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Volumn 9, Issue MAY, 2015, Pages

Differential expression of sirtuins in the aging rat brain

Author keywords

Aging; Brain; Longevity; P53; Sirtuins

Indexed keywords

CARBAMOYL PHOSPHATE SYNTHASE; DNA DIRECTED RNA POLYMERASE; HISTONE H3; MANGANESE SUPEROXIDE DISMUTASE; MESSENGER RNA; POL PROTEIN; PROTEIN P53; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; SIRTUIN 6; SIRTUIN 7; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR FKHRL1;

EID: 84929583381     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2015.00167     Document Type: Article
Times cited : (122)

References (88)
  • 1
    • 55749084738 scopus 로고    scopus 로고
    • A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • Ahn, B., Kim, H., Song, S., Lee, I., 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.1    Kim, H.2    Song, S.3    Lee, I.4    Liu, J.5    Vassilopoulos, A.6
  • 2
    • 0023200370 scopus 로고
    • Histopathological criteria for progressive dementia disorders: Clinical-pathological correlation and classification by multivariate data analysis
    • Alafuzoff, I., Iqbal, K., Friden, H., Adolfsson, R., and Winblad, B. (1987). Histopathological criteria for progressive dementia disorders: clinical-pathological correlation and classification by multivariate data analysis. Acta Neuropathol. (Berl) 74, 209-225. doi: 10.1007/BF00688184
    • (1987) Acta Neuropathol. (Berl) , vol.74 , pp. 209-225
    • Alafuzoff, I.1    Iqbal, K.2    Friden, H.3    Adolfsson, R.4    Winblad, B.5
  • 3
    • 33845327501 scopus 로고    scopus 로고
    • SIRT1: Linking adaptive cellular responses to aging-associated changes in organismal physiology
    • Anastasiou, D., and Krek, W. (2006). SIRT1: linking adaptive cellular responses to aging-associated changes in organismal physiology. Physiology (Bethesda) 21, 404-410. doi: 10.1152/physiol.00031.2006
    • (2006) Physiology (Bethesda) , vol.21 , pp. 404-410
    • Anastasiou, D.1    Krek, W.2
  • 4
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: Cause or consequence? Nat
    • Andersen, J. (2004). Oxidative stress in neurodegeneration: cause or consequence? Nat. Med. 10(Suppl.), S18-S25. doi: 10.1038/nrn1434
    • (2004) Med , vol.10
    • Andersen, J.1
  • 5
    • 33644875954 scopus 로고    scopus 로고
    • Neuronal protection by sirtuins in Alzheimer’s disease
    • Anekonda, T. S., and Reddy, P. H. (2006). Neuronal protection by sirtuins in Alzheimer’s disease. J. Neurochem. 96, 305-313. doi: 10.1111/j.1471-4159.2005.03492.x
    • (2006) J. Neurochem , vol.96 , pp. 305-313
    • Anekonda, T.S.1    Reddy, P.H.2
  • 6
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Arraki, T., Sasaki, A., and Milbrandt, J. (2004). Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305, 1010-1013. doi: 10.1126/science.1098014
    • (2004) Science , vol.305 , pp. 1010-1013
    • Arraki, T.1    Sasaki, A.2    Milbrandt, J.3
  • 7
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal, M. F. (1995). Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 38, 357-366. doi: 10.1002/ana.410380304
    • (1995) Ann. Neurol , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 8
    • 0038051345 scopus 로고    scopus 로고
    • Mitochondria, oxidative damage, and inflammation in Parkinson’s disease
    • Beal, M. F. (2003). Mitochondria, oxidative damage, and inflammation in Parkinson’s disease. Ann. N.Y. Acad. Sci. 991, 120-131. doi: 10.1111/j.1749-6632.2003.tb07470.x
    • (2003) Ann. N.Y. Acad. Sci , vol.991 , pp. 120-131
    • Beal, M.F.1
  • 9
    • 38449118776 scopus 로고    scopus 로고
    • Mitochondria and neurodegeneration
    • discussion: 192-186
    • Beal, M. F. (2007). Mitochondria and neurodegeneration. Novartis Found Symp. 287, 183-192. discussion: 192-186. doi: 10.1002/SERIES1767
    • (2007) Novartis Found Symp , vol.287 , pp. 183-192
    • Beal, M.F.1
  • 10
    • 33845921542 scopus 로고    scopus 로고
    • NAD+ metabolism in health and disease
    • Belenky, P., Bogan, K. L., and Brenner, C. (2007). NAD+ metabolism in health and disease. Trends Biochem. Sci. 32, 12-19. doi: 10.1016/j.tibs.2006.11.006
    • (2007) Trends Biochem. Sci , vol.32 , pp. 12-19
    • Belenky, P.1    Bogan, K.L.2    Brenner, C.3
  • 11
    • 33751246173 scopus 로고    scopus 로고
    • A stress response pathway involving sirtuins, forkheads and 14-3-3 proteins
    • Berdichevsky, A., and Guarente, L. (2006). A stress response pathway involving sirtuins, forkheads and 14-3-3 proteins. Cell Cycle 5, 2588-2591. doi:10.4161/cc.5.22.3513
    • (2006) Cell Cycle , vol.5 , pp. 2588-2591
    • Berdichevsky, A.1    Guarente, L.2
  • 12
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra, M. T., Smith, B. C., and Denu, J. M. (2005). Mechanism of human SIRT1 activation by resveratrol. J. Biol. Chem. 280, 17187-17195. doi:10.1074/jbc.M501250200
    • (2005) J. Biol. Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 53, 452-458.
    • (1976) Anal. Biochem , vol.53 , pp. 452-458
    • Bradford, M.M.1
  • 14
    • 79955591489 scopus 로고    scopus 로고
    • Age related changes in NAD+ metabolism, oxidative stress and Sirt1 Activity in Wistar Rats
    • Braidy, N., Guillemin, G. M. H., Chan-Ling, T., Poljak, A., and Grant, R. (2011). Age related changes in NAD+ metabolism, oxidative stress and Sirt1 Activity in Wistar Rats. PLoS ONE 6:e19194. doi: 10.1371/journal.pone.0019194
    • (2011) Plos ONE , vol.6
    • Braidy, N.1    Guillemin, G.2    Chan-Ling, T.3    Poljak, A.4    Grant, R.5
  • 15
    • 33744900322 scopus 로고    scopus 로고
    • Gene transfer of extracellular superoxide dismutase protects against vascular dysfunction with aging
    • Brown, K., Chu, Y., Lund, D., Heistad, D., and Faraci, F. (2006). Gene transfer of extracellular superoxide dismutase protects against vascular dysfunction with aging. Am. J. Physiol. Heart Circ. Physiol. 290, H2600-H2605. doi: 10.1152/ajpheart.00676.2005
    • (2006) Am. J. Physiol. Heart Circ. Physiol , vol.290 , pp. 2600-2605
    • Brown, K.1    Chu, Y.2    Lund, D.3    Heistad, D.4    Faraci, F.5
  • 16
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by SIRT1 deacetylase
    • Brunet, A., Sweeny, L. B., and Sturgill, J. F. (2004). Stress-dependent regulation of FOXO transcription factors by SIRT1 deacetylase. Science 303, 2011-2015. doi: 10.1126/science.1094637
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeny, L.B.2    Sturgill, J.F.3
  • 17
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondria, calcium regulation, and acute glutramate excitotoxicity in cultured cerebellar granule cells
    • Budd, S. L., and Nicholls, D. G. (1996). Mitochondria, calcium regulation, and acute glutramate excitotoxicity in cultured cerebellar granule cells. J. Neurochem. 67, 2282-2291. doi: 10.1046/j.1471-4159.1996.67062282.x
    • (1996) J. Neurochem , vol.67 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 18
    • 0034705057 scopus 로고    scopus 로고
    • Mitochondrial and extramitochondrial apoptotic signaling pathways in cerebrocortical neurons
    • Budd, S. L., Tenneti, L., Lishnak, T., and Lipton, S. A. (2000). Mitochondrial and extramitochondrial apoptotic signaling pathways in cerebrocortical neurons. Proc. Natl. Acad. Sci. U.S.A. 97, 6161-6166. doi: 10.1073/pnas.100121097
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 6161-6166
    • Budd, S.L.1    Tenneti, L.2    Lishnak, T.3    Lipton, S.A.4
  • 19
    • 0031023246 scopus 로고    scopus 로고
    • Glial, vascular, and neuronal cytogenesis in whole-mounted cat retina
    • Chan-Ling, T. (1997). Glial, vascular, and neuronal cytogenesis in whole-mounted cat retina. Microsc. Res. Tech. 36, 1-16.
    • (1997) Microsc. Res. Tech , vol.36 , pp. 1-16
    • Chan-Ling, T.1
  • 20
    • 33846583673 scopus 로고    scopus 로고
    • SIR2: A potential target for calorie restriction mimetics
    • Chen, D., and Guarente, L. (2007). SIR2: a potential target for calorie restriction mimetics. Trends Mol. Med. 13, 64-71. doi: 10.1016/j.molmed.2006.12.004
    • (2007) Trends Mol. Med , vol.13 , pp. 64-71
    • Chen, D.1    Guarente, L.2
  • 21
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling
    • Chen, J., Zhou, Y., Mueller-Steiner, S., Chen, L. F., Kwon, H., Yi, S., et al. (2005). SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB 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
  • 22
    • 0142212154 scopus 로고    scopus 로고
    • Constitutive expression of various xenobiotic and endobiotic transporter mRNAs in the choroid plexus of rats
    • Choudhuri, S., Cherrington, N. J., Li, N., and Klaassen, C. D. (2003). Constitutive expression of various xenobiotic and endobiotic transporter mRNAs in the choroid plexus of rats. Drug Metab. Dispos. 31, 1337-1345. doi: 10.1124/dmd.31.11.1337
    • (2003) Drug Metab. Dispos , vol.31 , pp. 1337-1345
    • Choudhuri, S.1    Cherrington, N.J.2    Li, N.3    Klaassen, C.D.4
  • 23
    • 0024633844 scopus 로고
    • How old is old? Neurobiol
    • Coleman, P. (1989). How old is old? Neurobiol. Aging 10, 115
    • (1989) Aging , vol.10 , pp. 115
    • Coleman, P.1
  • 24
    • 0026316550 scopus 로고
    • Divergence of biological and chronological aging: Evidence from rodent studies
    • Collier, T. J., and Coleman, P. D. (1991). Divergence of biological and chronological aging: evidence from rodent studies. Neurobiol. Aging 12, 685-693. doi: 10.1016/0197-4580(91)90122-Z
    • (1991) Neurobiol. Aging , vol.12 , pp. 685-693
    • Collier, T.J.1    Coleman, P.D.2
  • 25
    • 84929595619 scopus 로고    scopus 로고
    • Aging-related changes in oxidative stress response of human endothelial cells
    • [Epub ahead of print]
    • Conti, V., Corbi, G., Simeon, V., Russomanno, G., Manzo, V., Ferrara, N., et al. (2015). Aging-related changes in oxidative stress response of human endothelial cells. Aging Clin. Exp. Res. doi: 10.1007/s40520-015-0357-9. [Epub ahead of print].
    • (2015) Aging Clin. Exp. Res
    • Conti, V.1    Corbi, G.2    Simeon, V.3    Russomanno, G.4    Manzo, V.5    Ferrara, N.6
  • 26
    • 34547914840 scopus 로고    scopus 로고
    • Sirtuins: The ‘magnificent seven’, function, metabolism and longevity
    • Dali-Youcef, N., Lagouge, M., Froelich, S., Koehl, C., Schoonjans, K., and Auwerx, J. (2007). Sirtuins: the ‘magnificent seven’, function, metabolism and longevity. Ann. Med. 39, 335-345. doi: 10.1080/07853890701408194
    • (2007) Ann. Med , vol.39 , pp. 335-345
    • Dali-Youcef, N.1    Lagouge, M.2    Froelich, S.3    Koehl, C.4    Schoonjans, K.5    Auwerx, J.6
  • 27
    • 25144496904 scopus 로고    scopus 로고
    • The Sir 2 family of protein deacetylases
    • Denu, J. M. (2005). The Sir 2 family of protein deacetylases. Curr. Opin. Chem. Biol. 9, 431-440. doi: 10.1016/j.cbpa.2005.08.010
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 431-440
    • Denu, J.M.1
  • 28
    • 34247520466 scopus 로고    scopus 로고
    • Vitamins and aging: Pathways to NAD+ synthesis
    • Denu, J. M. (2007). Vitamins and aging: pathways to NAD+ synthesis. Cell 129, 453-454. doi: 10.1016/j.cell.2007.04.023
    • (2007) Cell , vol.129 , pp. 453-454
    • Denu, J.M.1
  • 29
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • Dryden, S., Nahhas, F., Nowak, J., Goustin, A., and Tainsky, M. (2003). Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol. 23, 3173-3185. doi: 10.1128/MCB.23.9.3173-3185.2003
    • (2003) Mol. Cell. Biol , vol.23 , pp. 3173-3185
    • Dryden, S.1    Nahhas, F.2    Nowak, J.3    Goustin, A.4    Tainsky, M.5
  • 31
    • 33744466971 scopus 로고    scopus 로고
    • Mammalian Sirt2 homolog SIRT7 is an activator of RNA polymerase I transcription
    • Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., and Guarente, L. (2006). Mammalian Sirt2 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
  • 32
    • 28544444366 scopus 로고    scopus 로고
    • Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival
    • Ford, J., Jiang, M., and Milner, J. (2005). Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival. Canc. Res. 65, 10457-10463. doi: 10.1158/0008-5472.CAN-05-1923
    • (2005) Canc. Res , vol.65 , pp. 10457-10463
    • Ford, J.1    Jiang, M.2    Milner, J.3
  • 33
    • 34547779036 scopus 로고    scopus 로고
    • Therapeutic potential of sirtuin-activating compounds in Alzheimer’s disease
    • Gan, L. (2007). Therapeutic potential of sirtuin-activating compounds in Alzheimer’s disease. Drug News Perspect. 20, 233-239. doi: 10.1358/dnp.2007.20.4.1101162
    • (2007) Drug News Perspect , vol.20 , pp. 233-239
    • Gan, L.1
  • 34
    • 0033848159 scopus 로고    scopus 로고
    • Mitochondrial damage in Alzheimer’s Disease varies with apolipoprotein E genotype
    • Gibson, G. E., Haroutunian, V., Zhang, H., Park, L. C., Shi, Q., Lesser, M., et al. (2000). Mitochondrial damage in Alzheimer’s Disease varies with apolipoprotein E genotype. Ann. Neurol. 48, 1594-1601. doi: 10.1002/1531-8249(200009)48:3<297::AID-ANA3>3.0.CO;2-Z
    • (2000) Ann. Neurol , vol.48 , pp. 1594-1601
    • Gibson, G.E.1    Haroutunian, V.2    Zhang, H.3    Park, L.C.4    Shi, Q.5    Lesser, M.6
  • 35
    • 84914145498 scopus 로고    scopus 로고
    • Age-dependent tissue expression patterns of Sirt1 in senescence-accelerated mice
    • Gong, H., Pang, J., Han, Y., Dai, Y., Dai, D., Cai, J., et al. (2014). Age-dependent tissue expression patterns of Sirt1 in senescence-accelerated mice. Mol. Med. Rep. 10, 3296-3302. doi: 10.3892/mmr.2014.2648
    • (2014) Mol. Med. Rep , vol.10 , pp. 3296-3302
    • Gong, H.1    Pang, J.2    Han, Y.3    Dai, Y.4    Dai, D.5    Cai, J.6
  • 36
    • 0038506040 scopus 로고    scopus 로고
    • Life on a planet of its own: Regulation of RNA polymerase I transcription in the nucleolus
    • Grummt, I. (2003). Life on a planet of its own: regulation of RNA polymerase I transcription in the nucleolus. Genes Dev. 17, 1691-1702. doi: 10.1101/gad.1098503R
    • (2003) Genes Dev , vol.17 , pp. 1691-1702
    • Grummt, I.1
  • 37
    • 33748316536 scopus 로고    scopus 로고
    • SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic β cells
    • Haigis, M., Mostoslavsky, R., Haigis, K., Fahie, K., Christodoulou, D., Murphy, A., et al. (2006). SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic β cells. Cell 126, 941-954. doi: 10.1016/j.cell.2006.06.057
    • (2006) Cell , vol.126 , pp. 941-954
    • Haigis, M.1    Mostoslavsky, R.2    Haigis, K.3    Fahie, K.4    Christodoulou, D.5    Murphy, A.6
  • 38
    • 24744467838 scopus 로고    scopus 로고
    • Transcriptional regulation of neuronal genes and its effect on neural functions: NAD-dependent histone deacetylase SIRT1 (Sir2alpha)
    • Hasahara, S., Chiba, S., Matsumoto, H., and Horio, Y (2005). Transcriptional regulation of neuronal genes and its effect on neural functions: NAD-dependent histone deacetylase SIRT1 (Sir2alpha). J. Pharmacol. Sci. 98, 200-204. doi: 10.1254/jphs.FMJ05001X2
    • (2005) J. Pharmacol. Sci , vol.98 , pp. 200-204
    • Hasahara, S.1    Chiba, S.2    Matsumoto, H.3    Horio, Y.4
  • 39
    • 70349306566 scopus 로고    scopus 로고
    • Direct, real-time monitoring of superoxide generation in isolated mitochondria
    • Henderson, J., Swalwell, H., Boulton, S., Manning, P., McNeil, C., and Birch-Machin, M. (2009). Direct, real-time monitoring of superoxide generation in isolated mitochondria. Free Radic. Res. 43, 796-802. doi: 10.1080/10715760903062895
    • (2009) Free Radic. Res , vol.43 , pp. 796-802
    • Henderson, J.1    Swalwell, H.2    Boulton, S.3    Manning, P.4    McNeil, C.5    Birch-Machin, M.6
  • 40
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., et al. (2003). Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425, 191-196. doi: 10.1038/nature01960
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1    Bitterman, K.J.2    Cohen, H.Y.3    Lamming, D.W.4    Lavu, S.5    Wood, J.G.6
  • 41
    • 84886816679 scopus 로고    scopus 로고
    • Frontiers of model animals for neuroscience: Two prosperous aging model animals for promoting neuroscience research
    • Ito, K. (2013). Frontiers of model animals for neuroscience: two prosperous aging model animals for promoting neuroscience research. Exp. Anim. 62, 275-280. doi: 10.1538/expanim.62.275
    • (2013) Exp. Anim , vol.62 , pp. 275-280
    • Ito, K.1
  • 42
    • 33845614355 scopus 로고    scopus 로고
    • Brain mitochondrial defects amplify intracellular [Ca2+] rise and neurodegeneration but not Ca2+ entry during NMDA receptor activation
    • Jacquard, C., Trioulier, Y., Cosker, F., Escartin, C., Bizat, N., Hantraye, P., et al. (2006). Brain mitochondrial defects amplify intracellular [Ca2+] rise and neurodegeneration but not Ca2+ entry during NMDA receptor activation. FASEB J. 20, 1021-1023. doi: 10.1096/fj.05-5085fje
    • (2006) FASEB J , vol.20 , pp. 1021-1023
    • Jacquard, C.1    Trioulier, Y.2    Cosker, F.3    Escartin, C.4    Bizat, N.5    Hantraye, P.6
  • 43
    • 33745670171 scopus 로고    scopus 로고
    • Oxidative stress in serum and peripheral blood leukocytes in patients with different disease courses of multiple sclerosis
    • Koch, M., Ramsaransing, G., Arutjunyan, A., Stepanov, M., Teelken, A., Heersema, D., et al. (2006). Oxidative stress in serum and peripheral blood leukocytes in patients with different disease courses of multiple sclerosis. J. Neurol. 253, 483-487. doi: 10.1007/s00415-005-0037-3
    • (2006) J. Neurol , vol.253 , pp. 483-487
    • Koch, M.1    Ramsaransing, G.2    Arutjunyan, A.3    Stepanov, M.4    Teelken, A.5    Heersema, D.6
  • 44
    • 74149085437 scopus 로고    scopus 로고
    • Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats
    • Koltai, E., Szabo, Z., Atalay, M., Bolodogh, I., Naito, H., Goto, S., et al. (2010). Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats. Mech. Ageing Dev. 131, 21-28. doi: 10.1016/j.mad.2009.11.002
    • (2010) Mech. Ageing Dev , vol.131 , pp. 21-28
    • Koltai, E.1    Szabo, Z.2    Atalay, M.3    Bolodogh, I.4    Naito, H.5    Goto, S.6
  • 45
    • 4344590155 scopus 로고    scopus 로고
    • Small molecules that regulate lifespan: Evidence for xenohormesis
    • Lamming, D. W., Wood, J. G., and Sinclair, D. A. (2004). Small molecules that regulate lifespan: evidence for xenohormesis. Mol. Microbiol. 53, 1003-1009. doi: 10.1111/j.1365-2958.2004.04209.x
    • (2004) Mol. Microbiol , vol.53 , pp. 1003-1009
    • Lamming, D.W.1    Wood, J.G.2    Sinclair, D.A.3
  • 46
    • 0032546461 scopus 로고    scopus 로고
    • Mitochondrial membrane potential supported by exogenous cytochrome c oxidation mimics the early stages of apoptosis
    • La Piana, G., Fransvea, E., Marzulli, D., and Lofrumento, N. (1998). Mitochondrial membrane potential supported by exogenous cytochrome c oxidation mimics the early stages of apoptosis. Biochem. Biophys. Res. Commun. 246, 556-561. doi: 10.1006/bbrc.1998.8664
    • (1998) Biochem. Biophys. Res. Commun , vol.246 , pp. 556-561
    • La Piana, G.1    Fransvea, E.2    Marzulli, D.3    Lofrumento, N.4
  • 47
    • 77649276290 scopus 로고    scopus 로고
    • Validation of reference genes for quantitative RT-PCR studies of gene expression in perennial ryegrass (Lolium perenne L.)
    • Lee, J. M., Roche, J. R., Donaghy, D. J., Thrush, A., and Sathish, P. (2010). Validation of reference genes for quantitative RT-PCR studies of gene expression in perennial ryegrass (Lolium perenne L.). BMC Mol. Biol. 11:8. doi: 10.1186/1471-2199-11-8
    • (2010) BMC Mol. Biol , vol.11 , pp. 8
    • Lee, J.M.1    Roche, J.R.2    Donaghy, D.J.3    Thrush, A.4    Sathish, P.5
  • 48
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating α-tubulin
    • Li, W., Zhang, B., Tang, J., Cao, Q., Wu, Y., Wu, C., et al. (2007). Sirtuin2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating α-tubulin. J. Neurosci. 27, 2606-2616. doi: 10.1523/JNEUROSCI.4181-06.2007
    • (2007) J. Neurosci , vol.27 , pp. 2606-2616
    • Li, W.1    Zhang, B.2    Tang, J.3    Cao, Q.4    Wu, Y.5    Wu, C.6
  • 49
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt, G., Ford, E., Kurtev, M., and Guarente, L. (2005). Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J. Biol. Chem. 280, 21313-21320. doi: 10.1074/jbc.M413296200
    • (2005) J. Biol. Chem , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 50
    • 37549002891 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIT3 regulates global mitchondrial lysine acetylation
    • Lombard, D., Alt, F., Cheng, H., Bunkenberg, J., Streeper, R., Mostoslavsky, R., et al. (2007). Mammalian Sir2 homolog SIT3 regulates global mitchondrial 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.1    Alt, F.2    Cheng, H.3    Bunkenberg, J.4    Streeper, R.5    Mostoslavsky, R.6
  • 51
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • Longo, V. D., and Kennedy, B. K. (2006). Sirtuins in aging and age-related disease. Cell 126, 257-268. doi: 10.1016/j.cell.2006.07.002
    • (2006) Cell , vol.126 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 52
    • 47349119670 scopus 로고    scopus 로고
    • Aging-related changes in astrocytes in the rat retina: Imbalance between cell proliferation and cell death reduces astrocyte availability
    • Mansour, H., Chamberlain, C. G., Michael, I., Weible, W., Hughes, S., Chu, Y., et al. (2008). Aging-related changes in astrocytes in the rat retina: imbalance between cell proliferation and cell death reduces astrocyte availability. Aging Cell 7, 526-540. doi: 10.1111/j.1474-9726.2008.00402.x
    • (2008) Aging Cell , vol.7 , pp. 526-540
    • Mansour, H.1    Chamberlain, C.G.2    Michael, I.3    Weible, W.4    Hughes, S.5    Chu, Y.6
  • 53
    • 0043065507 scopus 로고    scopus 로고
    • Single-cell analysis of mtDNA in amyotrophic lateral sclerosis: Towards the characterization of individual neurons in neurodegenerative disorders
    • Mawrin, C., Kirches, E., and Dietzmann, K. (2003). Single-cell analysis of mtDNA in amyotrophic lateral sclerosis: towards the characterization of individual neurons in neurodegenerative disorders. Pathol. Res. Pract. 199, 415-418. doi: 10.1078/0344-0338-00439
    • (2003) Pathol. Res. Pract , vol.199 , pp. 415-418
    • Mawrin, C.1    Kirches, E.2    Dietzmann, K.3
  • 54
    • 0036310142 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in a cell culture model of familial amyotrophic lateral sclerosis
    • Menzies, F. M., Cookson, M. R., Taylor, R. W., Turnbull, D. M., Chrzanowska-Lightowlers, Z. M., Dong, L., et al. (2002a). Mitochondrial dysfunction in a cell culture model of familial amyotrophic lateral sclerosis. Brain 125(Pt 7), 1522-1533. doi: 10.1093/brain/awf167
    • (2002) Brain , vol.125 , pp. 1522-1533
    • Menzies, F.M.1    Cookson, M.R.2    Taylor, R.W.3    Turnbull, D.M.4    Chrzanowska-Lightowlers, Z.M.5    Dong, L.6
  • 55
    • 0036176613 scopus 로고    scopus 로고
    • Mitochondrial involvement in amyotrophic lateral sclerosis
    • Menzies, F. M., Ince, P. G., and Shaw, P. J. (2002b). Mitochondrial involvement in amyotrophic lateral sclerosis. Neurochem. Int. 40, 543-551. doi: 10.1016/S0197-0186(01)00125-5
    • (2002) Neurochem. Int , vol.40 , pp. 543-551
    • Menzies, F.M.1    Ince, P.G.2    Shaw, P.J.3
  • 56
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • 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
  • 57
    • 40849135481 scopus 로고    scopus 로고
    • The Sirtuin family: Therapeutic targets to treat diseases of aging
    • Milne, J., and Denu, J. M. (2008). The Sirtuin family: therapeutic targets to treat diseases of aging. Curr. Pharm. Des. 12, 11-17. doi: 10.1016/j.cbpa.2008.01.019
    • (2008) Curr. Pharm. Des , vol.12 , pp. 11-17
    • Milne, J.1    Denu, J.M.2
  • 58
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky, R., Chua, K., Lombard, D., Pang, W., Fischer, M., Gellon, L., et al. (2006). Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 124, 315-329. doi: 10.1016/j.cell.2005.11.044
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1    Chua, K.2    Lombard, D.3    Pang, W.4    Fischer, M.5    Gellon, L.6
  • 59
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 Deacetylatescarbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa, T., Lomb, D., Haigis, M., and Guarente, L. (2009). SIRT5 Deacetylatescarbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137, 560-570. doi: 10.1016/j.cell.2009.02.026
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.2    Haigis, M.3    Guarente, L.4
  • 60
    • 77957762687 scopus 로고    scopus 로고
    • SIRT4 regulates fatty acid oxidation and mitochondrial gene expression in liver and muscle cells
    • Nasrin, N., Wu, X., Fortier, E., Feng, Y., Bare, O., Chen, S., et al. (2010). SIRT4 regulates fatty acid oxidation and mitochondrial gene expression in liver and muscle cells. J. Biol. Chem. 285, 31995-32002. doi: 10.1074/jbc.M110.124164
    • (2010) J. Biol. Chem , vol.285 , pp. 31995-32002
    • Nasrin, N.1    Wu, X.2    Fortier, E.3    Feng, Y.4    Bare, O.5    Chen, S.6
  • 61
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+ dependent tubulin deacetylase
    • North, B., Marshall, B., Borra, M., Denu, J., and Verdin, E. (2003). The human Sir2 ortholog, SIRT2, is an NAD+ dependent tubulin deacetylase. Mol. Cell 11, 437-444. doi: 10.1016/S1097-2765(03)00038-8
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.1    Marshall, B.2    Borra, M.3    Denu, J.4    Verdin, E.5
  • 62
    • 0024270397 scopus 로고
    • Role of antioxidant enzymes in cell immortalisation and transformation
    • Oberley, L., and Oberley, T. (1988). Role of antioxidant enzymes in cell immortalisation and transformation. Mol. Cell. Biochem. 84, 147-153. doi: 10.1007/BF00421049
    • (1988) Mol. Cell. Biochem , vol.84 , pp. 147-153
    • Oberley, L.1    Oberley, T.2
  • 63
    • 33845942205 scopus 로고    scopus 로고
    • Resveratrol protects dopaminergic neurons in midbrain slice culture from multiple insults
    • Okawara, M., Katsuki, H., Kurimoto, E., Shibata, H., Kume, T., and Akaike, A. (2007). Resveratrol protects dopaminergic neurons in midbrain slice culture from multiple insults. Biochem. Pharmacol. 73, 550-560. doi: 10.1016/j.bcp.2006.11.003
    • (2007) Biochem. Pharmacol , vol.73 , pp. 550-560
    • Okawara, M.1    Katsuki, H.2    Kurimoto, E.3    Shibata, H.4    Kume, T.5    Akaike, A.6
  • 64
    • 79959541505 scopus 로고    scopus 로고
    • Acetylation of MnSOD directes enzymatic activity responding to cellular nutrient status or oxidative stress
    • Ozden, O., Park, S.-H., Kim, H.-S., Jiang, H., Coleman, M., Spitz, D., et al. (2011). Acetylation of MnSOD directes enzymatic activity responding to cellular nutrient status or oxidative stress. Aging 3, 102-107.
    • (2011) Aging , vol.3 , pp. 102-107
    • Ozden, O.1    Park, S.-H.2    Kim, H.-S.3    Jiang, H.4    Coleman, M.5    Spitz, D.6
  • 66
    • 40849113090 scopus 로고    scopus 로고
    • The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility
    • Pandithage, R., Lilischkis, R., Harting, K., Wolf, A., Jedamzik, B., Luscher-Firzlaff, J., et al. (2008). The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility. J. Cell Biol. 180, 915-929. doi: 10.1083/jcb.200707126
    • (2008) J. Cell Biol , vol.180 , pp. 915-929
    • Pandithage, R.1    Lilischkis, R.2    Harting, K.3    Wolf, A.4    Jedamzik, B.5    Luscher-Firzlaff, J.6
  • 67
    • 30044443515 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sirt2 deacetylase activity
    • Pillai, J. B., Isbatan, A., Imai, S. I., and Gupta, M. P. (2005). Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sirt2 deacetylase activity. J. Biol. Chem. 280, 43121-43130. doi: 10.1074/jbc.M506162200
    • (2005) J. Biol. Chem , vol.280 , pp. 43121-43130
    • Pillai, J.B.1    Isbatan, A.2    Imai, S.I.3    Gupta, M.P.4
  • 68
    • 12844271254 scopus 로고    scopus 로고
    • The emerging therapeutic potential of sirtuin-interacting drugs: From cell death to lifespan extension
    • Porcu, M., and Chiarugi, A. (2005). The emerging therapeutic potential of sirtuin-interacting drugs: from cell death to lifespan extension. Trends Pharmacol. Sci. 26, 94-103. doi: 10.1016/j.tips.2004.12.009
    • (2005) Trends Pharmacol. Sci , vol.26 , pp. 94-103
    • Porcu, M.1    Chiarugi, A.2
  • 69
    • 33746824192 scopus 로고    scopus 로고
    • Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction
    • 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
  • 70
    • 58049132184 scopus 로고    scopus 로고
    • Exercise improves import of 8-oxoguanine DNA glycosylase into the mitochondrial matrix of skeletal muscle and enhances the relative activity
    • Radak, Z., Atalay, M., Jakus, J., Boldogh, I., Davies, K., and Goto, S. (2009). Exercise improves import of 8-oxoguanine DNA glycosylase into the mitochondrial matrix of skeletal muscle and enhances the relative activity. Free Radic. Biol. Med. 46, 153-159. doi: 10.1016/j.freeradbiomed.2008.10.022
    • (2009) Free Radic. Biol. Med , vol.46 , pp. 153-159
    • Radak, Z.1    Atalay, M.2    Jakus, J.3    Boldogh, I.4    Davies, K.5    Goto, S.6
  • 71
    • 54049158932 scopus 로고    scopus 로고
    • Brain SIRT1: Anatomical distribution and regulationn by energy availability
    • Ramadori, G., Lee, C., Bookout, A., Lee, S., Williams, K., Anderson, J., et al. (2008). Brain SIRT1: anatomical distribution and regulationn by energy availability. J. Neurosci. 28, 9989-9996. doi: 10.1523/JNEUROSCI.3257-08.2008
    • (2008) J. Neurosci , vol.28 , pp. 9989-9996
    • Ramadori, G.1    Lee, C.2    Bookout, A.3    Lee, S.4    Williams, K.5    Erson, J.6
  • 72
    • 33747587373 scopus 로고    scopus 로고
    • Resveratrol mimics ischemic preconditioning in the brain
    • Raval, A. P., Dave, K. R., and Perez-Pinzon, M. A. (2006). Resveratrol mimics ischemic preconditioning in the brain. J. Cereb. Blood Flow Metab. 26, 1141-1147. doi: 10.1038/sj.jcbfm.9600262
    • (2006) J. Cereb. Blood Flow Metab , vol.26 , pp. 1141-1147
    • Raval, A.P.1    Dave, K.R.2    Perez-Pinzon, M.A.3
  • 73
    • 33745203038 scopus 로고    scopus 로고
    • The biochemistry of sirtuins. Annu
    • Sauve, A. A., Wolberger, C., Schramm, V. L., and Boeke, J. D. (2006). The biochemistry of sirtuins. Annu. Rev. Biochem. 75, 435-465. doi: 10.1146/annurev.biochem.74.082803.133500
    • (2006) Rev. Biochem , vol.75 , pp. 435-465
    • Sauve, A.A.1    Wolberger, C.2    Schramm, V.L.3    Boeke, J.D.4
  • 74
    • 78650724968 scopus 로고    scopus 로고
    • Neural sirtuin 6 (Sirt6) ablation attenuates somatic growth and causes obesity
    • Schwer, B., Schumacher, B., Lombard, D., Cuiying, X., Kurtev, M., Gao, J., et al. (2010). Neural sirtuin 6 (Sirt6) ablation attenuates somatic growth and causes obesity. Proc. Natl. Acad. Sci. U.S.A. 107, 21790-21794. doi: 10.1073/pnas.1016306107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 21790-21794
    • Schwer, B.1    Schumacher, B.2    Lombard, D.3    Cuiying, X.4    Kurtev, M.5    Gao, J.6
  • 75
    • 38649123072 scopus 로고    scopus 로고
    • Conserved metabolic regulatory functions of sirtuins
    • Schwer, B., and Verdin, E. (2008). Conserved metabolic regulatory functions of sirtuins. Cell Metab. 7, 104-112. doi: 10.1016/j.cmet.2007.11.006
    • (2008) Cell Metab , vol.7 , pp. 104-112
    • Schwer, B.1    Verdin, E.2
  • 76
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi, T., Wang, F., Stieren, E., and Tong, Q. (2005). SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem. 280, 13560-13567. 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
  • 77
    • 84921354327 scopus 로고    scopus 로고
    • Differential expression of sirtuin family members in the developing, adult, and aged rat brain. Front
    • Sidorova-Darmos, E., Wither, R. G., Shulyakova, N., Fisher, C., Ratnam, M., Aarts, M., et al. (2014). Differential expression of sirtuin family members in the developing, adult, and aged rat brain. Front. Aging Neurosci. 6:333. doi: 10.3389/fnagi.2014.00333
    • (2014) Aging Neurosci , vol.6 , pp. 333
    • Sidorova-Darmos, E.1    Wither, R.G.2    Shulyakova, N.3    Fisher, C.4    Ratnam, M.5    Aarts, M.6
  • 78
    • 0031459980 scopus 로고    scopus 로고
    • Extrachromosomal rDNA circles—a cause of aging in yeast
    • Sinclair, D., and Guarente, L. (1997). Extrachromosomal rDNA circles—a cause of aging in yeast. Cell 91, 1033-1042. doi: 10.1016/S0092-8674(00)80493-6
    • (1997) Cell , vol.91 , pp. 1033-1042
    • Sinclair, D.1    Guarente, L.2
  • 79
    • 33746854376 scopus 로고    scopus 로고
    • Sirtuins caught in the act
    • Smith, B. C., and Denu, J. M. (2006). Sirtuins caught in the act. Structure 14, 1207-1208. doi: 10.1016/j.str.2006.07.004
    • (2006) Structure , vol.14 , pp. 1207-1208
    • Smith, B.C.1    Denu, J.M.2
  • 80
    • 0036709074 scopus 로고    scopus 로고
    • Human Sir2 and the ‘silencing’ of p53 activity
    • Smith, J. (2002). Human Sir2 and the ‘silencing’ of p53 activity. Trends Cell Biol. 12, 404-406. doi: 10.1016/S0962-8924(02)02342-5
    • (2002) Trends Cell Biol , vol.12 , pp. 404-406
    • Smith, J.1
  • 81
    • 0024402834 scopus 로고
    • An assay for superoxide dismutase activity in mammalian tissue homogenates
    • Spitz, D., and Oberley, L. (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.1    Oberley, L.2
  • 82
    • 42949125477 scopus 로고    scopus 로고
    • SIRT1 and neuronal diseases
    • Tang, B. L., and Chua, C. E. (2008). SIRT1 and neuronal diseases. Mol. Aspects Med. 29, 187-200. doi: 10.1016/j.mam.2007.02.001
    • (2008) Mol. Aspects Med , vol.29 , pp. 187-200
    • Tang, B.L.1    Chua, C.E.2
  • 83
    • 78650248160 scopus 로고    scopus 로고
    • Sirt3-mediated deacetylation of evolutionary conserved Lysine 122 regulates MnSOD activity in response to stress
    • Tao, R., Coleman, M., Pennington, J., Ozden, O., Park, S., Jiang, H., et al. (2010). Sirt3-mediated deacetylation of evolutionary 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.2    Pennington, J.3    Ozden, O.4    Park, S.5    Jiang, H.6
  • 84
    • 3142742707 scopus 로고    scopus 로고
    • FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSIRT2 (SIRT1)
    • van der Horst, A., Tertoolen, L. G., de Vries-Smts, L. M., Frye, R. A., Medema, R. H., and Burgering, B. M. (2004). FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSIRT2 (SIRT1). J. Biol. Chem. 279, 28873-28879. doi: 10.1074/jbc.M401138200
    • (2004) J. Biol. Chem , vol.279 , pp. 28873-28879
    • Van Der Horst, A.1    Tertoolen, L.G.2    De Vries-Smts, L.M.3    Frye, R.A.4    Medema, R.H.5    Burgering, B.M.6
  • 85
    • 84858795617 scopus 로고    scopus 로고
    • Deacetylation of FOXO3 by SIRT1 and SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation
    • Wang, F., Chan, C. H., Chen, K., Guan, X., Lin, H.-K., and Tong, Q. (2011). Deacetylation of FOXO3 by SIRT1 and SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation. Oncogene 31, 1546-1557. doi: 10.1038/onc.2011.347
    • (2011) Oncogene , vol.31 , pp. 1546-1557
    • Wang, F.1    Chan, C.H.2    Chen, K.3    Guan, X.4    Lin, H.-K.5    Tong, Q.6
  • 86
    • 34447638901 scopus 로고    scopus 로고
    • Proteolipid protein is required for transport of sirtuin 2 into CNS myelin
    • Werner, H., Kuhlmann, K., Shen, S., Uecker, M., Schardt, A., Dimova, K., et al. (2007). Proteolipid protein is required for transport of sirtuin 2 into CNS myelin. J. Neurosci. 27, 7717-7730. doi: 10.1523/JNEUROSCI.1254-07.2007
    • (2007) J. Neurosci , vol.27 , pp. 7717-7730
    • Werner, H.1    Kuhlmann, K.2    Shen, S.3    Uecker, M.4    Schardt, A.5    Dimova, K.6
  • 87
    • 51649115553 scopus 로고    scopus 로고
    • MiR-34a repression of SIRT1 regulates apoptosis
    • Yamakuchi, M., Ferlito, M., and Lowenstein, C. (2008). miR-34a repression of SIRT1 regulates apoptosis. Proc. Natl. Acad. Sci. U.S.A. 105, 13421-13426. doi: 10.1073/pnas.0801613105
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 13421-13426
    • Yamakuchi, M.1    Ferlito, M.2    Lowenstein, C.3
  • 88
    • 33750445309 scopus 로고    scopus 로고
    • NAD+ metabolism and sirtuins: Metabolic regulation of protein deacetylation in stress and toxicity
    • Yang, T., and Sauve, A. A. (2005). NAD+ metabolism and sirtuins: metabolic regulation of protein deacetylation in stress and toxicity. AAPS J. 8, E632-E643. doi: 10.1208/aapsj080472
    • (2005) AAPS J , vol.8
    • Yang, T.1    Sauve, A.A.2


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