 18244408596 scopus 로고    scopus 로고
    • DNA damage-dependent acetylation of p73 dictates the selective activation of apoptotic target genes
    • Costanzo A., et al. DNA damage-dependent acetylation of p73 dictates the selective activation of apoptotic target genes. Mol. Cell 9 (2002) 175-186
    • (2002) Mol. Cell , vol.9 , pp. 175-186
    • Costanzo, A.1
  • 68
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo J., et al. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 408 (2000) 377-381
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1
  • 69
    • 0037112901 scopus 로고    scopus 로고
    • MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation
    • Ito A., et al. MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation. EMBO J. 21 (2002) 6236-6245
    • (2002) EMBO J. , vol.21 , pp. 6236-6245
    • Ito, A.1
  • 70
    • 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., et al. Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor. J. Biol. Chem. 277 (2002) 25904-25913
    • (2002) J. Biol. Chem. , vol.277 , pp. 25904-25913
    • Gaughan, L.1
  • 71
    • 0035794552 scopus 로고    scopus 로고
    • A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program
    • Mal A., et al. A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program. EMBO J. 20 (2001) 1739-1753
    • (2001) EMBO J. , vol.20 , pp. 1739-1753
    • Mal, A.1
  • 72
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E., et al. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21 (2002) 2383-2396
    • (2002) EMBO J. , vol.21 , pp. 2383-2396
    • Langley, E.1
  • 73
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H., et al. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107 (2001) 149-159
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 74
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J., et al. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107 (2001) 137-148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 75
    • 33750367457 scopus 로고    scopus 로고
    • Hormonal control of androgen receptor function through SIRT1
    • Fu M., et al. Hormonal control of androgen receptor function through SIRT1. Mol. Cell. Biol. 26 (2006) 8122-8135
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8122-8135
    • Fu, M.1
  • 76
    • 67651210858 scopus 로고    scopus 로고
    • SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly (ADP-ribose) polymerase 1
    • Rajamohan S.B., et al. SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly (ADP-ribose) polymerase 1. Mol. Cell. Biol 29 (2009) 4116-4129
    • (2009) Mol. Cell. Biol , vol.29 , pp. 4116-4129
    • Rajamohan, S.B.1
  • 77
    • 57049120143 scopus 로고    scopus 로고
    • Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function
    • Wang L., et al. Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function. Curr. Opin. Struct. Biol. 18 (2008) 741-747
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 741-747
    • Wang, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.