메뉴 건너뛰기




Volumn 33, Issue 29, 2014, Pages 3764-3775

Sirtuins in stress response: Guardians of the genome

Author keywords

epigenetics; genome stability; SIRT1 7; Sirtuins; stress response

Indexed keywords

DNA; SIRTUIN; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; SIRTUIN 6; SIRTUIN 7;

EID: 84904609077     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2013.344     Document Type: Review
Times cited : (89)

References (181)
  • 2
    • 33644846842 scopus 로고    scopus 로고
    • Genetic instability in human tumors
    • Raptis S, Bapat B. Genetic instability in human tumors. EXS 2006; 96: 303-320
    • (2006) EXS , vol.96 , pp. 303-320
    • Raptis, S.1    Bapat, B.2
  • 3
    • 84890313801 scopus 로고    scopus 로고
    • Chromosomal instability (CIN) what it is and why it is crucial to cancer evolution
    • (e-pub ahead of print 19 April 2013)
    • Heng HH, Bremer SW, Stevens JB, Horne SD, Liu G, Abdallah BY.et al.. Chromosomal instability (CIN): what it is and why it is crucial to cancer evolution. Cancer Metastasis Rev. (e-pub ahead of print 19 April 2013).
    • Cancer Metastasis Rev
    • Heng, H.H.1    Bremer, S.W.2    Stevens, J.B.3    Horne, S.D.4    Liu, G.5    Abdallah, B.Y.6
  • 4
    • 34547875773 scopus 로고    scopus 로고
    • Sirtuins: Critical regulators at the crossroads between cancer and aging
    • Saunders LR, Verdin E. Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene 2007; 26: 5489-5504
    • (2007) Oncogene , vol.26 , pp. 5489-5504
    • Saunders, L.R.1    Verdin, E.2
  • 6
    • 0018564390 scopus 로고
    • A suppressor of mating-type locus mutations in Saccharomyces cerevisiae: Evidence for and identification of cryptic mating-type loci
    • Rine J, Strathern JN, Hicks JB, Herskowitz I. A suppressor of mating-type locus mutations in Saccharomyces cerevisiae: evidence for and identification of cryptic mating-type loci. Genetics 1979; 93: 877-901
    • (1979) Genetics , vol.93 , pp. 877-901
    • Rine, J.1    Strathern, J.N.2    Hicks, J.B.3    Herskowitz, I.4
  • 7
    • 84887491976 scopus 로고    scopus 로고
    • The diversity of histone versus nonhistone sirtuin substrates
    • e-pub ahead of print 9 April 2013; doi 10.1177 1947601913483767)
    • Martinez-Redondo P, Vaquero A. The diversity of histone versus nonhistone sirtuin substrates. Genes Cancer (e-pub ahead of print 9 April 2013; doi:10.1177 1947601913483767).
    • Genes Cancer
    • Martinez-Redondo, P.1    Vaquero, A.2
  • 8
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye RA. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 2000; 273: 793-798
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 10
    • 81055122671 scopus 로고    scopus 로고
    • Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
    • Du J, Zhou Y, Su X, Yu JJ, Khan S, Jiang H.et al.. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science 2011; 334: 806-809
    • (2011) Science , vol.334 , pp. 806-809
    • Du, J.1    Zhou, Y.2    Su, X.3    Yu, J.J.4    Khan, S.5    Jiang, H.6
  • 11
    • 84875881601 scopus 로고    scopus 로고
    • SIRT6 regulates TNFa secretion through hydrolysis of long-chain fatty acyl lysine
    • Jiang H, Khan S, Wang Y, Charron G, He B, Sebastian C.et al.. SIRT6 regulates TNFa secretion through hydrolysis of long-chain fatty acyl lysine. Nature 2013; 496: 110-113
    • (2013) Nature , vol.496 , pp. 110-113
    • Jiang, H.1    Khan, S.2    Wang, Y.3    Charron, G.4    He, B.5    Sebastian, C.6
  • 12
    • 70349138701 scopus 로고    scopus 로고
    • The conserved role of sirtuins in chromatin regulation
    • Vaquero A. The conserved role of sirtuins in chromatin regulation. Int J Dev Biol 2009; 53: 303-322
    • (2009) Int J Dev Biol , vol.53 , pp. 303-322
    • Vaquero, A.1
  • 13
    • 34547875013 scopus 로고    scopus 로고
    • NAD-dependent deacetylation of H4 lysine 16 by class III HDACs
    • Vaquero A, Sternglanz R, Reinberg D. NAD-dependent deacetylation of H4 lysine 16 by class III HDACs. Oncogene 2007; 26: 5505-5520
    • (2007) Oncogene , vol.26 , pp. 5505-5520
    • Vaquero, A.1    Sternglanz, R.2    Reinberg, D.3
  • 14
    • 80054782483 scopus 로고    scopus 로고
    • The dual role of sirtuins in cancer
    • Bosch-Presegue L, Vaquero A. The dual role of sirtuins in cancer. Genes Cancer 2011; 2: 648-662
    • (2011) Genes Cancer , vol.2 , pp. 648-662
    • Bosch-Presegue, L.1    Vaquero, A.2
  • 15
    • 53149137486 scopus 로고    scopus 로고
    • Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice
    • Wang RH, Sengupta K, Li C, Kim HS, Cao L, Xiao C.et al.. Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice. Cancer Cell 2008; 14: 312-323
    • (2008) Cancer Cell , vol.14 , pp. 312-323
    • Wang, R.H.1    Sengupta, K.2    Li, C.3    Kim, H.S.4    Cao, L.5    Xiao, C.6
  • 16
    • 80054769188 scopus 로고    scopus 로고
    • SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity
    • Kim HS, Vassilopoulos A, Wang RH, Lahusen T, Xiao Z, Xu X.et al.. SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity. Cancer Cell 2011; 20: 487-499
    • (2011) Cancer Cell , vol.20 , pp. 487-499
    • Kim, H.S.1    Vassilopoulos, A.2    Wang, R.H.3    Lahusen, T.4    Xiao, Z.5    Xu, X.6
  • 17
    • 84875309392 scopus 로고    scopus 로고
    • The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation
    • Serrano L, Martinez-Redondo P, Marazuela-Duque A, Vazquez BN, Dooley SJ, Voigt P.et al.. The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation. Genes Dev 2013; 27: 639-653
    • (2013) Genes Dev , vol.27 , pp. 639-653
    • Serrano, L.1    Martinez-Redondo, P.2    Marazuela-Duque, A.3    Vazquez, B.N.4    Dooley, S.J.5    Voigt, P.6
  • 18
    • 74049094817 scopus 로고    scopus 로고
    • SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress
    • Kim HS, Patel K, Muldoon-Jacobs K, Bisht KS, Aykin-Burns N, Pennington JD.et al.. SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress. Cancer Cell 2010; 17: 41-52
    • (2010) Cancer Cell , vol.17 , pp. 41-52
    • Kim, H.S.1    Patel, K.2    Muldoon-Jacobs, K.3    Bisht, K.S.4    Aykin-Burns, N.5    Pennington, J.D.6
  • 19
    • 84876359638 scopus 로고    scopus 로고
    • SIRT4 has tumorsuppressive activity and regulates the cellular metabolic response to DNA damage by inhibiting mitochondrial glutamine metabolism
    • Jeong SM, Xiao C, Finley LW, Lahusen T, Souza AL, Pierce K.et al.. SIRT4 has tumorsuppressive activity and regulates the cellular metabolic response to DNA damage by inhibiting mitochondrial glutamine metabolism. Cancer Cell 2013; 23: 450-463
    • (2013) Cancer Cell , vol.23 , pp. 450-463
    • Jeong, S.M.1    Xiao, C.2    Finley, L.W.3    Lahusen, T.4    Souza, A.L.5    Pierce, K.6
  • 20
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky R, Chua KF, Lombard DB, Pang WW, Fischer MR, Gellon L.et al.. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 2006; 124: 315-329
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1    Chua, K.F.2    Lombard, D.B.3    Pang, W.W.4    Fischer, M.R.5    Gellon, L.6
  • 22
    • 41349090663 scopus 로고    scopus 로고
    • SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
    • Michishita E, McCord RA, Berber E, Kioi M, Padilla-Nash H, Damian M.et al.. SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature 2008; 452: 492-496
    • (2008) Nature , vol.452 , pp. 492-496
    • Michishita, E.1    McCord, R.A.2    Berber, E.3    Kioi, M.4    Padilla-Nash, H.5    Damian, M.6
  • 23
    • 12344296753 scopus 로고    scopus 로고
    • Heterochromatin-many flavours, common themes
    • Craig JM. Heterochromatin-many flavours, common themes. Bioessays 2005; 27: 17-28
    • (2005) Bioessays , vol.27 , pp. 17-28
    • Craig, J.M.1
  • 24
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science 2001; 293: 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 25
    • 0242348752 scopus 로고    scopus 로고
    • Histone lysine methylation: A signature for chromatin function
    • Sims 3rd RJ, Nishioka K, Reinberg D. Histone lysine methylation: a signature for chromatin function. Trends Genet 2003; 19: 629-639
    • (2003) Trends Genet , vol.19 , pp. 629-639
    • Sims III, R.J.1    Nishioka, K.2    Reinberg, D.3
  • 26
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai S, Chen D, Su F, Shiloh A.et al.. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 2001; 107: 137-148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6
  • 28
    • 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. Acetylation of TAF(I)68, a subunit of TIF-IB/ SL1, activates RNA polymerase I transcription. EMBO J 2001; 20: 1353-1362
    • (2001) EMBO J , vol.20 , pp. 1353-1362
    • Muth, V.1    Nadaud, S.2    Grummt, I.3    Voit, R.4
  • 29
    • 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, Kashiwaya Y.et al.. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell 2003; 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    Kashiwaya, Y.6
  • 30
    • 0242322010 scopus 로고    scopus 로고
    • Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression
    • Senawong T, Peterson VJ, Avram D, Shepherd DM, Frye RA, Minucci S.et al.. Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression. J Biol Chem 2003; 278: 43041-43050
    • (2003) J Biol Chem , vol.278 , pp. 43041-43050
    • Senawong, T.1    Peterson, V.J.2    Avram, D.3    Shepherd, D.M.4    Frye, R.A.5    Minucci, S.6
  • 31
    • 0037474507 scopus 로고    scopus 로고
    • Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1-And HEY2-mediated transcriptional repression
    • Takata T, Ishikawa F. Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1-And HEY2-mediated transcriptional repression. Biochem Biophys Res Commun 2003; 301: 250-257
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 250-257
    • Takata, T.1    Ishikawa, F.2
  • 32
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell 2004; 16: 93-105
    • (2004) Mol Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 33
    • 1942502862 scopus 로고    scopus 로고
    • Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3
    • Kuzmichev A, Jenuwein T, Tempst P, Reinberg D. Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3. Mol Cell 2004; 14: 183-193
    • (2004) Mol Cell , vol.14 , pp. 183-193
    • Kuzmichev, A.1    Jenuwein, T.2    Tempst, P.3    Reinberg, D.4
  • 34
    • 36248954501 scopus 로고    scopus 로고
    • SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation
    • Vaquero A, Scher M, Erdjument-Bromage H, Tempst P, Serrano L, Reinberg D. SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation. Nature 2007; 450: 440-444
    • (2007) Nature , vol.450 , pp. 440-444
    • Vaquero, A.1    Scher, M.2    Erdjument-Bromage, H.3    Tempst, P.4    Serrano, L.5    Reinberg, D.6
  • 35
    • 0042671307 scopus 로고    scopus 로고
    • Epigenetic silencing of RNA polymerase i transcription
    • Grummt I, Pikaard CS. Epigenetic silencing of RNA polymerase I transcription. Nat Rev Mol Cell Biol 2003; 4: 641-649
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 641-649
    • Grummt, I.1    Pikaard, C.S.2
  • 36
    • 33846549173 scopus 로고    scopus 로고
    • A housekeeper with power of attorney: The rRNA genes in ribosome biogenesis
    • Moss T, Langlois F, Gagnon-Kugler T, Stefanovsky V. A housekeeper with power of attorney: the rRNA genes in ribosome biogenesis. Cell Mol Life Sci 2007; 64: 29-49
    • (2007) Cell Mol Life Sci , vol.64 , pp. 29-49
    • Moss, T.1    Langlois, F.2    Gagnon-Kugler, T.3    Stefanovsky, V.4
  • 38
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 2000; 403: 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 39
    • 33744466971 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase i transcription
    • Ford E, Voit R, Liszt G, Magin C, Grummt I, Guarente L. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev 2006; 20: 1075-1080
    • (2006) Genes Dev , vol.20 , pp. 1075-1080
    • Ford, E.1    Voit, R.2    Liszt, G.3    Magin, C.4    Grummt, I.5    Guarente, L.6
  • 41
  • 42
    • 13844315463 scopus 로고    scopus 로고
    • Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation
    • Kuzmichev A, Margueron R, Vaquero A, Preissner TS, Scher M, Kirmizis A.et al.. Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation. Proc Natl Acad Sci USA 2005; 102: 1859-1864
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1859-1864
    • Kuzmichev, A.1    Margueron, R.2    Vaquero, A.3    Preissner, T.S.4    Scher, M.5    Kirmizis, A.6
  • 43
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
    • Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev 2002; 16: 2893-2905
    • (2002) Genes Dev , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 44
    • 84856466661 scopus 로고    scopus 로고
    • The role of EZH2 in tumour progression
    • Chang CJ, Hung MC. The role of EZH2 in tumour progression. Br J Cancer 2012; 106: 243-247
    • (2012) Br J Cancer , vol.106 , pp. 243-247
    • Chang, C.J.1    Hung, M.C.2
  • 45
    • 79958037576 scopus 로고    scopus 로고
    • A SIRT1-LSD1 corepressor complex regulates Notch target gene expression and development
    • Mulligan P, Yang F, Di Stefano L, Ji JY, Ouyang J, Nishikawa JL.et al.. A SIRT1-LSD1 corepressor complex regulates Notch target gene expression and development. Mol Cell 2011; 42: 689-699
    • (2011) Mol Cell , vol.42 , pp. 689-699
    • Mulligan, P.1    Yang, F.2    Di Stefano, L.3    Ji, J.Y.4    Ouyang, J.5    Nishikawa, J.L.6
  • 47
    • 50849104230 scopus 로고    scopus 로고
    • Notch tumor suppressor function
    • Dotto GP. Notch tumor suppressor function. Oncogene 2008; 27: 5115-5123
    • (2008) Oncogene , vol.27 , pp. 5115-5123
    • Dotto, G.P.1
  • 48
    • 58149090925 scopus 로고    scopus 로고
    • SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span
    • Kawahara TL, Michishita E, Adler AS, Damian M, Berber E, Lin M.et al.. SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span. Cell 2009; 136: 62-74
    • (2009) Cell , vol.136 , pp. 62-74
    • Kawahara, T.L.1    Michishita, E.2    Adler, A.S.3    Damian, M.4    Berber, E.5    Lin, M.6
  • 49
    • 74549142287 scopus 로고    scopus 로고
    • The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1alpha
    • Zhong L, DUrso A, Toiber D, Sebastian C, Henry RE, Vadysirisack DD.et al.. The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1alpha. Cell 2010; 140: 280-293
    • (2010) Cell , vol.140 , pp. 280-293
    • Zhong, L.1    Durso, A.2    Toiber, D.3    Sebastian, C.4    Henry, R.E.5    Vadysirisack, D.D.6
  • 50
    • 84870874690 scopus 로고    scopus 로고
    • The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism
    • Sebastian C, Zwaans BM, Silberman DM, Gymrek M, Goren A, Zhong L.et al.. The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism. Cell 2012; 151: 1185-1199
    • (2012) Cell , vol.151 , pp. 1185-1199
    • Sebastian, C.1    Zwaans, B.M.2    Silberman, D.M.3    Gymrek, M.4    Goren, A.5    Zhong, L.6
  • 51
    • 84869082071 scopus 로고    scopus 로고
    • Liver cancer initiation is controlled by AP-1 through SIRT6-dependent inhibition of survivin
    • Min L, Ji Y, Bakiri L, Qiu Z, Cen J, Chen X.et al.. Liver cancer initiation is controlled by AP-1 through SIRT6-dependent inhibition of survivin. Nat Cell Biol 2013; 14: 1203-1211
    • (2013) Nat Cell Biol , vol.14 , pp. 1203-1211
    • Min, L.1    Ji, Y.2    Bakiri, L.3    Qiu, Z.4    Cen, J.5    Chen, X.6
  • 52
    • 84871852995 scopus 로고    scopus 로고
    • SIRT3 functions in the nucleus in the control of stress-related gene expression
    • Iwahara T, Bonasio R, Narendra V, Reinberg D. SIRT3 functions in the nucleus in the control of stress-related gene expression. Mol Cell Biol 2012; 32: 5022-5034
    • (2012) Mol Cell Biol , vol.32 , pp. 5022-5034
    • Iwahara, T.1    Bonasio, R.2    Narendra, V.3    Reinberg, D.4
  • 53
    • 34247271282 scopus 로고    scopus 로고
    • SirT3 is a nuclear NAD-dependent histone deacetylase that translocates to the mitochondria upon cellular stress
    • Scher MB, Vaquero A, Reinberg D. SirT3 is a nuclear NAD-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev 2007; 21: 920-928
    • (2007) Genes Dev , vol.21 , pp. 920-928
    • Scher, M.B.1    Vaquero, A.2    Reinberg, D.3
  • 54
    • 17944380227 scopus 로고    scopus 로고
    • Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability
    • Peters AH, OCarroll D, Scherthan H, Mechtler K, Sauer S, Schofer C.et al.. Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability. Cell 2001; 107: 323-337
    • (2001) Cell , vol.107 , pp. 323-337
    • Peters, A.H.1    Ocarroll, D.2    Scherthan, H.3    Mechtler, K.4    Sauer, S.5    Schofer, C.6
  • 55
    • 0347988045 scopus 로고    scopus 로고
    • Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases
    • Garcia-Cao M, OSullivan R, Peters AH, Jenuwein T, Blasco MA. Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases. Nat Genet 2004; 36: 94-99
    • (2004) Nat Genet , vol.36 , pp. 94-99
    • Garcia-Cao, M.1    Osullivan, R.2    Peters, A.H.3    Jenuwein, T.4    Blasco, M.A.5
  • 57
    • 0025279931 scopus 로고
    • Telomeres shorten during ageing of human fibroblasts
    • Harley CB, Futcher AB, Greider CW. Telomeres shorten during ageing of human fibroblasts. Nature 1990; 345: 458-460
    • (1990) Nature , vol.345 , pp. 458-460
    • Harley, C.B.1    Futcher, A.B.2    Greider, C.W.3
  • 58
    • 0022402513 scopus 로고
    • Identification of a specific telomere terminal transferase activity in Tetrahymena extracts
    • Greider CW, Blackburn EH. Identification of a specific telomere terminal transferase activity in Tetrahymena extracts. Cell 1985; 43: 405-413
    • (1985) Cell , vol.43 , pp. 405-413
    • Greider, C.W.1    Blackburn, E.H.2
  • 59
    • 0024325562 scopus 로고
    • The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes TTAGGG repeats
    • Morin GB. The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes TTAGGG repeats. Cell 1989; 59: 521-529
    • (1989) Cell , vol.59 , pp. 521-529
    • Morin, G.B.1
  • 60
    • 0030931491 scopus 로고    scopus 로고
    • Telomere shortening and tumor formation by mouse cells lacking telomerase RNA
    • Blasco MA, Lee HW, Hande MP, Samper E, Lansdorp PM, DePinho RA.et al.. Telomere shortening and tumor formation by mouse cells lacking telomerase RNA. Cell 1997; 91: 25-34
    • (1997) Cell , vol.91 , pp. 25-34
    • Blasco, M.A.1    Lee, H.W.2    Hande, M.P.3    Samper, E.4    Lansdorp, P.M.5    Depinho, R.A.6
  • 62
    • 0030668722 scopus 로고    scopus 로고
    • Human telomerase contains evolutionarily conserved catalytic and structural subunits
    • Harrington L, Zhou W, McPhail T, Oulton R, Yeung DS, Mar V.et al.. Human telomerase contains evolutionarily conserved catalytic and structural subunits. Genes Dev 1997; 11: 3109-3115
    • (1997) Genes Dev , vol.11 , pp. 3109-3115
    • Harrington, L.1    Zhou, W.2    McPhail, T.3    Oulton, R.4    Yeung, D.S.5    Mar, V.6
  • 63
    • 0030745448 scopus 로고    scopus 로고
    • HEST2, the putative human telomerase catalytic subunit gene, is up-regulated in tumor cells and during immortalization
    • Meyerson M, Counter CM, Eaton EN, Ellisen LW, Steiner P, Caddle SD.et al.. hEST2, the putative human telomerase catalytic subunit gene, is up-regulated in tumor cells and during immortalization. Cell 1997; 90: 785-795
    • (1997) Cell , vol.90 , pp. 785-795
    • Meyerson, M.1    Counter, C.M.2    Eaton, E.N.3    Ellisen, L.W.4    Steiner, P.5    Caddle, S.D.6
  • 66
    • 0031027618 scopus 로고    scopus 로고
    • Control of telomere length by the human telomeric protein TRF1
    • van Steensel B, de Lange T. Control of telomere length by the human telomeric protein TRF1. Nature 1997; 385: 740-743
    • (1997) Nature , vol.385 , pp. 740-743
    • Van Steensel, B.1    De Lange, T.2
  • 67
    • 0028004378 scopus 로고
    • Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1
    • Moretti P, Freeman K, Coodly L, Shore D. Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1. Genes Dev 1994; 8: 2257-2269
    • (1994) Genes Dev , vol.8 , pp. 2257-2269
    • Moretti, P.1    Freeman, K.2    Coodly, L.3    Shore, D.4
  • 68
    • 0033539095 scopus 로고    scopus 로고
    • DNA damage triggers disruption of telomeric silencing and Mec1p-dependent relocation of Sir3p
    • McAinsh AD, Scott-Drew S, Murray JA, Jackson SP. DNA damage triggers disruption of telomeric silencing and Mec1p-dependent relocation of Sir3p. Curr Biol 1999; 9: 963-966
    • (1999) Curr Biol , vol.9 , pp. 963-966
    • McAinsh, A.D.1    Scott-Drew, S.2    Murray, J.A.3    Jackson, S.P.4
  • 69
    • 0033612189 scopus 로고    scopus 로고
    • MEC1-dependent redistribution of the Sir3 silencing protein from telomeres to DNA double-strand breaks
    • Mills KD, Sinclair DA, Guarente L. MEC1-dependent redistribution of the Sir3 silencing protein from telomeres to DNA double-strand breaks. Cell 1999; 97: 609-620
    • (1999) Cell , vol.97 , pp. 609-620
    • Mills, K.D.1    Sinclair, D.A.2    Guarente, L.3
  • 70
    • 41649094992 scopus 로고    scopus 로고
    • SIRT1 acts as a nutrient-sensitive growth suppressor and its loss is associated with increased AMPK and telomerase activity
    • Narala SR, Allsopp RC, Wells TB, Zhang G, Prasad P, Coussens MJ.et al.. SIRT1 acts as a nutrient-sensitive growth suppressor and its loss is associated with increased AMPK and telomerase activity. Mol Biol Cell 2008; 19: 1210-1219
    • (2008) Mol Biol Cell , vol.19 , pp. 1210-1219
    • Narala, S.R.1    Allsopp, R.C.2    Wells, T.B.3    Zhang, G.4    Prasad, P.5    Coussens, M.J.6
  • 72
    • 79958787784 scopus 로고    scopus 로고
    • Sirtuin 1 is upregulated in a subset of hepatocellular carcinomas where it is essential for telomere maintenance and tumor cell growth
    • Chen J, Zhang B, Wong N, Lo AW, To KF, Chan AW.et al.. Sirtuin 1 is upregulated in a subset of hepatocellular carcinomas where it is essential for telomere maintenance and tumor cell growth. Cancer Res 2012; 71: 4138-4149
    • (2012) Cancer Res , vol.71 , pp. 4138-4149
    • Chen, J.1    Zhang, B.2    Wong, N.3    Lo, A.W.4    To, K.F.5    Chan, A.W.6
  • 73
    • 67650677845 scopus 로고    scopus 로고
    • Resveratrol induces senescence-like growth inhibition of U-2 OS cells associated with the instability of telomeric DNA and upregulation of BRCA1
    • Rusin M, Zajkowicz A, Butkiewicz D. Resveratrol induces senescence-like growth inhibition of U-2 OS cells associated with the instability of telomeric DNA and upregulation of BRCA1. Mech Ageing Dev 2009; 130: 528-537
    • (2009) Mech Ageing Dev , vol.130 , pp. 528-537
    • Rusin, M.1    Zajkowicz, A.2    Butkiewicz, D.3
  • 75
    • 79960005365 scopus 로고    scopus 로고
    • Limited role of Sirt1 in cancer protection by dietary restriction
    • Herranz D, Iglesias G, Munoz-Martin M, Serrano M. Limited role of Sirt1 in cancer protection by dietary restriction. Cell Cycle 2011; 10: 2215-2217
    • (2011) Cell Cycle , vol.10 , pp. 2215-2217
    • Herranz, D.1    Iglesias, G.2    Munoz-Martin, M.3    Serrano, M.4
  • 76
    • 69249221533 scopus 로고    scopus 로고
    • Cell cycledependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6
    • Michishita E, McCord RA, Boxer LD, Barber MF, Hong T, Gozani O.et al.. Cell cycledependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6. Cell Cycle 2009; 8: 2664-2666
    • (2009) Cell Cycle , vol.8 , pp. 2664-2666
    • Michishita, E.1    McCord, R.A.2    Boxer, L.D.3    Barber, M.F.4    Hong, T.5    Gozani, O.6
  • 77
    • 69249229772 scopus 로고    scopus 로고
    • The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability
    • Yang B, Zwaans BM, Eckersdorff M, Lombard DB. The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability. Cell Cycle 2009; 8: 2662-2663
    • (2009) Cell Cycle , vol.8 , pp. 2662-2663
    • Yang, B.1    Zwaans, B.M.2    Eckersdorff, M.3    Lombard, D.B.4
  • 78
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das C, Lucia MS, Hansen KC, Tyler JK. CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 2009; 459: 113-117
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 79
    • 80052399287 scopus 로고    scopus 로고
    • SIRT6 is required for maintenance of telomere position effect in human cells
    • Tennen RI, Bua DJ, Wright WE, Chua KF. SIRT6 is required for maintenance of telomere position effect in human cells. Nat Commun 2011; 2: 433
    • (2011) Nat Commun , vol.2 , pp. 433
    • Tennen, R.I.1    Bua, D.J.2    Wright, W.E.3    Chua, K.F.4
  • 81
    • 39149122568 scopus 로고    scopus 로고
    • Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis
    • North BJ, Verdin E. Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis. PLoS One 2007; 2: e784
    • (2007) PLoS One , vol.2
    • North, B.J.1    Verdin, E.2
  • 82
    • 33646550204 scopus 로고    scopus 로고
    • SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis
    • Vaquero A, Scher MB, Lee DH, Sutton A, Cheng HL, Alt FW.et al.. SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev 2006; 20: 1256-1261
    • (2006) Genes Dev , vol.20 , pp. 1256-1261
    • Vaquero, A.1    Scher, M.B.2    Lee, D.H.3    Sutton, A.4    Cheng, H.L.5    Alt, F.W.6
  • 83
    • 0037066738 scopus 로고    scopus 로고
    • Conserved enzymatic production and biological effect of O-Acetyl-ADP-ribose by silent information regulator 2-like NAD-dependent deacetylases
    • Borra MT, ONeill FJ, Jackson MD, Marshall B, Verdin E, Foltz KR.et al.. Conserved enzymatic production and biological effect of O-Acetyl-ADP-ribose by silent information regulator 2-like NAD-dependent deacetylases. J Biol Chem 2002; 277: 12632-12641
    • (2002) J Biol Chem , vol.277 , pp. 12632-12641
    • Borra, M.T.1    Oneill, F.J.2    Jackson, M.D.3    Marshall, B.4    Verdin, E.5    Foltz, K.R.6
  • 84
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • Dryden SC, Nahhas FA, Nowak JE, Goustin AS, Tainsky MA. Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol 2003; 23: 3173-3185
    • (2003) Mol Cell Biol , vol.23 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.S.4    Tainsky, M.A.5
  • 85
    • 3142548829 scopus 로고    scopus 로고
    • Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10
    • Bae NS, Swanson MJ, Vassilev A, Howard BH. Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10. J Biochem 2004; 135: 695-700
    • (2004) J Biochem , vol.135 , pp. 695-700
    • Bae, N.S.1    Swanson, M.J.2    Vassilev, A.3    Howard, B.H.4
  • 86
    • 8844248619 scopus 로고    scopus 로고
    • Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage
    • Sanders SL, Portoso M, Mata J, Bahler J, Allshire RC, Kouzarides T. Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. Cell 2004; 119: 603-614
    • (2004) Cell , vol.119 , pp. 603-614
    • Sanders, S.L.1    Portoso, M.2    Mata, J.3    Bahler, J.4    Allshire, R.C.5    Kouzarides, T.6
  • 87
    • 2642542643 scopus 로고    scopus 로고
    • A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin
    • Schotta G, Lachner M, Sarma K, Ebert A, Sengupta R, Reuter G.et al.. A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev 2004; 18: 1251-1262
    • (2004) Genes Dev , vol.18 , pp. 1251-1262
    • Schotta, G.1    Lachner, M.2    Sarma, K.3    Ebert, A.4    Sengupta, R.5    Reuter, G.6
  • 88
    • 48749102722 scopus 로고    scopus 로고
    • A chromatinwide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse
    • Schotta G, Sengupta R, Kubicek S, Malin S, Kauer M, Callen E.et al.. A chromatinwide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse. Genes Dev 2008; 22: 2048-2061
    • (2008) Genes Dev , vol.22 , pp. 2048-2061
    • Schotta, G.1    Sengupta, R.2    Kubicek, S.3    Malin, S.4    Kauer, M.5    Callen, E.6
  • 89
    • 13844269327 scopus 로고    scopus 로고
    • PR-Set7-dependent methylation of histone H4 Lys 20 functions in repression of gene expression and is essential for mitosis
    • Karachentsev D, Sarma K, Reinberg D, Steward R. PR-Set7-dependent methylation of histone H4 Lys 20 functions in repression of gene expression and is essential for mitosis. Genes Dev 2005; 19: 431-435
    • (2005) Genes Dev , vol.19 , pp. 431-435
    • Karachentsev, D.1    Sarma, K.2    Reinberg, D.3    Steward, R.4
  • 90
    • 64749106929 scopus 로고    scopus 로고
    • Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development
    • Oda H, Okamoto I, Murphy N, Chu J, Price SM, Shen MM.et al.. Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development. Mol Cell Biol 2009; 29: 2278-2295
    • (2009) Mol Cell Biol , vol.29 , pp. 2278-2295
    • Oda, H.1    Okamoto, I.2    Murphy, N.3    Chu, J.4    Price, S.M.5    Shen, M.M.6
  • 91
    • 34547098165 scopus 로고    scopus 로고
    • Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation
    • North BJ, Verdin E. Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation. J Biol Chem 2007; 282: 19546-19555
    • (2007) J Biol Chem , vol.282 , pp. 19546-19555
    • North, B.J.1    Verdin, E.2
  • 92
    • 78349272437 scopus 로고    scopus 로고
    • Dynamic regulation of the PR-Set7 histone methyltransferase is required for normal cell cycle progression
    • Wu S, Wang W, Kong X, Congdon LM, Yokomori K, Kirschner MW.et al.. Dynamic regulation of the PR-Set7 histone methyltransferase is required for normal cell cycle progression. Genes Dev 2010; 24: 2531-2542
    • (2010) Genes Dev , vol.24 , pp. 2531-2542
    • Wu, S.1    Wang, W.2    Kong, X.3    Congdon, L.M.4    Yokomori, K.5    Kirschner, M.W.6
  • 93
    • 0141744707 scopus 로고    scopus 로고
    • Histone hyperacetylation in mitosis prevents sister chromatid separation and produces chromosome segregation defects
    • Cimini D, Mattiuzzo M, Torosantucci L, Degrassi F. Histone hyperacetylation in mitosis prevents sister chromatid separation and produces chromosome segregation defects. Mol Biol Cell 2003; 14: 3821-3833
    • (2003) Mol Biol Cell , vol.14 , pp. 3821-3833
    • Cimini, D.1    Mattiuzzo, M.2    Torosantucci, L.3    Degrassi, F.4
  • 94
    • 33646020705 scopus 로고    scopus 로고
    • Histone deacetylase activity is necessary for chromosome condensation during meiotic maturation in Xenopus laevis
    • Magnaghi-Jaulin L, Jaulin C. Histone deacetylase activity is necessary for chromosome condensation during meiotic maturation in Xenopus laevis. Chromosome Res 2006; 14: 319-332
    • (2006) Chromosome Res , vol.14 , pp. 319-332
    • Magnaghi-Jaulin, L.1    Jaulin, C.2
  • 95
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: Codified crosstalk with other posttranslational modifications
    • Yang XJ, Seto E. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol Cell 2008; 31: 449-461
    • (2008) Mol Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 96
    • 33847053144 scopus 로고    scopus 로고
    • SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress
    • Inoue T, Hiratsuka M, Osaki M, Yamada H, Kishimoto I, Yamaguchi S.et al.. SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress. Oncogene 2007; 26: 945-957
    • (2007) Oncogene , vol.26 , pp. 945-957
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Yamada, H.4    Kishimoto, I.5    Yamaguchi, S.6
  • 97
    • 34248151365 scopus 로고    scopus 로고
    • The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation
    • Inoue T, Hiratsuka M, Osaki M, Oshimura M. The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation. Cell Cycle 2007; 6: 1011-1018
    • (2007) Cell Cycle , vol.6 , pp. 1011-1018
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Oshimura, M.4
  • 98
    • 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. The human Sir2 ortholog, SIRT2, is an NAD-dependent tubulin deacetylase. Mol Cell 2003; 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
  • 99
    • 33748331132 scopus 로고    scopus 로고
    • Progressive loss of SIRT1 with cell cycle withdrawal
    • Sasaki T, Maier B, Bartke A, Scrable H. Progressive loss of SIRT1 with cell cycle withdrawal. Aging Cell 2006; 5: 413-422
    • (2006) Aging Cell , vol.5 , pp. 413-422
    • Sasaki, T.1    Maier, B.2    Bartke, A.3    Scrable, H.4
  • 100
    • 79960466223 scopus 로고    scopus 로고
    • Human SIRT1 associates with mitotic chromatin and contributes to chromosomal condensation
    • Fatoba ST, Okorokov AL. Human SIRT1 associates with mitotic chromatin and contributes to chromosomal condensation. Cell Cycle 2011; 10: 2317-2322
    • (2011) Cell Cycle , vol.10 , pp. 2317-2322
    • Fatoba, S.T.1    Okorokov, A.L.2
  • 101
    • 35748949600 scopus 로고    scopus 로고
    • Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1
    • Wong S, Weber JD. Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1. Biochem J 2007; 407: 451-460
    • (2007) Biochem J , vol.407 , pp. 451-460
    • Wong, S.1    Weber, J.D.2
  • 102
    • 0037079677 scopus 로고    scopus 로고
    • Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases
    • Vaute O, Nicolas E, Vandel L, Trouche D. Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases. Nucleic Acids Res 2002; 30: 475-481
    • (2002) Nucleic Acids Res , vol.30 , pp. 475-481
    • Vaute, O.1    Nicolas, E.2    Vandel, L.3    Trouche, D.4
  • 103
    • 33748200050 scopus 로고    scopus 로고
    • Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage
    • Wang C, Chen L, Hou X, Li Z, Kabra N, Ma Y.et al.. Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. Nat Cell Biol 2006; 8: 1025-1031
    • (2006) Nat Cell Biol , vol.8 , pp. 1025-1031
    • Wang, C.1    Chen, L.2    Hou, X.3    Li, Z.4    Kabra, N.5    Ma, Y.6
  • 104
    • 44449141876 scopus 로고    scopus 로고
    • SIRT1 negatively regulates HDAC1-dependent transcriptional repression by the RBP1 family of proteins
    • Binda O, Nassif C, Branton PE. SIRT1 negatively regulates HDAC1-dependent transcriptional repression by the RBP1 family of proteins. Oncogene 2008; 27: 3384-3392
    • (2008) Oncogene , vol.27 , pp. 3384-3392
    • Binda, O.1    Nassif, C.2    Branton, P.E.3
  • 105
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E, Pearson M, Faretta M, Bauer UM, Frye RA, Minucci S.et al.. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J 2002; 21: 2383-2396
    • (2002) EMBO J , vol.21 , pp. 2383-2396
    • Langley, E.1    Pearson, M.2    Faretta, M.3    Bauer, U.M.4    Frye, R.A.5    Minucci, S.6
  • 106
    • 15944365507 scopus 로고    scopus 로고
    • Role of NAD-dependent deacetylases SIRT1 and SIRT2 in radiation and cisplatin-induced cell death in vertebrate cells
    • Matsushita N, Takami Y, Kimura M, Tachiiri S, Ishiai M, Nakayama T.et al.. Role of NAD-dependent deacetylases SIRT1 and SIRT2 in radiation and cisplatin-induced cell death in vertebrate cells. Genes Cells 2005; 10: 321-332
    • (2005) Genes Cells , vol.10 , pp. 321-332
    • Matsushita, N.1    Takami, Y.2    Kimura, M.3    Tachiiri, S.4    Ishiai, M.5    Nakayama, T.6
  • 107
    • 78650638268 scopus 로고    scopus 로고
    • SIRT2 downregulation in HeLa can induce p53 accumulation via p38 MAPK activationdependent p300 decrease, eventually leading to apoptosis
    • Li Y, Matsumori H, Nakayama Y, Osaki M, Kojima H, Kurimasa A.et al.. SIRT2 downregulation in HeLa can induce p53 accumulation via p38 MAPK activationdependent p300 decrease, eventually leading to apoptosis. Genes Cells 2011; 16: 34-45
    • (2011) Genes Cells , vol.16 , pp. 34-45
    • Li, Y.1    Matsumori, H.2    Nakayama, Y.3    Osaki, M.4    Kojima, H.5    Kurimasa, A.6
  • 108
    • 27844497945 scopus 로고    scopus 로고
    • FOXO transcription factors at the interface between longevity and tumor suppression
    • Greer EL, Brunet A. FOXO transcription factors at the interface between longevity and tumor suppression. Oncogene 2005; 24: 7410-7425
    • (2005) Oncogene , vol.24 , pp. 7410-7425
    • Greer, E.L.1    Brunet, A.2
  • 109
    • 17644379936 scopus 로고    scopus 로고
    • FOXO transcription factors in cell-cycle regulation and the response to oxidative stress
    • Furukawa-Hibi Y, Kobayashi Y, Chen C, Motoyama N. FOXO transcription factors in cell-cycle regulation and the response to oxidative stress. Antioxid Redox Signal 2005; 7: 752-760
    • (2005) Antioxid Redox Signal , vol.7 , pp. 752-760
    • Furukawa-Hibi, Y.1    Kobayashi, Y.2    Chen, C.3    Motoyama, N.4
  • 110
    • 4644324186 scopus 로고    scopus 로고
    • NF-kappaB functions as a tumour promoter in inflammation-Associated cancer
    • Pikarsky E, Porat RM, Stein I, Abramovitch R, Amit S, Kasem S.et al.. NF-kappaB functions as a tumour promoter in inflammation-Associated cancer. Nature 2004; 431: 461-466
    • (2004) Nature , vol.431 , pp. 461-466
    • Pikarsky, E.1    Porat, R.M.2    Stein, I.3    Abramovitch, R.4    Amit, S.5    Kasem, S.6
  • 111
    • 79951482450 scopus 로고    scopus 로고
    • Genomic instability and cancer: An introduction
    • Shen Z. Genomic instability and cancer: an introduction. J Mol Cell Biol 2011; 3: 1-3
    • (2011) J Mol Cell Biol , vol.3 , pp. 1-3
    • Shen, Z.1
  • 112
    • 27244435939 scopus 로고    scopus 로고
    • Mammalian SIRT1 limits replicative life span in response to chronic genotoxic stress
    • Chua KF, Mostoslavsky R, Lombard DB, Pang WW, Saito S, Franco S.et al.. Mammalian SIRT1 limits replicative life span in response to chronic genotoxic stress. Cell Metab 2005; 2: 67-76
    • (2005) Cell Metab , vol.2 , pp. 67-76
    • Chua, K.F.1    Mostoslavsky, R.2    Lombard, D.B.3    Pang, W.W.4    Saito, S.5    Franco, S.6
  • 113
    • 36849002444 scopus 로고    scopus 로고
    • SIRT3 is pro-Apoptotic and participates in distinct basal apoptotic pathways
    • Allison SJ, Milner J. SIRT3 is pro-Apoptotic and participates in distinct basal apoptotic pathways. Cell Cycle 2007; 6: 2669-2677
    • (2007) Cell Cycle , vol.6 , pp. 2669-2677
    • Allison, S.J.1    Milner, J.2
  • 114
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang F, Nguyen M, Qin FX, Tong Q. SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 2007; 6: 505-514
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 115
    • 39749087530 scopus 로고    scopus 로고
    • SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization
    • Han MK, Song EK, Guo Y, Ou X, Mantel C, Broxmeyer HE. SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization. Cell Stem Cell 2008; 2: 241-251
    • (2008) Cell Stem Cell , vol.2 , pp. 241-251
    • Han, M.K.1    Song, E.K.2    Guo, Y.3    Ou, X.4    Mantel, C.5    Broxmeyer, H.E.6
  • 116
    • 84865793242 scopus 로고    scopus 로고
    • AMPK promotes p53 acetylation via phosphorylation and inactivation of SIRT1 in liver cancer cells
    • Lee CW, Wong LL, Tse EY, Liu HF, Leong VY, Lee JM.et al.. AMPK promotes p53 acetylation via phosphorylation and inactivation of SIRT1 in liver cancer cells. Cancer Res 2012; 72: 4394-4404
    • (2012) Cancer Res , vol.72 , pp. 4394-4404
    • Lee, C.W.1    Wong, L.L.2    Tse, E.Y.3    Liu, H.F.4    Leong, V.Y.5    Lee, J.M.6
  • 117
    • 79952235291 scopus 로고    scopus 로고
    • Dynamics of DNA damage response proteins at DNA breaks: A focus on protein modifications
    • Polo SE, Jackson SP. Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. Genes Dev 2011; 25: 409-433
    • (2011) Genes Dev , vol.25 , pp. 409-433
    • Polo, S.E.1    Jackson, S.P.2
  • 118
    • 77955501963 scopus 로고    scopus 로고
    • SIRT1 regulates UV-induced DNA repair through deacetylating XPA
    • Fan W, Luo J. SIRT1 regulates UV-induced DNA repair through deacetylating XPA. Mol Cell 2010; 39: 247-258
    • (2010) Mol Cell , vol.39 , pp. 247-258
    • Fan, W.1    Luo, J.2
  • 119
    • 78651105018 scopus 로고    scopus 로고
    • Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C
    • Ming M, Shea CR, Guo X, Li X, Soltani K, Han W.et al.. Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C. Proc Natl Acad Sci USA 2010; 107: 22623-22628
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 22623-22628
    • Ming, M.1    Shea, C.R.2    Guo, X.3    Li, X.4    Soltani, K.5    Han, W.6
  • 120
    • 37549016377 scopus 로고    scopus 로고
    • A functional link between SIRT1 deacetylase and NBS1 in DNA damage response
    • Yuan Z, Seto E. A functional link between SIRT1 deacetylase and NBS1 in DNA damage response. Cell Cycle 2007; 6: 2869-2871
    • (2007) Cell Cycle , vol.6 , pp. 2869-2871
    • Yuan, Z.1    Seto, E.2
  • 121
    • 34250897968 scopus 로고    scopus 로고
    • SIRT1 regulates the function of the Nijmegen breakage syndrome protein
    • Yuan Z, Zhang X, Sengupta N, Lane WS, Seto E. SIRT1 regulates the function of the Nijmegen breakage syndrome protein. Mol Cell 2007; 27: 149-162
    • (2007) Mol Cell , vol.27 , pp. 149-162
    • Yuan, Z.1    Zhang, X.2    Sengupta, N.3    Lane, W.S.4    Seto, E.5
  • 122
    • 0034576494 scopus 로고    scopus 로고
    • The many substrates and functions of ATM
    • Kastan MB, Lim DS. The many substrates and functions of ATM. Nat Rev Mol Cell Biol 2000; 1: 179-186
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 179-186
    • Kastan, M.B.1    Lim, D.S.2
  • 123
    • 0034611728 scopus 로고    scopus 로고
    • ATM phosphorylates p95/ nbs1 in an S-phase checkpoint pathway
    • Lim DS, Kim ST, Xu B, Maser RS, Lin J, Petrini JH.et al.. ATM phosphorylates p95/ nbs1 in an S-phase checkpoint pathway. Nature 2000; 404: 613-617
    • (2000) Nature , vol.404 , pp. 613-617
    • Lim, D.S.1    Kim, S.T.2    Xu, B.3    Maser, R.S.4    Lin, J.5    Petrini, J.H.6
  • 124
    • 56749156405 scopus 로고    scopus 로고
    • SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging
    • Oberdoerffer P, Michan S, McVay M, Mostoslavsky R, Vann J, Park SK.et al.. SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging. Cell 2008; 135: 907-918
    • (2008) Cell , vol.135 , pp. 907-918
    • Oberdoerffer, P.1    Michan, S.2    McVay, M.3    Mostoslavsky, R.4    Vann, J.5    Park, S.K.6
  • 125
    • 84864020743 scopus 로고    scopus 로고
    • SIRT1 negatively regulates the activities, functions, and protein levels of hMOF and TIP60
    • Peng L, Ling H, Yuan Z, Fang B, Bloom G, Fukasawa K.et al.. SIRT1 negatively regulates the activities, functions, and protein levels of hMOF and TIP60. Mol Cell Biol 2012; 32: 2823-2836
    • (2012) Mol Cell Biol , vol.32 , pp. 2823-2836
    • Peng, L.1    Ling, H.2    Yuan, Z.3    Fang, B.4    Bloom, G.5    Fukasawa, K.6
  • 126
    • 37549014206 scopus 로고    scopus 로고
    • The mammalian ortholog of Drosophila MOF that acetylates histone H4 lysine 16 is essential for embryogenesis and oncogenesis
    • Gupta A, Guerin-Peyrou TG, Sharma GG, Park C, Agarwal M, Ganju RK.et al.. The mammalian ortholog of Drosophila MOF that acetylates histone H4 lysine 16 is essential for embryogenesis and oncogenesis. Mol Cell Biol 2008; 28: 397-409
    • (2008) Mol Cell Biol , vol.28 , pp. 397-409
    • Gupta, A.1    Guerin-Peyrou, T.G.2    Sharma, G.G.3    Park, C.4    Agarwal, M.5    Ganju, R.K.6
  • 127
    • 34547913733 scopus 로고    scopus 로고
    • Males absent on the first (MOF): From flies to humans
    • Rea S, Xouri G, Akhtar A. Males absent on the first (MOF): from flies to humans. Oncogene 2007; 26: 5385-5394
    • (2007) Oncogene , vol.26 , pp. 5385-5394
    • Rea, S.1    Xouri, G.2    Akhtar, A.3
  • 128
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M.et al.. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 2000; 102: 463-473
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1    Ogryzko, V.V.2    Grigoriev, M.3    Groisman, R.4    Wang, J.5    Horikoshi, M.6
  • 129
    • 24944516931 scopus 로고    scopus 로고
    • A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM
    • Sun Y, Jiang X, Chen S, Fernandes N, Price BD. A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc Natl Acad Sci USA 2005; 102: 13182-13187
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13182-13187
    • Sun, Y.1    Jiang, X.2    Chen, S.3    Fernandes, N.4    Price, B.D.5
  • 130
    • 70449518412 scopus 로고    scopus 로고
    • Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60
    • Sun Y, Jiang X, Xu Y, Ayrapetov MK, Moreau LA, Whetstine JR.et al.. Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60. Nat Cell Biol 2009; 11: 1376-1382
    • (2009) Nat Cell Biol , vol.11 , pp. 1376-1382
    • Sun, Y.1    Jiang, X.2    Xu, Y.3    Ayrapetov, M.K.4    Moreau, L.A.5    Whetstine, J.R.6
  • 132
    • 46749109938 scopus 로고    scopus 로고
    • Sirtuin-mediated deacetylation pathway stabilizes Werner syndrome protein
    • Kahyo T, Mostoslavsky R, Goto M, Setou M. Sirtuin-mediated deacetylation pathway stabilizes Werner syndrome protein. FEBS Lett 2008; 582: 2479-2483
    • (2008) FEBS Lett , vol.582 , pp. 2479-2483
    • Kahyo, T.1    Mostoslavsky, R.2    Goto, M.3    Setou, M.4
  • 133
    • 43149118368 scopus 로고    scopus 로고
    • Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation
    • Li K, Casta A, Wang R, Lozada E, Fan W, Kane S.et al.. Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation. J Biol Chem 2008; 283: 7590-7598
    • (2008) J Biol Chem , vol.283 , pp. 7590-7598
    • Li, K.1    Casta, A.2    Wang, R.3    Lozada, E.4    Fan, W.5    Kane, S.6
  • 134
    • 66249144685 scopus 로고    scopus 로고
    • Identification and characterization of proteins interacting with SIRT1 and SIRT3: Implications in the anti-Aging and metabolic effects of sirtuins
    • Law IK, Liu L, Xu A, Lam KS, Vanhoutte PM, Che CM.et al.. Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-Aging and metabolic effects of sirtuins. Proteomics 2009; 9: 2444-2456
    • (2009) Proteomics , vol.9 , pp. 2444-2456
    • Law, I.K.1    Liu, L.2    Xu, A.3    Lam, K.S.4    Vanhoutte, P.M.5    Che, C.M.6
  • 136
    • 33847647624 scopus 로고    scopus 로고
    • SIRT1 promotes DNA repair activity and deacetylation of Ku70
    • Jeong J, Juhn K, Lee H, Kim SH, Min BH, Lee KM.et al.. SIRT1 promotes DNA repair activity and deacetylation of Ku70. Exp Mol Med 2007; 39: 8-13
    • (2007) Exp Mol Med , vol.39 , pp. 8-13
    • Jeong, J.1    Juhn, K.2    Lee, H.3    Kim, S.H.4    Min, B.H.5    Lee, K.M.6
  • 138
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, Miller C, Bitterman KJ, Wall NR, Hekking B, Kessler B.et al.. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 2004; 305: 390-392
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3    Wall, N.R.4    Hekking, B.5    Kessler, B.6
  • 139
    • 84863981612 scopus 로고    scopus 로고
    • Emerging roles of SIRT6 on telomere maintenance, DNA repair, metabolism and mammalian aging
    • Jia G, Su L, Singhal S, Liu X. Emerging roles of SIRT6 on telomere maintenance, DNA repair, metabolism and mammalian aging. Mol Cell Biochem 2012; 364: 345-350
    • (2012) Mol Cell Biochem , vol.364 , pp. 345-350
    • Jia, G.1    Su, L.2    Singhal, S.3    Liu, X.4
  • 140
    • 79959363092 scopus 로고    scopus 로고
    • SIRT6 promotes DNA repair under stress by activating PARP1
    • Mao Z, Hine C, Tian X, Van Meter M, Au M, Vaidya A.et al.. SIRT6 promotes DNA repair under stress by activating PARP1. Science 2011; 332: 1443-1446
    • (2011) Science , vol.332 , pp. 1443-1446
    • Mao, Z.1    Hine, C.2    Tian, X.3    Van Meter, M.4    Au, M.5    Vaidya, A.6
  • 141
    • 84863974838 scopus 로고    scopus 로고
    • Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence
    • Mao Z, Tian X, Van Meter M, Ke Z, Gorbunova V, Seluanov A. Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence. Proc Natl Acad Sci USA 2012; 109: 11800-11805
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 11800-11805
    • Mao, Z.1    Tian, X.2    Van Meter, M.3    Ke, Z.4    Gorbunova, V.5    Seluanov, A.6
  • 142
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: Where are we today and where are we going?
    • Hassa PO, Haenni SS, Elser M, Hottiger MO. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going? Microbiol Mol Biol Rev 2006; 70: 789-829
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 143
    • 0034575578 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation: A posttranslational protein modification linked with genome protection and mammalian longevity
    • Burkle A. Poly(ADP-ribosyl)ation: a posttranslational protein modification linked with genome protection and mammalian longevity. Biogerontology 2000; 1: 41-46
    • (2000) Biogerontology , vol.1 , pp. 41-46
    • Burkle, A.1
  • 144
    • 33645288259 scopus 로고    scopus 로고
    • Parp-1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells
    • Hochegger H, Dejsuphong D, Fukushima T, Morrison C, Sonoda E, Schreiber V.et al.. Parp-1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells. EMBO J 2006; 25: 1305-1314
    • (2006) EMBO J , vol.25 , pp. 1305-1314
    • Hochegger, H.1    Dejsuphong, D.2    Fukushima, T.3    Morrison, C.4    Sonoda, E.5    Schreiber, V.6
  • 145
    • 77955037815 scopus 로고    scopus 로고
    • The BRCT domain of PARP-1 is required for immunoglobulin gene conversion
    • Paddock MN, Buelow BD, Takeda S, Scharenberg AM. The BRCT domain of PARP-1 is required for immunoglobulin gene conversion. PLoS Biol 2010; 8: e1000428
    • (2010) PLoS Biol , vol.8
    • Paddock, M.N.1    Buelow, B.D.2    Takeda, S.3    Scharenberg, A.M.4
  • 146
    • 0032518339 scopus 로고    scopus 로고
    • DNA repair: PARP-Another guardian angel?
    • Jeggo PA. DNA repair: PARP-Another guardian angel? Curr Biol 1998; 8: R49-R51
    • (1998) Curr Biol , vol.8
    • Jeggo, P.A.1
  • 148
    • 77956550868 scopus 로고    scopus 로고
    • Human SIRT6 promotes DNA end resection through CtIP deacetylation
    • Kaidi A, Weinert BT, Choudhary C, Jackson SP. Human SIRT6 promotes DNA end resection through CtIP deacetylation. Science 2010; 329: 1348-1353
    • (2010) Science , vol.329 , pp. 1348-1353
    • Kaidi, A.1    Weinert, B.T.2    Choudhary, C.3    Jackson, S.P.4
  • 149
    • 66049150672 scopus 로고    scopus 로고
    • SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair
    • McCord RA, Michishita E, Hong T, Berber E, Boxer LD, Kusumoto R.et al.. SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair. Aging (Albany, NY) 2009; 1: 109-121
    • (2009) Aging (Albany, NY) , vol.1 , pp. 109-121
    • McCord, R.A.1    Michishita, E.2    Hong, T.3    Berber, E.4    Boxer, L.D.5    Kusumoto, R.6
  • 150
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan J, Pu M, Zhang Z, Lou Z. Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 2009; 8: 1747-1753
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4
  • 151
    • 33745520486 scopus 로고    scopus 로고
    • The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation
    • Celic I, Masumoto H, Griffith WP, Meluh P, Cotter RJ, Boeke JD.et al.. The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation. Curr Biol 2006; 16: 1280-1289
    • (2006) Curr Biol , vol.16 , pp. 1280-1289
    • Celic, I.1    Masumoto, H.2    Griffith, W.P.3    Meluh, P.4    Cotter, R.J.5    Boeke, J.D.6
  • 152
    • 53549105529 scopus 로고    scopus 로고
    • SIRT3 is a stressresponsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70
    • Sundaresan NR, Samant SA, Pillai VB, Rajamohan SB, Gupta MP. SIRT3 is a stressresponsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol Cell Biol 2008; 28: 6384-6401
    • (2008) Mol Cell Biol , vol.28 , pp. 6384-6401
    • Sundaresan, N.R.1    Samant, S.A.2    Pillai, V.B.3    Rajamohan, S.B.4    Gupta, M.P.5
  • 153
    • 33744465025 scopus 로고    scopus 로고
    • Mitochondria damage checkpoint, aging, and cancer
    • Singh KK. Mitochondria damage checkpoint, aging, and cancer. Ann NY Acad Sci 2006; 1067: 182-190
    • (2006) Ann NY Acad Sci , vol.1067 , pp. 182-190
    • Singh, K.K.1
  • 154
    • 52649107626 scopus 로고    scopus 로고
    • Cancer cell metabolism: Warburg and beyond
    • Hsu PP, Sabatini DM. Cancer cell metabolism: Warburg and beyond. Cell 2008; 134: 703-707
    • (2008) Cell , vol.134 , pp. 703-707
    • Hsu, P.P.1    Sabatini, D.M.2
  • 155
    • 59849084800 scopus 로고    scopus 로고
    • Increased levels of superoxide and H2O2 mediate the differential susceptibility of cancer cells versus normal cells to glucose deprivation
    • Aykin-Burns N, Ahmad IM, Zhu Y, Oberley LW, Spitz DR. Increased levels of superoxide and H2O2 mediate the differential susceptibility of cancer cells versus normal cells to glucose deprivation. Biochem J 2009; 418: 29-37
    • (2009) Biochem J , vol.418 , pp. 29-37
    • Aykin-Burns, N.1    Ahmad, I.M.2    Zhu, Y.3    Oberley, L.W.4    Spitz, D.R.5
  • 157
    • 0037108799 scopus 로고    scopus 로고
    • SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria
    • Onyango P, Celic I, McCaffery JM, Boeke JD, Feinberg AP. SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proc Natl Acad Sci USA 2002; 99: 13653-13658
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13653-13658
    • Onyango, P.1    Celic, I.2    McCaffery, J.M.3    Boeke, J.D.4    Feinberg, A.P.5
  • 158
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer B, North BJ, Frye RA, Ott M, Verdin E. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol 2002; 158: 647-657
    • (2002) J Cell Biol , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 159
    • 0024402834 scopus 로고
    • An assay for superoxide dismutase activity in mammalian tissue homogenates
    • Spitz DR, Oberley LW. An assay for superoxide dismutase activity in mammalian tissue homogenates. Anal Biochem 1989; 179: 8-18
    • (1989) Anal Biochem , vol.179 , pp. 8-18
    • Spitz, D.R.1    Oberley, L.W.2
  • 160
    • 78650248160 scopus 로고    scopus 로고
    • Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress
    • Tao R, Coleman MC, Pennington JD, Ozden O, Park SH, Jiang H.et al.. Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress. Mol Cell 2010; 40: 893-904
    • (2010) Mol Cell , vol.40 , pp. 893-904
    • Tao, R.1    Coleman, M.C.2    Pennington, J.D.3    Ozden, O.4    Park, S.H.5    Jiang, H.6
  • 161
    • 78651468722 scopus 로고    scopus 로고
    • Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
    • Someya S, Yu W, Hallows WC, Xu J, Vann JM, Leeuwenburgh C.et al.. Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 2010; 143: 802-812
    • (2010) Cell , vol.143 , pp. 802-812
    • Someya, S.1    Yu, W.2    Hallows, W.C.3    Xu, J.4    Vann, J.M.5    Leeuwenburgh, C.6
  • 165
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • Cheng HL, Mostoslavsky R, Saito S, Manis JP, Gu Y, Patel P.et al.. Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc Natl Acad Sci USA 2003; 100: 10794-10799
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10794-10799
    • Cheng, H.L.1    Mostoslavsky, R.2    Saito, S.3    Manis, J.P.4    Gu, Y.5    Patel, P.6
  • 166
    • 84865555215 scopus 로고    scopus 로고
    • Dilated cardiomyopathy and mitochondrial dysfunction in Sirt1-deficient mice: A role for Sirt1-Mef2 in adult heart
    • Planavila A, Dominguez E, Navarro M, Vinciguerra M, Iglesias R, Giralt M.et al.. Dilated cardiomyopathy and mitochondrial dysfunction in Sirt1-deficient mice: a role for Sirt1-Mef2 in adult heart. J Mol Cell Cardiol 2012; 53: 521-531
    • (2012) J Mol Cell Cardiol , vol.53 , pp. 521-531
    • Planavila, A.1    Dominguez, E.2    Navarro, M.3    Vinciguerra, M.4    Iglesias, R.5    Giralt, M.6
  • 167
    • 78751506082 scopus 로고    scopus 로고
    • SIRT1 deficiency compromises mouse embryonic stem cell hematopoietic differentiation, and embryonic and adult hematopoiesis in the mouse
    • Ou X, Chae HD, Wang RH, Shelley WC, Cooper S, Taylor T.et al.. SIRT1 deficiency compromises mouse embryonic stem cell hematopoietic differentiation, and embryonic and adult hematopoiesis in the mouse. Blood 2011; 117: 440-450
    • (2011) Blood , vol.117 , pp. 440-450
    • Ou, X.1    Chae, H.D.2    Wang, R.H.3    Shelley, W.C.4    Cooper, S.5    Taylor, T.6
  • 168
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-Acid oxidation by reversible enzyme deacetylation
    • Hirschey MD, Shimazu T, Goetzman E, Jing E, Schwer B, Lombard DB.et al.. SIRT3 regulates mitochondrial fatty-Acid oxidation by reversible enzyme deacetylation. Nature 2010; 464: 121-125
    • (2010) Nature , vol.464 , pp. 121-125
    • Hirschey, M.D.1    Shimazu, T.2    Goetzman, E.3    Jing, E.4    Schwer, B.5    Lombard, D.B.6
  • 169
    • 78649509214 scopus 로고    scopus 로고
    • SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production
    • Shimazu T, Hirschey MD, Hua L, Dittenhafer-Reed KE, Schwer B, Lombard DB.et al.. SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production. Cell Metab 2010; 12: 654-661
    • (2010) Cell Metab , vol.12 , pp. 654-661
    • Shimazu, T.1    Hirschey, M.D.2    Hua, L.3    Dittenhafer-Reed, K.E.4    Schwer, B.5    Lombard, D.B.6
  • 170
    • 80052291180 scopus 로고    scopus 로고
    • Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production
    • Jing E, Emanuelli B, Hirschey MD, Boucher J, Lee KY, Lombard D.et al.. Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. Proc Natl Acad Sci USA 2011; 108: 14608-14613
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14608-14613
    • Jing, E.1    Emanuelli, B.2    Hirschey, M.D.3    Boucher, J.4    Lee, K.Y.5    Lombard, D.6
  • 171
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • Qiu X, Brown K, Hirschey MD, Verdin E, Chen D. Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab 2010; 12: 662-667
    • (2010) Cell Metab , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 172
    • 70349208608 scopus 로고    scopus 로고
    • Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3adependent antioxidant defense mechanisms in mice
    • Sundaresan NR, Gupta M, Kim G, Rajamohan SB, Isbatan A, Gupta MP. Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3adependent antioxidant defense mechanisms in mice. J Clin Invest 2009; 119: 2758-2771
    • (2009) J Clin Invest , vol.119 , pp. 2758-2771
    • Sundaresan, N.R.1    Gupta, M.2    Kim, G.3    Rajamohan, S.B.4    Isbatan, A.5    Gupta, M.P.6
  • 173
    • 82455212901 scopus 로고    scopus 로고
    • SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome
    • Hirschey MD, Shimazu T, Jing E, Grueter CA, Collins AM, Aouizerat B.et al.. SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome. Mol Cell 2011; 44: 177-190
    • (2011) Mol Cell , vol.44 , pp. 177-190
    • Hirschey, M.D.1    Shimazu, T.2    Jing, E.3    Grueter, C.A.4    Collins, A.M.5    Aouizerat, B.6
  • 174
  • 175
    • 78651468707 scopus 로고    scopus 로고
    • Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
    • Hallows WC, Yu W, Smith BC, Devries MK, Ellinger JJ, Someya S.et al.. Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction. Mol Cell 2011; 41: 139-149
    • (2011) Mol Cell , vol.41 , pp. 139-149
    • Hallows, W.C.1    Yu, W.2    Smith, B.C.3    Devries, M.K.4    Ellinger, J.J.5    Someya, S.6
  • 177
    • 77951235122 scopus 로고    scopus 로고
    • NAD-dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10
    • Yang Y, Cimen H, Han MJ, Shi T, Deng JH, Koc H.et al.. NAD-dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10. J Biol Chem 2009; 285: 7417-7429
    • (2009) J Biol Chem , vol.285 , pp. 7417-7429
    • Yang, Y.1    Cimen, H.2    Han, M.J.3    Shi, T.4    Deng, J.H.5    Koc, H.6
  • 178
    • 33748316536 scopus 로고    scopus 로고
    • SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells
    • Haigis MC, Mostoslavsky R, Haigis KM, Fahie K, Christodoulou DC, Murphy AJ.et al.. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 2006; 126: 941-954
    • (2006) Cell , vol.126 , pp. 941-954
    • Haigis, M.C.1    Mostoslavsky, R.2    Haigis, K.M.3    Fahie, K.4    Christodoulou, D.C.5    Murphy, A.J.6
  • 179
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa T, Lomb DJ, Haigis MC, Guarente L. SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 2009; 137: 560-570
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 180
    • 83055173304 scopus 로고    scopus 로고
    • The first identification of lysine malonylation substrates and its regulatory enzyme
    • M111.012658
    • Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M.et al.. The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics 2011; 10: M111.012658
    • (2011) Mol Cell Proteomics , vol.10
    • Peng, C.1    Lu, Z.2    Xie, Z.3    Cheng, Z.4    Chen, Y.5    Tan, M.6
  • 181
    • 41449083867 scopus 로고    scopus 로고
    • Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice
    • Vakhrusheva O, Smolka C, Gajawada P, Kostin S, Boettger T, Kubin T.et al.. Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ Res 2008; 102: 703-710.
    • (2008) Circ Res , vol.102 , pp. 703-710
    • Vakhrusheva, O.1    Smolka, C.2    Gajawada, P.3    Kostin, S.4    Boettger, T.5    Kubin, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.