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Volumn 68, Issue 7, 2011, Pages 1147-1156

MYST-family histone acetyltransferases: Beyond chromatin

Author keywords

Acetyltransferases; HBO1; Histones; Lysines; MOF; MYST; NuA4; TIP60

Indexed keywords

ESSENTIAL SAS2 RELATED ACETYLTRANSFERASE 1; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE BINDING TO ORC1; MALES ABSENT ON THE FIRST PROTEIN; MONOCYTIC LEUKEMIA ZINC FINGER PROTEIN; TAT INTERACTING PROTEIN 60; UNCLASSIFIED DRUG;

EID: 79953712902     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-010-0599-9     Document Type: Review
Times cited : (153)

References (97)
  • 2
    • 70349971418 scopus 로고    scopus 로고
    • Introducing the acetylome
    • 19816449 10.1038/nbt1009-917 1:CAS:528:DC%2BD1MXht1CisLnP
    • KT Smith JL Workman 2009 Introducing the acetylome Nat Biotechnol 27 917 919 19816449 10.1038/nbt1009-917 1:CAS:528:DC%2BD1MXht1CisLnP
    • (2009) Nat Biotechnol , vol.27 , pp. 917-919
    • Smith, K.T.1    Workman, J.L.2
  • 3
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • 19608861 10.1126/science.1175371 1:CAS:528:DC%2BD1MXps1Ogt70%3D
    • C Choudhary C Kumar F Gnad ML Nielsen M Rehman TC Walther JV Olsen M Mann 2009 Lysine acetylation targets protein complexes and co-regulates major cellular functions Science 325 834 840 19608861 10.1126/science.1175371 1:CAS:528:DC%2BD1MXps1Ogt70%3D
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Olsen, J.V.7    Mann, M.8
  • 4
    • 29544438797 scopus 로고    scopus 로고
    • Proteomic analysis of organ-specific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies
    • DOI 10.1002/pmic.200500042
    • H Iwabata M Yoshida Y Komatsu 2005 Proteomic analysis of organ-specific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies Proteomics 5 4653 4664 16247734 10.1002/pmic.200500042 1:CAS:528:DC%2BD28Xktlegtg%3D%3D (Pubitemid 43016886)
    • (2005) Proteomics , vol.5 , Issue.18 , pp. 4653-4664
    • Iwabata, H.1    Yoshida, M.2    Komatsu, Y.3
  • 6
    • 56649114286 scopus 로고    scopus 로고
    • The diversity of lysine-acetylated proteins in Escherichia coli
    • 18852508 1:CAS:528:DC%2BD1MXotFSktrk%3D
    • BJ Yu JA Kim JH Moon SE Ryu JG Pan 2008 The diversity of lysine-acetylated proteins in Escherichia coli J Microbiol Biotechnol 18 1529 1536 18852508 1:CAS:528:DC%2BD1MXotFSktrk%3D
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 1529-1536
    • Yu, B.J.1    Kim, J.A.2    Moon, J.H.3    Ryu, S.E.4    Pan, J.G.5
  • 8
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • DOI 10.1038/nsmb1338, PII NSMB1338
    • SD Taverna H Li AJ Ruthenburg CD Allis DJ Patel 2007 How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers Nat Struct Mol Biol 14 1025 1040 17984965 10.1038/nsmb1338 1:CAS:528:DC%2BD2sXht1Kjs7vE (Pubitemid 350060344)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.11 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 9
    • 35848936709 scopus 로고    scopus 로고
    • Cross-regulation of histone modifications
    • DOI 10.1038/nsmb1307, PII NSMB1307
    • JA Latham SY Dent 2007 Cross-regulation of histone modifications Nat Struct Mol Biol 14 1017 1024 17984964 10.1038/nsmb1307 1:CAS:528: DC%2BD2sXht1Kjs7jF (Pubitemid 350060331)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.11 , pp. 1017-1024
    • Latham, J.A.1    Dent, S.Y.R.2
  • 10
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • 14172992 10.1073/pnas.51.5.786 1:CAS:528:DyaF2cXktlekurg%3D
    • VG Allfrey R Faulkner AE Mirsky 1964 Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis Proc Natl Acad Sci USA 51 786 794 14172992 10.1073/pnas.51.5.786 1:CAS:528: DyaF2cXktlekurg%3D
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 11
    • 0037133040 scopus 로고    scopus 로고
    • Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion
    • DOI 10.1016/S0960-9822(02)00681-4, PII S0960982202006814
    • D Ivanov A Schleiffer F Eisenhaber K Mechtler CH Haering K Nasmyth 2002 Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion Curr Biol 12 323 328 11864574 10.1016/S0960-9822(02)00681-4 1:CAS:528:DC%2BD38XhslWgtLw%3D (Pubitemid 34161478)
    • (2002) Current Biology , vol.12 , Issue.4 , pp. 323-328
    • Ivanov, D.1    Schleiffer, A.2    Eisenhaber, F.3    Mechtler, K.4    Haering, C.H.5    Nasmyth, K.6
  • 12
    • 0038204415 scopus 로고    scopus 로고
    • The diverse functions of histone acetyltransferase complexes
    • DOI 10.1016/S0168-9525(03)00115-X
    • MJ Carrozza RT Utley JL Workman J Cote 2003 The diverse functions of histone acetyltransferase complexes Trends Genet 19 321 329 12801725 10.1016/S0168-9525(03)00115-X 1:CAS:528:DC%2BD3sXksVyqtbo%3D (Pubitemid 36694615)
    • (2003) Trends in Genetics , vol.19 , Issue.6 , pp. 321-329
    • Carrozza, M.J.1    Utley, R.T.2    Workman, J.L.3    Cote, J.4
  • 13
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: One size doesn't fit all
    • DOI 10.1038/nrm2145, PII NRM2145
    • KK Lee JL Workman 2007 Histone acetyltransferase complexes: one size doesn't fit all Nat Rev Mol Cell Biol 8 284 295 17380162 10.1038/nrm2145 1:CAS:528:DC%2BD2sXjtlygsrw%3D (Pubitemid 46474661)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.4 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 14
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • 17362198 10.1146/annurev.biochem.76.052705.162114 1:CAS:528: DC%2BD2sXhtVehtb7O
    • MD Shahbazian M Grunstein 2007 Functions of site-specific histone acetylation and deacetylation Annu Rev Biochem 76 75 100 17362198 10.1146/annurev.biochem.76.052705.162114 1:CAS:528:DC%2BD2sXhtVehtb7O
    • (2007) Annu Rev Biochem , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 15
    • 34547896549 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases and their intimate links to cancer
    • DOI 10.1038/sj.onc.1210608, PII 1210608
    • N Avvakumov J Cote 2007 The MYST family of histone acetyltransferases and their intimate links to cancer Oncogene 26 5395 5407 17694081 10.1038/sj.onc.1210608 1:CAS:528:DC%2BD2sXovFeku7g%3D (Pubitemid 47255922)
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5395-5407
    • Avvakumov, N.1    Cote, J.2
  • 16
    • 34047229996 scopus 로고    scopus 로고
    • The diverse biological roles of MYST histone acetyltransferase family proteins
    • T Thomas AK Voss 2007 The diverse biological roles of MYST histone acetyltransferase family proteins Cell Cycle 6 696 704 17374998 10.4161/cc.6.6.4013 1:CAS:528:DC%2BD2sXnvFCltb4%3D (Pubitemid 46535682)
    • (2007) Cell Cycle , vol.6 , Issue.6 , pp. 696-704
    • Thomas, T.1    Voss, A.K.2
  • 18
    • 2342599619 scopus 로고    scopus 로고
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
    • DOI 10.1093/nar/gkh252
    • XJ Yang 2004 The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases Nucleic Acids Res 32 959 976 14960713 10.1093/nar/gkh252 1:CAS:528:DC%2BD2cXhslWktLs%3D (Pubitemid 38864676)
    • (2004) Nucleic Acids Research , vol.32 , Issue.3 , pp. 959-976
    • Yang, X.-J.1
  • 19
    • 42449092861 scopus 로고    scopus 로고
    • (de) MYSTification and INGenuity of tumor suppressors
    • 18239855 10.1007/s00018-008-7459-x 1:CAS:528:DC%2BD1cXkvFynsLk%3D
    • N Saksouk N Avvakumov J Cote 2008 (de) MYSTification and INGenuity of tumor suppressors Cell Mol Life Sci 65 1013 1018 18239855 10.1007/s00018-008- 7459-x 1:CAS:528:DC%2BD1cXkvFynsLk%3D
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1013-1018
    • Saksouk, N.1    Avvakumov, N.2    Cote, J.3
  • 20
    • 70349557613 scopus 로고    scopus 로고
    • MYST family histone acetyltransferases take center stage in stem cells and development
    • 19722182 10.1002/bies.200900051 1:CAS:528:DC%2BD1MXhtlynsL7J
    • AK Voss T Thomas 2009 MYST family histone acetyltransferases take center stage in stem cells and development Bioessays 31 1050 1061 19722182 10.1002/bies.200900051 1:CAS:528:DC%2BD1MXhtlynsL7J
    • (2009) Bioessays , vol.31 , pp. 1050-1061
    • Voss, A.K.1    Thomas, T.2
  • 21
    • 33747882071 scopus 로고    scopus 로고
    • Tip60 in DNA damage response and growth control: many tricks in one HAT
    • DOI 10.1016/j.tcb.2006.07.007, PII S0962892406001966
    • M Squatrito C Gorrini B Amati 2006 Tip60 in DNA damage response and growth control: many tricks in one HAT Trends Cell Biol 16 433 442 16904321 10.1016/j.tcb.2006.07.007 1:CAS:528:DC%2BD28XptFChsb0%3D (Pubitemid 44293403)
    • (2006) Trends in Cell Biology , vol.16 , Issue.9 , pp. 433-442
    • Squatrito, M.1    Gorrini, C.2    Amati, B.3
  • 22
    • 62149143727 scopus 로고    scopus 로고
    • Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis
    • 19303850 10.1016/j.cell.2009.01.033 1:CAS:528:DC%2BD1MXltFSntrc%3D
    • YY Lin JY Lu J Zhang W Walter W Dang J Wan SC Tao J Qian Y Zhao JD Boeke SL Berger H Zhu 2009 Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis Cell 136 1073 1084 19303850 10.1016/j.cell.2009.01.033 1:CAS:528:DC%2BD1MXltFSntrc%3D
    • (2009) Cell , vol.136 , pp. 1073-1084
    • Lin, Y.Y.1    Lu, J.Y.2    Zhang, J.3    Walter, W.4    Dang, W.5    Wan, J.6    Tao, S.C.7    Qian, J.8    Zhao, Y.9    Boeke, J.D.10    Berger, S.L.11    Zhu, H.12
  • 23
    • 34547895492 scopus 로고    scopus 로고
    • MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells
    • DOI 10.1038/sj.onc.1210609, PII 1210609
    • XJ Yang M Ullah 2007 MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells Oncogene 26 5408 5419 17694082 10.1038/sj.onc.1210609 1:CAS:528:DC%2BD2sXovFeku7k%3D (Pubitemid 47255923)
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5408-5419
    • Yang, X.-J.1    Ullah, M.2
  • 25
    • 33745141913 scopus 로고    scopus 로고
    • Monocytic leukemia zinc finger protein is essential for the development of long-term reconstituting hematopoietic stem cells
    • 16651658 10.1101/gad.1382606 1:CAS:528:DC%2BD28XkslCjsbc%3D
    • T Thomas LM Corcoran R Gugasyan MP Dixon T Brodnicki SL Nutt D Metcalf AK Voss 2006 Monocytic leukemia zinc finger protein is essential for the development of long-term reconstituting hematopoietic stem cells Genes Dev 20 1175 1186 16651658 10.1101/gad.1382606 1:CAS:528:DC%2BD28XkslCjsbc%3D
    • (2006) Genes Dev , vol.20 , pp. 1175-1186
    • Thomas, T.1    Corcoran, L.M.2    Gugasyan, R.3    Dixon, M.P.4    Brodnicki, T.5    Nutt, S.L.6    Metcalf, D.7    Voss, A.K.8
  • 26
    • 71549124331 scopus 로고    scopus 로고
    • Moz and retinoic acid coordinately regulate H3K9 acetylation, Hox gene expression, and segment identity
    • 19922872 10.1016/j.devcel.2009.10.006 1:CAS:528:DC%2BD1MXhsFKltb7M
    • AK Voss C Collin MP Dixon T Thomas 2009 Moz and retinoic acid coordinately regulate H3K9 acetylation, Hox gene expression, and segment identity Dev Cell 17 674 686 19922872 10.1016/j.devcel.2009.10.006 1:CAS:528:DC%2BD1MXhsFKltb7M
    • (2009) Dev Cell , vol.17 , pp. 674-686
    • Voss, A.K.1    Collin, C.2    Dixon, M.P.3    Thomas, T.4
  • 28
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • DOI 10.1101/gad.931401
    • L Howe D Auston P Grant S John RG Cook JL Workman L Pillus 2001 Histone H3 specific acetyltransferases are essential for cell cycle progression Genes Dev 15 3144 3154 11731478 10.1101/gad.931401 1:CAS:528:DC%2BD3MXptVKmsL4%3D (Pubitemid 33115678)
    • (2001) Genes and Development , vol.15 , Issue.23 , pp. 3144-3154
    • Howe, L.1    Auston, D.2    Grant, P.3    John, S.4    Cook, R.G.5    Workman, J.L.6    Pillus, L.7
  • 29
    • 0037126635 scopus 로고    scopus 로고
    • Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein
    • DOI 10.1093/emboj/20.24.7184
    • I Kitabayashi Y Aikawa LA Nguyen A Yokoyama M Ohki 2001 Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein EMBO J 20 7184 7196 11742995 10.1093/emboj/20.24.7184 1:CAS:528:DC%2BD38XpsFym (Pubitemid 34062310)
    • (2001) EMBO Journal , vol.20 , Issue.24 , pp. 7184-7196
    • Kitabayashi, I.1    Aikawa, Y.2    Nguyen, L.A.3    Yokoyama, A.4    Ohki, M.5
  • 31
    • 33746988776 scopus 로고    scopus 로고
    • Differential gene regulation by selective association of transcriptional coactivators and bZIP DNA-binding domains
    • DOI 10.1128/MCB.00696-06
    • B Miotto K Struhl 2006 Differential gene regulation by selective association of transcriptional coactivators and bZIP DNA-binding domains Mol Cell Biol 26 5969 5982 16880509 10.1128/MCB.00696-06 1:CAS:528: DC%2BD28Xot1yltrw%3D (Pubitemid 44204517)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.16 , pp. 5969-5982
    • Miotto, B.1    Struhl, K.2
  • 32
    • 53549122748 scopus 로고    scopus 로고
    • HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1
    • 18832067 10.1101/gad.1674108 1:CAS:528:DC%2BD1cXht1ClsbvM
    • B Miotto K Struhl 2008 HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1 Genes Dev 22 2633 2638 18832067 10.1101/gad.1674108 1:CAS:528:DC%2BD1cXht1ClsbvM
    • (2008) Genes Dev , vol.22 , pp. 2633-2638
    • Miotto, B.1    Struhl, K.2
  • 33
    • 73649089696 scopus 로고    scopus 로고
    • HBO1 histone acetylase activity is essential for DNA replication licensing and inhibited by Geminin
    • 20129055 10.1016/j.molcel.2009.12.012 1:CAS:528:DC%2BC3cXkvFKgsLY%3D
    • B Miotto K Struhl 2010 HBO1 histone acetylase activity is essential for DNA replication licensing and inhibited by Geminin Mol Cell 37 57 66 20129055 10.1016/j.molcel.2009.12.012 1:CAS:528:DC%2BC3cXkvFKgsLY%3D
    • (2010) Mol Cell , vol.37 , pp. 57-66
    • Miotto, B.1    Struhl, K.2
  • 34
    • 29544444195 scopus 로고    scopus 로고
    • ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation
    • DOI 10.1016/j.molcel.2005.12.007, PII S1097276505018496
    • Y Doyon C Cayrou M Ullah AJ Landry V Cote W Selleck WS Lane S Tan XJ Yang J Cote 2006 ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation Mol Cell 21 51 64 16387653 10.1016/j.molcel.2005.12.007 1:CAS:528:DC%2BD28Xptlelsw%3D%3D (Pubitemid 43017848)
    • (2006) Molecular Cell , vol.21 , Issue.1 , pp. 51-64
    • Doyon, Y.1    Cayrou, C.2    Ullah, M.3    Landry, A.-J.4    Cote, V.5    Selleck, W.6    Lane, W.S.7    Tan, S.8    Yang, X.-J.9    Cote, J.10
  • 35
    • 31344462362 scopus 로고    scopus 로고
    • Regulation of replication licensing by acetyltransferase Hbo1
    • DOI 10.1128/MCB.26.3.1098-1108.2006
    • M Iizuka T Matsui H Takisawa MM Smith 2006 Regulation of replication licensing by acetyltransferase Hbo1 Mol Cell Biol 26 1098 1108 16428461 10.1128/MCB.26.3.1098-1108.2006 1:CAS:528:DC%2BD28XhtVOns7s%3D (Pubitemid 43146501)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.3 , pp. 1098-1108
    • Iizuka, M.1    Matsui, T.2    Takisawa, H.3    Smith, M.M.4
  • 36
    • 22544480772 scopus 로고    scopus 로고
    • HMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells
    • DOI 10.1128/MCB.25.15.6798-6810.2005
    • M Taipale S Rea K Richter A Vilar P Lichter A Imhof A Akhtar 2005 hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells Mol Cell Biol 25 6798 6810 16024812 10.1128/MCB.25.15.6798-6810. 2005 1:CAS:528:DC%2BD2MXntVSgs7w%3D (Pubitemid 41023250)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.15 , pp. 6798-6810
    • Taipale, M.1    Rea, S.2    Richter, K.3    Vilar, A.4    Lichter, P.5    Imhof, A.6    Akhtar, A.7
  • 37
    • 27144546434 scopus 로고    scopus 로고
    • A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16
    • DOI 10.1128/MCB.25.21.9175-9188.2005
    • ER Smith C Cayrou R Huang WS Lane J Cote JC Lucchesi 2005 A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16 Mol Cell Biol 25 9175 9188 16227571 10.1128/MCB.25.21.9175-9188.2005 1:CAS:528:DC%2BD2MXhtFOnsrjK (Pubitemid 41507821)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.21 , pp. 9175-9188
    • Smith, E.R.1    Cayrou, C.2    Huang, R.3    Lane, W.S.4    Cote, J.5    Lucchesi, J.C.6
  • 38
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • DOI 10.1038/ng993
    • A Kimura T Umehara M Horikoshi 2002 Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing Nat Genet 32 370 377 12410229 10.1038/ng993 (Pubitemid 35266110)
    • (2002) Nature Genetics , vol.32 , Issue.3 , pp. 370-377
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 39
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin
    • DOI 10.1038/ng1017
    • N Suka K Luo M Grunstein 2002 Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin Nat Genet 32 378 383 12379856 10.1038/ng1017 1:CAS:528:DC%2BD38Xot1Kls7k%3D (Pubitemid 35266111)
    • (2002) Nature Genetics , vol.32 , Issue.3 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 41
    • 70350012477 scopus 로고    scopus 로고
    • Two mammalian MOF complexes regulate transcription activation by distinct mechanisms
    • 19854137 10.1016/j.molcel.2009.07.031 1:CAS:528:DC%2BD1MXhsFWht7vI
    • X Li L Wu CA Corsa S Kunkel Y Dou 2009 Two mammalian MOF complexes regulate transcription activation by distinct mechanisms Mol Cell 36 290 301 19854137 10.1016/j.molcel.2009.07.031 1:CAS:528:DC%2BD1MXhsFWht7vI
    • (2009) Mol Cell , vol.36 , pp. 290-301
    • Li, X.1    Wu, L.2    Corsa, C.A.3    Kunkel, S.4    Dou, Y.5
  • 43
    • 34547913733 scopus 로고    scopus 로고
    • Males absent on the first (MOF): From flies to humans
    • DOI 10.1038/sj.onc.1210607, PII 1210607
    • S Rea G Xouri A Akhtar 2007 Males absent on the first (MOF): from flies to humans Oncogene 26 5385 5394 17694080 10.1038/sj.onc.1210607 1:CAS:528:DC%2BD2sXovFeku7s%3D (Pubitemid 47255921)
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5385-5394
    • Rea, S.1    Xouri, G.2    Akhtar, A.3
  • 44
    • 3042541533 scopus 로고    scopus 로고
    • Functional integration of the histone acetyltransferase MOF into the dosage compensation complex
    • DOI 10.1038/sj.emboj.7600235
    • V Morales T Straub MF Neumann G Mengus A Akhtar PB Becker 2004 Functional integration of the histone acetyltransferase MOF into the dosage compensation complex EMBO J 23 2258 2268 15141166 10.1038/sj.emboj.7600235 1:CAS:528:DC%2BD2cXksV2htr4%3D (Pubitemid 38833235)
    • (2004) EMBO Journal , vol.23 , Issue.11 , pp. 2258-2268
    • Morales, V.1    Straub, T.2    Neumann, M.F.3    Mengus, G.4    Akhtar, A.5    Becker, P.B.6
  • 45
    • 0038730928 scopus 로고    scopus 로고
    • MOF-regulated acetylation of MSL-3 in the Drosophila dosage compensation complex
    • DOI 10.1016/S1097-2765(03)00140-0
    • A Buscaino T Kocher JH Kind H Holz M Taipale K Wagner M Wilm A Akhtar 2003 MOF-regulated acetylation of MSL-3 in the Drosophila dosage compensation complex Mol Cell 11 1265 1277 12769850 10.1016/S1097-2765(03)00140-0 1:CAS:528:DC%2BD3sXksVOjt7Y%3D (Pubitemid 36645145)
    • (2003) Molecular Cell , vol.11 , Issue.5 , pp. 1265-1277
    • Buscaino, A.1    Kocher, T.2    Kind, J.H.3    Holz, H.4    Taipale, M.5    Wagner, K.6    Wilm, M.7    Akhtar, A.8
  • 46
    • 0034699391 scopus 로고    scopus 로고
    • Chromodomains are protein-RNA interaction modules
    • 11014199 10.1038/35030169 1:CAS:528:DC%2BD3cXntF2ntb4%3D
    • A Akhtar D Zink PB Becker 2000 Chromodomains are protein-RNA interaction modules Nature 407 405 409 11014199 10.1038/35030169 1:CAS:528: DC%2BD3cXntF2ntb4%3D
    • (2000) Nature , vol.407 , pp. 405-409
    • Akhtar, A.1    Zink, D.2    Becker, P.B.3
  • 47
    • 77951182263 scopus 로고    scopus 로고
    • Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex
    • 20018852 10.1074/jbc.C109.087981 1:CAS:528:DC%2BC3cXhs1altLk%3D
    • Y Cai J Jin SK Swanson MD Cole SH Choi L Florens MP Washburn JW Conaway RC Conaway 2010 Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex J Biol Chem 285 4268 4272 20018852 10.1074/jbc.C109.087981 1:CAS:528:DC%2BC3cXhs1altLk%3D
    • (2010) J Biol Chem , vol.285 , pp. 4268-4272
    • Cai, Y.1    Jin, J.2    Swanson, S.K.3    Cole, M.D.4    Choi, S.H.5    Florens, L.6    Washburn, M.P.7    Conaway, J.W.8    Conaway, R.C.9
  • 49
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-Binding Domain Regulates Apoptosis Induction
    • DOI 10.1016/j.molcel.2006.11.026, PII S1097276506008215
    • SM Sykes HS Mellert MA Holbert K Li R Marmorstein WS Lane SB McMahon 2006 Acetylation of the p53 DNA-binding domain regulates apoptosis induction Mol Cell 24 841 851 17189187 10.1016/j.molcel.2006.11.026 1:CAS:528: DC%2BD2sXmvVyqug%3D%3D (Pubitemid 44960096)
    • (2006) Molecular Cell , vol.24 , Issue.6 , pp. 841-851
    • Sykes, S.M.1    Mellert, H.S.2    Holbert, M.A.3    Li, K.4    Marmorstein, R.5    Lane, W.S.6    McMahon, S.B.7
  • 50
    • 33845668241 scopus 로고    scopus 로고
    • Tip60-Dependent Acetylation of p53 Modulates the Decision between Cell-Cycle Arrest and Apoptosis
    • DOI 10.1016/j.molcel.2006.11.021, PII S109727650600815X
    • Y Tang J Luo W Zhang W Gu 2006 Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis Mol Cell 24 827 839 17189186 10.1016/j.molcel.2006.11.021 1:CAS:528:DC%2BD2sXmvVyqtQ%3D%3D (Pubitemid 44960094)
    • (2006) Molecular Cell , vol.24 , Issue.6 , pp. 827-839
    • Tang, Y.1    Luo, J.2    Zhang, W.3    Gu, W.4
  • 51
    • 68249094672 scopus 로고    scopus 로고
    • Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing
    • 19578370 10.1038/ncb1914 1:CAS:528:DC%2BD1MXpsVaktb4%3D
    • Y Zhou KM Schmitz C Mayer X Yuan A Akhtar I Grummt 2009 Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing Nat Cell Biol 11 1010 1016 19578370 10.1038/ncb1914 1:CAS:528:DC%2BD1MXpsVaktb4%3D
    • (2009) Nat Cell Biol , vol.11 , pp. 1010-1016
    • Zhou, Y.1    Schmitz, K.M.2    Mayer, C.3    Yuan, X.4    Akhtar, A.5    Grummt, I.6
  • 53
    • 30344444484 scopus 로고    scopus 로고
    • Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks
    • DOI 10.1038/ncb1343, PII N1343
    • R Murr JI Loizou YG Yang C Cuenin H Li ZQ Wang Z Herceg 2006 Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks Nat Cell Biol 8 91 99 16341205 10.1038/ncb1343 1:CAS:528:DC%2BD28Xmt1eh (Pubitemid 43064802)
    • (2006) Nature Cell Biology , vol.8 , Issue.1 , pp. 91-99
    • Murr, R.1    Loizou, J.I.2    Yang, Y.-G.3    Cuenin, C.4    Li, H.5    Wang, Z.-Q.6    Herceg, Z.7
  • 55
    • 42149162883 scopus 로고    scopus 로고
    • Human Rvb1/Tip49 is required for the histone acetyltransferase activity of Tip60/NuA4 and for the downregulation of phosphorylation on H2AX after DNA damage
    • DOI 10.1128/MCB.01983-07
    • S Jha E Shibata A Dutta 2008 Human Rvb1/Tip49 is required for the histone acetyltransferase activity of Tip60/NuA4 and for the downregulation of phosphorylation on H2AX after DNA damage Mol Cell Biol 28 2690 2700 18285460 10.1128/MCB.01983-07 1:CAS:528:DC%2BD1cXksFWqtrk%3D (Pubitemid 351542368)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.8 , pp. 2690-2700
    • Jha, S.1    Shibata, E.2    Dutta, A.3
  • 57
    • 46149110511 scopus 로고    scopus 로고
    • An RNAi Screen of Chromatin Proteins Identifies Tip60-p400 as a Regulator of Embryonic Stem Cell Identity
    • DOI 10.1016/j.cell.2008.05.031, PII S0092867408006922
    • TG Fazzio JT Huff B Panning 2008 An RNAi screen of chromatin proteins identifies Tip60-p400 as a regulator of embryonic stem cell identity Cell 134 162 174 18614019 10.1016/j.cell.2008.05.031 1:CAS:528:DC%2BD1cXoslyjtbw%3D (Pubitemid 351905738)
    • (2008) Cell , vol.134 , Issue.1 , pp. 162-174
    • Fazzio, T.G.1    Huff, J.T.2    Panning, B.3
  • 58
    • 33746035661 scopus 로고    scopus 로고
    • ARF promotes RB accumulation through inhibition of its Tip60-dependent acetylation
    • DOI 10.1038/sj.onc.1209446, PII 1209446
    • C Leduc P Claverie B Eymin E Col S Khochbin E Brambilla S Gazzeri 2006 p14ARF promotes RB accumulation through inhibition of its Tip60-dependent acetylation Oncogene 25 4147 4154 16501607 10.1038/sj.onc.1209446 1:CAS:528:DC%2BD28XmvFais74%3D (Pubitemid 44079448)
    • (2006) Oncogene , vol.25 , Issue.30 , pp. 4147-4154
    • Leduc, C.1    Claverie, P.2    Eymin, B.3    Col, E.4    Khochbin, S.5    Brambilla, E.6    Gazzeri, S.7
  • 60
    • 27944448727 scopus 로고    scopus 로고
    • Dual regulation of c-Myc by p300 via acetylation-dependent control of Myc protein turnover and coactivation of Myc-induced transcription
    • DOI 10.1128/MCB.25.23.10220-10234.2005
    • F Faiola X Liu S Lo S Pan K Zhang E Lymar A Farina E Martinez 2005 Dual regulation of c-Myc by p300 via acetylation-dependent control of Myc protein turnover and coactivation of Myc-induced transcription Mol Cell Biol 25 10220 10234 16287840 10.1128/MCB.25.23.10220-10234.2005 1:CAS:528:DC%2BD2MXht1Ons7fL (Pubitemid 41681950)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.23 , pp. 10220-10234
    • Faiola, F.1    Liu, X.2    Lo, S.3    Pan, S.4    Zhang, K.5    Lymar, E.6    Farina, A.7    Martinez, E.8
  • 61
    • 1342346531 scopus 로고    scopus 로고
    • Structural and Functional Conservation of the NuA4 Histone Acetyltransferase Complex from Yeast to Humans
    • DOI 10.1128/MCB.24.5.1884-1896.2004
    • Y Doyon W Selleck WS Lane S Tan J Cote 2004 Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans Mol Cell Biol 24 1884 1896 14966270 10.1128/MCB.24.5.1884-1896.2004 1:CAS:528:DC%2BD2cXhvVWgt7o%3D (Pubitemid 38248930)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.5 , pp. 1884-1896
    • Doyon, Y.1    Selleck, W.2    Lane, W.S.3    Tan, S.4    Cote, J.5
  • 62
    • 0035395872 scopus 로고    scopus 로고
    • The ATM-related domain of TRRAP is required for histone acetyltransferase recruitment and Myc-dependent oncogenesis
    • DOI 10.1101/gad.900101
    • J Park S Kunjibettu SB McMahon MD Cole 2001 The ATM-related domain of TRRAP is required for histone acetyltransferase recruitment and Myc-dependent oncogenesis Genes Dev 15 1619 1624 11445536 10.1101/gad.900101 1:CAS:528:DC%2BD3MXltFKqt7o%3D (Pubitemid 32702583)
    • (2001) Genes and Development , vol.15 , Issue.13 , pp. 1619-1624
    • Park, J.1    Kunjibettu, S.2    McMahon, S.B.3    Cole, M.D.4
  • 63
    • 0041590889 scopus 로고    scopus 로고
    • MYC recruits the TIP60 histone acetyltransferase complex to chromatin
    • DOI 10.1038/sj.embor.embor861
    • SR Frank T Parisi S Taubert P Fernandez M Fuchs HM Chan DM Livingston B Amati 2003 MYC recruits the TIP60 histone acetyltransferase complex to chromatin EMBO Rep 4 575 580 12776177 10.1038/sj.embor.embor861 1:CAS:528: DC%2BD3sXktFOgtrY%3D (Pubitemid 36939948)
    • (2003) EMBO Reports , vol.4 , Issue.6 , pp. 575-580
    • Frank, S.R.1    Parisi, T.2    Taubert, S.3    Fernandez, P.4    Fuchs, M.5    Chan, H.-M.6    Livingston, D.M.7    Amati, B.8
  • 64
    • 56649107917 scopus 로고    scopus 로고
    • Analysis of Myc-induced histone modifications on target chromatin
    • 18985155 10.1371/journal.pone.0003650
    • F Martinato M Cesaroni B Amati E Guccione 2008 Analysis of Myc-induced histone modifications on target chromatin PLoS One 3 e3650 18985155 10.1371/journal.pone.0003650
    • (2008) PLoS One , vol.3 , pp. 3650
    • Martinato, F.1    Cesaroni, M.2    Amati, B.3    Guccione, E.4
  • 65
    • 77957757417 scopus 로고    scopus 로고
    • A Myc network accounts for similarities between embryonic stem and cancer cell transcription programs
    • 20946988 10.1016/j.cell.2010.09.010 1:CAS:528:DC%2BC3cXht12qurbM
    • J Kim AJ Woo J Chu JW Snow Y Fujiwara CG Kim AB Cantor SH Orkin 2010 A Myc network accounts for similarities between embryonic stem and cancer cell transcription programs Cell 143 313 324 20946988 10.1016/j.cell.2010.09.010 1:CAS:528:DC%2BC3cXht12qurbM
    • (2010) Cell , vol.143 , pp. 313-324
    • Kim, J.1    Woo, A.J.2    Chu, J.3    Snow, J.W.4    Fujiwara, Y.5    Kim, C.G.6    Cantor, A.B.7    Orkin, S.H.8
  • 67
    • 3042533087 scopus 로고    scopus 로고
    • Putative involvement of the histone acetyltransferase Tip60 in ribosomal gene transcription
    • DOI 10.1093/nar/gkh296
    • K Halkidou IR Logan S Cook DE Neal CN Robson 2004 Putative involvement of the histone acetyltransferase Tip60 in ribosomal gene transcription Nucleic Acids Res 32 1654 1665 15016909 10.1093/nar/gkh296 1:CAS:528: DC%2BD2cXisF2lu7g%3D (Pubitemid 38842408)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1654-1665
    • Halkidou, K.1    Logan, I.R.2    Cook, S.3    Neal, D.E.4    Robson, C.N.5
  • 69
    • 39049116217 scopus 로고    scopus 로고
    • Tip60 modulates PLAGL2-mediated transactivation by acetylation
    • DOI 10.1002/jcb.21444
    • J Ning G Zheng YC Yang 2008 Tip60 modulates PLAGL2-mediated transactivation by acetylation J Cell Biochem 103 730 739 17551969 10.1002/jcb.21444 1:CAS:528:DC%2BD1cXit1Shsrw%3D (Pubitemid 351240610)
    • (2008) Journal of Cellular Biochemistry , vol.103 , Issue.3 , pp. 730-739
    • Ning, J.1    Zheng, G.2    Yang, Y.-C.3
  • 70
    • 0037135566 scopus 로고    scopus 로고
    • Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor
    • DOI 10.1074/jbc.M203423200
    • L Gaughan IR Logan S Cook DE Neal CN Robson 2002 Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor J Biol Chem 277 25904 25913 11994312 10.1074/jbc.M203423200 1:CAS:528:DC%2BD38XlsFKrsL4%3D (Pubitemid 34967070)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 25904-25913
    • Gaughan, L.1    Logan, I.R.2    Cook, S.3    Neal, D.E.4    Robson, C.N.5
  • 71
    • 34548772930 scopus 로고    scopus 로고
    • Tip60 histone acetyltransferase acts as a negative regulator of notch1 signaling by means of acetylation
    • DOI 10.1128/MCB.01515-06
    • MY Kim EJ Ann JY Kim JS Mo JH Park SY Kim MS Seo HS Park 2007 Tip60 histone acetyltransferase acts as a negative regulator of Notch1 signaling by means of acetylation Mol Cell Biol 27 6506 6519 17636029 10.1128/MCB.01515-06 1:CAS:528:DC%2BD2sXhtVKls7nL (Pubitemid 47435755)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.18 , pp. 6506-6519
    • Kim, M.-Y.1    Ann, E.-J.2    Kim, J.-Y.3    Mo, J.-S.4    Park, J.-H.5    Kim, S.-Y.6    Seo, M.-S.7    Park, H.-S.8
  • 72
    • 67749103995 scopus 로고    scopus 로고
    • Acetylation of the DNA binding domain regulates transcription-independent apoptosis by p53
    • 19494119 10.1074/jbc.M109.026096 1:CAS:528:DC%2BD1MXos1ensL8%3D
    • SM Sykes TJ Stanek A Frank ME Murphy SB McMahon 2009 Acetylation of the DNA binding domain regulates transcription-independent apoptosis by p53 J Biol Chem 284 20197 20205 19494119 10.1074/jbc.M109.026096 1:CAS:528: DC%2BD1MXos1ensL8%3D
    • (2009) J Biol Chem , vol.284 , pp. 20197-20205
    • Sykes, S.M.1    Stanek, T.J.2    Frank, A.3    Murphy, M.E.4    McMahon, S.B.5
  • 75
    • 38949178369 scopus 로고    scopus 로고
    • Methylation of p53 by Set7/9 Mediates p53 Acetylation and Activity In Vivo
    • DOI 10.1016/j.molcel.2007.12.025, PII S1097276508000683
    • JK Kurash H Lei Q Shen WL Marston BW Granda H Fan D Wall E Li F Gaudet 2008 Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo Mol Cell 29 392 400 18280244 10.1016/j.molcel.2007.12.025 1:CAS:528: DC%2BD1cXisFSnsL4%3D (Pubitemid 351215939)
    • (2008) Molecular Cell , vol.29 , Issue.3 , pp. 392-400
    • Kurash, J.K.1    Lei, H.2    Shen, Q.3    Marston, W.L.4    Granda, B.W.5    Fan, H.6    Wall, D.7    Li, E.8    Gaudet, F.9
  • 76
    • 37549028411 scopus 로고    scopus 로고
    • DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity
    • 17923702 10.1128/MCB.01382-07 1:CAS:528:DC%2BD1cXmt1eqtQ%3D%3D
    • Y Sun Y Xu K Roy BD Price 2007 DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity Mol Cell Biol 27 8502 8509 17923702 10.1128/MCB.01382-07 1:CAS:528:DC%2BD1cXmt1eqtQ%3D%3D
    • (2007) Mol Cell Biol , vol.27 , pp. 8502-8509
    • Sun, Y.1    Xu, Y.2    Roy, K.3    Price, B.D.4
  • 77
    • 10944267160 scopus 로고    scopus 로고
    • Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites
    • DOI 10.1016/j.molcel.2004.12.003, PII S1097276504007580
    • JA Downs S Allard O Jobin-Robitaille A Javaheri A Auger N Bouchard SJ Kron SP Jackson J Cote 2004 Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites Mol Cell 16 979 990 15610740 10.1016/j.molcel.2004.12.003 1:CAS:528:DC%2BD2MXjvVWjtA%3D%3D (Pubitemid 40018407)
    • (2004) Molecular Cell , vol.16 , Issue.6 , pp. 979-990
    • Downs, J.A.1    Allard, S.2    Jobin-Robitaille, O.3    Javaheri, A.4    Auger, A.5    Bouchard, N.6    Kron, S.J.7    Jackson, S.P.8    Cote, J.9
  • 79
    • 70349662183 scopus 로고    scopus 로고
    • NuA4 and SWR1-C: Two chromatin-modifying complexes with overlapping functions and components
    • 19898529 10.1139/O09-062 1:CAS:528:DC%2BD1MXht1antL7L
    • PY Lu N Levesque MS Kobor 2009 NuA4 and SWR1-C: two chromatin-modifying complexes with overlapping functions and components Biochem Cell Biol 87 799 815 19898529 10.1139/O09-062 1:CAS:528:DC%2BD1MXht1antL7L
    • (2009) Biochem Cell Biol , vol.87 , pp. 799-815
    • Lu, P.Y.1    Levesque, N.2    Kobor, M.S.3
  • 80
    • 1942439646 scopus 로고    scopus 로고
    • The highly conserved and multifunctional NuA4 HAT complex
    • DOI 10.1016/j.gde.2004.02.009, PII S0959437X04000310
    • Y Doyon J Cote 2004 The highly conserved and multifunctional NuA4 HAT complex Curr Opin Genet Dev 14 147 154 15196461 10.1016/j.gde.2004.02.009 1:CAS:528:DC%2BD2cXivVKktLs%3D (Pubitemid 38520142)
    • (2004) Current Opinion in Genetics and Development , vol.14 , Issue.2 , pp. 147-154
    • Doyon, Y.1    Cote, J.2
  • 81
    • 65249154288 scopus 로고    scopus 로고
    • Connection between histone H2A variants and chromatin remodeling complexes
    • 19234522 10.1139/O08-140 1:CAS:528:DC%2BD1MXit1agt78%3D
    • M Altaf A Auger M Covic J Cote 2009 Connection between histone H2A variants and chromatin remodeling complexes Biochem Cell Biol 87 35 50 19234522 10.1139/O08-140 1:CAS:528:DC%2BD1MXit1agt78%3D
    • (2009) Biochem Cell Biol , vol.87 , pp. 35-50
    • Altaf, M.1    Auger, A.2    Covic, M.3    Cote, J.4
  • 82
    • 48849089284 scopus 로고    scopus 로고
    • Systematic genetic array analysis links the Saccharomyces cerevisiae SAGA/SLIK and NuA4 component Tra1 to multiple cellular processes
    • 18616809 10.1186/1471-2156-9-46
    • SM Hoke J Guzzo B Andrews CJ Brandl 2008 Systematic genetic array analysis links the Saccharomyces cerevisiae SAGA/SLIK and NuA4 component Tra1 to multiple cellular processes BMC Genet 9 46 18616809 10.1186/1471-2156-9-46
    • (2008) BMC Genet , vol.9 , pp. 46
    • Hoke, S.M.1    Guzzo, J.2    Andrews, B.3    Brandl, C.J.4
  • 83
    • 41149083933 scopus 로고    scopus 로고
    • Functional dissection of the NuA4 histone acetyltransferase reveals its role as a genetic hub and that Eaf1 is essential for complex integrity
    • DOI 10.1128/MCB.01653-07
    • L Mitchell JP Lambert M Gerdes AS Al-Madhoun IS Skerjanc D Figeys K Baetz 2008 Functional dissection of the NuA4 histone acetyltransferase reveals its role as a genetic hub and that Eaf1 is essential for complex integrity Mol Cell Biol 28 2244 2256 18212056 10.1128/MCB.01653-07 1:CAS:528:DC%2BD1cXjvFemtL0%3D (Pubitemid 351429971)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.7 , pp. 2244-2256
    • Mitchell, L.1    Lambert, J.-P.2    Gerdes, M.3    Al-Madhoun, A.S.4    Skerjanc, I.S.5    Figeys, D.6    Baetz, K.7
  • 84
    • 48749114997 scopus 로고    scopus 로고
    • A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation
    • 18676811 10.1101/gad.1679508 1:CAS:528:DC%2BD1cXpslKqsbo%3D
    • YY Lin Y Qi JY Lu X Pan DS Yuan Y Zhao JS Bader JD Boeke 2008 A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation Genes Dev 22 2062 2074 18676811 10.1101/gad.1679508 1:CAS:528:DC%2BD1cXpslKqsbo%3D
    • (2008) Genes Dev , vol.22 , pp. 2062-2074
    • Lin, Y.Y.1    Qi, Y.2    Lu, J.Y.3    Pan, X.4    Yuan, D.S.5    Zhao, Y.6    Bader, J.S.7    Boeke, J.D.8
  • 85
    • 0001446184 scopus 로고
    • The regulation of glycolysis and gluconeogenesis in animal tissues
    • 10.1146/annurev.bi.37.070168.001341 1:CAS:528:DyaF1MXjsVajtA%3D%3D
    • MC Scrutton FU Utter 1968 The regulation of glycolysis and gluconeogenesis in animal tissues Annu Rev Biochem 37 249 302 10.1146/annurev.bi.37.070168.001341 1:CAS:528:DyaF1MXjsVajtA%3D%3D
    • (1968) Annu Rev Biochem , vol.37 , pp. 249-302
    • Scrutton, M.C.1    Utter, F.U.2
  • 86
    • 27744596999 scopus 로고    scopus 로고
    • Sir2 blocks extreme life-span extension
    • DOI 10.1016/j.cell.2005.08.042, PII S009286740500913X
    • P Fabrizio C Gattazzo L Battistella M Wei C Cheng K McGrew VD Longo 2005 Sir2 blocks extreme life-span extension Cell 123 655 667 16286010 10.1016/j.cell.2005.08.042 1:CAS:528:DC%2BD2MXht1yktrjP (Pubitemid 41608467)
    • (2005) Cell , vol.123 , Issue.4 , pp. 655-667
    • Fabrizio, P.1    Gattazzo, C.2    Battistella, L.3    Wei, M.4    Cheng, C.5    McGrew, K.6    Longo, V.D.7
  • 87
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • DOI 10.1101/gad.13.19.2570
    • M Kaeberlein M McVey L Guarente 1999 The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms Genes Dev 13 2570 2580 10521401 10.1101/gad.13.19.2570 1:CAS:528:DyaK1MXmvFOitbc%3D (Pubitemid 29489648)
    • (1999) Genes and Development , vol.13 , Issue.19 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 88
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation
    • T Kouzarides 2000 Acetylation: a regulatory modification to rival phosphorylation? EMBO J 19 1176 1179 10716917 10.1093/emboj/19.6.1176 1:CAS:528:DC%2BD3cXit1Gms7o%3D (Pubitemid 30151013)
    • (2000) EMBO Journal , vol.19 , Issue.6 , pp. 1176-1179
    • Kouzarides, T.1
  • 89
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • DOI 10.1126/science.1077650
    • VJ Starai I Celic RN Cole JD Boeke JC Escalante-Semerena 2002 Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine Science 298 2390 2392 12493915 10.1126/science.1077650 1:CAS:528:DC%2BD38Xps1Sju70%3D (Pubitemid 36014212)
    • (2002) Science , vol.298 , Issue.5602 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 90
    • 33745557847 scopus 로고    scopus 로고
    • Nucleocytosolic Acetyl-Coenzyme A Synthetase Is Required for Histone Acetylation and Global Transcription
    • DOI 10.1016/j.molcel.2006.05.040, PII S1097276506003844
    • H Takahashi JM McCaffery RA Irizarry JD Boeke 2006 Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription Mol Cell 23 207 217 16857587 10.1016/j.molcel.2006.05.040 1:CAS:528:DC%2BD28XotVCjurk%3D (Pubitemid 44081880)
    • (2006) Molecular Cell , vol.23 , Issue.2 , pp. 207-217
    • Takahashi, H.1    McCaffery, J.M.2    Irizarry, R.A.3    Boeke, J.D.4
  • 91
    • 66249105703 scopus 로고    scopus 로고
    • ATP-citrate lyase links cellular metabolism to histone acetylation
    • 19461003 10.1126/science.1164097 1:CAS:528:DC%2BD1MXmtVKlsb8%3D
    • KE Wellen G Hatzivassiliou UM Sachdeva TV Bui JR Cross CB Thompson 2009 ATP-citrate lyase links cellular metabolism to histone acetylation Science 324 1076 1080 19461003 10.1126/science.1164097 1:CAS:528:DC%2BD1MXmtVKlsb8%3D
    • (2009) Science , vol.324 , pp. 1076-1080
    • Wellen, K.E.1    Hatzivassiliou, G.2    Sachdeva, U.M.3    Bui, T.V.4    Cross, J.R.5    Thompson, C.B.6
  • 93
    • 67651183861 scopus 로고    scopus 로고
    • A glycolytic burst drives glucose induction of global histone acetylation by picNuA4 and SAGA
    • 19406923 10.1093/nar/gkp270 1:CAS:528:DC%2BD1MXovVektLs%3D
    • RM Friis BP Wu SN Reinke DJ Hockman BD Sykes MC Schultz 2009 A glycolytic burst drives glucose induction of global histone acetylation by picNuA4 and SAGA Nucleic Acids Res 37 3969 3980 19406923 10.1093/nar/gkp270 1:CAS:528:DC%2BD1MXovVektLs%3D
    • (2009) Nucleic Acids Res , vol.37 , pp. 3969-3980
    • Friis, R.M.1    Wu, B.P.2    Reinke, S.N.3    Hockman, D.J.4    Sykes, B.D.5    Schultz, M.C.6
  • 94
    • 0036728197 scopus 로고    scopus 로고
    • TAGging the target for damage control
    • DOI 10.1038/nsb0902-638
    • Y Yan S Harper DW Speicher R Marmorstein 2002 The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate Nat Struct Biol 9 862 869 12368900 10.1038/nsb0902-638 1:CAS:528: DC%2BD38XosFCjsLk%3D (Pubitemid 34977291)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 638-640
    • Yan, K.S.1    Zhou, M.-M.2
  • 95
    • 33846374117 scopus 로고    scopus 로고
    • Catalytic mechanism of a MYST family histone acetyltransferase
    • DOI 10.1021/bi602513x
    • CE Berndsen BN Albaugh S Tan JM Denu 2007 Catalytic mechanism of a MYST family histone acetyltransferase Biochemistry 46 623 629 17223684 10.1021/bi602513x 1:CAS:528:DC%2BD28XhtlCgs7zM (Pubitemid 46133582)
    • (2007) Biochemistry , vol.46 , Issue.3 , pp. 623-629
    • Berndsen, C.E.1    Albaugh, B.N.2    Tan, S.3    Denu, J.M.4
  • 96
    • 77951217683 scopus 로고    scopus 로고
    • SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60
    • 20100829 10.1074/jbc.M109.087585 1:CAS:528:DC%2BC3cXktFGlt74%3D
    • J Wang J Chen 2010 SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60 J Biol Chem 285 11458 11464 20100829 10.1074/jbc.M109.087585 1:CAS:528:DC%2BC3cXktFGlt74%3D
    • (2010) J Biol Chem , vol.285 , pp. 11458-11464
    • Wang, J.1    Chen, J.2
  • 97
    • 34249779851 scopus 로고    scopus 로고
    • Functions of myst family histone acetyltransferases and their link to disease
    • 17484133
    • N Avvakumov J Cote 2007 Functions of myst family histone acetyltransferases and their link to disease Subcell Biochem 41 295 317 17484133
    • (2007) Subcell Biochem , vol.41 , pp. 295-317
    • Avvakumov, N.1    Cote, J.2


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