메뉴 건너뛰기




Volumn 206, Issue , 2011, Pages 189-224

Characterization of nuclear sirtuins: Molecular mechanisms and physiological relevance

Author keywords

synuclein; Angiogenesis; Caenorhabditis elegans; Caloric restriction; Cellular senescence; Chronological life span; Drosophila; Fragile X syndrome; Glucose metabolism; HML and HMR; Hst proteins; Hypoxia; Nucleotide; Parkinson's disease; Senescence; Sir2

Indexed keywords

APOLIPOPROTEIN E; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN P53; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SIRTUIN; SIRTUIN 1; SIRTUIN 2; SIRTUIN 6; SIRTUIN 7; TRANSCRIPTION FACTOR FKHRL1; TUBULIN;

EID: 80054736119     PISSN: 01712004     EISSN: 18650325     Source Type: Book Series    
DOI: 10.1007/978-3-642-21631-2_9     Document Type: Article
Times cited : (44)

References (198)
  • 1
  • 2
    • 0242585476 scopus 로고    scopus 로고
    • Asymmetric inheritance of oxidatively damaged proteins during cytokinesis
    • DOI 10.1126/science.1080418
    • Aguilaniu H, Gustafsson L, Rigoulet M, Nystrom T (2003) Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 299:1751-1753 (Pubitemid 36337204)
    • (2003) Science , vol.299 , Issue.5613 , pp. 1751-1753
    • Aguilaniu, H.1    Gustafsson, L.2    Rigoulet, M.3    Nystrom, T.4
  • 6
    • 45749094496 scopus 로고    scopus 로고
    • Analysis of DBC1 and its homologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolites
    • Anantharaman V, Aravind L (2008) Analysis of DBC1 and its homologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolites. Cell Cycle 7:1467-1472 (Pubitemid 351872586)
    • (2008) Cell Cycle , vol.7 , Issue.10 , pp. 1467-1472
    • Anantharaman, V.1    Aravind, L.2
  • 7
    • 0038329323 scopus 로고    scopus 로고
    • Nicatinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • DOI 10.1038/nature01578
    • Anderson RM, Bitterman KJ, Wood JG, Medvedik O, Sinclair DA (2003) Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 423: 181-185 (Pubitemid 36569542)
    • (2003) Nature , vol.423 , Issue.6936 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 8
    • 0037355004 scopus 로고    scopus 로고
    • + gene is nonessential and has only minor effects on position-effect variegation
    • Astrom SU, Cline TW, Rine J (2003) The Drosophila melanogaster sir2(+) gene is nonessential and has only minor effects on position-effect variegation. Genetics 163:931-937 (Pubitemid 36417937)
    • (2003) Genetics , vol.163 , Issue.3 , pp. 931-937
    • Astrom, S.U.1    Cline, T.W.2    Rine, J.3
  • 9
    • 33744976074 scopus 로고    scopus 로고
    • C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span
    • DOI 10.1016/j.cell.2006.04.036, PII S0092867406006180
    • Berdichevsky A, Viswanathan M, Horvitz HR, Guarente L (2006) C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell 125:1165-1177 (Pubitemid 43866202)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1165-1177
    • Berdichevsky, A.1    Viswanathan, M.2    Horvitz, H.R.3    Guarente, L.4
  • 10
    • 41949125454 scopus 로고    scopus 로고
    • SIRT1 inhibition alleviates gene silencing in Fragile X mental retardation syndrome
    • Biacsi R, Kumari D, Usdin K (2008) SIRT1 inhibition alleviates gene silencing in Fragile X mental retardation syndrome. PLoS Genet 4:e1000017
    • (2008) PLoS Genet , vol.4
    • Biacsi, R.1    Kumari, D.2    Usdin, K.3
  • 11
    • 77950968403 scopus 로고    scopus 로고
    • Neuron dysfunction is induced by prion protein with an insertional mutation via a Fyn kinase and reversed by sirtuin activation in Caenorhabditis elegans
    • Bizat N, Peyrin JM, Haik S, Cochois V, Beaudry P, Laplanche JL, Neri C (2010) Neuron dysfunction is induced by prion protein with an insertional mutation via a Fyn kinase and reversed by sirtuin activation in Caenorhabditis elegans. J Neurosci 30:5394-5403
    • (2010) J Neurosci , vol.30 , pp. 5394-5403
    • Bizat, N.1    Peyrin, J.M.2    Haik, S.3    Cochois, V.4    Beaudry, P.5    Laplanche, J.L.6    Neri, C.7
  • 12
    • 27844578650 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease
    • Bonifati V (2005) Genetics of Parkinson's disease. Minerva Med 96:175-186 (Pubitemid 41641249)
    • (2005) Minerva Medica , vol.96 , Issue.3 , pp. 175-186
    • Bonifati, V.1
  • 14
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann CB, Sherman JM, Devine SE, Cameron EE, Pillus L, Boeke JD (1995) The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev 9:2888-2902
    • (1995) Genes Dev , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1    Sherman, J.M.2    Devine, S.E.3    Cameron, E.E.4    Pillus, L.5    Boeke, J.D.6
  • 15
    • 27144475816 scopus 로고    scopus 로고
    • Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors
    • DOI 10.1038/sj.leu.2403910, PII 2403910
    • Bradbury CA, Khanim FL, Hayden R, Bunce CM, White DA, Drayson MT, Craddock C, Turner BM (2005) Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors. Leukemia 19: 1751-1759 (Pubitemid 41486152)
    • (2005) Leukemia , vol.19 , Issue.10 , pp. 1751-1759
    • Bradbury, C.A.1    Khanim, F.L.2    Hayden, R.3    Bunce, C.M.4    White, D.A.5    Drayson, M.T.6    Craddock, C.7    Turner, B.M.8
  • 20
    • 0028876673 scopus 로고
    • Genetic interactions and dosage effects of Polycomb group genes of Drosophila
    • Campbell RB, Sinclair DA, Couling M, Brock HW (1995) Genetic interactions and dosage effects of Polycomb group genes of Drosophila. Mol Gen Genet 246:291-300
    • (1995) Mol Gen Genet , vol.246 , pp. 291-300
    • Campbell, R.B.1    Sinclair, D.A.2    Couling, M.3    Brock, H.W.4
  • 21
    • 33745520486 scopus 로고    scopus 로고
    • The sirtuins Hst3 and Hst4p preserve genome integrity by controlling histone H3 lysine 56 deacetylation
    • DOI 10.1016/j.cub.2006.06.023, PII S0960982206017490
    • Celic I, Masumoto H, Griffith WP, Meluh P, Cotter RJ, Boeke JD, Verreault A (2006) The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation. Curr Biol 16:1280-1289 (Pubitemid 43977885)
    • (2006) Current Biology , vol.16 , Issue.13 , pp. 1280-1289
    • Celic, I.1    Masumoto, H.2    Griffith, W.P.3    Meluh, P.4    Cotter, R.J.5    Boeke, J.D.6    Verreault, A.7
  • 24
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent amyloid-β toxicity through inhibiting NF-κB signaling
    • DOI 10.1074/jbc.M509329200
    • Chen J, Zhou Y, Mueller-Steiner S, Chen LF, Kwon H, Yi S, Mucke L, Gan L (2005a) SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling. J Biol Chem 280:40364-40374 (Pubitemid 41779174)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 40364-40374
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3    Chen, L.-F.4    Kwon, H.5    Yi, S.6    Mucke, L.7    Gan, L.8
  • 25
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses
    • DOI 10.1016/j.cell.2005.08.011, PII S0092867405008159
    • Chen WY, Wang DH, Yen RC, Luo J, Gu W, Baylin SB (2005b) Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell 123:437-448 (Pubitemid 41546674)
    • (2005) Cell , vol.123 , Issue.3 , pp. 437-448
    • Wen, Y.C.1    Wang, D.H.2    RayWhay, C.Y.3    Luo, J.4    Gu, W.5    Baylin, S.B.6
  • 26
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • DOI 10.1016/j.cell.2008.06.035, PII S0092867408008222
    • Chen CC, Carson JJ, Feser J, Tamburini B, Zabaronick S, Linger J, Tyler JK (2008) Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 134:231-243 (Pubitemid 352010334)
    • (2008) Cell , vol.134 , Issue.2 , pp. 231-243
    • Chen, C.-C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5    Linger, J.6    Tyler, J.K.7
  • 35
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das C, Lucia MS, Hansen KC, Tyler JK (2009) CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 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
  • 36
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum EM, Chen R, Alexander MS, Zhang Q, Hogg RT, Gerard RD, Garcia JA (2009) Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1. Science 324:1289-1293
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3    Zhang, Q.4    Hogg, R.T.5    Gerard, R.D.6    Garcia, J.A.7
  • 37
    • 77955046461 scopus 로고    scopus 로고
    • SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10
    • Donmez G, Wang D, Cohen DE, Guarente L (2010) SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10. Cell 142:320-332
    • (2010) Cell , vol.142 , pp. 320-332
    • Donmez, G.1    Wang, D.2    Cohen, D.E.3    Guarente, L.4
  • 38
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • DOI 10.1128/MCB.23.9.3173-3185.2003
    • Dryden SC, Nahhas FA, Nowak JE, Goustin AS, Tainsky MA (2003) Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol 23:3173-3185 (Pubitemid 36459231)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.9 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.-S.4    Tainsky, M.A.5
  • 39
    • 34249001997 scopus 로고    scopus 로고
    • Specific functions for the fission yeast Sirtuins Hst2 and Hst4 in gene regulation and retrotransposon silencing
    • DOI 10.1038/sj.emboj.7601690, PII 7601690
    • Durand-Dubief M, Sinha I, Fagerstrom-Billai F, Bonilla C, Wright A, Grunstein M, Ekwall K (2007) Specific functions for the fission yeast Sirtuins Hst2 and Hst4 in gene regulation and retrotransposon silencing. EMBO J 26:2477-2488 (Pubitemid 46788316)
    • (2007) EMBO Journal , vol.26 , Issue.10 , pp. 2477-2488
    • Durand-Dubief, M.1    Sinha, I.2    Fagerstrom-Billai, F.3    Bonilla, C.4    Wright, A.5    Grunstein, M.6    Ekwall, K.7
  • 40
    • 34948846000 scopus 로고    scopus 로고
    • Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
    • DOI 10.1101/gad.439307
    • Erjavec N, Larsson L, Grantham J, Nystrom T (2007) Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregationremodeling factor Hsp104p. Genes Dev 21:2410-2421 (Pubitemid 47529371)
    • (2007) Genes and Development , vol.21 , Issue.19 , pp. 2410-2421
    • Erjavec, N.1    Larsson, L.2    Grantham, J.3    Nystrom, T.4
  • 42
    • 77955501963 scopus 로고    scopus 로고
    • SIRT1 regulates UV-induced DNA repair through deacetylating XPA
    • Fan W, Luo J (2010) SIRT1 regulates UV-induced DNA repair through deacetylating XPA. Mol Cell 39:247-258
    • (2010) Mol Cell , vol.39 , pp. 247-258
    • Fan, W.1    Luo, J.2
  • 43
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel T, Deng CX, Mostoslavsky R (2009) Recent progress in the biology and physiology of sirtuins. Nature 30:587-591
    • (2009) Nature , vol.30 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 46
    • 79954631819 scopus 로고    scopus 로고
    • DSir2 and longevity in Drosophila
    • Frankel S, Ziafazeli T, Rogina B (2010) dSir2 and longevity in Drosophila. Exp Gerontol 46 (5):391-396
    • (2010) Exp Gerontol , vol.46 , Issue.5 , pp. 391-396
    • Frankel, S.1    Ziafazeli, T.2    Rogina, B.3
  • 48
    • 20144365700 scopus 로고    scopus 로고
    • Nuclear trapping of the forkhead transcription factor FoxO1 via sirt-dependent deacetylation promotes expression of glucogenetic genes
    • DOI 10.1074/jbc.M412357200
    • Frescas D, Valenti L, Accili D (2005) Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes. J Biol Chem 280:20589-20595 (Pubitemid 40776761)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 49
    • 0030831573 scopus 로고    scopus 로고
    • Direct evidence for SIR2 modulation of chromatin structure in yeast rDNA
    • DOI 10.1093/emboj/16.21.6495
    • Fritze CE, Verschueren K, Strich R, Easton Esposito R (1997) Direct evidence for SIR2 modulation of chromatin structure in yeast rDNA. EMBO J 16:6495-6509 (Pubitemid 27483275)
    • (1997) EMBO Journal , vol.16 , Issue.21 , pp. 6495-6509
    • Fritze, C.E.1    Verschueren, K.2    Strich, R.3    Esposito, R.E.4
  • 50
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (Sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • DOI 10.1006/bbrc.1999.0897
    • Frye RA (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 260:273-279 (Pubitemid 29351819)
    • (1999) Biochemical and Biophysical Research Communications , vol.260 , Issue.1 , pp. 273-279
    • Frye, R.A.1
  • 51
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • DOI 10.1006/bbrc.2000.3000
    • Frye RA (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273:793-798 (Pubitemid 30599063)
    • (2000) Biochemical and Biophysical Research Communications , vol.273 , Issue.2 , pp. 793-798
    • Frye, R.A.1
  • 52
    • 34648816970 scopus 로고    scopus 로고
    • Cellular senescence and chromatin structure
    • DOI 10.1007/s00412-007-0115-7
    • Funayama R, Ishikawa F (2007) Cellular senescence and chromatin structure. Chromosoma 116:431-440 (Pubitemid 47456911)
    • (2007) Chromosoma , vol.116 , Issue.5 , pp. 431-440
    • Funayama, R.1    Ishikawa, F.2
  • 53
    • 6944253702 scopus 로고    scopus 로고
    • SIR2 is required for polycomb silencing and is associated with an E(Z) histone methyltransferase complex
    • DOI 10.1016/j.cub.2004.09.060, PII S0960982204007742
    • Furuyama T, Banerjee R, Breen TR, Harte PJ (2004) SIR2 is required for polycomb silencing and is associated with an E(Z) histone methyltransferase complex. Curr Biol 14:1812-1821 (Pubitemid 39408770)
    • (2004) Current Biology , vol.14 , Issue.20 , pp. 1812-1821
    • Furuyama, T.1    Banerjee, R.2    Breen, T.R.3    Harte, P.J.4
  • 57
    • 39749087530 scopus 로고    scopus 로고
    • SIRT1 regulates apoptosis and nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization
    • DOI 10.1016/j.stem.2008.01.002, PII S1934590908000039
    • Han MK, Song EK, Guo Y, Ou X, Mantel C, Broxmeyer HE (2008) SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization. Cell Stem Cell 2:241-251 (Pubitemid 351298591)
    • (2008) Cell Stem Cell , vol.2 , Issue.3 , pp. 241-251
    • Han, M.-K.1    Song, E.-K.2    Guo, Y.3    Ou, X.4    Mantel, C.5    Broxmeyer, H.E.6
  • 58
    • 0028919756 scopus 로고
    • Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
    • Hecht A, Laroche T, Strahl-Bolsinger S, Gasser SM, Grunstein M (1995) Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell 80:583-592
    • (1995) Cell , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Bolsinger, S.3    Gasser, S.M.4    Grunstein, M.5
  • 60
    • 34247570492 scopus 로고    scopus 로고
    • Strong expression of a longevity-related protein, SIRT1, in Bowen's disease
    • DOI 10.1007/s00403-006-0725-6
    • Hida Y, Kubo Y, Murao K, Arase S (2007) Strong expression of a longevity-related protein, SIRT1, in Bowen's disease. Arch Dermatol Res 299:103-106 (Pubitemid 46669407)
    • (2007) Archives of Dermatological Research , vol.299 , Issue.2 , pp. 103-106
    • Hida, Y.1    Kubo, Y.2    Murao, K.3    Arase, S.4
  • 63
    • 0036261650 scopus 로고    scopus 로고
    • Steps in assembly of silent chromatin in yeast: Sir3-independent binding of a Sir2/Sir4 complex to silencers and role for Sir2-dependent deacetylation
    • DOI 10.1128/MCB.22.12.4167-4180.2002
    • Hoppe GJ, Tanny JC, Rudner AD, Gerber SA, Danaie S, Gygi SP, Moazed D (2002) Steps in assembly of silent chromatin in yeast: Sir3-independent binding of a Sir2/Sir4 complex to silencers and role for Sir2-dependent deacetylation. Mol Cell Biol 22:4167-4180 (Pubitemid 34556587)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.12 , pp. 4167-4180
    • Hoppe, G.J.1    Tanny, J.C.2    Rudner, A.D.3    Gerber, S.A.4    Danaie, S.5    Gygi, S.P.6    Moazed, D.7
  • 64
    • 45849137875 scopus 로고    scopus 로고
    • SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6k1 signaling in human diploid fibroblasts
    • Huang J, Gan Q, Han L, Li J, Zhang H, Sun Y, Zhang Z, Tong T (2008) SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6k1 signaling in human diploid fibroblasts. PLoS One 3:e1710
    • (2008) PLoS One , vol.3
    • Huang, J.1    Gan, Q.2    Han, L.3    Li, J.4    Zhang, H.5    Sun, Y.6    Zhang, Z.7    Tong, T.8
  • 66
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • DOI 10.1038/35001622
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403:795-800 (Pubitemid 30111843)
    • (2000) Nature , vol.403 , Issue.6771 , pp. 795-800
    • Imai, S.-I.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 67
    • 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 (2007) The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation. Cell Cycle 6:1011-1018 (Pubitemid 46708571)
    • (2007) Cell Cycle , vol.6 , Issue.9 , pp. 1011-1018
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Oshimura, M.4
  • 69
    • 0036696982 scopus 로고    scopus 로고
    • Distinct roles of processes modulated by histone deacetylases Rpd3p, Hda1p, and Sir2p in life extension by caloric restriction in yeast
    • Jiang J, Wawryn J, Shantha Kumara H, Jazwinski S (2002) Distinct roles of processes modulated by histone deacetylases Rpd3p, Hda1p, and Sir2p in life extension by caloric restriction in yeast. Exp Gerontol 37:1023
    • (2002) Exp Gerontol , vol.37 , pp. 1023
    • Jiang, J.1    Wawryn, J.2    Shantha Kumara, H.3    Jazwinski, S.4
  • 70
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation
    • DOI 10.1016/j.cmet.2007.07.003, PII S155041310700191X
    • Jing E, Gesta S, Kahn CR (2007) SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab 6:105-114 (Pubitemid 47163621)
    • (2007) Cell Metabolism , vol.6 , Issue.2 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 71
    • 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
    • Kaeberlein M, McVey M, Guarente L (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev 13:2570-2580 (Pubitemid 29489648)
    • (1999) Genes and Development , vol.13 , Issue.19 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 72
  • 73
    • 77956550868 scopus 로고    scopus 로고
    • Human SIRT6 promotes DNA end resection through CtIP deacetylation
    • Kaidi A, Weinert BT, Choudhary C, Jackson S (2010) Human SIRT6 promotes DNA end resection through CtIP deacetylation. Science 329:1348-1353
    • (2010) Science , vol.329 , pp. 1348-1353
    • Kaidi, A.1    Weinert, B.T.2    Choudhary, C.3    Jackson, S.4
  • 76
    • 0024280881 scopus 로고
    • Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast
    • Kayne PS, Kim UJ, Han M, Mullen JR, Yoshizaki F, Grunstein M (1988) Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast. Cell 55:27-39
    • (1988) Cell , vol.55 , pp. 27-39
    • Kayne, P.S.1    Kim, U.J.2    Han, M.3    Mullen, J.R.4    Yoshizaki, F.5    Grunstein, M.6
  • 78
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • DOI 10.1038/nature06500, PII NATURE06500
    • Kim JE, Chen J, Lou Z (2008) DBC1 is a negative regulator of SIRT1. Nature 451:583-586 (Pubitemid 351186264)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 583-586
    • Kim, J.-E.1    Chen, J.2    Lou, Z.3
  • 79
    • 0019364691 scopus 로고
    • Regulation of transcription in expressed and unexpressed mating type cassettes of yeast
    • DOI 10.1038/289239a0
    • Klar AJ, Strathern JN, Borach JR, Hicks JB (1981) Regulation of transcription in expressed and unexpressed mating type cassettes of yeast. Nature 289:239-244 (Pubitemid 11180670)
    • (1981) Nature , vol.289 , Issue.5795 , pp. 239-244
    • Klar, A.J.S.1    Strathern, J.N.2    Broach, J.R.3    Hicks, J.B.4
  • 83
    • 0034735990 scopus 로고    scopus 로고
    • Role of NAD(+) in the deacetylase activity of the SIR2- like proteins
    • Landry J, Slama JT, Sternglanz R (2000) Role of NAD(+) in the deacetylase activity of the SIR2- like proteins. Biochem Biophys Res Commun 278:685-690
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 685-690
    • Landry, J.1    Slama, J.T.2    Sternglanz, R.3
  • 84
    • 0033565609 scopus 로고    scopus 로고
    • Role of yeast SIR genes and mating type in directing DNA double-strand breaks to homologous and non-homologous repair paths
    • DOI 10.1016/S0960-9822(99)80339-X
    • Lee SE, Paques F, Sylvan J, Haber JE (1999) Role of yeast SIR genes and mating type in directing DNA double-strand breaks to homologous and non-homologous repair paths. Curr Biol 9:767-770 (Pubitemid 29350858)
    • (1999) Current Biology , vol.9 , Issue.14 , pp. 767-770
    • Lee, S.E.1    Paques, F.2    Sylvan, J.3    Haber, J.E.4
  • 85
    • 32044435126 scopus 로고    scopus 로고
    • Coordination and communication between the p53 and IGF-1-AKT-TOR signal transduction pathways
    • DOI 10.1101/gad.1363206
    • Levine AJ, Feng Z, Mak TW, You H, Jin S (2006) Coordination and communication between the p53 and IGF-1-AKT-TOR signal transduction pathways. Genes Dev 20:267-275 (Pubitemid 43200281)
    • (2006) Genes and Development , vol.20 , Issue.3 , pp. 267-275
    • Levine, A.J.1    Feng, Z.2    Mak, T.W.3    You, H.4    Jin, S.5
  • 86
    • 34948883324 scopus 로고    scopus 로고
    • SIRT1 deacetylates and positively regulates the nuclear receptor LXR
    • DOI 10.1016/j.molcel.2007.07.032, PII S109727650700620X
    • Li X, Zhang S, Blander G, Tse JG, Krieger M, Guarente L (2007) SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol Cell 28:91-106 (Pubitemid 47531974)
    • (2007) Molecular Cell , vol.28 , Issue.1 , pp. 91-106
    • Li, X.1    Zhang, S.2    Blander, G.3    Tse, J.G.4    Krieger, M.5    Guarente, L.6
  • 87
    • 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, Ge Q, Gu W, Orren D, Luo J (2008a) Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation. J Biol Chem 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    Ge, Q.7    Gu, W.8    Orren, D.9    Luo, J.10
  • 88
    • 45549096918 scopus 로고    scopus 로고
    • SirT1 inhibition reduces IGF-I/IRS-2/Ras/ERK1/2 signaling and protects neurons
    • DOI 10.1016/j.cmet.2008.05.004, PII S1550413108001484
    • Li Y, Xu W, McBurney MW, Longo VD (2008b) SirT1 inhibition reduces IGF-I/IRS-2/ Ras/ERK1/2 signaling and protects neurons. Cell Metab 8:38-48 (Pubitemid 351859225)
    • (2008) Cell Metabolism , vol.8 , Issue.1 , pp. 38-48
    • Li, Y.1    Xu, W.2    McBurney, M.W.3    Longo, V.D.4
  • 89
    • 0034611728 scopus 로고    scopus 로고
    • ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway
    • DOI 10.1038/35007091
    • Lim DS, Kim ST, Xu B, Maser RS, Lin J, Petrini JH, Kastan MB (2000) ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway. Nature 404:613-617 (Pubitemid 30205060)
    • (2000) Nature , vol.404 , Issue.6778 , pp. 613-617
    • Lim, D.-S.1    Kim, S.-T.2    Xu, B.3    Maser, R.S.4    Lin, J.5    Petrini, J.H.J.6    Kastan, M.B.7
  • 90
    • 36549025835 scopus 로고    scopus 로고
    • Prevention of cardiovascular disease in high-risk individuals in low-income and middle-income countries: Health effects and costs
    • DOI 10.1016/S0140-6736(07)61699-7, PII S0140673607616997
    • Lim SS, Gaziano TA, Gakidou E, Reddy KS, Farzadfar F, Lozano R, Rodgers A (2007) Prevention of cardiovascular disease in high-risk individuals in low-income and middle-income countries: health effects and costs. Lancet 370:2054-2062 (Pubitemid 50007974)
    • (2007) Lancet , vol.370 , Issue.9604 , pp. 2054-2062
    • Lim, S.S.1    Gaziano, T.A.2    Gakidou, E.3    Reddy, K.S.4    Farzadfar, F.5    Lozano, R.6    Rodgers, A.7
  • 91
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha
    • Lim JH, Lee YM, Chun YS, Chen J, Kim JE, Park JW (2010) Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha. Mol Cell 38:864-878
    • (2010) Mol Cell , vol.38 , pp. 864-878
    • Lim, J.H.1    Lee, Y.M.2    Chun, Y.S.3    Chen, J.4    Kim, J.E.5    Park, J.W.6
  • 92
    • 33645774382 scopus 로고    scopus 로고
    • Increased life span due to calorie restriction in respiratory-deficient yeast
    • author reply e34
    • Lin SJ, Guarente L (2006) Increased life span due to calorie restriction in respiratory-deficient yeast. PLoS Genet 2:e33, author reply e34
    • (2006) PLoS Genet , vol.2
    • Lin, S.J.1    Guarente, L.2
  • 93
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • Lin SJ, Defossez PA, Guarente L (2000) Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289:2126-2128
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 95
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • DOI 10.1101/gad.1164804
    • Lin SJ, Ford E, Haigis M, Liszt G, Guarente L (2004) Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev 18:12-16 (Pubitemid 38090683)
    • (2004) Genes and Development , vol.18 , Issue.1 , pp. 12-16
    • Lin, S.-J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 96
    • 19344377042 scopus 로고    scopus 로고
    • Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation
    • DOI 10.1016/j.cell.2005.03.035, PII S0092867405003545
    • Liou GG, Tanny JC, Kruger RG, Walz T, Moazed D (2005) Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell 121:515-527 (Pubitemid 40720006)
    • (2005) Cell , vol.121 , Issue.4 , pp. 515-527
    • Liou, G.-G.1    Tanny, J.C.2    Kruger, R.G.3    Walz, T.4    Moazed, D.5
  • 97
    • 74549184412 scopus 로고    scopus 로고
    • The polarisome is required for segregation and retrograde transport of protein aggregates
    • Liu B, Larsson L, Caballero A, Hao X, Oling D, Grantham J, Nystrom T (2010) The polarisome is required for segregation and retrograde transport of protein aggregates. Cell 140:257-267
    • (2010) Cell , vol.140 , pp. 257-267
    • Liu, B.1    Larsson, L.2    Caballero, A.3    Hao, X.4    Oling, D.5    Grantham, J.6    Nystrom, T.7
  • 100
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • DOI 10.1016/j.cell.2006.07.002, PII S0092867406008920
    • Longo VD, Kennedy BK (2006) Sirtuins in aging and age-related disease. Cell 126:257-268 (Pubitemid 44092970)
    • (2006) Cell , vol.126 , Issue.2 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 101
    • 0031009829 scopus 로고    scopus 로고
    • Human Bcl-2 reverses survival defects in yeast lacking superoxide dismutase and delays death of wild-type yeast
    • DOI 10.1083/jcb.137.7.1581
    • Longo VD, Ellerby LM, Bredesen DE, Valentine JS, Gralla EB (1997) Human Bcl-2 reverses survival defects in yeast lacking superoxide dismutase and delays death of wild-type yeast. J Cell Biol 137:1581-1588 (Pubitemid 27282238)
    • (1997) Journal of Cell Biology , vol.137 , Issue.7 , pp. 1581-1588
    • Longo, V.D.1    Ellerby, L.M.2    Bredesen, D.E.3    Valentine, J.S.4    Gralla, E.B.5
  • 102
    • 0029591894 scopus 로고
    • Silencing and heritable domains of gene expression
    • Loo S, Rine J (1995) Silencing and heritable domains of gene expression. Annu Rev Cell Dev Biol 11:519-548
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 519-548
    • Loo, S.1    Rine, J.2
  • 103
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • DOI 10.1016/S0092-8674(01)00524-4
    • Luo J, Nikolaev AY, Imai S, Chen D, Su F, Shiloh A, Guarente L, Gu W (2001) Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107:137-148 (Pubitemid 33035941)
    • (2001) Cell , vol.107 , Issue.2 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.-I.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 104
    • 0037097940 scopus 로고    scopus 로고
    • Rap1-Sir4 binding independent of other Sir, yKu, or histone interactions initiates the assembly of telomeric heterochromatin in yeast
    • DOI 10.1101/gad.988802
    • Luo K, Vega-Palas MA, Grunstein M (2002) Rap1-Sir4 binding independent of other Sir, yKu, or histone interactions initiates the assembly of telomeric heterochromatin in yeast. Genes Dev 16:1528-1539 (Pubitemid 34686334)
    • (2002) Genes and Development , vol.16 , Issue.12 , pp. 1528-1539
    • Luo, K.1    Vega-Palas, M.A.2    Grunstein, M.3
  • 106
    • 33745496607 scopus 로고    scopus 로고
    • Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4
    • DOI 10.1016/j.molcel.2006.06.006, PII S1097276506004114
    • Maas NL, Miller KM, DeFazio LG, Toczyski DP (2006) Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4. Mol Cell 23:109-119 (Pubitemid 43963450)
    • (2006) Molecular Cell , vol.23 , Issue.1 , pp. 109-119
    • Maas, N.L.1    Miller, K.M.2    DeFazio, L.G.3    Toczyski, D.P.4
  • 107
    • 0033612287 scopus 로고    scopus 로고
    • Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast
    • DOI 10.1016/S0092-8674(00)80773-4
    • Martin SG, Laroche T, Suka N, Grunstein M, Gasser SM (1999) Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast. Cell 97:621-633 (Pubitemid 29256965)
    • (1999) Cell , vol.97 , Issue.5 , pp. 621-633
    • Martin, S.G.1    Laroche, T.2    Suka, N.3    Grunstein, M.4    Gasser, S.M.5
  • 108
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • DOI 10.1038/nature03714
    • Masumoto H, Hawke D, Kobayashi R, Verreault A (2005) A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436:294-298 (Pubitemid 41021284)
    • (2005) Nature , vol.436 , Issue.7048 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 111
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • DOI 10.1042/BJ20070140
    • Michan S, Sinclair D (2007) Sirtuins in mammals: insights into their biological function. Biochem J 404:1-13 (Pubitemid 46788079)
    • (2007) Biochemical Journal , vol.404 , Issue.1 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 114
    • 0033612189 scopus 로고    scopus 로고
    • MEC1-dependent redistribution of the Sir3 silencing protein from telomeres to DNA double-strand breaks
    • DOI 10.1016/S0092-8674(00)80772-2
    • Mills KD, Sinclair DA, Guarente L (1999) MEC1-dependent redistribution of the Sir3 silencing protein from telomeres to DNA double-strand breaks. Cell 97:609-620 (Pubitemid 29256964)
    • (1999) Cell , vol.97 , Issue.5 , pp. 609-620
    • Mills, K.D.1    Sinclair, D.A.2    Guarente, L.3
  • 115
    • 0030951007 scopus 로고    scopus 로고
    • Silent information regulator protein complexes in Saccharomyces cerevisiae: A SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3
    • DOI 10.1073/pnas.94.6.2186
    • Moazed D, Kistler A, Axelrod A, Rine J, Johnson AD (1997) Silent information regulator protein complexes in Saccharomyces cerevisiae: a SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3. Proc Natl Acad Sci USA 94:2186-2191 (Pubitemid 27136849)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.6 , pp. 2186-2191
    • Moazed, D.1    Kistler, A.2    Axelrod, A.3    Rine, J.4    Johnson, A.D.5
  • 116
    • 0004760134 scopus 로고
    • Life span of individual yeast cells
    • Mortimer RK, Johnston JR (1959) Life span of individual yeast cells. Nature 183:1751-1752
    • (1959) Nature , vol.183 , pp. 1751-1752
    • Mortimer, R.K.1    Johnston, J.R.2
  • 120
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead-dependent pathway
    • DOI 10.1126/science.1101731
    • Nemoto S, Fergusson MM, Finkel T (2004) Nutrient availability regulates SIRT1 through a forkhead-dependent pathway. Science 306:2105-2108 (Pubitemid 40007664)
    • (2004) Science , vol.306 , Issue.5704 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 121
    • 0037291214 scopus 로고    scopus 로고
    • +-dependent tubulin deacetylase
    • DOI 10.1016/S1097-2765(03)00038-8
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (2003) The human Sir2 ortholog, SIRT2, is an NAD(+)-dependent tubulin deacetylase. Mol Cell 11:437-444 (Pubitemid 36293837)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 126
    • 0035863153 scopus 로고    scopus 로고
    • A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast
    • DOI 10.1093/emboj/20.1.197
    • Perrod S, Cockell MM, Laroche T, Renauld H, Ducrest AL, Bonnard C, Gasser SM (2001) A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast. EMBO J 20:197-209 (Pubitemid 32099116)
    • (2001) EMBO Journal , vol.20 , Issue.1-2 , pp. 197-209
    • Perrod, S.1    Cockell, M.M.2    Laroche, T.3    Renauld, H.4    Ducrest, A.-L.5    Bonnard, C.6    Gasser, S.M.7
  • 127
    • 58149339917 scopus 로고    scopus 로고
    • Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity
    • Pfister JA, Ma C, Morrison BE, D'Mello SR (2008) Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity. PLoS One 3:e4090
    • (2008) PLoS One , vol.3
    • Pfister, J.A.1    Ma, C.2    Morrison, B.E.3    D'mello, S.R.4
  • 130
    • 0026536066 scopus 로고
    • Generation of mice carrying a mutant apolipoprotein e gene inactivated by gene targeting in embryonic stem cells
    • Piedrahita JA, Zhang SH, Hagaman JR, Oliver PM, Maeda N (1992) Generation of mice carrying a mutant apolipoprotein E gene inactivated by gene targeting in embryonic stem cells. Proc Natl Acad Sci USA 89:4471-4475
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4471-4475
    • Piedrahita, J.A.1    Zhang, S.H.2    Hagaman, J.R.3    Oliver, P.M.4    Maeda, N.5
  • 131
    • 0026725757 scopus 로고
    • Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells
    • Plump AS, Smith JD, Hayek T, Aalto-Setala K, Walsh A, Verstuyft JG, Rubin EM, Breslow JL (1992) Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells. Cell 71:343-353
    • (1992) Cell , vol.71 , pp. 343-353
    • Plump, A.S.1    Smith, J.D.2    Hayek, T.3    Aalto-Setala, K.4    Walsh, A.5    Verstuyft, J.G.6    Rubin, E.M.7    Breslow, J.L.8
  • 132
    • 47849088748 scopus 로고    scopus 로고
    • Emerging roles of SIRT1 in vascular endothelial homeostasis
    • Potente M, Dimmeler S (2008) Emerging roles of SIRT1 in vascular endothelial homeostasis. Cell Cycle 7:2117-2122 (Pubitemid 352036236)
    • (2008) Cell Cycle , vol.7 , Issue.14 , pp. 2117-2122
    • Potente, M.1    Dimmeler, S.2
  • 136
    • 34347338702 scopus 로고    scopus 로고
    • Adiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-Lα
    • DOI 10.1128/MCB.02279-06
    • Qiang L, Wang H, Farmer SR (2007) Adiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-L alpha. Mol Cell Biol 27:4698-4707 (Pubitemid 47016124)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.13 , pp. 4698-4707
    • Qiang, L.1    Wang, H.2    Farmer, S.R.3
  • 138
    • 74049161289 scopus 로고    scopus 로고
    • Calorie restriction reduces rDNA recombination independently of rDNA silencing
    • Riesen M, Morgan A (2009) Calorie restriction reduces rDNA recombination independently of rDNA silencing. Aging Cell 8:624-632
    • (2009) Aging Cell , vol.8 , pp. 624-632
    • Riesen, M.1    Morgan, A.2
  • 139
    • 0023340731 scopus 로고
    • Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae
    • Rine J, Herskowitz I (1987) Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae. Genetics 116:9-22
    • (1987) Genetics , vol.116 , pp. 9-22
    • Rine, J.1    Herskowitz, I.2
  • 140
    • 0037123765 scopus 로고    scopus 로고
    • Drosophila Sir2 is required for heterochromatic silencing and by euchromatic Hairy/E(Spl) bHLH repressors in segmentation and sex determination
    • DOI 10.1016/S0092-8674(02)00732-8
    • Rosenberg MI, Parkhurst SM (2002) Drosophila Sir2 is required for heterochromatic silencing and by euchromatic Hairy/E(Spl) bHLH repressors in segmentation and sex determination. Cell 109:447-458 (Pubitemid 34564472)
    • (2002) Cell , vol.109 , Issue.4 , pp. 447-458
    • Rosenberg, M.I.1    Parkhurst, S.M.2
  • 141
    • 0036324497 scopus 로고    scopus 로고
    • Ordered nucleation and spreading of silenced chromatin in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E02-03-0175
    • Rusche LN, Kirchmaier AL, Rine J (2002) Ordered nucleation and spreading of silenced chromatin in Saccharomyces cerevisiae. Mol Biol Cell 13:2207-2222 (Pubitemid 34831327)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.7 , pp. 2207-2222
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 142
    • 34247271282 scopus 로고    scopus 로고
    • +-dependent histone deacetylase that translocates to the mitochondria upon cellular stress
    • DOI 10.1101/gad.1527307
    • Scher MB, Vaquero A, Reinberg D (2007) SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev 21:920-928 (Pubitemid 46625641)
    • (2007) Genes and Development , vol.21 , Issue.8 , pp. 920-928
    • Scher, M.B.1    Vaquero, A.2    Reinberg, D.3
  • 144
    • 34748850786 scopus 로고    scopus 로고
    • Glucose Restriction Extends Caenorhabditis elegans Life Span by Inducing Mitochondrial Respiration and Increasing Oxidative Stress
    • DOI 10.1016/j.cmet.2007.08.011, PII S1550413107002562
    • Schulz TJ, Zarse K, Voigt A, Urban N, Birringer M, Ristow M (2007) Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress. Cell Metab 6:280-293 (Pubitemid 47468090)
    • (2007) Cell Metabolism , vol.6 , Issue.4 , pp. 280-293
    • Schulz, T.J.1    Zarse, K.2    Voigt, A.3    Urban, N.4    Birringer, M.5    Ristow, M.6
  • 145
    • 0035545802 scopus 로고    scopus 로고
    • Putting the stress on senescence
    • DOI 10.1016/S0955-0674(00)00278-7
    • Serrano M, Blasco MA (2001) Putting the stress on senescence. Curr Opin Cell Biol 13:748-753 (Pubitemid 33042736)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.6 , pp. 748-753
    • Serrano, M.1    Blasco, M.A.2
  • 146
    • 0038714132 scopus 로고    scopus 로고
    • Sir2 regulates histone H3 lysine 9 methylation and heterochromatin assembly in fission yeast
    • DOI 10.1016/S0960-9822(03)00489-5
    • Shankaranarayana GD, Motamedi MR, Moazed D, Grewal SI (2003) Sir2 regulates histone H3 lysine 9 methylation and heterochromatin assembly in fission yeast. Curr Biol 13:1240-1246 (Pubitemid 36872948)
    • (2003) Current Biology , vol.13 , Issue.14 , pp. 1240-1246
    • Shankaranarayana, G.D.1    Motamedi, M.R.2    Moazed, D.3    Grewal, S.I.S.4
  • 149
    • 0031459980 scopus 로고    scopus 로고
    • Extrachromosomal rDNA circles - A cause of aging in yeast
    • DOI 10.1016/S0092-8674(00)80493-6
    • Sinclair DA, Guarente L (1997) Extrachromosomal rDNA circles - a cause of aging in yeast. Cell 91:1033-1042 (Pubitemid 28027835)
    • (1997) Cell , vol.91 , Issue.7 , pp. 1033-1042
    • Sinclair, D.A.1    Guarente, L.2
  • 151
    • 0031056907 scopus 로고    scopus 로고
    • An unusual form of transcriptional silencing in yeast ribosomal DNA
    • Smith JS, Boeke JD (1997) An unusual form of transcriptional silencing in yeast ribosomal DNA. Genes Dev 11:241-254 (Pubitemid 27081899)
    • (1997) Genes and Development , vol.11 , Issue.2 , pp. 241-254
    • Smith, J.S.1    Boeke, J.D.2
  • 153
    • 34548615053 scopus 로고    scopus 로고
    • Calorie restriction extends the chronological lifespan of Saccharomyces cerevisiae independently of the Sirtuins
    • DOI 10.1111/j.1474-9726.2007.00326.x
    • Smith DL Jr, McClure JM, Matecic M, Smith JS (2007) Calorie restriction extends the chronological lifespan of Saccharomyces cerevisiae independently of the Sirtuins. Aging Cell 6: 649-662 (Pubitemid 47400047)
    • (2007) Aging Cell , vol.6 , Issue.5 , pp. 649-662
    • Smith Jr., D.L.1    McClure, J.M.2    Matecic, M.3    Smith, J.S.4
  • 154
    • 74049131893 scopus 로고    scopus 로고
    • Calorie restriction effects on silencing and recombination at the yeast rDNA
    • Smith DL Jr, Li C, Matecic M, Maqani N, Bryk M, Smith JS (2009) Calorie restriction effects on silencing and recombination at the yeast rDNA. Aging Cell 8:633-642
    • (2009) Aging Cell , vol.8 , pp. 633-642
    • Smith Jr., D.L.1    Li, C.2    Matecic, M.3    Maqani, N.4    Bryk, M.5    Smith, J.S.6
  • 155
    • 0033574603 scopus 로고    scopus 로고
    • Net1, a Sir2-associated nucleolar protein required for rDNA silencing and nucleolar integrity
    • Straight AF, Shou W, Dowd GJ, Turck CW, Deshaies RJ, Johnson AD, Moazed D (1999) Net1, a Sir2-associated nucleolar protein required for rDNA silencing and nucleolar integrity. Cell 97:245-256 (Pubitemid 29194275)
    • (1999) Cell , vol.97 , Issue.2 , pp. 245-256
    • Straight, A.F.1    Shou, W.2    Dowd, G.J.3    Turck, C.W.4    Deshaies, R.J.5    Johnson, A.D.6    Moazed, D.7
  • 157
    • 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
    • DOI 10.1016/S0006-291X(02)03020-6
    • Takata T, Ishikawa F (2003) 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 301:250-257 (Pubitemid 36268876)
    • (2003) Biochemical and Biophysical Research Communications , vol.301 , Issue.1 , pp. 250-257
    • Takata, T.1    Ishikawa, F.2
  • 158
    • 20344364883 scopus 로고    scopus 로고
    • Localized histone acetylation and deacetylation triggered by the homologous recombination pathway of double-strand DNA repair
    • DOI 10.1128/MCB.25.12.4903-4913.2005
    • Tamburini BA, Tyler JK (2005) Localized histone acetylation and deacetylation triggered by the homologous recombination pathway of double-strand DNA repair. Mol Cell Biol 25: 4903-4913 (Pubitemid 40781092)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.12 , pp. 4903-4913
    • Tamburini, B.A.1    Tyler, J.K.2
  • 160
    • 0035895275 scopus 로고    scopus 로고
    • Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product
    • DOI 10.1073/pnas.031563798
    • Tanny JC, Moazed D (2001) Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: evidence for acetyl transfer from substrate to an NAD breakdown product. Proc Natl Acad Sci USA 98:415-420 (Pubitemid 32105055)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.2 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 161
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny JC, Dowd GJ, Huang J, Hilz H, Moazed D (1999) An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99:735-745 (Pubitemid 30017644)
    • (1999) Cell , vol.99 , Issue.7 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 162
    • 38049115760 scopus 로고    scopus 로고
    • Hst3 is regulated by Mec1-dependent proteolysis and controls the S phase checkpoint and sister chromatid cohesion by deacetylating histone H3 at lysine 56
    • Thaminy S, Newcomb B, Kim J, Gatbonton T, Foss E, Simon J, Bedalov A (2007) Hst3 is regulated by Mec1-dependent proteolysis and controls the S phase checkpoint and sister chromatid cohesion by deacetylating histone H3 at lysine 56. J Biol Chem 282: 37805-37814
    • (2007) J Biol Chem , vol.282 , pp. 37805-37814
    • Thaminy, S.1    Newcomb, B.2    Kim, J.3    Gatbonton, T.4    Foss, E.5    Simon, J.6    Bedalov, A.7
  • 163
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • DOI 10.1038/35065638
    • Tissenbaum HA, Guarente L (2001) Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410:227-230 (Pubitemid 32216597)
    • (2001) Nature , vol.410 , Issue.6825 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 164
    • 0030964526 scopus 로고    scopus 로고
    • Silencing factors participate in DNA repair and rscombination in Saccharomyces cersvisiae
    • DOI 10.1038/42288
    • Tsukamoto Y, Kato J, Ikeda H (1997) Silencing factors participate in DNA repair and recombination in Saccharomyces cerevisiae. Nature 388:900-903 (Pubitemid 27377065)
    • (1997) Nature , vol.388 , Issue.6645 , pp. 900-903
    • Tsukamoto, Y.1    Kato, J.-I.2    Ikeda, H.3
  • 165
    • 64049090625 scopus 로고    scopus 로고
    • Sirt7-dependent inhibition of cell growth and proliferation might be instrumental to mediate tissue integrity during aging
    • Vakhrusheva O, Braeuer D, Liu Z, Braun T, Bober E (2008a) Sirt7-dependent inhibition of cell growth and proliferation might be instrumental to mediate tissue integrity during aging. J Physiol Pharmacol 59(suppl 9):201-212
    • (2008) J Physiol Pharmacol , vol.59 , Issue.SUPPL. 9 , pp. 201-212
    • Vakhrusheva, O.1    Braeuer, D.2    Liu, Z.3    Braun, T.4    Bober, E.5
  • 166
    • 41449083867 scopus 로고    scopus 로고
    • Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice
    • DOI 10.1161/CIRCRESAHA.107.164558
    • Vakhrusheva O, Smolka C, Gajawada P, Kostin S, Boettger T, Kubin T, Braun T, Bober E (2008b) Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ Res 102:703-710 (Pubitemid 351457857)
    • (2008) Circulation Research , vol.102 , Issue.6 , pp. 703-710
    • Vakhrusheva, O.1    Smolka, C.2    Gajawada, P.3    Kostin, S.4    Boettger, T.5    Kubin, T.6    Braun, T.7    Bober, E.8
  • 167
    • 34249281690 scopus 로고    scopus 로고
    • Stressing the role of FoxO proteins in lifespan and disease
    • DOI 10.1038/nrm2190, PII NRM2190
    • van der Horst A, Burgering BM (2007) Stressing the role of FoxO proteins in lifespan and disease. Nat Rev Mol Cell Biol 8:440-450 (Pubitemid 46809159)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.6 , pp. 440-450
    • Van Der Horst, A.1    Burgering, B.M.T.2
  • 171
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • DOI 10.1016/j.molcel.2004.08.031, PII S1097276504005180
    • Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D (2004) Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell 16: 93-105 (Pubitemid 39330155)
    • (2004) Molecular Cell , vol.16 , Issue.1 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 174
    • 77953386141 scopus 로고    scopus 로고
    • Local IGF-1 isoform protects cardiomyiocytes from hypertrophic and oxidative stresses via Sirt1 activity
    • Vinciguerra M, Santini MP, Claycomb WC, Ladurner AG, Rosenthal N (2009) Local IGF-1 isoform protects cardiomyiocytes from hypertrophic and oxidative stresses via Sirt1 activity. Aging 10:43-62
    • (2009) Aging , vol.10 , pp. 43-62
    • Vinciguerra, M.1    Santini, M.P.2    Claycomb, W.C.3    Ladurner, A.G.4    Rosenthal, N.5
  • 175
    • 28244475950 scopus 로고    scopus 로고
    • Overlapping and distinct functions for a Caenorhabditis elegans SIR2 and DAF-16/FOXO
    • DOI 10.1016/j.mad.2005.09.005, PII S0047637405002216
    • Wang Y, Tissenbaum HA (2006) Overlapping and distinct functions for a Caenorhabditis elegans SIR2 and DAF-16/FOXO. Mech Ageing Dev 127:48-56 (Pubitemid 41713513)
    • (2006) Mechanisms of Ageing and Development , vol.127 , Issue.1 , pp. 48-56
    • Wang, Y.1    Tissenbaum, H.A.2
  • 176
    • 17144416530 scopus 로고    scopus 로고
    • Differential gene up-regulation by hypoxia-inducible factor-1α and hypoxia-inducible factor-2α in HEK293T cells
    • Wang V, Davis DA, Haque M, Huang LE, Yarchoan R (2005) Differential gene up-regulation by hypoxia-inducible factor-1alpha and hypoxia-inducible factor-2alpha in HEK293T cells. Cancer Res 65:3299-3306 (Pubitemid 40524614)
    • (2005) Cancer Research , vol.65 , Issue.8 , pp. 3299-3306
    • Wang, V.1    Davis, D.A.2    Haque, M.3    Huang, L.E.4    Yarchoan, R.5
  • 178
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • DOI 10.1111/j.1474-9726.2007.00304.x
    • Wang F, Nguyen M, Qin FX, Tong Q (2007) SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6:505-514 (Pubitemid 47087055)
    • (2007) Aging Cell , vol.6 , Issue.4 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.-F.3    Tong, Q.4
  • 180
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • arburg O (1956) On respiratory impairment in cancer cells. Science 124:269-270
    • (1956) Science , vol.124 , pp. 269-270
  • 184
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong PC, Pardo CA, Borchelt DR, LeeMK, Copeland NG, Jenkins NA, Sisodia SS, Cleveland DW, Price DL (1995) An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14:1105-1116
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Leemk Copeland, N.G.4    Jenkins, N.A.5    Sisodia, S.S.6    Cleveland, D.W.7    Price, D.L.8
  • 186
    • 33847060910 scopus 로고    scopus 로고
    • Sirtuin regulates cigarette smoke-induced proinflammatory mediator release via RelA/p65 NF-kappaB in macrophages in vitro and in rat lungs in vivo: Implications for chronic inflammation and aging
    • Yang SR, Wright J, Bauter M, Seweryniak K, Kode A, Rahman I (2007) Sirtuin regulates cigarette smoke-induced proinflammatory mediator release via RelA/p65 NF-kappaB in macrophages in vitro and in rat lungs in vivo: implications for chronic inflammation and aging. Am J Physiol Lung Cell Mol Physiol 292:L567-L576
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.292
    • Yang, S.R.1    Wright, J.2    Bauter, M.3    Seweryniak, K.4    Kode, A.5    Rahman, I.6
  • 187
    • 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 (2009) The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability. Cell Cycle 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
  • 188
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase
    • DOI 10.1038/sj.emboj.7600244
    • Yeung F, Hoberg JE, Ramsey CS, Keller MD, Jones DR, Frye RA, Mayo MW (2004) Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J 23(12):2369-2380 (Pubitemid 38954844)
    • (2004) EMBO Journal , vol.23 , Issue.12 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6    Mayo, M.W.7
  • 191
    • 34250897968 scopus 로고    scopus 로고
    • SIRT1 regulates the function of the Nijmegen breakage syndrome protein
    • DOI 10.1016/j.molcel.2007.05.029, PII S1097276507003309
    • Yuan Z, Zhang X, Sengupta N, Lane WS, Seto E (2007) SIRT1 regulates the function of the Nijmegen breakage syndrome protein. Mol Cell 27:149-162 (Pubitemid 46991383)
    • (2007) Molecular Cell , vol.27 , Issue.1 , pp. 149-162
    • Yuan, Z.1    Zhang, X.2    Sengupta, N.3    Lane, W.S.4    Seto, E.5
  • 192
    • 65349096174 scopus 로고    scopus 로고
    • A c-Myc-SIRT1 feedback loop regulates cell growth and transformation
    • Yuan J, Minter-Dykhouse K, Lou Z (2009a) A c-Myc-SIRT1 feedback loop regulates cell growth and transformation. J Cell Biol 185:203-211
    • (2009) J Cell Biol , vol.185 , pp. 203-211
    • Yuan, J.1    Minter-Dykhouse, K.2    Lou, Z.3
  • 193
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan J, Pu M, Zhang Z, Lou Z (2009b) Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 8:1747-1753
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4
  • 194
    • 54149103338 scopus 로고    scopus 로고
    • Endothelium-specific overexpression of class III deacetylase SIRT1 decreases atherosclerosis in apolipoprotein E-deficient mice
    • Zhang QJ, Wang Z, Chen HZ, Zhou S, Zheng W, Liu G, Wei YS, Cai H, Liu DP, Liang CC (2008) Endothelium-specific overexpression of class III deacetylase SIRT1 decreases atherosclerosis in apolipoprotein E-deficient mice. Cardiovasc Res 80:191-199
    • (2008) Cardiovasc Res , vol.80 , pp. 191-199
    • Zhang, Q.J.1    Wang, Z.2    Chen, H.Z.3    Zhou, S.4    Zheng, W.5    Liu, G.6    Wei, Y.S.7    Cai, H.8    Liu, D.P.9    Liang, C.C.10
  • 197
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • DOI 10.1038/nature06515, PII NATURE06515
    • Zhao W, Kruse JP, Tang Y, Jung SY, Qin J, Gu W (2008) Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451:587-590 (Pubitemid 351186268)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 587-590
    • Zhao, W.1    Kruse, J.-P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.