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Volumn 5, Issue SEP, 2013, Pages

Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration

Author keywords

Aging; Antioxidants; Caloric restriction; Mitochondria; Neurodegeneration; Neuroprotection; SIRT3

Indexed keywords

MITOCHONDRIAL PERMEABILITY TRANSITION PORE; REACTIVE OXYGEN METABOLITE; SIRTUIN 3;

EID: 84895835925     PISSN: None     EISSN: 16634365     Source Type: Journal    
DOI: 10.3389/fnagi.2013.00048     Document Type: Review
Times cited : (267)

References (139)
  • 1
    • 2342496712 scopus 로고    scopus 로고
    • FoxOs at the crossroads of cellular metabolism, differentiation, and transformation
    • doi: 10.1016/S0092-8674(04)00452-0
    • Accili, D., and Arden, K. C. (2004). FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell 117, 421-426. doi: 10.1016/S0092-8674(04)00452-0.
    • (2004) Cell , vol.117 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 2
    • 55749084738 scopus 로고    scopus 로고
    • A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • doi: 10.1073/pnas.0803790105
    • Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., et al. (2008). A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc. Natl. Acad. Sci. U.S.A. 105, 14447-14452. doi: 10.1073/pnas.0803790105.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14447-14452
    • Ahn, B.-H.1    Kim, H.-S.2    Song, S.3    Lee, I.H.4    Liu, J.5    Vassilopoulos, A.6
  • 3
    • 2442624618 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1-mediated cell death in astrocytes requires NAD+ depletion and mitochondrial permeability transition
    • doi: 10.1074/jbc. M313329200
    • Alano, C. C., Ying, W., and Swanson, R. A. (2004). Poly(ADP-ribose) polymerase-1-mediated cell death in astrocytes requires NAD+ depletion and mitochondrial permeability transition. J. Biol. Chem. 279, 18895-18902. doi: 10.1074/jbc. M313329200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18895-18902
    • Alano, C.C.1    Ying, W.2    Swanson, R.A.3
  • 4
    • 3042802690 scopus 로고    scopus 로고
    • Glutathione: an overview of biosynthesis and modulation
    • doi: 10.1016/S0009-2797(97)00146-4.
    • Anderson, M. E. (1998). Glutathione: an overview of biosynthesis and modulation. Chem. Biol. Interact. 111-112, 1-14. doi: 10.1016/S0009-2797(97)00146-4.
    • (1998) Chem. Biol. Interact. , vol.111-112 , pp. 1-14
    • Anderson, M.E.1
  • 5
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • doi: 10.1074/jbc. M505970200
    • Arnoult, D., Grodet, A., Lee, Y.-J., Estaquier, J., and Blackstone, C. (2005). Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J. Biol. Chem. 280, 35742-35750. doi: 10.1074/jbc. M505970200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.-J.3    Estaquier, J.4    Blackstone, C.5
  • 6
    • 79953752384 scopus 로고    scopus 로고
    • PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation
    • doi: 10.1016/j.cmet.2011.03.004
    • Bai, P., Cantó, C., Oudart, H., Brunyánszki, A., Cen, Y., Thomas, C., et al. (2011). PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation. Cell Metab. 13, 461-468. doi: 10.1016/j.cmet.2011.03.004.
    • (2011) Cell Metab. , vol.13 , pp. 461-468
    • Bai, P.1    Cantó, C.2    Oudart, H.3    Brunyánszki, A.4    Cen, Y.5    Thomas, C.6
  • 7
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • doi: 10.1016/j.cell.2005.02.001
    • Balaban, R. S., Nemoto, S., and Finkel, T. (2005). Mitochondria, oxidants, and aging. Cell 120, 483-495. doi: 10.1016/j.cell.2005.02.001.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 8
    • 19944433088 scopus 로고    scopus 로고
    • A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages
    • doi: 10.1016/j.ygeno.2004.11.003
    • Bellizzi, D., Rose, G., Cavalcante, P., Covello, G., Dato, S., De Rango, F., et al. (2005). A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages. Genomics 85, 258-263. doi: 10.1016/j.ygeno.2004.11.003.
    • (2005) Genomics , vol.85 , pp. 258-263
    • Bellizzi, D.1    Rose, G.2    Cavalcante, P.3    Covello, G.4    Dato, S.5    De Rango, F.6
  • 10
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: channels, exchangers, and permeability transition
    • Bernardi, P. (1999). Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 79, 1127-1155.
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 11
    • 33847746679 scopus 로고    scopus 로고
    • Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system
    • doi: 10.1152/ajpheart.01162.2006
    • Berndt, C., Lillig, C. H., and Holmgren, A. (2007). Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am. J. Physiol. Heart Circ. Physiol. 292, H1227-H1236. doi: 10.1152/ajpheart.01162.2006.
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 12
    • 0036629251 scopus 로고    scopus 로고
    • Cell cycle and death control: long live Forkheads
    • doi: 10.1016/S0968-0004(02)02113-8
    • Burgering, B. M. T., and Kops, G. J. P. L. (2002). Cell cycle and death control: long live Forkheads. Trends Biochem. Sci. 27, 352-360. doi: 10.1016/S0968-0004(02)02113-8.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 352-360
    • Burgering, B.M.T.1    Kops, G.J.P.L.2
  • 13
    • 84858153162 scopus 로고    scopus 로고
    • Cellular stress responses, hormetic phytochemicals and vitagenes in aging and longevity
    • doi: 10.1016/j.bbadis.2011.11.002
    • Calabrese, V., Cornelius, C., Dinkova-Kostova, A. T., Iavicoli, I., Di Paola, R., Koverech, A., et al. (2012). Cellular stress responses, hormetic phytochemicals and vitagenes in aging and longevity. Biochim. Biophys. Acta 1822, 753-783. doi: 10.1016/j.bbadis.2011.11.002.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 753-783
    • Calabrese, V.1    Cornelius, C.2    Dinkova-Kostova, A.T.3    Iavicoli, I.4    Di Paola, R.5    Koverech, A.6
  • 14
    • 46249100836 scopus 로고    scopus 로고
    • Tissue-specific regulation of SIRT1 by calorie restriction
    • doi: 10.1101/gad.1650608
    • Chen, D., Bruno, J., Easlon, E., Lin, S.-J., Cheng, H.-L., Alt, F. W., et al. (2008). Tissue-specific regulation of SIRT1 by calorie restriction. Genes Dev. 22, 1753-1757. doi: 10.1101/gad.1650608.
    • (2008) Genes Dev. , vol.22 , pp. 1753-1757
    • Chen, D.1    Bruno, J.2    Easlon, E.3    Lin, S.-J.4    Cheng, H.-L.5    Alt, F.W.6
  • 15
    • 84881076472 scopus 로고    scopus 로고
    • Interaction of Sirt3 with OGG1 contributes to repair of mitochondrial DNA and protects from apoptotic cell death under oxidative stress
    • doi: 10.1038/cddis.2013.254
    • Cheng, Y., Ren, X., Gowda, A. S., Shan, Y., Zhang, L., Yuan, Y.-S., et al. (2013). Interaction of Sirt3 with OGG1 contributes to repair of mitochondrial DNA and protects from apoptotic cell death under oxidative stress. Cell Death Dis. 4, e731. doi: 10.1038/cddis.2013.254.
    • (2013) Cell Death Dis. , vol.4
    • Cheng, Y.1    Ren, X.2    Gowda, A.S.3    Shan, Y.4    Zhang, L.5    Yuan, Y.-S.6
  • 16
    • 79959567900 scopus 로고    scopus 로고
    • Reduced mitochondrial function in obesity-associated fatty liver: SIRT3 takes on the fat
    • Choudhury, M., Jonscher, K. R., and Friedman, J. E. (2011). Reduced mitochondrial function in obesity-associated fatty liver: SIRT3 takes on the fat. Aging (Albany NY) 3, 175-178.
    • (2011) Aging (Albany NY) , vol.3 , pp. 175-178
    • Choudhury, M.1    Jonscher, K.R.2    Friedman, J.E.3
  • 17
    • 63749099484 scopus 로고    scopus 로고
    • A new splice variant of the mouse SIRT3 gene encodes the mitochondrial precursor protein
    • doi: 10.1371/journal.pone.0004986
    • Cooper, H. M., Huang, J.-Y., Verdin, E., and Spelbrink, J. N. (2009). A new splice variant of the mouse SIRT3 gene encodes the mitochondrial precursor protein. PLoS ONE 4:e4986. doi: 10.1371/journal.pone.0004986.
    • (2009) PLoS ONE , vol.4
    • Cooper, H.M.1    Huang, J.-Y.2    Verdin, E.3    Spelbrink, J.N.4
  • 18
    • 42449132299 scopus 로고    scopus 로고
    • The human SIRT3 protein deacetylase is exclusively mitochondrial
    • doi: 10.1042/BJ20071624
    • Cooper, H. M., and Spelbrink, J. N. (2008). The human SIRT3 protein deacetylase is exclusively mitochondrial. Biochem. J. 411, 279-285. doi: 10.1042/BJ20071624.
    • (2008) Biochem. J. , vol.411 , pp. 279-285
    • Cooper, H.M.1    Spelbrink, J.N.2
  • 19
    • 80051508807 scopus 로고    scopus 로고
    • Midlife vascular risk factor exposure accelerates structural brain aging and cognitive decline
    • doi: 10.1212/WNL.0b013e318227b227
    • Debette, S., Seshadri, S., Beiser, A., Au, R., Himali, J. J., Palumbo, C., et al. (2011). Midlife vascular risk factor exposure accelerates structural brain aging and cognitive decline. Neurology 77, 461-468. doi: 10.1212/WNL.0b013e318227b227.
    • (2011) Neurology , vol.77 , pp. 461-468
    • Debette, S.1    Seshadri, S.2    Beiser, A.3    Au, R.4    Himali, J.J.5    Palumbo, C.6
  • 20
    • 84857739664 scopus 로고    scopus 로고
    • Sirtuin 4 identification in normal human epidermal keratinocytes and its relation to sirtuin 3 and energy metabolism under normal conditions and UVB-induced stress
    • doi: 10.1111/j.1600-0625.2011.01439.x
    • Dong, K., Pelle, E., Yarosh, D. B., and Pernodet, N. (2012). Sirtuin 4 identification in normal human epidermal keratinocytes and its relation to sirtuin 3 and energy metabolism under normal conditions and UVB-induced stress. Exp. Dermatol. 21, 231-233. doi: 10.1111/j.1600-0625.2011.01439.x.
    • (2012) Exp. Dermatol. , vol.21 , pp. 231-233
    • Dong, K.1    Pelle, E.2    Yarosh, D.B.3    Pernodet, N.4
  • 21
    • 72149118206 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore in Alzheimer's disease: cyclophilin D and amyloid beta
    • doi: 10.1016/j.bbadis.2009.07.005
    • Du, H., and Yan, S. S. (2010). Mitochondrial permeability transition pore in Alzheimer's disease: cyclophilin D and amyloid beta. Biochim. Biophys. Acta 1802, 198-204. doi: 10.1016/j.bbadis.2009.07.005.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 198-204
    • Du, H.1    Yan, S.S.2
  • 22
    • 81055122671 scopus 로고    scopus 로고
    • Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
    • doi: 10.1126/science.1207861
    • Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., et al. (2011). Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science 334, 806-809. doi: 10.1126/science.1207861.
    • (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
  • 23
    • 0038043242 scopus 로고    scopus 로고
    • Intra-mitochondrial poly(ADP-ribosylation) contributes to NAD+ depletion and cell death induced by oxidative stress
    • doi: 10.1074/jbc. M301295200
    • Du, L., Zhang, X., Han, Y. Y., Burke, N. A., Kochanek, P. M., Watkins, S. C., et al. (2003). Intra-mitochondrial poly(ADP-ribosylation) contributes to NAD+ depletion and cell death induced by oxidative stress. J. Biol. Chem. 278, 18426-18433. doi: 10.1074/jbc. M301295200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18426-18433
    • Du, L.1    Zhang, X.2    Han, Y.Y.3    Burke, N.A.4    Kochanek, P.M.5    Watkins, S.C.6
  • 24
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • doi: 10.1038/35041687
    • Finkel, T., and Holbrook, N. J. (2000). Oxidants, oxidative stress and the biology of ageing. Nature 408, 239-247. doi: 10.1038/35041687.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 25
    • 80051716282 scopus 로고    scopus 로고
    • Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity
    • doi: 10.1371/journal.pone.0023295
    • Finley, L. W. S., Haas, W., Desquiret-Dumas, V., Wallace, D. C., Procaccio, V., Gygi, S. P., et al. (2011). Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity. PLoS ONE 6:e23295. doi: 10.1371/journal.pone.0023295.
    • (2011) PLoS ONE , vol.6
    • Finley, L.W.S.1    Haas, W.2    Desquiret-Dumas, V.3    Wallace, D.C.4    Procaccio, V.5    Gygi, S.P.6
  • 26
    • 84857883360 scopus 로고    scopus 로고
    • Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice
    • doi: 10.1021/pr2008384
    • Fritz, K. S., Galligan, J. J., Hirschey, M. D., Verdin, E., and Petersen, D. R. (2012). Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice. J. Proteome Res. 11, 1633-1643. doi: 10.1021/pr2008384.
    • (2012) J. Proteome Res. , vol.11 , pp. 1633-1643
    • Fritz, K.S.1    Galligan, J.J.2    Hirschey, M.D.3    Verdin, E.4    Petersen, D.R.5
  • 27
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • doi: 10.1006/bbrc.2000.3000
    • Frye, R. A. (2000). Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273, 793-798. doi: 10.1006/bbrc.2000.3000.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 28
    • 84863794891 scopus 로고    scopus 로고
    • trans-(-)-e-Viniferin increases mitochondrial sirtuin 3 (SIRT3), activates AMP-activated protein kinase (AMPK), and protects cells in models of Huntington disease
    • doi: 10.1074/jbc. M112.382226
    • Fu, J., Jin, J., Cichewicz, R. H., Hageman, S. A., Ellis, T. K., Xiang, L., et al. (2012). trans-(-)-e-Viniferin increases mitochondrial sirtuin 3 (SIRT3), activates AMP-activated protein kinase (AMPK), and protects cells in models of Huntington disease. J. Biol. Chem. 287, 24460-24472. doi: 10.1074/jbc. M112.382226.
    • (2012) J. Biol. Chem. , vol.287 , pp. 24460-24472
    • Fu, J.1    Jin, J.2    Cichewicz, R.H.3    Hageman, S.A.4    Ellis, T.K.5    Xiang, L.6
  • 29
    • 0035815751 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate
    • doi: 10.1074/jbc. M008782200
    • Fujino, T., Kondo, J., Ishikawa, M., Morikawa, K., and Yamamoto, T. T. (2001). Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate. J. Biol. Chem. 276, 11420-11426. doi: 10.1074/jbc. M008782200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11420-11426
    • Fujino, T.1    Kondo, J.2    Ishikawa, M.3    Morikawa, K.4    Yamamoto, T.T.5
  • 30
    • 80053424677 scopus 로고    scopus 로고
    • Mitochondrial elongation during autophagy: a stereotypical response to survive in difficult times
    • doi: 10.4161/auto.7.10.16771
    • Gomes, L. C., and Scorrano, L. (2011). Mitochondrial elongation during autophagy: a stereotypical response to survive in difficult times. Autophagy 7, 1251-1253. doi: 10.4161/auto.7.10.16771.
    • (2011) Autophagy , vol.7 , pp. 1251-1253
    • Gomes, L.C.1    Scorrano, L.2
  • 31
    • 38149131289 scopus 로고    scopus 로고
    • Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance
    • Gomez-Cabrera, M.-C., Domenech, E., Romagnoli, M., Arduini, A., Borras, C., Pallardo, F. V., et al. (2008). Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance. Am. J. Clin. Nutr. 87, 142-149.
    • (2008) Am. J. Clin. Nutr. , vol.87 , pp. 142-149
    • Gomez-Cabrera, M.-C.1    Domenech, E.2    Romagnoli, M.3    Arduini, A.4    Borras, C.5    Pallardo, F.V.6
  • 32
    • 0030026613 scopus 로고    scopus 로고
    • Ceramide protects hippocampal neurons against excitotoxic and oxidative insults, and amyloid beta-peptide toxicity
    • doi: 10.1046/j.1471-4159.1996.66020869.x
    • Goodman, Y., and Mattson, M. P. (1996). Ceramide protects hippocampal neurons against excitotoxic and oxidative insults, and amyloid beta-peptide toxicity. J. Neurochem. 66, 869-872. doi: 10.1046/j.1471-4159.1996.66020869.x.
    • (1996) J. Neurochem. , vol.66 , pp. 869-872
    • Goodman, Y.1    Mattson, M.P.2
  • 33
    • 0034626747 scopus 로고    scopus 로고
    • Genetic pathways that regulate ageing in model organisms
    • doi: 10.1038/35041700
    • Guarente, L., and Kenyon, C. (2000). Genetic pathways that regulate ageing in model organisms. Nature 408, 255-262. doi: 10.1038/35041700.
    • (2000) Nature , vol.408 , pp. 255-262
    • Guarente, L.1    Kenyon, C.2
  • 34
    • 84860228592 scopus 로고    scopus 로고
    • In mammalian muscle, SIRT3 is present in mitochondria and not in the nucleus; and SIRT3 is upregulated by chronic muscle contraction in an adenosine monophosphate-activated protein kinase-independent manner
    • doi: 10.1016/j.metabol.2011.09.016
    • Gurd, B. J., Holloway, G. P., Yoshida, Y., and Bonen, A. (2012). In mammalian muscle, SIRT3 is present in mitochondria and not in the nucleus; and SIRT3 is upregulated by chronic muscle contraction in an adenosine monophosphate-activated protein kinase-independent manner. Metabolism 61, 733-741. doi: 10.1016/j.metabol.2011.09.016.
    • (2012) Metabolism , vol.61 , pp. 733-741
    • Gurd, B.J.1    Holloway, G.P.2    Yoshida, Y.3    Bonen, A.4
  • 35
    • 79952266729 scopus 로고    scopus 로고
    • Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy
    • Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C.-Y., Palmeira, C. M., Rosenzweig, A., et al. (2010). Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy. Aging (Albany NY) 2, 914-923.
    • (2010) Aging (Albany NY) , vol.2 , pp. 914-923
    • Hafner, A.V.1    Dai, J.2    Gomes, A.P.3    Xiao, C.-Y.4    Palmeira, C.M.5    Rosenzweig, A.6
  • 36
    • 33748316536 scopus 로고    scopus 로고
    • SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells
    • doi: 10.1016/j.cell.2006.06.057
    • Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., et al. (2006). SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126, 941-954. doi: 10.1016/j.cell.2006.06.057.
    • (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
  • 37
    • 0034992947 scopus 로고    scopus 로고
    • Aging lowers steady-state antioxidant enzyme and stress protein expression in primary hepatocytes
    • doi: 10.1093/gerona/56.6.B259
    • Hall, D. M., Sattler, G. L., Sattler, C. A., Zhang, H. J., Oberley, L. W., Pitot, H. C., et al. (2001). Aging lowers steady-state antioxidant enzyme and stress protein expression in primary hepatocytes. J. Gerontol. A Biol. Sci. Med. Sci. 56, B259-B267. doi: 10.1093/gerona/56.6.B259.
    • (2001) J. Gerontol. A Biol. Sci. Med. Sci. , vol.56
    • Hall, D.M.1    Sattler, G.L.2    Sattler, C.A.3    Zhang, H.J.4    Oberley, L.W.5    Pitot, H.C.6
  • 38
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • doi: 10.1073/pnas.0604392103
    • Hallows, W. C., Lee, S., and Denu, J. M. (2006). Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. U.S.A. 103, 10230-10235. doi: 10.1073/pnas.0604392103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 39
    • 78651468707 scopus 로고    scopus 로고
    • Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
    • doi: 10.1016/j.molcel.2011.01.002
    • Hallows, W. C., Yu, W., Smith, B. C., Devries, M. K., Devires, M. K., Ellinger, J. J., et al. (2011). Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction. Mol. Cell 41, 139-149. doi: 10.1016/j.molcel.2011.01.002.
    • (2011) Mol. Cell , vol.41 , pp. 139-149
    • Hallows, W.C.1    Yu, W.2    Smith, B.C.3    Devries, M.K.4    Devires, M.K.5    Ellinger, J.J.6
  • 40
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • doi: 10.1038/nature04724
    • Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., et al. (2006). Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441, 885-889. doi: 10.1038/nature04724.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 41
    • 77049308856 scopus 로고
    • Aging: a theory based on free radical and radiation chemistry
    • doi: 10.1093/geronj/11.3.298
    • Harman, D. (1956). Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 11, 298-300. doi: 10.1093/geronj/11.3.298.
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 42
    • 84865421953 scopus 로고    scopus 로고
    • Mitochondrial sirtuins: regulators of protein acylation and metabolism
    • doi: 10.1016/j.tem.2012.07.004
    • He, W., Newman, J. C., Wang, M. Z., Ho, L., and Verdin, E. (2012). Mitochondrial sirtuins: regulators of protein acylation and metabolism. Trends Endocrinol. Metab. 23, 467-476. doi: 10.1016/j.tem.2012.07.004.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 467-476
    • He, W.1    Newman, J.C.2    Wang, M.Z.3    Ho, L.4    Verdin, E.5
  • 43
    • 84872276165 scopus 로고    scopus 로고
    • Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
    • doi: 10.1016/j.molcel.2012.10.024
    • Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., et al. (2013). Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome. Mol. Cell 49, 186-199. doi: 10.1016/j.molcel.2012.10.024.
    • (2013) Mol. Cell , vol.49 , pp. 186-199
    • Hebert, A.S.1    Dittenhafer-Reed, K.E.2    Yu, W.3    Bailey, D.J.4    Selen, E.S.5    Boersma, M.D.6
  • 44
    • 0035855905 scopus 로고    scopus 로고
    • CREB regulates hepatic gluconeogenesis through the coactivator PGC-1
    • doi: 10.1038/35093131
    • Herzig, S., Long, F., Jhala, U. S., Hedrick, S., Quinn, R., Bauer, A., et al. (2001). CREB regulates hepatic gluconeogenesis through the coactivator PGC-1. Nature 413, 179-183. doi: 10.1038/35093131.
    • (2001) Nature , vol.413 , pp. 179-183
    • Herzig, S.1    Long, F.2    Jhala, U.S.3    Hedrick, S.4    Quinn, R.5    Bauer, A.6
  • 45
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • doi: 10.1038/nature08778
    • Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., et al. (2010). SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 464, 121-125. doi: 10.1038/nature08778.
    • (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
  • 46
    • 82455212901 scopus 로고    scopus 로고
    • SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome
    • doi: 10.1016/j.molcel.2011.07.019
    • Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., et al. (2011). SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome. Mol. Cell 44, 177-190. doi: 10.1016/j.molcel.2011.07.019.
    • (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
  • 47
    • 0036890388 scopus 로고    scopus 로고
    • Natural selection promotes the conservation of linkage of co-expressed genes
    • doi: 10.1016/S0168-9525(02)02813-5
    • Hurst, L. D., Williams, E. J. B., and Pál, C. (2002). Natural selection promotes the conservation of linkage of co-expressed genes. Trends Genet. 18, 604-606. doi: 10.1016/S0168-9525(02)02813-5.
    • (2002) Trends Genet. , vol.18 , pp. 604-606
    • Hurst, L.D.1    Williams, E.J.B.2    Pál, C.3
  • 48
    • 84871852995 scopus 로고    scopus 로고
    • SIRT3 functions in the nucleus in the control of stress-related gene expression
    • doi: 10.1128/MCB.00822-12
    • Iwahara, T., Bonasio, R., Narendra, V., and Reinberg, D. (2012). SIRT3 functions in the nucleus in the control of stress-related gene expression. Mol. Cell. Biol. 32, 5022-5034. doi: 10.1128/MCB.00822-12.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 5022-5034
    • Iwahara, T.1    Bonasio, R.2    Narendra, V.3    Reinberg, D.4
  • 49
    • 51449083112 scopus 로고    scopus 로고
    • SIRT3 interacts with the daf-16 homolog FOXO3a in the mitochondria, as well as increases FOXO3a dependent gene expression
    • doi: 10.7150/ijbs.4.291
    • Jacobs, K. M., Pennington, J. D., Bisht, K. S., Aykin-Burns, N., Kim, H.-S., Mishra, M., et al. (2008). SIRT3 interacts with the daf-16 homolog FOXO3a in the mitochondria, as well as increases FOXO3a dependent gene expression. Int. J. Biol. Sci. 4, 291-299. doi: 10.7150/ijbs.4.291.
    • (2008) Int. J. Biol. Sci. , vol.4 , pp. 291-299
    • Jacobs, K.M.1    Pennington, J.D.2    Bisht, K.S.3    Aykin-Burns, N.4    Kim, H.-S.5    Mishra, M.6
  • 50
    • 34547545892 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha
    • doi: 10.1073/pnas.0705070104
    • Jäger, S., Handschin, C., St-Pierre, J., and Spiegelman, B. M. (2007). AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha. Proc. Natl. Acad. Sci. U.S.A. 104, 12017-12022. doi: 10.1073/pnas.0705070104.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12017-12022
    • Jäger, S.1    Handschin, C.2    St-Pierre, J.3    Spiegelman, B.M.4
  • 51
    • 61449209922 scopus 로고    scopus 로고
    • Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3
    • doi: 10.1002/pro.50
    • Jin, L., Galonek, H., Israelian, K., Choy, W., Morrison, M., Xia, Y., et al. (2009). Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3. Protein Sci. 18, 514-525. doi: 10.1002/pro.50.
    • (2009) Protein Sci. , vol.18 , pp. 514-525
    • Jin, L.1    Galonek, H.2    Israelian, K.3    Choy, W.4    Morrison, M.5    Xia, Y.6
  • 52
    • 80052291180 scopus 로고    scopus 로고
    • Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production
    • doi: 10.1073/pnas.1111308108
    • Jing, E., Emanuelli, B., Hirschey, M. D., Boucher, J., Lee, K. Y., Lombard, D., et al. (2011). Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. Proc. Natl. Acad. Sci. U.S.A. 108, 14608-14613. doi: 10.1073/pnas.1111308108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 53
    • 84866444702 scopus 로고    scopus 로고
    • The impact of aging on mitochondrial function and biogenesis pathways in skeletal muscle of sedentary high-and low-functioning elderly individuals
    • doi: 10.1111/j.1474-9726.2012.00844.x
    • Joseph, A.-M., Adhihetty, P. J., Buford, T. W., Wohlgemuth, S. E., Lees, H. A., Nguyen, L. M.-D., et al. (2012). The impact of aging on mitochondrial function and biogenesis pathways in skeletal muscle of sedentary high-and low-functioning elderly individuals. Aging Cell 11, 801-809. doi: 10.1111/j.1474-9726.2012.00844.x.
    • (2012) Aging Cell , vol.11 , pp. 801-809
    • Joseph, A.-M.1    Adhihetty, P.J.2    Buford, T.W.3    Wohlgemuth, S.E.4    Lees, H.A.5    Nguyen, L.M.-D.6
  • 54
    • 79955433960 scopus 로고    scopus 로고
    • Metabolomic analysis of livers and serum from high-fat diet induced obese mice
    • doi: 10.1021/pr100892r
    • Kim, H.-J., Kim, J. H., Noh, S., Hur, H. J., Sung, M. J., Hwang, J.-T., et al. (2011a). Metabolomic analysis of livers and serum from high-fat diet induced obese mice. J. Proteome Res. 10, 722-731. doi: 10.1021/pr100892r.
    • (2011) J. Proteome Res. , vol.10 , pp. 722-731
    • Kim, H.-J.1    Kim, J.H.2    Noh, S.3    Hur, H.J.4    Sung, M.J.5    Hwang, J.-T.6
  • 55
    • 79952353862 scopus 로고    scopus 로고
    • Neuronal Sirt3 protects against excitotoxic injury in mouse cortical neuron culture
    • doi: 10.1371/journal.pone.0014731
    • Kim, S. H., Lu, H. F., and Alano, C. C. (2011b). Neuronal Sirt3 protects against excitotoxic injury in mouse cortical neuron culture. PLoS ONE 6:e14731. doi: 10.1371/journal.pone.0014731.
    • (2011) PLoS ONE , vol.6
    • Kim, S.H.1    Lu, H.F.2    Alano, C.C.3
  • 56
    • 74049094817 scopus 로고    scopus 로고
    • SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress
    • doi: 10.1016/j.ccr.2009.11.023
    • Kim, H.-S., Patel, K., Muldoon-Jacobs, K., Bisht, K. S., Aykin-Burns, N., Pennington, J. D., et al. (2010). SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress. Cancer Cell 17, 41-52. doi: 10.1016/j.ccr.2009.11.023.
    • (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
  • 57
    • 34249934085 scopus 로고    scopus 로고
    • Selective degradation of mitochondria by mitophagy
    • doi: 10.1016/j.abb.2007.03.034
    • Kim, I., Rodriguez-Enriquez, S., and Lemasters, J. J. (2007). Selective degradation of mitochondria by mitophagy. Arch. Biochem. Biophys. 462, 245-253. doi: 10.1016/j.abb.2007.03.034.
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 245-253
    • Kim, I.1    Rodriguez-Enriquez, S.2    Lemasters, J.J.3
  • 58
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • doi: 10.1016/j.molcel.2006.06.026
    • Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., et al. (2006). Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol. Cell 23, 607-618. doi: 10.1016/j.molcel.2006.06.026.
    • (2006) Mol. Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5    Pei, J.6
  • 59
    • 79952257025 scopus 로고    scopus 로고
    • Perspectives on cellular senescence and short term dietary restriction in adults
    • Kirkland, J. L. (2010). Perspectives on cellular senescence and short term dietary restriction in adults. Aging (Albany NY) 2, 894-896.
    • (2010) Aging (Albany NY) , vol.2 , pp. 894-896
    • Kirkland, J.L.1
  • 61
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • doi: 10.1038/nature04723
    • Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J., Tanida, I., et al. (2006). Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441, 880-884. doi: 10.1038/nature04723.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 62
    • 77955347446 scopus 로고    scopus 로고
    • Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis
    • doi: 10.1371/journal.pone.0011707
    • Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., et al. (2010). Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis. PLoS ONE 5:e11707. doi: 10.1371/journal.pone.0011707.
    • (2010) PLoS ONE , vol.5
    • Kong, X.1    Wang, R.2    Xue, Y.3    Liu, X.4    Zhang, H.5    Chen, Y.6
  • 63
    • 77956256449 scopus 로고    scopus 로고
    • Beneficial effects of mild stress (hormetic effects): dietary restriction and health
    • doi: 10.2114/jpa2.29.127
    • Kouda, K., and Iki, M. (2010). Beneficial effects of mild stress (hormetic effects): dietary restriction and health. J. Physiol. Anthropol. 29, 127-132. doi: 10.2114/jpa2.29.127.
    • (2010) J. Physiol. Anthropol. , vol.29 , pp. 127-132
    • Kouda, K.1    Iki, M.2
  • 64
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • doi: 10.1038/nature03029
    • Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., et al. (2004). The role of autophagy during the early neonatal starvation period. Nature 432, 1032-1036. doi: 10.1038/nature03029.
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1    Hatano, M.2    Matsui, M.3    Yamamoto, A.4    Nakaya, H.5    Yoshimori, T.6
  • 65
    • 0033400713 scopus 로고    scopus 로고
    • Ketone bodies: a review of physiology, pathophysiology and application of monitoring to diabetes
    • doi: 10.1002/(SICI)1520-7560(199911/12)15:6<412::AID-DMRR72>3.0.CO;2-8
    • Laffel, L. (1999). Ketone bodies: a review of physiology, pathophysiology and application of monitoring to diabetes. Diabetes Metab. Res. Rev. 15, 412-426. doi: 10.1002/(SICI)1520-7560(199911/12)15:6<412::AID-DMRR72>3.0.CO;2-8.
    • (1999) Diabetes Metab. Res. Rev. , vol.15 , pp. 412-426
    • Laffel, L.1
  • 66
    • 58149345928 scopus 로고    scopus 로고
    • Endurance exercise as a countermeasure for aging
    • doi: 10.2337/db08-0349
    • Lanza, I. R., Short, D. K., Short, K. R., Raghavakaimal, S., Basu, R., Joyner, M. J., et al. (2008). Endurance exercise as a countermeasure for aging. Diabetes 57, 2933-2942. doi: 10.2337/db08-0349.
    • (2008) Diabetes , vol.57 , pp. 2933-2942
    • Lanza, I.R.1    Short, D.K.2    Short, K.R.3    Raghavakaimal, S.4    Basu, R.5    Joyner, M.J.6
  • 67
    • 68649095201 scopus 로고    scopus 로고
    • Mitochondrial calcium and the permeability transition in cell death
    • doi: 10.1016/j.bbabio.2009.06.009
    • Lemasters, J. J., Theruvath, T. P., Zhong, Z., and Nieminen, A.-L. (2009). Mitochondrial calcium and the permeability transition in cell death. Biochim. Biophys. Acta 1787, 1395-1401. doi: 10.1016/j.bbabio.2009.06.009.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1395-1401
    • Lemasters, J.J.1    Theruvath, T.P.2    Zhong, Z.3    Nieminen, A.-L.4
  • 68
    • 84862741341 scopus 로고    scopus 로고
    • Resveratrol stimulates cortisol biosynthesis by activating SIRT-dependent deacetylation of P450scc
    • doi: 10.1210/en.2011-2088
    • Li, D., Dammer, E. B., and Sewer, M. B. (2012). Resveratrol stimulates cortisol biosynthesis by activating SIRT-dependent deacetylation of P450scc. Endocrinology 153, 3258-3268. doi: 10.1210/en.2011-2088.
    • (2012) Endocrinology , vol.153 , pp. 3258-3268
    • Li, D.1    Dammer, E.B.2    Sewer, M.B.3
  • 69
    • 84875906572 scopus 로고    scopus 로고
    • Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure
    • doi: 10.1016/j.cmet.2013.03.002
    • Liesa, M., and Shirihai, O. S. (2013). Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure. Cell Metab. 17, 491-506. doi: 10.1016/j.cmet.2013.03.002.
    • (2013) Cell Metab. , vol.17 , pp. 491-506
    • Liesa, M.1    Shirihai, O.S.2
  • 70
    • 5344252327 scopus 로고    scopus 로고
    • Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1alpha null mice
    • doi: 10.1016/j.cell.2004.09.013
    • Lin, J., Wu, P.-H., Tarr, P. T., Lindenberg, K. S., St-Pierre, J., and Zhang, C.-Y., et al. (2004). Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1alpha null mice. Cell 119, 121-135. doi: 10.1016/j.cell.2004.09.013.
    • (2004) Cell , vol.119 , pp. 121-135
    • Lin, J.1    Wu, P.-H.2    Tarr, P.T.3    Lindenberg, K.S.4    St-Pierre, J.5    Zhang, C.-Y.6
  • 71
    • 37549002891 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
    • doi: 10.1128/MCB.01636-07
    • Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., et al. (2007). Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol. Cell. Biol. 27, 8807-8814. doi: 10.1128/MCB.01636-07.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8807-8814
    • Lombard, D.B.1    Alt, F.W.2    Cheng, H.-L.3    Bunkenborg, J.4    Streeper, R.S.5    Mostoslavsky, R.6
  • 72
    • 40149108041 scopus 로고    scopus 로고
    • The tricarboxylic acid cycle, an ancient metabolic network with a novel twist
    • doi: 10.1371/journal.pone.0000690
    • Mailloux, R. J., Bériault, R., Lemire, J., Singh, R., Chénier, D. R., Hamel, R. D., et al. (2007). The tricarboxylic acid cycle, an ancient metabolic network with a novel twist. PLoS ONE 2:e690. doi: 10.1371/journal.pone.0000690.
    • (2007) PLoS ONE , vol.2
    • Mailloux, R.J.1    Bériault, R.2    Lemire, J.3    Singh, R.4    Chénier, D.R.5    Hamel, R.D.6
  • 73
    • 48949117163 scopus 로고    scopus 로고
    • Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily
    • doi: 10.1517/17425255.4.6.697
    • Marchitti, S. A., Brocker, C., Stagos, D., and Vasiliou, V. (2008). Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily. Expert Opin. Drug Metab. Toxicol. 4, 697-720. doi: 10.1517/17425255.4.6.697.
    • (2008) Expert Opin. Drug Metab. Toxicol. , vol.4 , pp. 697-720
    • Marchitti, S.A.1    Brocker, C.2    Stagos, D.3    Vasiliou, V.4
  • 74
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • doi: 10.1038/35040009
    • Mattson, M. P. (2000). Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 1, 120-129. doi: 10.1038/35040009.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 75
    • 0024656069 scopus 로고
    • The effect of retarded growth upon the length of life span and upon the ultimate body size
    • discussion 172
    • McCay, C. M., Crowell, M. F., and Maynard, L. A. (1989). The effect of retarded growth upon the length of life span and upon the ultimate body size. 1935. Nutrition 5, 155-171; discussion 172.
    • (1989) 1935. Nutrition , vol.5 , pp. 155-171
    • McCay, C.M.1    Crowell, M.F.2    Maynard, L.A.3
  • 76
    • 0018864840 scopus 로고
    • Regulation of hepatic fatty acid oxidation and ketone body production
    • doi: 10.1146/annurev.bi.49.070180.002143
    • McGarry, J. D., and Foster, D. W. (1980). Regulation of hepatic fatty acid oxidation and ketone body production. Annu. Rev. Biochem. 49, 395-420. doi: 10.1146/annurev.bi.49.070180.002143.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 395-420
    • McGarry, J.D.1    Foster, D.W.2
  • 77
    • 77949801029 scopus 로고    scopus 로고
    • Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex
    • doi: 10.1523/JNEUROSCI.6248-09.2010
    • Misko, A., Jiang, S., Wegorzewska, I., Milbrandt, J., and Baloh, R. H. (2010). Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex. J. Neurosci. 30, 4232-4240. doi: 10.1523/JNEUROSCI.6248-09.2010.
    • (2010) J. Neurosci. , vol.30 , pp. 4232-4240
    • Misko, A.1    Jiang, S.2    Wegorzewska, I.3    Milbrandt, J.4    Baloh, R.H.5
  • 78
    • 70349650451 scopus 로고    scopus 로고
    • Mitochondrial networking protects beta-cells from nutrient-induced apoptosis
    • doi: 10.2337/db07-1781
    • Molina, A. J. A., Wikstrom, J. D., Stiles, L., Las, G., Mohamed, H., Elorza, A., et al. (2009). Mitochondrial networking protects beta-cells from nutrient-induced apoptosis. Diabetes 58, 2303-2315. doi: 10.2337/db07-1781.
    • (2009) Diabetes , vol.58 , pp. 2303-2315
    • Molina, A.J.A.1    Wikstrom, J.D.2    Stiles, L.3    Las, G.4    Mohamed, H.5    Elorza, A.6
  • 79
    • 37549050876 scopus 로고    scopus 로고
    • Effect of short-term ketogenic diet on redox status of human blood
    • doi: 10.1089/rej.2007.0540
    • Nazarewicz, R. R., Ziolkowski, W., Vaccaro, P. S., and Ghafourifar, P. (2007). Effect of short-term ketogenic diet on redox status of human blood. Rejuvenation Res. 10, 435-440. doi: 10.1089/rej.2007.0540.
    • (2007) Rejuvenation Res. , vol.10 , pp. 435-440
    • Nazarewicz, R.R.1    Ziolkowski, W.2    Vaccaro, P.S.3    Ghafourifar, P.4
  • 80
    • 0037108799 scopus 로고    scopus 로고
    • SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria
    • doi: 10.1073/pnas.222538099
    • Onyango, P., Celic, I., McCaffery, J. M., Boeke, J. D., and Feinberg, A. P. (2002). SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proc. Natl. Acad. Sci. U.S.A. 99, 13653-13658. doi: 10.1073/pnas.222538099.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13653-13658
    • Onyango, P.1    Celic, I.2    McCaffery, J.M.3    Boeke, J.D.4    Feinberg, A.P.5
  • 82
    • 77952940043 scopus 로고    scopus 로고
    • Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1alpha in skeletal muscle
    • Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., Ward, J. L. III, et al. (2009). Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1alpha in skeletal muscle. Aging (Albany NY) 1, 771-783.
    • (2009) Aging (Albany NY) , vol.1 , pp. 771-783
    • Palacios, O.M.1    Carmona, J.J.2    Michan, S.3    Chen, K.Y.4    Manabe, Y.5    Ward III, J.L.6
  • 83
    • 84878305687 scopus 로고    scopus 로고
    • A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels
    • doi: 10.1007/s00018-012-1244-6
    • Peserico, A., Chiacchiera, F., Grossi, V., Matrone, A., Latorre, D., Simonatto, M., et al. (2013). A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels. Cell. Mol. Life Sci. 70, 2015-2029. doi: 10.1007/s00018-012-1244-6.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 2015-2029
    • Peserico, A.1    Chiacchiera, F.2    Grossi, V.3    Matrone, A.4    Latorre, D.5    Simonatto, M.6
  • 84
    • 77449120223 scopus 로고    scopus 로고
    • Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway
    • doi: 10.1074/jbc. M109.077271
    • Pillai, V. B., Sundaresan, N. R., Kim, G., Gupta, M., Rajamohan, S. B., Pillai, J. B., et al. (2010). Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway. J. Biol. Chem. 285, 3133-3144. doi: 10.1074/jbc. M109.077271.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3133-3144
    • Pillai, V.B.1    Sundaresan, N.R.2    Kim, G.3    Gupta, M.4    Rajamohan, S.B.5    Pillai, J.B.6
  • 85
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • doi: 10.1016/j.cmet.2010.11.015
    • Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., and Chen, D. (2010). Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab. 12, 662-667. doi: 10.1016/j.cmet.2010.11.015.
    • (2010) Cell Metab. , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 87
    • 70450233716 scopus 로고    scopus 로고
    • Up-regulation of orphan nuclear estrogen-related receptor alpha expression during long-term caloric restriction in mice
    • doi: 10.1007/s11010-009-0174-6
    • Ranhotra, H. S. (2009). Up-regulation of orphan nuclear estrogen-related receptor alpha expression during long-term caloric restriction in mice. Mol. Cell. Biochem. 332, 59-65. doi: 10.1007/s11010-009-0174-6.
    • (2009) Mol. Cell. Biochem. , vol.332 , pp. 59-65
    • Ranhotra, H.S.1
  • 88
    • 0041326831 scopus 로고    scopus 로고
    • Effects of age and caloric restriction on glutathione redox state in mice
    • doi: 10.1016/S0891-5849(03)00388-5
    • Rebrin, I., Kamzalov, S., and Sohal, R. S. (2003). Effects of age and caloric restriction on glutathione redox state in mice. Free Radic. Biol. Med. 35, 626-635. doi: 10.1016/S0891-5849(03)00388-5.
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 626-635
    • Rebrin, I.1    Kamzalov, S.2    Sohal, R.S.3
  • 89
    • 51249104026 scopus 로고    scopus 로고
    • Pro-oxidant shift in glutathione redox state during aging
    • doi: 10.1016/j.addr.2008.06.001
    • Rebrin, I., and Sohal, R. S. (2008). Pro-oxidant shift in glutathione redox state during aging. Adv. Drug Deliv. Rev. 60, 1545-1552. doi: 10.1016/j.addr.2008.06.001.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 1545-1552
    • Rebrin, I.1    Sohal, R.S.2
  • 90
    • 66649109663 scopus 로고    scopus 로고
    • Antioxidants prevent health-promoting effects of physical exercise in humans
    • doi: 10.1073/pnas.0903485106
    • Ristow, M., Zarse, K., Oberbach, A., Klöting, N., Birringer, M., Kiehntopf, M., et al. (2009). Antioxidants prevent health-promoting effects of physical exercise in humans. Proc. Natl. Acad. Sci. U.S.A. 106, 8665-8670. doi: 10.1073/pnas.0903485106.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8665-8670
    • Ristow, M.1    Zarse, K.2    Oberbach, A.3    Klöting, N.4    Birringer, M.5    Kiehntopf, M.6
  • 91
    • 0036856578 scopus 로고    scopus 로고
    • Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis
    • doi: 10.1002/1521-4141(200211)32:11
    • Rongvaux, A., Shea, R. J., Mulks, M. H., Gigot, D., Urbain, J., Leo, O., et al. (2002). Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis. Eur. J. Immunol. 32, 3225-3234. doi: 10.1002/1521-4141(200211)32:11.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 3225-3234
    • Rongvaux, A.1    Shea, R.J.2    Mulks, M.H.3    Gigot, D.4    Urbain, J.5    Leo, O.6
  • 92
    • 10744232772 scopus 로고    scopus 로고
    • Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly
    • doi: 10.1016/S0531-5565(03)00209-2
    • Rose, G., Dato, S., Altomare, K., Bellizzi, D., Garasto, S., Greco, V., et al. (2003). Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly. Exp. Gerontol. 38, 1065-1070. doi: 10.1016/S0531-5565(03)00209-2.
    • (2003) Exp. Gerontol. , vol.38 , pp. 1065-1070
    • Rose, G.1    Dato, S.2    Altomare, K.3    Bellizzi, D.4    Garasto, S.5    Greco, V.6
  • 93
    • 79952753140 scopus 로고    scopus 로고
    • Endurance exercise rescues progeroid aging and induces systemic mitochondrial rejuvenation in mtDNA mutator mice
    • doi: 10.1073/pnas.1019581108
    • Safdar, A., Bourgeois, J. M., Ogborn, D. I., Little, J. P., Hettinga, B. P., Akhtar, M., et al. (2011). Endurance exercise rescues progeroid aging and induces systemic mitochondrial rejuvenation in mtDNA mutator mice. Proc. Natl. Acad. Sci. U.S.A. 108, 4135-4140. doi: 10.1073/pnas.1019581108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 4135-4140
    • Safdar, A.1    Bourgeois, J.M.2    Ogborn, D.I.3    Little, J.P.4    Hettinga, B.P.5    Akhtar, M.6
  • 94
    • 0023550043 scopus 로고
    • Changes in superoxide radical and lipid peroxide formation in the brain, heart and liver during the lifetime of the rat
    • doi: 10.1016/0047-6374(87)90057-1
    • Sawada, M., and Carlson, J. C. (1987). Changes in superoxide radical and lipid peroxide formation in the brain, heart and liver during the lifetime of the rat. Mech. Ageing Dev. 41, 125-137. doi: 10.1016/0047-6374(87)90057-1.
    • (1987) Mech. Ageing Dev. , vol.41 , pp. 125-137
    • Sawada, M.1    Carlson, J.C.2
  • 95
    • 33845876643 scopus 로고    scopus 로고
    • Reducing mitochondrial fission results in increased life span and fitness of two fungal ageing models
    • doi: 10.1038/ncb1524
    • Scheckhuber, C. Q., Erjavec, N., Tinazli, A., Hamann, A., Nyström, T., and Osiewacz, H. D. (2007). Reducing mitochondrial fission results in increased life span and fitness of two fungal ageing models. Nat. Cell Biol. 9, 99-105. doi: 10.1038/ncb1524.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 99-105
    • Scheckhuber, C.Q.1    Erjavec, N.2    Tinazli, A.3    Hamann, A.4    Nyström, T.5    Osiewacz, H.D.6
  • 96
    • 34247271282 scopus 로고    scopus 로고
    • +-dependent histone deacetylase that translocates to the mitochondria upon cellular stress
    • doi: 10.1101/gad.1527307
    • +-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 21, 920-928. doi: 10.1101/gad.1527307.
    • (2007) Genes Dev. , vol.21 , pp. 920-928
    • Scher, M.B.1    Vaquero, A.2    Reinberg, D.3
  • 97
    • 50149103440 scopus 로고    scopus 로고
    • Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
    • doi: 10.1016/j.jmb.2008.07.048
    • Schlicker, C., Gertz, M., Papatheodorou, P., Kachholz, B., Becker, C. F. W., and Steegborn, C. (2008). Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J. Mol. Biol. 382, 790-801. doi: 10.1016/j.jmb.2008.07.048.
    • (2008) J. Mol. Biol. , vol.382 , pp. 790-801
    • Schlicker, C.1    Gertz, M.2    Papatheodorou, P.3    Kachholz, B.4    Becker, C.F.W.5    Steegborn, C.6
  • 98
    • 21144434217 scopus 로고    scopus 로고
    • Extension of murine life span by overexpression of catalase targeted to mitochondria
    • doi: 10.1126/science.1106653
    • Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., et al. (2005). Extension of murine life span by overexpression of catalase targeted to mitochondria. Science 308, 1909-1911. doi: 10.1126/science.1106653.
    • (2005) Science , vol.308 , pp. 1909-1911
    • Schriner, S.E.1    Linford, N.J.2    Martin, G.M.3    Treuting, P.4    Ogburn, C.E.5    Emond, M.6
  • 99
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • doi: 10.1073/pnas.0603968103
    • Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., and Verdin, E. (2006). Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. U.S.A. 103, 10224-10229. doi: 10.1073/pnas.0603968103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 100
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • doi: 10.1083/jcb.200205057
    • Schwer, B., North, B. J., Frye, R. A., Ott, M., and Verdin, E. (2002). The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 158, 647-657. doi: 10.1083/jcb.200205057.
    • (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
  • 101
    • 77955351652 scopus 로고    scopus 로고
    • New insights into the role of mitochondria in aging: mitochondrial dynamics and more
    • doi: 10.1242/jcs.070490
    • Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., and Leeuwenburgh, C. (2010). New insights into the role of mitochondria in aging: mitochondrial dynamics and more. J. Cell Sci. 123, 2533-2542. doi: 10.1242/jcs.070490.
    • (2010) J. Cell Sci. , vol.123 , pp. 2533-2542
    • Seo, A.Y.1    Joseph, A.-M.2    Dutta, D.3    Hwang, J.C.Y.4    Aris, J.P.5    Leeuwenburgh, C.6
  • 102
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • doi: 10.1074/jbc. M414670200
    • 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. doi: 10.1074/jbc. M414670200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 103
    • 78649509214 scopus 로고    scopus 로고
    • SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production
    • doi: 10.1016/j.cmet.2010.11.003
    • Shimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., et al. (2010). SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production. Cell Metab. 12, 654-661. doi: 10.1016/j.cmet.2010.11.003.
    • (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
  • 104
    • 77951176793 scopus 로고    scopus 로고
    • Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria
    • doi: 10.1242/jcs.061846
    • Shulga, N., Wilson-Smith, R., and Pastorino, J. G. (2010). Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria. J. Cell Sci. 123, 894-902. doi: 10.1242/jcs.061846.
    • (2010) J. Cell Sci. , vol.123 , pp. 894-902
    • Shulga, N.1    Wilson-Smith, R.2    Pastorino, J.G.3
  • 105
    • 33744465025 scopus 로고    scopus 로고
    • Mitochondria damage checkpoint, aging, and cancer
    • doi: 10.1196/annals.1354.022
    • Singh, K. K. (2006). Mitochondria damage checkpoint, aging, and cancer. Ann. N.Y. Acad. Sci. 1067, 182-190. doi: 10.1196/annals.1354.022.
    • (2006) Ann. N.Y. Acad. Sci. , vol.1067 , pp. 182-190
    • Singh, K.K.1
  • 106
    • 0019829662 scopus 로고
    • Relationships among local functional activity, energy metabolism, and blood flow in the central nervous system
    • Sokoloff, L. (1981). Relationships among local functional activity, energy metabolism, and blood flow in the central nervous system. Fed. Proc. 40, 2311-2316.
    • (1981) Fed. Proc. , vol.40 , pp. 2311-2316
    • Sokoloff, L.1
  • 107
    • 78651468722 scopus 로고    scopus 로고
    • Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
    • doi: 10.1016/j.cell.2010.10.002
    • Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., et al. (2010). Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 143, 802-812. doi: 10.1016/j.cell.2010.10.002.
    • (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
  • 108
    • 84872683148 scopus 로고    scopus 로고
    • Mutant SOD1(G93A) triggers mitochondrial fragmentation in spinal cord motor neurons: neuroprotection by SIRT3 and PGC-1a
    • doi: 10.1016/j.nbd.2012.07.004
    • Song, W., Song, Y., Kincaid, B., Bossy, B., and Bossy-Wetzel, E. (2012). Mutant SOD1(G93A) triggers mitochondrial fragmentation in spinal cord motor neurons: neuroprotection by SIRT3 and PGC-1a. Neurobiol. Dis. 51, 72-81. doi: 10.1016/j.nbd.2012.07.004.
    • (2012) Neurobiol. Dis. , vol.51 , pp. 72-81
    • Song, W.1    Song, Y.2    Kincaid, B.3    Bossy, B.4    Bossy-Wetzel, E.5
  • 109
    • 33748314528 scopus 로고    scopus 로고
    • Evidence for a mitochondrial regulatory pathway defined by peroxisome proliferator-activated receptor-gamma coactivator-1 alpha, estrogen-related receptor-alpha, and mitofusin 2
    • doi: 10.2337/db05-0509
    • Soriano, F. X., Liesa, M., Bach, D., Chan, D. C., Palacín, M., and Zorzano, A. (2006). Evidence for a mitochondrial regulatory pathway defined by peroxisome proliferator-activated receptor-gamma coactivator-1 alpha, estrogen-related receptor-alpha, and mitofusin 2. Diabetes 55, 1783-1791. doi: 10.2337/db05-0509.
    • (2006) Diabetes , vol.55 , pp. 1783-1791
    • Soriano, F.X.1    Liesa, M.2    Bach, D.3    Chan, D.C.4    Palacín, M.5    Zorzano, A.6
  • 110
    • 0024402834 scopus 로고
    • An assay for superoxide dismutase activity in mammalian tissue homogenates
    • doi: 10.1016/0003-2697(89)90192-9
    • Spitz, D. R., and Oberley, L. W. (1989). An assay for superoxide dismutase activity in mammalian tissue homogenates. Anal. Biochem. 179, 8-18. doi: 10.1016/0003-2697(89)90192-9.
    • (1989) Anal. Biochem. , vol.179 , pp. 8-18
    • Spitz, D.R.1    Oberley, L.W.2
  • 111
    • 33749999530 scopus 로고    scopus 로고
    • Suppression of reactive oxygen species and neurodegeneration by the PGC-1 transcriptional coactivators
    • doi: 10.1016/j.cell.2006.09.024
    • St-Pierre, J., Drori, S., Uldry, M., Silvaggi, J. M., Rhee, J., Jäger, S., et al. (2006). Suppression of reactive oxygen species and neurodegeneration by the PGC-1 transcriptional coactivators. Cell 127, 397-408. doi: 10.1016/j.cell.2006.09.024.
    • (2006) Cell , vol.127 , pp. 397-408
    • St-Pierre, J.1    Drori, S.2    Uldry, M.3    Silvaggi, J.M.4    Rhee, J.5    Jäger, S.6
  • 112
    • 0035989388 scopus 로고    scopus 로고
    • Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster
    • Sun, J., Folk, D., Bradley, T. J., and Tower, J. (2002). Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster. Genetics 161, 661-672.
    • (2002) Genetics , vol.161 , pp. 661-672
    • Sun, J.1    Folk, D.2    Bradley, T.J.3    Tower, J.4
  • 113
    • 70349208608 scopus 로고    scopus 로고
    • Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice
    • doi: 10.1172/JCI39162
    • Sundaresan, N. R., Gupta, M., Kim, G., Rajamohan, S. B., Isbatan, A., and Gupta, M. P. (2009). Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J. Clin. Invest. 119, 2758-2771. doi: 10.1172/JCI39162.
    • (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
  • 114
    • 53549105529 scopus 로고    scopus 로고
    • SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70
    • doi: 10.1128/MCB.00426-08
    • Sundaresan, N. R., Samant, S. A., Pillai, V. B., Rajamohan, S. B., and Gupta, M. P. (2008). SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol. Cell. Biol. 28, 6384-6401. doi: 10.1128/MCB.00426-08.
    • (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
  • 115
    • 0036403838 scopus 로고    scopus 로고
    • Oxidative stress increases expression and activity of BACE in NT2 neurons
    • doi: 10.1006/nbdi.2002.0515
    • Tamagno, E., Bardini, P., Obbili, A., Vitali, A., Borghi, R., Zaccheo, D., et al. (2002). Oxidative stress increases expression and activity of BACE in NT2 neurons. Neurobiol. Dis. 10, 279-288. doi: 10.1006/nbdi.2002.0515.
    • (2002) Neurobiol. Dis. , vol.10 , pp. 279-288
    • Tamagno, E.1    Bardini, P.2    Obbili, A.3    Vitali, A.4    Borghi, R.5    Zaccheo, D.6
  • 116
    • 78650248160 scopus 로고    scopus 로고
    • Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress
    • doi: 10.1016/j.molcel.2010.12.013
    • Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., et al. (2010). Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress. Mol. Cell 40, 893-904. doi: 10.1016/j.molcel.2010.12.013.
    • (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
  • 117
    • 31844439407 scopus 로고    scopus 로고
    • Sublethal mitochondrial stress with an attendant stoichiometric augmentation of reactive oxygen species may precipitate many of the beneficial alterations in cellular physiology produced by caloric restriction, intermittent fasting, exercise and dietary phytonutrients: "mitohormesis" for health and vitality
    • doi: 10.1016/j.mehy.2005.09.009
    • Tapia, P. C. (2006). Sublethal mitochondrial stress with an attendant stoichiometric augmentation of reactive oxygen species may precipitate many of the beneficial alterations in cellular physiology produced by caloric restriction, intermittent fasting, exercise and dietary phytonutrients: "mitohormesis" for health and vitality. Med. Hypotheses 66, 832-843. doi: 10.1016/j.mehy.2005.09.009.
    • (2006) Med. Hypotheses , vol.66 , pp. 832-843
    • Tapia, P.C.1
  • 118
    • 84863114113 scopus 로고    scopus 로고
    • Distinct effects of calorie restriction and resveratrol on diet-induced obesity and fatty liver formation
    • doi: 10.1155/2011/525094
    • Tauriainen, E., Luostarinen, M., Martonen, E., Finckenberg, P., Kovalainen, M., Huotari, A., et al. (2011). Distinct effects of calorie restriction and resveratrol on diet-induced obesity and fatty liver formation. J. Nutr. Metab. 2011, 525094. doi: 10.1155/2011/525094.
    • (2011) J. Nutr. Metab. , vol.2011 , pp. 525094
    • Tauriainen, E.1    Luostarinen, M.2    Martonen, E.3    Finckenberg, P.4    Kovalainen, M.5    Huotari, A.6
  • 119
    • 38949119766 scopus 로고    scopus 로고
    • AMP-activated protein kinase phosphorylates transcription factors of the CREB family
    • doi: 10.1152/japplphysiol.00900.2007
    • Thomson, D. M., Herway, S. T., Fillmore, N., Kim, H., Brown, J. D., Barrow, J. R., et al. (2008). AMP-activated protein kinase phosphorylates transcription factors of the CREB family. J. Appl. Physiol. 104, 429-438. doi: 10.1152/japplphysiol.00900.2007.
    • (2008) J. Appl. Physiol. , vol.104 , pp. 429-438
    • Thomson, D.M.1    Herway, S.T.2    Fillmore, N.3    Kim, H.4    Brown, J.D.5    Barrow, J.R.6
  • 120
    • 77549086301 scopus 로고    scopus 로고
    • Calcium and normal brain ageing
    • doi: 10.1016/j.ceca.2009.11.013
    • Toescu, E. C., and Vreugdenhil, M. (2010). Calcium and normal brain ageing. Cell Calcium 47, 158-164. doi: 10.1016/j.ceca.2009.11.013.
    • (2010) Cell Calcium , vol.47 , pp. 158-164
    • Toescu, E.C.1    Vreugdenhil, M.2
  • 121
    • 2642580016 scopus 로고    scopus 로고
    • Premature ageing in mice expressing defective mitochondrial DNA polymerase
    • doi: 10.1038/nature02517
    • Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., et al. (2004). Premature ageing in mice expressing defective mitochondrial DNA polymerase. Nature 429, 417-423. doi: 10.1038/nature02517.
    • (2004) Nature , vol.429 , pp. 417-423
    • Trifunovic, A.1    Wredenberg, A.2    Falkenberg, M.3    Spelbrink, J.N.4    Rovio, A.T.5    Bruder, C.E.6
  • 122
    • 78649328799 scopus 로고    scopus 로고
    • Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling
    • doi: 10.1016/j.tibs.2010.07.003
    • Verdin, E., Hirschey, M. D., Finley, L. W. S., and Haigis, M. C. (2010). Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling. Trends Biochem. Sci. 35, 669-675. doi: 10.1016/j.tibs.2010.07.003.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 669-675
    • Verdin, E.1    Hirschey, M.D.2    Finley, L.W.S.3    Haigis, M.C.4
  • 123
    • 0022517746 scopus 로고
    • The retardation of aging in mice by dietary restriction: longevity, cancer, immunity and lifetime energy intake
    • Weindruch, R., Walford, R. L., Fligiel, S., and Guthrie, D. (1986). The retardation of aging in mice by dietary restriction: longevity, cancer, immunity and lifetime energy intake. J. Nutr. 116, 641-654.
    • (1986) J. Nutr. , vol.116 , pp. 641-654
    • Weindruch, R.1    Walford, R.L.2    Fligiel, S.3    Guthrie, D.4
  • 124
    • 84876445381 scopus 로고    scopus 로고
    • CNS SIRT3 expression is altered by reactive oxygen species and in Alzheimer's disease
    • doi: 10.1371/journal.pone.0048225
    • Weir, H. J. M., Murray, T. K., Kehoe, P. G., Love, S., Verdin, E. M., O'Neill, M. J., et al. (2012). CNS SIRT3 expression is altered by reactive oxygen species and in Alzheimer's disease. PLoS ONE 7:e48225. doi: 10.1371/journal.pone.0048225.
    • (2012) PLoS ONE , vol.7
    • Weir, H.J.M.1    Murray, T.K.2    Kehoe, P.G.3    Love, S.4    Verdin, E.M.5    O'Neill, M.J.6
  • 125
    • 34548802393 scopus 로고    scopus 로고
    • Defective DNA base excision repair in brain from individuals with Alzheimer's disease and amnestic mild cognitive impairment
    • doi: 10.1093/nar/gkm605
    • Weissman, L., Jo, D.-G., Sørensen, M. M., de Souza-Pinto, N. C., Markesbery, W. R., Mattson, M. P., et al. (2007). Defective DNA base excision repair in brain from individuals with Alzheimer's disease and amnestic mild cognitive impairment. Nucleic Acids Res. 35, 5545-5555. doi: 10.1093/nar/gkm605.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5545-5555
    • Weissman, L.1    Jo, D.-G.2    Sørensen, M.M.3    de Souza-Pinto, N.C.4    Markesbery, W.R.5    Mattson, M.P.6
  • 126
    • 52949122885 scopus 로고    scopus 로고
    • FOXO3A genotype is strongly associated with human longevity
    • doi: 10.1073/pnas.0801030105
    • Willcox, B. J., Donlon, T. A., He, Q., Chen, R., Grove, J. S., Yano, K., et al. (2008). FOXO3A genotype is strongly associated with human longevity. Proc. Natl. Acad. Sci. U.S.A. 105, 13987-13992. doi: 10.1073/pnas.0801030105.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13987-13992
    • Willcox, B.J.1    Donlon, T.A.2    He, Q.3    Chen, R.4    Grove, J.S.5    Yano, K.6
  • 127
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • doi: 10.1038/nn.2575
    • Wong, E., and Cuervo, A. M. (2010). Autophagy gone awry in neurodegenerative diseases. Nat. Neurosci. 13, 805-811. doi: 10.1038/nn.2575.
    • (2010) Nat. Neurosci. , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 128
    • 10744230065 scopus 로고    scopus 로고
    • LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
    • doi: 10.1016/j.cub.2003.10.031
    • Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., et al. (2003). LKB1 is the upstream kinase in the AMP-activated protein kinase cascade. Curr. Biol. 13, 2004-2008. doi: 10.1016/j.cub.2003.10.031.
    • (2003) Curr. Biol. , vol.13 , pp. 2004-2008
    • Woods, A.1    Johnstone, S.R.2    Dickerson, K.3    Leiper, F.C.4    Fryer, L.G.D.5    Neumann, D.6
  • 129
    • 84868562852 scopus 로고    scopus 로고
    • Regulation of mitochondrial F(o)F(1)ATPase activity by Sirt3-catalyzed deacetylation and its deficiency in human cells harboring 4977bp deletion of mitochondrial DNA
    • doi: 10.1016/j.bbadis.2012.10.002
    • Wu, Y.-T., Lee, H.-C., Liao, C.-C., and Wei, Y.-H. (2013). Regulation of mitochondrial F(o)F(1)ATPase activity by Sirt3-catalyzed deacetylation and its deficiency in human cells harboring 4977bp deletion of mitochondrial DNA. Biochim. Biophys. Acta 1832, 216-227. doi: 10.1016/j.bbadis.2012.10.002.
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 216-227
    • Wu, Y.-T.1    Lee, H.-C.2    Liao, C.-C.3    Wei, Y.-H.4
  • 130
    • 0037115050 scopus 로고    scopus 로고
    • Changes in mitochondrial status associated with altered Ca2+ homeostasis in aged cerebellar granule neurons in brain slices
    • Xiong, J., Verkhratsky, A., and Toescu, E. C. (2002). Changes in mitochondrial status associated with altered Ca2+ homeostasis in aged cerebellar granule neurons in brain slices. J. Neurosci. 22, 10761-10771.
    • (2002) J. Neurosci. , vol.22 , pp. 10761-10771
    • Xiong, J.1    Verkhratsky, A.2    Toescu, E.C.3
  • 131
    • 84855757015 scopus 로고    scopus 로고
    • Acetylation-dependent regulation of mitochondrial ALDH2 activation by SIRT3 mediates acute ethanol-induced eNOS activation
    • doi: 10.1016/j.febslet.2011.11.031
    • Xue, L., Xu, F., Meng, L., Wei, S., Wang, J., Hao, P., et al. (2012). Acetylation-dependent regulation of mitochondrial ALDH2 activation by SIRT3 mediates acute ethanol-induced eNOS activation. FEBS Lett. 586, 137-142. doi: 10.1016/j.febslet.2011.11.031.
    • (2012) FEBS Lett. , vol.586 , pp. 137-142
    • Xue, L.1    Xu, F.2    Meng, L.3    Wei, S.4    Wang, J.5    Hao, P.6
  • 132
    • 79960339919 scopus 로고    scopus 로고
    • The dynamin-related protein DRP-1 and the insulin signaling pathway cooperate to modulate Caenorhabditis elegans longevity
    • doi: 10.1111/j.1474-9726.2011.00711.x
    • Yang, C. C., Chen, D., Lee, S. S., and Walter, L. (2011). The dynamin-related protein DRP-1 and the insulin signaling pathway cooperate to modulate Caenorhabditis elegans longevity. Aging Cell 10, 724-728. doi: 10.1111/j.1474-9726.2011.00711.x.
    • (2011) Aging Cell , vol.10 , pp. 724-728
    • Yang, C.C.1    Chen, D.2    Lee, S.S.3    Walter, L.4
  • 133
    • 34548627517 scopus 로고    scopus 로고
    • Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival
    • doi: 10.1016/j.cell.2007.07.035
    • Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., et al. (2007). Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival. Cell 130, 1095-1107. doi: 10.1016/j.cell.2007.07.035.
    • (2007) Cell , vol.130 , pp. 1095-1107
    • Yang, H.1    Yang, T.2    Baur, J.A.3    Perez, E.4    Matsui, T.5    Carmona, J.J.6
  • 134
    • 77951235122 scopus 로고    scopus 로고
    • +-dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10
    • doi: 10.1074/jbc. M109.053421
    • +-dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10. J. Biol. Chem. 285, 7417-7429. doi: 10.1074/jbc. M109.053421.
    • (2010) 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
  • 135
    • 0035855858 scopus 로고    scopus 로고
    • Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1
    • doi: 10.1038/35093050
    • Yoon, J. C., Puigserver, P., Chen, G., Donovan, J., Wu, Z., Rhee, J., et al. (2001). Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1. Nature 413, 131-138. doi: 10.1038/35093050.
    • (2001) Nature , vol.413 , pp. 131-138
    • Yoon, J.C.1    Puigserver, P.2    Chen, G.3    Donovan, J.4    Wu, Z.5    Rhee, J.6
  • 136
    • 84859951790 scopus 로고    scopus 로고
    • SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
    • doi: 10.1074/jbc. M112.355206
    • Yu, W., Dittenhafer-Reed, K. E., and Denu, J. M. (2012). SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status. J. Biol. Chem. 287, 14078-14086. doi: 10.1074/jbc. M112.355206.
    • (2012) J. Biol. Chem. , vol.287 , pp. 14078-14086
    • Yu, W.1    Dittenhafer-Reed, K.E.2    Denu, J.M.3
  • 137
    • 0029591486 scopus 로고
    • Identification and purification of a bovine liver mitochondrial NAD(+)-glycohydrolase
    • doi: 10.1016/0014-5793(95)01366-0
    • Zhang, J., Ziegler, M., Schneider, R., Klocker, H., Auer, B., and Schweiger, M. (1995). Identification and purification of a bovine liver mitochondrial NAD(+)-glycohydrolase. FEBS Lett. 377, 530-534. doi: 10.1016/0014-5793(95)01366-0.
    • (1995) FEBS Lett. , vol.377 , pp. 530-534
    • Zhang, J.1    Ziegler, M.2    Schneider, R.3    Klocker, H.4    Auer, B.5    Schweiger, M.6
  • 138
    • 0033581321 scopus 로고    scopus 로고
    • Dietary restriction protects hippocampal neurons against the death-promoting action of a presenilin-1 mutation
    • doi: 10.1016/S0006-8993(99)01827-2
    • Zhu, H., Guo, Q., and Mattson, M. P. (1999). Dietary restriction protects hippocampal neurons against the death-promoting action of a presenilin-1 mutation. Brain Res. 842, 224-229. doi: 10.1016/S0006-8993(99)01827-2.
    • (1999) Brain Res. , vol.842 , pp. 224-229
    • Zhu, H.1    Guo, Q.2    Mattson, M.P.3
  • 139
    • 0037058977 scopus 로고    scopus 로고
    • AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation
    • doi: 10.1073/pnas.252625599w
    • Zong, H., Ren, J. M., Young, L. H., Pypaert, M., Mu, J., Birnbaum, M. J., et al. (2002). AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. Proc. Natl. Acad. Sci. U.S.A. 99, 15983-15987. doi: 10.1073/pnas.252625599w.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 15983-15987
    • Zong, H.1    Ren, J.M.2    Young, L.H.3    Pypaert, M.4    Mu, J.5    Birnbaum, M.J.6


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