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Volumn 3 MAY, Issue , 2012, Pages

SIRT2 as a therapeutic target for age-related disorders

Author keywords

Aging; Cancer; Metabolic syndrome; Neurodegenerative disorder; SIRT2

Indexed keywords

ALPHA SYNUCLEIN; AUTOPHAGY PROTEIN 5; CYTOPLASM PROTEIN; PHOSPHOENOLPYRUVATE CARBOXYKINASE 1; PROTEOLIPID PROTEIN; SILENT INFORMATION REGULATOR PROTEIN 2; SIRTUIN 1; SIRTUIN 2; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR FKHRL1; UNCLASSIFIED DRUG;

EID: 84866013044     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2012.00082     Document Type: Article
Times cited : (110)

References (91)
  • 2
    • 3142548829 scopus 로고    scopus 로고
    • Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10
    • Bae, N. S., Swanson, M. J., Vassilev, A., and Howard, B. H. (2004). Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10. J. Biochem. 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
  • 3
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates, G. (2003). Huntingtin aggregation and toxicity in Huntington's disease. Lancet 361, 1642-1644.
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 5
    • 55049117907 scopus 로고    scopus 로고
    • The SIRT2 deacetylase regulates autoacetylation of p300
    • Black, J. C., Mosley, A., Kitada, T., Washburn, M., and Carey, M. (2008). The SIRT2 deacetylase regulates autoacetylation of p300. Mol. Cell 32, 449-455.
    • (2008) Mol. Cell , vol.32 , pp. 449-455
    • Black, J.C.1    Mosley, A.2    Kitada, T.3    Washburn, M.4    Carey, M.5
  • 6
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G., and Guarente, L. (2004). The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 73, 417-435.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 7
    • 80054782483 scopus 로고    scopus 로고
    • The dual role of sirtuins in cancer
    • Bosch-Presegue, L., and Vaquero, A.. (2011). The dual role of sirtuins in cancer. Genes Cancer 2, 648-662.
    • (2011) Genes Cancer , vol.2 , pp. 648-662
    • Bosch-Presegue, L.1    Vaquero, A.2
  • 9
    • 41849128523 scopus 로고    scopus 로고
    • The FoxO code
    • Calnan, D. R., and Brunet, A. (2008). The FoxO code. Oncogene 27, 2276-2288.
    • (2008) Oncogene , vol.27 , pp. 2276-2288
    • Calnan, D.R.1    Brunet, A.2
  • 10
    • 33846583673 scopus 로고    scopus 로고
    • SIR2: a potential target for calorie restriction mimetics
    • Chen, D., and Guarente, L. (2007). SIR2: a potential target for calorie restriction mimetics. Trends Mol. Med. 13, 64-71.
    • (2007) Trends Mol. Med. , vol.13 , pp. 64-71
    • Chen, D.1    Guarente, L.2
  • 11
    • 28844469898 scopus 로고    scopus 로고
    • Increase in activity during calorie restriction requires Sirt1
    • Chen, D., Steele, A. D., Lindquist, S., and Guarente, L. (2005). Increase in activity during calorie restriction requires Sirt1. Science 310, 1641.
    • (2005) Science , vol.310 , pp. 1641
    • Chen, D.1    Steele, A.D.2    Lindquist, S.3    Guarente, L.4
  • 13
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das, C., Lucia, M. S., Hansen, K. C., and Tyler, J. K. (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
  • 15
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A. S., and Tainsky, M. A. (2003). Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol. 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
  • 16
    • 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., and Guarente, L. (2006). Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev. 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
  • 17
    • 0037116641 scopus 로고    scopus 로고
    • Prevalence of the metabolic syndrome among US adults: findings from the third National Health and Nutrition Examination Survey
    • Ford, E. S., Giles,W. H., and Dietz,W. H. (2002). Prevalence of the metabolic syndrome among US adults: findings from the third National Health and Nutrition Examination Survey. JAMA 287, 356-359.
    • (2002) JAMA , vol.287 , pp. 356-359
    • Ford, E.S.1    Giles, W.H.2    Dietz, W.H.3
  • 18
    • 23744443327 scopus 로고    scopus 로고
    • Nosology of Parkinson's disease: looking for the way out of a quagmire
    • Forman, M. S., Lee, V. M., and Trojanowski, J. Q. (2005). Nosology of Parkinson's disease: looking for the way out of a quagmire. Neuron 47, 479-482
    • (2005) Neuron , vol.47 , pp. 479-482
    • Forman, M.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 19
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye, R. A. (2000). Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273, 793-798.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 20
    • 0032937059 scopus 로고    scopus 로고
    • Diagnostic criteria for Parkinson disease
    • Gelb, D. J., Oliver, E., and Gilman, S. (1999). Diagnostic criteria for Parkinson disease. Arch. Neurol. 56, 33-39
    • (1999) Arch. Neurol. , vol.56 , pp. 33-39
    • Gelb, D.J.1    Oliver, E.2    Gilman, S.3
  • 21
    • 33845868198 scopus 로고    scopus 로고
    • Sirtuins as potential targets for metabolic syndrome
    • Guarente, L. (2006). Sirtuins as potential targets for metabolic syndrome. Nature 444, 868-874
    • (2006) Nature , vol.444 , pp. 868-874
    • Guarente, L.1
  • 22
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction
    • Haigis, M. C., and Guarente, L. P. (2006). Mammalian sirtuins emerging roles in physiology, aging, and calorie restriction. Genes Dev. 20, 2913-2921
    • (2006) Genes Dev , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 23
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: biological insights and disease relevance
    • Haigis, M. C., and Sinclair, D. A. (2010). Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253-295
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 25
    • 77149172855 scopus 로고    scopus 로고
    • SIRT2-mediated protein deacetylation: An emerging key regulator in brain physiology and pathology
    • Harting, K., and Knoll, B. (2010). SIRT2-mediated protein deacetylation: An emerging key regulator in brain physiology and pathology. Eur. J. Cell Biol. 89, 262-269
    • (2010) Eur. J. Cell Biol. , vol.89 , pp. 262-269
    • Harting, K.1    Knoll, B.2
  • 26
    • 25844457693 scopus 로고    scopus 로고
    • Obesity
    • Haslam, D. W., and James, W. P. (2005). Obesity. Lancet 366, 1197-1209
    • (2005) Lancet , vol.366 , pp. 1197-1209
    • Haslam, D.W.1    James, W.P.2
  • 28
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C. M., Kaeberlein, M., and Guarente, L. (2000). Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 29
    • 34248151365 scopus 로고    scopus 로고
    • The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation
    • Inoue, T., Hiratsuka, M., Osaki, M., and Oshimura, M. (2007). The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation. Cell Cycle 6, 1011-1018
    • (2007) Cell Cycle , vol.6 , pp. 1011-1018
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Oshimura, M.4
  • 30
    • 0034683226 scopus 로고    scopus 로고
    • Accumulation of human alphasynuclein in different cytoskeletons in Lewy bodies in brains of dementia with Lewy bodies
    • Iseki, E., Marui, W., Sawada, H., Ueda, K., and Kosaka, K. (2000). Accumulation of human alphasynuclein in different cytoskeletons in Lewy bodies in brains of dementia with Lewy bodies. Neurosci. Lett. 290, 41-44
    • (2000) Neurosci. Lett. , vol.290 , pp. 41-44
    • Iseki, E.1    Marui, W.2    Sawada, H.3    Ueda, K.4    Kosaka, K.5
  • 31
    • 79959906869 scopus 로고    scopus 로고
    • Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase
    • Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K. L., and Zhao, S. (2011). Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol. Cell 43, 33-44
    • (2011) Mol. Cell , vol.43 , pp. 33-44
    • Jiang, W.1    Wang, S.2    Xiao, M.3    Lin, Y.4    Zhou, L.5    Lei, Q.6    Xiong, Y.7    Guan, K.L.8    Zhao, S.9
  • 33
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation
    • Jing, E., Gesta, S., and Kahn, C. R. (2007). SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab. 6, 105-114
    • (2007) Cell Metab , vol.6 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 34
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., Mcvey, M., and 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
    • (1999) Genes Dev , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    Mcvey, M.2    Guarente, L.3
  • 37
    • 0037312020 scopus 로고    scopus 로고
    • How does calorie restriction work?
    • Koubova, J., and Guarente, L. (2003). How does calorie restriction work? Genes Dev. 17, 313-321
    • (2003) Genes Dev , vol.17 , pp. 313-321
    • Koubova, J.1    Guarente, L.2
  • 38
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy:ubiquitin-mediated recognition and beyond
    • Kraft, C., Peter, M., and Hofmann, K. (2010). Selective autophagy:ubiquitin-mediated recognition and beyond. Nat. Cell Biol. 12, 836-841.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 43
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alphatubulin
    • Li, W., Zhang, B., Tang, J., Cao, Q., Wu, Y., Wu, C., Guo, J., Ling, E. A., and Liang, F. (2007). Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alphatubulin. J. Neurosci. 27, 2606-2616.
    • (2007) J. Neurosci. , vol.27 , pp. 2606-2616
    • Li, W.1    Zhang, B.2    Tang, J.3    Cao, Q.4    Wu, Y.5    Wu, C.6    Guo, J.7    Ling, E.A.8    Liang, F.9
  • 44
    • 78650638268 scopus 로고    scopus 로고
    • SIRT2 down-regulation in HeLa can induce p53 accumulation via p38 MAPK activation-dependent p300 decrease, eventually leading to apoptosis
    • Li, Y., Matsumori, H., Nakayama, Y., Osaki, M., Kojima, H., Kurimasa, A., Ito, H., Mori, S., Katoh, M., Oshimura, M., and Inoue, T. (2011). SIRT2 down-regulation in HeLa can induce p53 accumulation via p38 MAPK activation-dependent p300 decrease, eventually leading to apoptosis. Genes Cells 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    Ito, H.7    Mori, S.8    Katoh, M.9    Oshimura, M.10    Inoue, T.11
  • 45
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin, S. J., Ford, E., Haigis, M., Liszt, G., and Guarente, L. (2004). Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev. 18, 12-16
    • (2004) Genes Dev , vol.18 , pp. 12-16
    • Lin, S.J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 46
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADPribosyltransferase
    • Liszt, G., Ford, E., Kurtev, M., and Guarente, L. (2005). Mouse Sir2 homolog SIRT6 is a nuclear ADPribosyltransferase. J. Biol. Chem. 280, 21313-21320
    • (2005) J. Biol. Chem. , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 48
    • 33645299025 scopus 로고    scopus 로고
    • Ageing and neuronal vulnerability
    • Mattson, M. P., and Magnus, T. (2006). Ageing and neuronal vulnerability. Nat. Rev. Neurosci. 7, 278-294
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 278-294
    • Mattson, M.P.1    Magnus, T.2
  • 50
    • 13544253065 scopus 로고    scopus 로고
    • Metabolic syndrome: a clinical and molecular perspective
    • Moller, D. E., and Kaufman, K. D. (2005). Metabolic syndrome: a clinical and molecular perspective. Annu. Rev. Med. 56, 45-62
    • (2005) Annu. Rev. Med. , vol.56 , pp. 45-62
    • Moller, D.E.1    Kaufman, K.D.2
  • 51
    • 34547920351 scopus 로고    scopus 로고
    • Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin
    • Nahhas, F., Dryden, S. C., Abrams, J., and Tainsky, M. A. (2007). Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin. Mol. Cell. Biochem. 303, 221-230
    • (2007) Mol. Cell. Biochem. , vol.303 , pp. 221-230
    • Nahhas, F.1    Dryden, S.C.2    Abrams, J.3    Tainsky, M.A.4
  • 52
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa, T., Lomb, D. J., Haigis, M. C., and Guarente, L. (2009). SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137, 560-570
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 53
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., and Verdin, E. (2003). The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11, 437-444
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 54
    • 39149122568 scopus 로고    scopus 로고
    • Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis
    • doi:10.1371/journal.pone.0000784
    • North, B. J., and Verdin, E. (2007a). Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis. PLoS ONE 2, e784. doi:10.1371/journal.pone.0000784
    • (2007) PLoS ONE , vol.2
    • North, B.J.1    Verdin, E.2
  • 55
    • 34547098165 scopus 로고    scopus 로고
    • Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation
    • North, B. J., and Verdin, E. (2007b). Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation. J. Biol. Chem. 282, 19546-19555
    • (2007) J. Biol. Chem , vol.282 , pp. 19546-19555
    • North, B.J.1    Verdin, E.2
  • 57
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos, J., Bodai, L., Lukacsovich, T., Purcell, J. M., Steffan, J. S., Thompson, L. M., and Marsh, J. L. (2008). Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum. Mol. Genet. 17, 3767-3775
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3    Purcell, J.M.4    Steffan, J.S.5    Thompson, L.M.6    Marsh, J.L.7
  • 59
    • 0035500991 scopus 로고    scopus 로고
    • Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells
    • Payton, J. E., Perrin, R. J., Clayton, D. F., and George, J. M. (2001). Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells. Brain Res. Mol. Brain Res. 95, 138-145
    • (2001) Brain Res. Mol. Brain Res. , vol.95 , pp. 138-145
    • Payton, J.E.1    Perrin, R.J.2    Clayton, D.F.3    George, J.M.4
  • 60
    • 0035863153 scopus 로고    scopus 로고
    • A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast
    • Perrod, S., Cockell, M. M., Laroche, T., Renauld, H., Ducrest, A. L., Bonnard, C., and Gasser, S. M. (2001). A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast. EMBO J. 20, 197-209.
    • (2001) EMBO J , vol.20 , 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
  • 64
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina, B., and Helfand, S. L. (2004). Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. U.S.A. 101, 15998-16003
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 65
    • 78649738291 scopus 로고    scopus 로고
    • SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310
    • Rothgiesser, K. M., Erener, S., Waibel, S., Luscher, B., and Hottiger, M. O. (2010). SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310. J. Cell Sci. 123, 4251-4258
    • (2010) J. Cell Sci. , vol.123 , pp. 4251-4258
    • Rothgiesser, K.M.1    Erener, S.2    Waibel, S.3    Luscher, B.4    Hottiger, M.O.5
  • 66
    • 67651207793 scopus 로고    scopus 로고
    • NF-kappaB signaling in the aging process
    • Salminen, A., and Kaarniranta, K. (2009). NF-kappaB signaling in the aging process. J. Clin. Immunol. 29, 397-405
    • (2009) J. Clin. Immunol. , vol.29 , pp. 397-405
    • Salminen, A.1    Kaarniranta, K.2
  • 67
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi, T., Wang, F., Stieren, E., and Tong, Q. (2005). SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem. 280, 13560-13567
    • (2005) J. Biol. Chem. , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 68
    • 0031459980 scopus 로고    scopus 로고
    • Extrachromosomal rDNA circles-a cause of aging in yeast
    • Sinclair, D. A., and Guarente, L. (1997). Extrachromosomal rDNA circles a cause of aging in yeast. Cell 91, 1033-1042
    • (1997) Cell , vol.91 , pp. 1033-1042
    • Sinclair, D.A.1    Guarente, L.2
  • 70
    • 33846930889 scopus 로고    scopus 로고
    • Microtubule deacetylases, SirT2 and HDAC6, in the nervous system
    • Southwood, C. M., Peppi, M., Dryden, S., Tainsky, M. A., and Gow, A. (2007). Microtubule deacetylases, SirT2 and HDAC6, in the nervous system. Neurochem. Res. 32, 187-195
    • (2007) Neurochem. Res. , vol.32 , pp. 187-195
    • Southwood, C.M.1    Peppi, M.2    Dryden, S.3    Tainsky, M.A.4    Gow, A.5
  • 72
    • 40049093522 scopus 로고    scopus 로고
    • SIRT2, tubulin deacetylation, and oligodendroglia differentiation
    • Tang, B. L., and Chua, C. E. (2008). SIRT2, tubulin deacetylation, and oligodendroglia differentiation. Cell Motil. Cytoskeleton 65, 179-182
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 179-182
    • Tang, B.L.1    Chua, C.E.2
  • 73
    • 0034687694 scopus 로고    scopus 로고
    • Silent information regulator 2 family of NADdependent histone/protein deacetylases generates a unique product 1-O-acetyl-ADP-ribose
    • Tanner, K. G., Landry, J., Sternglanz, R., and Denu, J. M. (2000). Silent information regulator 2 family of NADdependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc. Natl. Acad. Sci. U.S.A. 97, 14178-14182
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 76
    • 67349216689 scopus 로고    scopus 로고
    • The non-apoptotic role of p53 in neuronal biology: enlightening the dark side of the moon
    • Tedeschi,A.,and Di Giovanni,S. (2009). The non-apoptotic role of p53 in neuronal biology: enlightening the dark side of the moon. EMBO Rep. 10, 576-583
    • (2009) EMBO Rep , vol.10 , pp. 576-583
    • Tedeschi, A.1    Di Giovanni, S.2
  • 77
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum, H. A., and Guarente, L. (2001). Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410, 227-230
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 78
    • 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., and Reinberg, D. (2004). Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell 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
  • 80
    • 80053134340 scopus 로고    scopus 로고
    • Regulation of Caenorhabditis elegans lifespan by sir-2
    • Viswanathan, M., and Guarente, L. (2011). Regulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes. Nature 477, E1-E2
    • (2011) 1 transgenes. Nature , vol.477
    • Viswanathan, M.1    Guarente, L.2
  • 81
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein, B., and Kinzler, K. W. (2004). Cancer genes and the pathways they control. Nat. Med. 10, 789-799
    • (2004) Nat. Med. , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 83
    • 84858795617 scopus 로고    scopus 로고
    • Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation
    • Wang, F., Chan, C. H., Chen, K., Guan, X., Lin, H. K., and Tong, Q. (2012). Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation. Oncogene 31, 1546-1557
    • (2012) Oncogene , vol.31 , pp. 1546-1557
    • Wang, F.1    Chan, C.H.2    Chen, K.3    Guan, X.4    Lin, H.K.5    Tong, Q.6
  • 84
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang, F., Nguyen, M., Qin, F. X., and Tong, Q. (2007). SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6, 505-514
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 85
    • 64049089450 scopus 로고    scopus 로고
    • SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma
    • Wang, F., and Tong, Q. (2009). SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma. Mol. Biol. Cell 20, 801-808
    • (2009) Mol. Biol. Cell , vol.20 , pp. 801-808
    • Wang, F.1    Tong, Q.2
  • 87
    • 77954116814 scopus 로고    scopus 로고
    • Autophagygoneawryinneurodegenerative diseases
    • Wong, E., and Cuervo, A. M. (2010). Autophagygoneawryinneurodegenerative diseases. Nat. Neurosci. 13, 805-811.
    • (2010) Nat. Neurosci. , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 88
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., and Mayo, M. W. (2004). Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23, 2369-2380.
    • (2004) EMBO J , vol.23 , 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
  • 89
    • 77957652556 scopus 로고    scopus 로고
    • Anti-neoplastic activity of the cytosolic FoxO1 results from autophagic cell death
    • Zhao, Y., Wang, L., Yang, J., Zhang, P., Ma, K., Zhou, J., Liao, W., and Zhu, W. G. (2010a). Anti-neoplastic activity of the cytosolic FoxO1 results from autophagic cell death. Autophagy 6, 988-990.
    • (2010) Autophagy , vol.6 , pp. 988-990
    • Zhao, Y.1    Wang, L.2    Yang, J.3    Zhang, P.4    Ma, K.5    Zhou, J.6    Liao, W.7    Zhu, W.G.8
  • 90
    • 77954225200 scopus 로고    scopus 로고
    • Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity
    • Zhao, Y., Yang, J., Liao, W., Liu, X., Zhang, H., Wang, S., Wang, D., Feng, J., Yu, L., and Zhu, W. G. (2010b). Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity. Nat. Cell Biol. 12, 665-675.
    • (2010) Nat. Cell Biol , vol.12 , pp. 665-675
    • Zhao, Y.1    Yang, J.2    Liao, W.3    Liu, X.4    Zhang, H.5    Wang, S.6    Wang, D.7    Feng, J.8    Yu, L.9    Zhu, W.G.10
  • 91
    • 81155155536 scopus 로고    scopus 로고
    • The QKI-PLP pathway controls SIRT2 abundance in CNS myelin
    • Zhu, H., Zhao, L., Wang, E., Dimova, N., Liu, G., Feng, Y., and Cambi, F. (2012). The QKI-PLP pathway controls SIRT2 abundance in CNS myelin. Glia 60, 69-82.
    • (2012) Glia , vol.60 , pp. 69-82
    • Zhu, H.1    Zhao, L.2    Wang, E.3    Dimova, N.4    Liu, G.5    Feng, Y.6    Cambi, F.7


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