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Volumn 5, Issue SEP, 2013, Pages

Sirtuins in neurodegenerative diseases: An update on potential mechanisms

Author keywords

Amyloid ; Epigenetic regulation; Inflammation; Mitochondria; Neurodegeneration; NF B; SIRT1; Tau

Indexed keywords

DNA; HISTONE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN; SIRTUIN; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; SIRTUIN 6; SIRTUIN 7;

EID: 84895817637     PISSN: None     EISSN: 16634365     Source Type: Journal    
DOI: 10.3389/fnagi.2013.00053     Document Type: Review
Times cited : (110)

References (105)
  • 1
    • 41849136515 scopus 로고    scopus 로고
    • Reversal of aging by NFkappaB blockade
    • doi: 10.4161/cc.7.5.5490
    • Adler, A. S., Kawahara, T. L., Segal, E., and Chang, H. Y. (2008). Reversal of aging by NFkappaB blockade. Cell Cycle 7, 556-569. doi: 10.4161/cc.7.5.5490.
    • (2008) Cell Cycle , vol.7 , pp. 556-569
    • Adler, A.S.1    Kawahara, T.L.2    Segal, E.3    Chang, H.Y.4
  • 2
    • 37249009271 scopus 로고    scopus 로고
    • Motif module map reveals enforcement of aging by continual NF-kappaB activity
    • doi: 10.1101/gad.1588507
    • Adler, A. S., Sinha, S., Kawahara, T. L., Zhang, J. Y., Segal, E., and Chang, H. Y. (2007). Motif module map reveals enforcement of aging by continual NF-kappaB activity. Genes Dev. 21, 3244-3257. doi: 10.1101/gad.1588507.
    • (2007) Genes Dev. , vol.21 , pp. 3244-3257
    • Adler, A.S.1    Sinha, S.2    Kawahara, T.L.3    Zhang, J.Y.4    Segal, E.5    Chang, H.Y.6
  • 3
    • 68949206606 scopus 로고    scopus 로고
    • The SIRT1 activator resveratrol protects SK-N-BE cells from oxidative stress and against toxicity caused by alpha-synuclein or amyloid-beta (1-42) peptide
    • doi: 10.1111/j.1471-4159.2009.06228.x
    • Albani, D., Polito, L., Batelli, S., De Mauro, S., Fracasso, C., Martelli, G., et al. (2009). The SIRT1 activator resveratrol protects SK-N-BE cells from oxidative stress and against toxicity caused by alpha-synuclein or amyloid-beta (1-42) peptide. J. Neurochem. 110, 1445-1456. doi: 10.1111/j.1471-4159.2009.06228.x.
    • (2009) J. Neurochem. , vol.110 , pp. 1445-1456
    • Albani, D.1    Polito, L.2    Batelli, S.3    De Mauro, S.4    Fracasso, C.5    Martelli, G.6
  • 4
    • 0028280455 scopus 로고
    • C/EBP is an immediate-early gene required for the consolidation of long-term facilitation in Aplysia
    • doi: 10.1016/0092-8674(94)90386-7
    • Alberini, C. M., Ghirardi, M., Metz, R., and Kandel, E. R. (1994). C/EBP is an immediate-early gene required for the consolidation of long-term facilitation in Aplysia. Cell 76, 1099-114. doi: 10.1016/0092-8674(94)90386-7.
    • (1994) Cell , vol.76 , pp. 1099-1114
    • Alberini, C.M.1    Ghirardi, M.2    Metz, R.3    Kandel, E.R.4
  • 5
    • 69249116960 scopus 로고    scopus 로고
    • SIRT1 controls the transcription of the peroxisome proliferator-activated receptor-{gamma} co-activator-1{alpha} (PGC-1{alpha}) gene in skeletal muscle through the PGC-1{alpha} autoregulatory loop and interaction with MyoD
    • doi: 10.1074/jbc. M109.022749
    • Amat, R., Planavila, A., Chen, S. L., Iglesias, R., Giralt, M., and Villarroya, F. (2009). SIRT1 controls the transcription of the peroxisome proliferator-activated receptor-{gamma} co-activator-1{alpha} (PGC-1{alpha}) gene in skeletal muscle through the PGC-1{alpha} autoregulatory loop and interaction with MyoD. J. Biol. Chem. 284, 21872-21880. doi: 10.1074/jbc. M109.022749.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21872-21880
    • Amat, R.1    Planavila, A.2    Chen, S.L.3    Iglesias, R.4    Giralt, M.5    Villarroya, F.6
  • 6
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: cause or consequence?
    • doi: 10.1038/nrn1434.
    • Andersen, J. K. (2004). Oxidative stress in neurodegeneration: cause or consequence? Nat. Med. 10(Suppl.) S18-S25. doi: 10.1038/nrn1434.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Andersen, J.K.1
  • 7
    • 79953752384 scopus 로고    scopus 로고
    • PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation
    • doi: 10.1016/j.cmet.2011.03.004
    • Bai, P., Canto, C., Oudart, H., Brunyanszki, 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    Canto, C.2    Oudart, H.3    Brunyanszki, A.4    Cen, Y.5    Thomas, C.6
  • 8
    • 84871695502 scopus 로고    scopus 로고
    • dSir2 in the adult fat body, but not in muscles, regulates life span in a diet-dependent manner
    • doi: 10.1016/j.celrep.2012.11.013
    • Banerjee, K. K., Ayyub, C., Ali, S. Z., Mandot, V., Prasad, N. G., and Kolthur-Seetharam, U. (2012). dSir2 in the adult fat body, but not in muscles, regulates life span in a diet-dependent manner. Cell Rep. 2, 1485-1491. doi: 10.1016/j.celrep.2012.11.013.
    • (2012) Cell Rep. , vol.2 , pp. 1485-1491
    • Banerjee, K.K.1    Ayyub, C.2    Ali, S.Z.3    Mandot, V.4    Prasad, N.G.5    Kolthur-Seetharam, U.6
  • 9
    • 84861852370 scopus 로고    scopus 로고
    • Are sirtuins viable targets for improving healthspan and lifespan?
    • doi: 10.1038/nrd3738
    • Baur, J. A., Ungvari, Z., Minor, R. K., Le Couteur, D. G., and de Cabo, R. (2012). Are sirtuins viable targets for improving healthspan and lifespan? Nat. Rev. Drug Discov. 11, 443-461. doi: 10.1038/nrd3738.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 443-461
    • Baur, J.A.1    Ungvari, Z.2    Minor, R.K.3    Le Couteur, D.G.4    de Cabo, R.5
  • 10
    • 84871538934 scopus 로고    scopus 로고
    • Regulation of chromatin structure by poly(ADP-ribosyl)ation
    • doi: 10.3389/fgene.2012.00169
    • Beneke, S. (2012). Regulation of chromatin structure by poly(ADP-ribosyl)ation. Front. Genet. 3:169. doi: 10.3389/fgene.2012.00169.
    • (2012) Front. Genet. , vol.3 , pp. 169
    • Beneke, S.1
  • 11
    • 14444285507 scopus 로고    scopus 로고
    • Clinicopathologic studies in cognitively healthy aging and Alzheimer's disease: relation of histologic markers to dementia severity, age, sex, and apolipoprotein E genotype
    • doi: 10.1001/archneur.55.3.326
    • Berg, L., McKeel, D. W. Jr., Miller, J. P., Storandt, M., Rubin, E. H., Morris, J. C., et al. (1998). Clinicopathologic studies in cognitively healthy aging and Alzheimer's disease: relation of histologic markers to dementia severity, age, sex, and apolipoprotein E genotype. Arch. Neurol. 55, 326-335. doi: 10.1001/archneur.55.3.326.
    • (1998) Arch. Neurol. , vol.55 , pp. 326-335
    • Berg, L.1    McKeel Jr., D.W.2    Miller, J.P.3    Storandt, M.4    Rubin, E.H.5    Morris, J.C.6
  • 12
    • 33847032960 scopus 로고    scopus 로고
    • The mammalian epigenome
    • doi: 10.1016/j.cell.2007.01.033
    • Bernstein, B. E., Meissner, A., and Lander, E. S. (2007). The mammalian epigenome. Cell 128, 669-681. doi: 10.1016/j.cell.2007.01.033.
    • (2007) Cell , vol.128 , pp. 669-681
    • Bernstein, B.E.1    Meissner, A.2    Lander, E.S.3
  • 13
    • 0027476024 scopus 로고
    • A synaptic model of memory: long-term potentiation in the hippocampus
    • doi: 10.1038/361031a0
    • Bliss, T. V., and Collingridge, G. L. (1993). A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361, 31-39. doi: 10.1038/361031a0.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.1    Collingridge, G.L.2
  • 14
    • 84887020906 scopus 로고    scopus 로고
    • Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3
    • doi: 10.1016/j.mito.2013.04.002 [Epub ahead of print].
    • Brenmoehl, J., and Hoeflich, A. (2013). Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3. Mitochondrion. doi: 10.1016/j.mito.2013.04.002 [Epub ahead of print].
    • (2013) Mitochondrion
    • Brenmoehl, J.1    Hoeflich, A.2
  • 16
    • 34447096691 scopus 로고    scopus 로고
    • Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the consortium for frontotemporal lobar degeneration
    • doi: 10.1007/s00401-007-0237-2
    • Cairns, N. J., Bigio, E. H., Mackenzie, I. R., Neumann, M., Lee, V. M., Hatanpaa, K. J., et al. (2007). Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the consortium for frontotemporal lobar degeneration. Acta Neuropathol. 114, 5-22. doi: 10.1007/s00401-007-0237-2.
    • (2007) Acta Neuropathol. , vol.114 , pp. 5-22
    • Cairns, N.J.1    Bigio, E.H.2    Mackenzie, I.R.3    Neumann, M.4    Lee, V.M.5    Hatanpaa, K.J.6
  • 17
    • 84886717428 scopus 로고    scopus 로고
    • Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes
    • doi: 10.1016/j.mam.2013.01.004 [Epub ahead of print].
    • Canto, C., Sauve, A. A., and Bai, P. (2013). Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes. Mol. Aspects Med. doi: 10.1016/j.mam.2013.01.004 [Epub ahead of print].
    • (2013) Mol. Aspects Med
    • Canto, C.1    Sauve, A.A.2    Bai, P.3
  • 18
    • 0035845492 scopus 로고    scopus 로고
    • Genomic profiling of short-and long-term caloric restriction effects in the liver of aging mice
    • doi: 10.1073/pnas.191313598
    • Cao, S. X., Dhahbi, J. M., Mote, P. L., and Spindler, S. R. (2001). Genomic profiling of short-and long-term caloric restriction effects in the liver of aging mice. Proc. Natl. Acad. Sci. U.S.A. 98, 10630-10635. doi: 10.1073/pnas.191313598.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10630-10635
    • Cao, S.X.1    Dhahbi, J.M.2    Mote, P.L.3    Spindler, S.R.4
  • 19
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent amyloid-{beta} toxicity through inhibiting NF-{kappa}B signaling
    • doi: 10.1074/jbc. M509329200
    • Chen, J., Zhou, Y., Mueller-Steiner, S., Chen, L. F., Kwon, H., and Yi, S. (2005). SIRT1 protects against microglia-dependent amyloid-{beta} toxicity through inhibiting NF-{kappa}B signaling. J. Biol. Chem. 280, 40364-40374. doi: 10.1074/jbc. M509329200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40364-40374
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3    Chen, L.F.4    Kwon, H.5    Yi, S.6
  • 20
    • 0141594607 scopus 로고    scopus 로고
    • Regulation of distinct biological activities of the NF-kappaB transcription factor complex by acetylation
    • doi: 10.1007/s00109-003-0469-0
    • Chen, L. F., and Greene, W. C. (2003). Regulation of distinct biological activities of the NF-kappaB transcription factor complex by acetylation. J. Mol. Med. (Berl.) 81, 549-57. doi: 10.1007/s00109-003-0469-0.
    • (2003) J. Mol. Med. (Berl.) , vol.81 , pp. 549-557
    • Chen, L.F.1    Greene, W.C.2
  • 21
    • 79953087890 scopus 로고    scopus 로고
    • The acetylation of tau inhibits its function and promotes pathological tau aggregation
    • doi: 10.1038/ncomms1255
    • Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., and Trojanowski, J. Q. (2011). The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat. Commun. 2, 252. doi: 10.1038/ncomms1255.
    • (2011) Nat. Commun. , vol.2 , pp. 252
    • Cohen, T.J.1    Guo, J.L.2    Hurtado, D.E.3    Kwong, L.K.4    Mills, I.P.5    Trojanowski, J.Q.6
  • 22
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • doi: 10.1016/j.cell.2006.09.015
    • Cui, L., Jeong, H., Borovecki, F., Parkhurst, C. N., Tanese, N., and Krainc, D. (2006). Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 127, 59-69. doi: 10.1016/j.cell.2006.09.015.
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 23
    • 79958038559 scopus 로고    scopus 로고
    • Epigenetic mechanisms in cognition
    • doi: 10.1016/j.neuron.2011.05.019
    • Day, J. J., and Sweatt, J. D. (2011). Epigenetic mechanisms in cognition. Neuron 70, 813-829. doi: 10.1016/j.neuron.2011.05.019.
    • (2011) Neuron , vol.70 , pp. 813-829
    • Day, J.J.1    Sweatt, J.D.2
  • 24
    • 84855929223 scopus 로고    scopus 로고
    • SIRT1 protects against alpha-synuclein aggregation by activating molecular chaperones
    • doi: 10.1523/JNEUROSCI.3442-11.2012
    • Donmez, G., Arun, A., Chung, C. Y., McLean, P. J., Lindquist, S., and Guarente, L. (2012). SIRT1 protects against alpha-synuclein aggregation by activating molecular chaperones. J. Neurosci. 32, 124-132. doi: 10.1523/JNEUROSCI.3442-11.2012.
    • (2012) J. Neurosci. , vol.32 , pp. 124-132
    • Donmez, G.1    Arun, A.2    Chung, C.Y.3    McLean, P.J.4    Lindquist, S.5    Guarente, L.6
  • 25
    • 84874709843 scopus 로고    scopus 로고
    • SIRT1 and SIRT2: emerging targets in neurodegeneration
    • doi: 10.1002/emmm.201302451
    • Donmez, G., and Outeiro, T. F. (2013). SIRT1 and SIRT2: emerging targets in neurodegeneration. EMBO Mol. Med. 5, 344-352. doi: 10.1002/emmm.201302451.
    • (2013) EMBO Mol. Med. , vol.5 , pp. 344-352
    • Donmez, G.1    Outeiro, T.F.2
  • 26
    • 77955046461 scopus 로고    scopus 로고
    • SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10
    • doi: 10.1016/j.cell.2010.06.020
    • Donmez, G., Wang, D., Cohen, D. E., and Guarente, L. (2010). SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10. Cell 142, 320-332. doi: 10.1016/j.cell.2010.06.020.
    • (2010) Cell , vol.142 , pp. 320-332
    • Donmez, G.1    Wang, D.2    Cohen, D.E.3    Guarente, L.4
  • 27
    • 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
  • 28
    • 34248523169 scopus 로고    scopus 로고
    • Recovery of learning and memory is associated with chromatin remodelling
    • doi: 10.1038/nature05772
    • Fischer, A., Sananbenesi, F., Wang, X., Dobbin, M., and Tsai, L. H. (2007). Recovery of learning and memory is associated with chromatin remodelling. Nature 447, 178-182. doi: 10.1038/nature05772.
    • (2007) Nature , vol.447 , pp. 178-182
    • Fischer, A.1    Sananbenesi, F.2    Wang, X.3    Dobbin, M.4    Tsai, L.H.5
  • 29
    • 33744466971 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
    • doi: 10.1101/gad.1399706
    • 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. doi: 10.1101/gad.1399706.
    • (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
  • 30
    • 33846111415 scopus 로고    scopus 로고
    • Inflammaging and anti-inflammaging: a systemic perspective on aging and longevity emerged from studies in humans
    • doi: 10.1016/j.mad.2006.11.016
    • Franceschi, C., Capri, M., Monti, D., Giunta, S., Olivieri, F., Sevini, F., et al. (2007). Inflammaging and anti-inflammaging: a systemic perspective on aging and longevity emerged from studies in humans. Mech. Ageing Dev. 128, 92-105. doi: 10.1016/j.mad.2006.11.016.
    • (2007) Mech. Ageing Dev. , vol.128 , pp. 92-105
    • Franceschi, C.1    Capri, M.2    Monti, D.3    Giunta, S.4    Olivieri, F.5    Sevini, F.6
  • 31
    • 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
  • 32
    • 84863794891 scopus 로고    scopus 로고
    • Trans-(-)-epsilon-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-(-)-epsilon-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
  • 33
    • 84855994224 scopus 로고    scopus 로고
    • A role for neuronal cAMP responsive-element binding (CREB)-1 in brain responses to calorie restriction
    • doi: 10.1073/pnas.1109237109
    • Fusco, S., Ripoli, C., Podda, M. V., Ranieri, S. C., Leone, L. G., Toietta, M. W., et al. (2012). A role for neuronal cAMP responsive-element binding (CREB)-1 in brain responses to calorie restriction. Proc. Natl. Acad. Sci. U.S.A. 109, 621-626. doi: 10.1073/pnas.1109237109.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 621-626
    • Fusco, S.1    Ripoli, C.2    Podda, M.V.3    Ranieri, S.C.4    Leone, L.G.5    Toietta, M.W.6
  • 34
    • 84870052890 scopus 로고    scopus 로고
    • SIRT2 interferes with autophagy-mediated degradation of protein aggregates in neuronal cells under proteasome inhibition
    • doi: 10.1016/j.neuint.2012.07.010
    • Gal, J., Bang, Y., and Choi, H. J. (2012). SIRT2 interferes with autophagy-mediated degradation of protein aggregates in neuronal cells under proteasome inhibition. Neurochem. Int. 61, 992-1000. doi: 10.1016/j.neuint.2012.07.010.
    • (2012) Neurochem. Int. , vol.61 , pp. 992-1000
    • Gal, J.1    Bang, Y.2    Choi, H.J.3
  • 35
    • 77956185062 scopus 로고    scopus 로고
    • A novel pathway regulates memory and plasticity via SIRT1 and miR-134
    • doi: 10.1038/nature09271
    • Gao, J., Wang, W. Y., Mao, Y. W., Graff, J., Guan, J. S., Pan, L., et al. (2010). A novel pathway regulates memory and plasticity via SIRT1 and miR-134. Nature 466, 1105-1109. doi: 10.1038/nature09271.
    • (2010) Nature , vol.466 , pp. 1105-1109
    • Gao, J.1    Wang, W.Y.2    Mao, Y.W.3    Graff, J.4    Guan, J.S.5    Pan, L.6
  • 36
    • 77950363010 scopus 로고    scopus 로고
    • Mechanisms underlying inflammation in neurodegeneration
    • doi: 10.1016/j.cell.2010.02.016
    • Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., and Gage, F. H. (2010). Mechanisms underlying inflammation in neurodegeneration. Cell 140, 918-934. doi: 10.1016/j.cell.2010.02.016.
    • (2010) Cell , vol.140 , pp. 918-934
    • Glass, C.K.1    Saijo, K.2    Winner, B.3    Marchetto, M.C.4    Gage, F.H.5
  • 38
    • 84876695265 scopus 로고    scopus 로고
    • Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation
    • doi: 10.1007/s00401-013-1080-2
    • Grinberg, L. T., Wang, X., Wang, C., Sohn, P. D., Theofilas, P., Sidhu, M., et al. (2013). Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation. Acta Neuropathol. 125, 581-593. doi: 10.1007/s00401-013-1080-2.
    • (2013) Acta Neuropathol. , vol.125 , pp. 581-593
    • Grinberg, L.T.1    Wang, X.2    Wang, C.3    Sohn, P.D.4    Theofilas, P.5    Sidhu, M.6
  • 39
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • doi: 10.1126/science.1072994
    • Hardy, J., and Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356. doi: 10.1126/science.1072994.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 40
    • 84857577343 scopus 로고    scopus 로고
    • Inflammation, DNA methylation and colitis-associated cancer
    • doi: 10.1093/carcin/bgs006
    • Hartnett, L., and Egan, L. J. (2012). Inflammation, DNA methylation and colitis-associated cancer. Carcinogenesis 33, 723-731. doi: 10.1093/carcin/bgs006.
    • (2012) Carcinogenesis , vol.33 , pp. 723-731
    • Hartnett, L.1    Egan, L.J.2
  • 41
    • 84875999020 scopus 로고    scopus 로고
    • Regulated transcription of human matrix metalloproteinase 13 (MMP13) and interleukin-1beta (IL1B) genes in chondrocytes depends on methylation of specific proximal promoter CpG sites
    • doi: 10.1074/jbc. M112.421156
    • Hashimoto, K., Otero, M., Imagawa, K., de Andres, M. C., Coico, J. M., Roach, R. O., et al. (2013). Regulated transcription of human matrix metalloproteinase 13 (MMP13) and interleukin-1beta (IL1B) genes in chondrocytes depends on methylation of specific proximal promoter CpG sites. J. Biol. Chem. 288, 10061-10072. doi: 10.1074/jbc. M112.421156.
    • (2013) J. Biol. Chem. , vol.288 , pp. 10061-10072
    • Hashimoto, K.1    Otero, M.2    Imagawa, K.3    de Andres, M.C.4    Coico, J.M.5    Roach, R.O.6
  • 42
    • 84856641109 scopus 로고    scopus 로고
    • NF-kappaB, the first quarter-century: remarkable progress and outstanding questions
    • doi: 10.1101/gad.183434.111
    • Hayden, M. S., and Ghosh, S. (2012). NF-kappaB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev. 26, 203-234. doi: 10.1101/gad.183434.111.
    • (2012) Genes Dev. , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 43
    • 3042693940 scopus 로고    scopus 로고
    • Glutamate-mediated excitotoxicity and neurodegeneration in Alzheimer's disease
    • doi: 10.1016/j.neuint.2004.03.007
    • Hynd, M. R., Scott, H. L., and Dodd, P. R. (2004). Glutamate-mediated excitotoxicity and neurodegeneration in Alzheimer's disease. Neurochem. Int. 45, 583-595. doi: 10.1016/j.neuint.2004.03.007.
    • (2004) Neurochem. Int. , vol.45 , pp. 583-595
    • Hynd, M.R.1    Scott, H.L.2    Dodd, P.R.3
  • 44
    • 84857620173 scopus 로고    scopus 로고
    • Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies
    • doi: 10.1093/brain/aws013
    • Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., Xie, S. X., and Lee, V. M. (2012). Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies. Brain 135, 807-818. doi: 10.1093/brain/aws013.
    • (2012) Brain , vol.135 , pp. 807-818
    • Irwin, D.J.1    Cohen, T.J.2    Grossman, M.3    Arnold, S.E.4    Xie, S.X.5    Lee, V.M.6
  • 45
    • 84855563516 scopus 로고    scopus 로고
    • Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway
    • doi: 10.1038/nm.2559
    • Jeong, H., Cohen, D. E., Cui, L., Supinski, A., Savas, J. N., Mazzulli, J. R., et al. (2012). Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway. Nat. Med. 18, 159-165. doi: 10.1038/nm.2559.
    • (2012) Nat. Med. , vol.18 , pp. 159-165
    • Jeong, H.1    Cohen, D.E.2    Cui, L.3    Supinski, A.4    Savas, J.N.5    Mazzulli, J.R.6
  • 46
    • 84868139191 scopus 로고    scopus 로고
    • Autophagy induced by the class III histone deacetylase Sirt1 prevents prion peptide neurotoxicity
    • doi: 10.1016/j.neurobiolaging.2012.04.002
    • Jeong, J. K., Moon, M. H., Lee, Y. J., Seol, J. W., and Park, S. Y. (2013). Autophagy induced by the class III histone deacetylase Sirt1 prevents prion peptide neurotoxicity. Neurobiol. Aging 34, 146-156. doi: 10.1016/j.neurobiolaging.2012.04.002.
    • (2013) Neurobiol. Aging , vol.34 , pp. 146-156
    • Jeong, J.K.1    Moon, M.H.2    Lee, Y.J.3    Seol, J.W.4    Park, S.Y.5
  • 47
    • 84863981612 scopus 로고    scopus 로고
    • Emerging roles of SIRT6 on telomere maintenance, DNA repair, metabolism and mammalian aging
    • doi: 10.1007/s11010-012-1236-8
    • Jia, G., Su, L., Singhal, S., and Liu, X. (2012). Emerging roles of SIRT6 on telomere maintenance, DNA repair, metabolism and mammalian aging. Mol. Cell. Biochem. 364, 345-350. doi: 10.1007/s11010-012-1236-8.
    • (2012) Mol. Cell. Biochem. , vol.364 , pp. 345-350
    • Jia, G.1    Su, L.2    Singhal, S.3    Liu, X.4
  • 48
    • 84855544817 scopus 로고    scopus 로고
    • Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets
    • doi: 10.1038/nm.2558
    • Jiang, M., Wang, J., Fu, J., Du, L., Jeong, H., West, T., et al. (2012). Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets. Nat. Med. 18, 153-8. doi: 10.1038/nm.2558.
    • (2012) Nat. Med. , vol.18 , pp. 153-158
    • Jiang, M.1    Wang, J.2    Fu, J.3    Du, L.4    Jeong, H.5    West, T.6
  • 50
    • 64049092736 scopus 로고    scopus 로고
    • Sirtuin 1 reduction parallels the accumulation of tau in Alzheimer disease
    • doi: 10.1097/NEN.0b013e3181922348
    • Julien, C., Tremblay, C., Emond, V., Lebbadi, M., Salem, N. Jr., Bennett, D. A., et al. (2009). Sirtuin 1 reduction parallels the accumulation of tau in Alzheimer disease. J. Neuropathol. Exp. Neurol. 68, 48-58. doi: 10.1097/NEN.0b013e3181922348.
    • (2009) J. Neuropathol. Exp. Neurol. , vol.68 , pp. 48-58
    • Julien, C.1    Tremblay, C.2    Emond, V.3    Lebbadi, M.4    Salem Jr., N.5    Bennett, D.A.6
  • 51
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NF-kappaB activation: distinct redox regulation between the cytoplasm and the nucleus
    • doi: 10.1089/ars.2005.7.395
    • Kabe, Y., Ando, K., Hirao, S., Yoshida, M., and Handa, H. (2005). Redox regulation of NF-kappaB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid. Redox Signal. 7, 395-403. doi: 10.1089/ars.2005.7.395.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 395-403
    • Kabe, Y.1    Ando, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 52
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • doi: 10.1101/gad.13.19.2570
    • Kaeberlein, M., McVey, M., 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. doi: 10.1101/gad.13.19.2570.
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 53
    • 84858000209 scopus 로고    scopus 로고
    • The sirtuin SIRT6 regulates lifespan in male mice
    • doi: 10.1038/nature10815
    • Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., et al. (2012). The sirtuin SIRT6 regulates lifespan in male mice. Nature 483, 218-221. doi: 10.1038/nature10815.
    • (2012) Nature , vol.483 , pp. 218-221
    • Kanfi, Y.1    Naiman, S.2    Amir, G.3    Peshti, V.4    Zinman, G.5    Nahum, L.6
  • 54
    • 84877795435 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor-kappaB transcriptional activity by preventing p65 de-acetylation
    • doi: 10.1016/j.bbamcr.2013.04.005
    • Kauppinen, T. M., Gan, L., and Swanson, R. A. (2013). Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor-kappaB transcriptional activity by preventing p65 de-acetylation. Biochim. Biophys. Acta 1833, 1985-1991. doi: 10.1016/j.bbamcr.2013.04.005.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 1985-1991
    • Kauppinen, T.M.1    Gan, L.2    Swanson, R.A.3
  • 55
    • 58149090925 scopus 로고    scopus 로고
    • SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span
    • doi: 10.1016/j.cell.2008.10.052
    • Kawahara, T. L., Michishita, E., Adler, A. S., Damian, M., Berber, E., Lin, M., et al. (2009). SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span. Cell 136, 62-74. doi: 10.1016/j.cell.2008.10.052.
    • (2009) Cell , vol.136 , pp. 62-74
    • Kawahara, T.L.1    Michishita, E.2    Adler, A.S.3    Damian, M.4    Berber, E.5    Lin, M.6
  • 56
    • 77950200010 scopus 로고    scopus 로고
    • The genetics of ageing
    • doi: 10.1038/nature08980
    • Kenyon, C. J. (2010). The genetics of ageing. Nature 464, 504-512. doi: 10.1038/nature08980.
    • (2010) Nature , vol.464 , pp. 504-512
    • Kenyon, C.J.1
  • 57
    • 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. (2011). 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
  • 58
    • 0035993237 scopus 로고    scopus 로고
    • Ab toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets
    • doi: 10.1016/S0197-0186(02)00050-5
    • Klein, W. L. (2002). Ab toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem. Int. 41, 345-352. doi: 10.1016/S0197-0186(02)00050-5.
    • (2002) Neurochem. Int. , vol.41 , pp. 345-352
    • Klein, W.L.1
  • 59
    • 84871922036 scopus 로고    scopus 로고
    • Deciphering the mechanism underlying late-onset Alzheimer disease
    • doi: 10.1038/nrneurol.2012.236
    • Krstic, D., and Knuesel, I. (2013). Deciphering the mechanism underlying late-onset Alzheimer disease. Nat. Rev. Neurol. 9, 25-34. doi: 10.1038/nrneurol.2012.236.
    • (2013) Nat. Rev. Neurol. , vol.9 , pp. 25-34
    • Krstic, D.1    Knuesel, I.2
  • 60
    • 41549138483 scopus 로고    scopus 로고
    • A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy
    • doi: 10.1073/pnas.0712145105
    • Lee, I. H., Cao, L., Mostoslavsky, R., Lombard, D. B., Liu, J., Bruns, N. E., et al. (2008). A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proc. Natl. Acad. Sci. U.S.A. 105, 3374-3379. doi: 10.1073/pnas.0712145105.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 3374-3379
    • Lee, I.H.1    Cao, L.2    Mostoslavsky, R.3    Lombard, D.B.4    Liu, J.5    Bruns, N.E.6
  • 61
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • doi: 10.1038/nature04533
    • Lesne, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., et al. (2006). A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440, 352-357. doi: 10.1038/nature04533.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3    Kayed, R.4    Glabe, C.G.5    Yang, A.6
  • 62
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • doi: 10.1016/j.cell.2007.12.018
    • Levine, B., and Kroemer, G. (2008). Autophagy in the pathogenesis of disease. Cell 132, 27-42. doi: 10.1016/j.cell.2007.12.018.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 63
    • 84873686589 scopus 로고    scopus 로고
    • Metabolic and neuropsychiatric effects of calorie restriction and sirtuins
    • doi: 10.1146/annurev-physiol-030212-183800
    • Libert, S., and Guarente, L. (2013). Metabolic and neuropsychiatric effects of calorie restriction and sirtuins. Annu. Rev. Physiol. 75, 669-684. doi: 10.1146/annurev-physiol-030212-183800.
    • (2013) Annu. Rev. Physiol. , vol.75 , pp. 669-684
    • Libert, S.1    Guarente, L.2
  • 64
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • doi: 10.1038/nature05292
    • Lin, M. T., and Beal, M. F. (2006). Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443, 787-795. doi: 10.1038/nature05292.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 65
    • 37049030994 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor in neuronal survival and behavior-related plasticity
    • doi: 10.1196/annals.1403.009
    • Lipsky, R. H., and Marini, A. M. (2007). Brain-derived neurotrophic factor in neuronal survival and behavior-related plasticity. Ann. N.Y. Acad. Sci. 1122, 130-143. doi: 10.1196/annals.1403.009.
    • (2007) Ann. N.Y. Acad. Sci. , vol.1122 , pp. 130-143
    • Lipsky, R.H.1    Marini, A.M.2
  • 66
    • 79953230829 scopus 로고    scopus 로고
    • NAD+-dependent SIRT1 deacetylase participates in epigenetic reprogramming during endotoxin tolerance
    • doi: 10.1074/jbc. M110.196790
    • Liu, T. F., Yoza, B. K., El Gazzar, M., Vachharajani, V. T., and McCall, C. E. (2011). NAD+-dependent SIRT1 deacetylase participates in epigenetic reprogramming during endotoxin tolerance. J. Biol. Chem. 286, 9856-9864. doi: 10.1074/jbc. M110.196790.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9856-9864
    • Liu, T.F.1    Yoza, B.K.2    El Gazzar, M.3    Vachharajani, V.T.4    McCall, C.E.5
  • 67
    • 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
  • 68
    • 3042631024 scopus 로고    scopus 로고
    • Gene regulation and DNA damage in the ageing human brain
    • doi: 10.1038/nature02661
    • Lu, T., Pan, Y., Kao, S. Y., Li, C., Kohane, I., Chan, J., et al. (2004). Gene regulation and DNA damage in the ageing human brain. Nature 429, 883-891. doi: 10.1038/nature02661.
    • (2004) Nature , vol.429 , pp. 883-891
    • Lu, T.1    Pan, Y.2    Kao, S.Y.3    Li, C.4    Kohane, I.5    Chan, J.6
  • 69
    • 60049091402 scopus 로고    scopus 로고
    • Tauopathies with parkinsonism: clinical spectrum, neuropathologic basis, biological markers, and treatment options
    • doi: 10.1111/j.1468-1331.2008.02513.x
    • Ludolph, A. C., Kassubek, J., Landwehrmeyer, B. G., Mandelkow, E., Mandelkow, E. M., Burn, D. J., et al. (2009). Tauopathies with parkinsonism: clinical spectrum, neuropathologic basis, biological markers, and treatment options. Eur. J. Neurol. 16, 297-309. doi: 10.1111/j.1468-1331.2008.02513.x.
    • (2009) Eur. J. Neurol. , vol.16 , pp. 297-309
    • Ludolph, A.C.1    Kassubek, J.2    Landwehrmeyer, B.G.3    Mandelkow, E.4    Mandelkow, E.M.5    Burn, D.J.6
  • 70
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression
    • doi: 10.1093/hmg/ddl066
    • Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., and Reddy, P. H. (2006). Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 15, 1437-1449. doi: 10.1093/hmg/ddl066.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 71
    • 33646010041 scopus 로고    scopus 로고
    • Roles for NF-kappaB in nerve cell survival, plasticity, and disease
    • doi: 10.1038/sj.cdd.4401837
    • Mattson, M. P., and Meffert, M. K. (2006). Roles for NF-kappaB in nerve cell survival, plasticity, and disease. Cell Death Differ. 13, 852-860. doi: 10.1038/sj.cdd.4401837.
    • (2006) Cell Death Differ. , vol.13 , pp. 852-860
    • Mattson, M.P.1    Meffert, M.K.2
  • 72
    • 80052344983 scopus 로고    scopus 로고
    • Epigenetics, bioenergetics, and microRNA coordinate gene-specific reprogramming during acute systemic inflammation
    • doi: 10.1189/jlb.0211075
    • McCall, C. E., El Gazzar, M., Liu, T., Vachharajani, V., and Yoza, B. (2011). Epigenetics, bioenergetics, and microRNA coordinate gene-specific reprogramming during acute systemic inflammation. J. Leukoc. Biol. 90, 439-446. doi: 10.1189/jlb.0211075.
    • (2011) J. Leukoc. Biol. , vol.90 , pp. 439-446
    • McCall, C.E.1    El Gazzar, M.2    Liu, T.3    Vachharajani, V.4    Yoza, B.5
  • 73
    • 70349443224 scopus 로고    scopus 로고
    • Transcriptional control of the inflammatory response
    • doi: 10.1038/nri2634
    • Medzhitov, R., and Horng, T. (2009). Transcriptional control of the inflammatory response. Nat. Rev. Immunol. 9, 692-703. doi: 10.1038/nri2634.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 692-703
    • Medzhitov, R.1    Horng, T.2
  • 74
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: insights into their biological function
    • doi: 10.1042/BJ20070140
    • Michan, S., and Sinclair, D. (2007). Sirtuins in mammals: insights into their biological function. Biochem. J. 404, 1-13. doi: 10.1042/BJ20070140.
    • (2007) Biochem. J. , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 75
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • doi: 10.1016/j.neuron.2010.08.044
    • Min, S. W., Cho, S. H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., et al. (2010). Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67, 953-966. doi: 10.1016/j.neuron.2010.08.044.
    • (2010) Neuron , vol.67 , pp. 953-966
    • Min, S.W.1    Cho, S.H.2    Zhou, Y.3    Schroeder, S.4    Haroutunian, V.5    Seeley, W.W.6
  • 76
    • 84871107379 scopus 로고    scopus 로고
    • Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease
    • doi: 10.1074/jbc. R112.404863
    • Newman, J. C., He, W., and Verdin, E. (2012). Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease. J. Biol. Chem. 287, 42436-42443. doi: 10.1074/jbc. R112.404863.
    • (2012) J. Biol. Chem. , vol.287 , pp. 42436-42443
    • Newman, J.C.1    He, W.2    Verdin, E.3
  • 77
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease
    • doi: 10.1126/science.1143780
    • Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., Amore, A. M., et al. (2007). Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 317, 516-519. doi: 10.1126/science.1143780.
    • (2007) Science , vol.317 , pp. 516-519
    • Outeiro, T.F.1    Kontopoulos, E.2    Altmann, S.M.3    Kufareva, I.4    Strathearn, K.E.5    Amore, A.M.6
  • 78
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • doi: 10.1038/ng1534
    • Parker, J. A., Arango, M., Abderrahmane, S., Lambert, E., Tourette, C., and Catoire, H. (2005). Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nat. Genet. 37, 349-350. doi: 10.1038/ng1534.
    • (2005) Nat. Genet. , vol.37 , pp. 349-350
    • Parker, J.A.1    Arango, M.2    Abderrahmane, S.3    Lambert, E.4    Tourette, C.5    Catoire, H.6
  • 79
    • 83255186739 scopus 로고    scopus 로고
    • SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities
    • doi: 10.1128/MCB.06147-11
    • Peng, L., Yuan, Z., Ling, H., Fukasawa, K., Robertson, K., Olashaw, N., et al. (2011). SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities. Mol. Cell. Biol. 31, 4720-4734. doi: 10.1128/MCB.06147-11.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4720-4734
    • Peng, L.1    Yuan, Z.2    Ling, H.3    Fukasawa, K.4    Robertson, K.5    Olashaw, N.6
  • 80
    • 82955169641 scopus 로고    scopus 로고
    • Proatherogenic abnormalities of lipid metabolism in SirT1 transgenic mice are mediated through Creb deacetylation
    • doi: 10.1016/j.cmet.2011.10.007
    • Qiang, L., Lin, H. V., Kim-Muller, J. Y., Welch, C. L., Gu, W., and Accili, D. (2011). Proatherogenic abnormalities of lipid metabolism in SirT1 transgenic mice are mediated through Creb deacetylation. Cell Metab. 14, 758-767. doi: 10.1016/j.cmet.2011.10.007.
    • (2011) Cell Metab. , vol.14 , pp. 758-767
    • Qiang, L.1    Lin, H.V.2    Kim-Muller, J.Y.3    Welch, C.L.4    Gu, W.5    Accili, D.6
  • 81
    • 33746824192 scopus 로고    scopus 로고
    • Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction
    • doi: 10.1074/jbc. M602909200
    • Qin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., Chen, L., et al. (2006). Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction. J. Biol. Chem. 281, 21745-21754. doi: 10.1074/jbc. M602909200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21745-21754
    • Qin, W.1    Yang, T.2    Ho, L.3    Zhao, Z.4    Wang, J.5    Chen, L.6
  • 82
    • 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
  • 83
    • 75449102536 scopus 로고    scopus 로고
    • Alzheimer's disease
    • doi: 10.1056/NEJMra0909142
    • Querfurth, H. W., and LaFerla, F. M. (2010). Alzheimer's disease. N. Engl. J. Med. 362, 329-344. doi: 10.1056/NEJMra0909142.
    • (2010) N. Engl. J. Med. , vol.362 , pp. 329-344
    • Querfurth, H.W.1    LaFerla, F.M.2
  • 84
    • 67651210858 scopus 로고    scopus 로고
    • SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1
    • doi: 10.1128/MCB.00121-09
    • Rajamohan, S. B., Pillai, V. B., Gupta, M., Sundaresan, N. R., Birukov, K. G., and Samant, S. (2009). SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol. Cell. Biol. 29, 4116-4129. doi: 10.1128/MCB.00121-09.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 4116-4129
    • Rajamohan, S.B.1    Pillai, V.B.2    Gupta, M.3    Sundaresan, N.R.4    Birukov, K.G.5    Samant, S.6
  • 85
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • doi: 10.1038/nature03354
    • Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., and Puigserver, P. (2005). Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434, 113-118. doi: 10.1038/nature03354.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 86
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • doi: 10.1073/pnas.0404184101
    • 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. doi: 10.1073/pnas.0404184101.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 87
    • 79956148168 scopus 로고    scopus 로고
    • Activation of nuclear factor-kappa B signalling promotes cellular senescence
    • doi: 10.1038/onc.2010.611
    • Rovillain, E., Mansfield, L., Caetano, C., Alvarez-Fernandez, M., Caballero, O. L., Medema, R. H., et al. (2011). Activation of nuclear factor-kappa B signalling promotes cellular senescence. Oncogene 30, 2356-2366. doi: 10.1038/onc.2010.611.
    • (2011) Oncogene , vol.30 , pp. 2356-2366
    • Rovillain, E.1    Mansfield, L.2    Caetano, C.3    Alvarez-Fernandez, M.4    Caballero, O.L.5    Medema, R.H.6
  • 88
    • 0036712454 scopus 로고    scopus 로고
    • Dynamic changes in histone H3 Lys 9 methylation occurring at tightly regulated inducible inflammatory genes
    • doi: 10.1101/gad.232502
    • Saccani, S., and Natoli, G. (2002). Dynamic changes in histone H3 Lys 9 methylation occurring at tightly regulated inducible inflammatory genes. Genes Dev. 16, 2219-2224. doi: 10.1101/gad.232502.
    • (2002) Genes Dev. , vol.16 , pp. 2219-2224
    • Saccani, S.1    Natoli, G.2
  • 89
    • 84867280590 scopus 로고    scopus 로고
    • SNCA (alpha-synuclein)-induced toxicity in yeast cells is dependent on sirtuin 2 (Sir2)-mediated mitophagy
    • doi: 10.4161/auto.21275
    • Sampaio-Marques, B., Felgueiras, C., Silva, A., Rodrigues, M., Tenreiro, S., Franssens, V., et al. (2012). SNCA (alpha-synuclein)-induced toxicity in yeast cells is dependent on sirtuin 2 (Sir2)-mediated mitophagy. Autophagy 8, 1494-1509. doi: 10.4161/auto.21275.
    • (2012) Autophagy , vol.8 , pp. 1494-1509
    • Sampaio-Marques, B.1    Felgueiras, C.2    Silva, A.3    Rodrigues, M.4    Tenreiro, S.5    Franssens, V.6
  • 90
    • 77956677458 scopus 로고    scopus 로고
    • Myeloid deletion of SIRT1 induces inflammatory signaling in response to environmental stress
    • doi: 10.1128/MCB.00657-10
    • Schug, T. T., Xu, Q., Gao, H., Peres da Silva, A., Draper, D. W., Fessler, M. B., et al. (2010). Myeloid deletion of SIRT1 induces inflammatory signaling in response to environmental stress. Mol. Cell. Biol. 30, 4712-4721. doi: 10.1128/MCB.00657-10.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4712-4721
    • Schug, T.T.1    Xu, Q.2    Gao, H.3    Peres da Silva, A.4    Draper, D.W.5    Fessler, M.B.6
  • 91
    • 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
  • 92
    • 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., Jager, 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    Jager, S.6
  • 93
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective
    • doi: 10.1016/j.cell.2005.02.008
    • Tanzi, R. E., and Bertram, L. (2005). Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120, 545-555. doi: 10.1016/j.cell.2005.02.008.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 94
    • 84863550186 scopus 로고    scopus 로고
    • NF-kappaB inhibition delays DNA damage-induced senescence and aging in mice
    • doi: 10.1172/JCI45785
    • Tilstra, J. S., Robinson, A. R., Wang, J., Gregg, S. Q., Clauson, C. L., Reay, D. P., et al. (2012). NF-kappaB inhibition delays DNA damage-induced senescence and aging in mice. J. Clin. Invest. 122, 2601-2612. doi: 10.1172/JCI45785.
    • (2012) J. Clin. Invest. , vol.122 , pp. 2601-2612
    • Tilstra, J.S.1    Robinson, A.R.2    Wang, J.3    Gregg, S.Q.4    Clauson, C.L.5    Reay, D.P.6
  • 95
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • doi: 10.1038/35065638
    • Tissenbaum, H. A., and Guarente, L. (2001). Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410, 227-230. doi: 10.1038/35065638.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 96
    • 41949097891 scopus 로고    scopus 로고
    • C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging
    • doi: 10.1371/journal.pgen.1000027
    • van Ham, T. J., Thijssen, K. L., Breitling, R., Hofstra, R. M., Plasterk, R. H., and Nollen, E. A. (2008). C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging. PLoS Genet. 4:e1000027. doi: 10.1371/journal.pgen.1000027.
    • (2008) PLoS Genet. , vol.4
    • van Ham, T.J.1    Thijssen, K.L.2    Breitling, R.3    Hofstra, R.M.4    Plasterk, R.H.5    Nollen, E.A.6
  • 97
    • 36248954501 scopus 로고    scopus 로고
    • SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation
    • doi: 10.1038/nature06268
    • Vaquero, A., Scher, M., Erdjument-Bromage, H., Tempst, P., Serrano, L., and Reinberg, D. (2007). SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation. Nature 450, 440-444. doi: 10.1038/nature06268.
    • (2007) Nature , vol.450 , pp. 440-444
    • Vaquero, A.1    Scher, M.2    Erdjument-Bromage, H.3    Tempst, P.4    Serrano, L.5    Reinberg, D.6
  • 98
    • 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., 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.3    Haigis, M.C.4
  • 99
    • 80053134340 scopus 로고    scopus 로고
    • Regulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes
    • doi: 10.1038/nature10440
    • Viswanathan, M., and Guarente, L. (2011). Regulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes. Nature 477, E1-E2. doi: 10.1038/nature10440.
    • (2011) Nature , vol.477
    • Viswanathan, M.1    Guarente, L.2
  • 100
    • 84866371474 scopus 로고    scopus 로고
    • MicroRNAs in learning, memory, and neurological diseases
    • doi: 10.1101/lm.026492.112
    • Wang, W., Kwon, E. J., and Tsai, L. H. (2012). MicroRNAs in learning, memory, and neurological diseases. Learn. Mem. 19, 359-368. doi: 10.1101/lm.026492.112.
    • (2012) Learn. Mem. , vol.19 , pp. 359-368
    • Wang, W.1    Kwon, E.J.2    Tsai, L.H.3
  • 101
    • 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., 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.1    Murray, T.K.2    Kehoe, P.G.3    Love, S.4    Verdin, E.M.5    O'Neill, M.J.6
  • 102
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • doi: 10.1126/science.1165946
    • Westerheide, S. D., Anckar, J., Stevens, S. M. Jr., Sistonen, L., and Morimoto, R. I. (2009). Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323, 1063-1066. doi: 10.1126/science.1165946.
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens Jr., S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 103
    • 80052359850 scopus 로고    scopus 로고
    • Resveratrol-activated AMPK/SIRT1/autophagy in cellular models of Parkinson's disease
    • doi: 10.1159/000328516
    • Wu, Y., Li, X., Zhu, J. X., Xie, W., Le, W., Fan, Z., et al. (2011). Resveratrol-activated AMPK/SIRT1/autophagy in cellular models of Parkinson's disease. Neurosignals 19, 163-174. doi: 10.1159/000328516.
    • (2011) Neurosignals , vol.19 , pp. 163-174
    • Wu, Y.1    Li, X.2    Zhu, J.X.3    Xie, W.4    Le, W.5    Fan, Z.6
  • 104
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase
    • doi: 10.1038/sj.emboj.7600244
    • Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., et al. (2004). Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23, 2369-2380. doi: 10.1038/sj.emboj.7600244.
    • (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
  • 105
    • 84863808547 scopus 로고    scopus 로고
    • SIRT1-mediated deacetylation of MeCP2 contributes to BDNF expression
    • doi: 10.4161/epi.20733
    • Zocchi, L., and Sassone-Corsi, P. (2012). SIRT1-mediated deacetylation of MeCP2 contributes to BDNF expression. Epigenetics 7, 695-700. doi: 10.4161/epi.20733.
    • (2012) Epigenetics , vol.7 , pp. 695-700
    • Zocchi, L.1    Sassone-Corsi, P.2


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