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Volumn 739, Issue , 2012, Pages 252-261

Involvement of sirtuins in life-span and aging related diseases

Author keywords

[No Author keywords available]

Indexed keywords

CARBAMOYL PHOSPHATE SYNTHASE; CYTOCHROME C; GLUTAMATE DEHYDROGENASE; HISTONE DEACETYLASE; INSULIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; REACTIVE OXYGEN METABOLITE; RESVERATROL; SIRTUIN; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; SIRTUIN 6; SIRTUIN 7;

EID: 84859520675     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-1704-0_16     Document Type: Article
Times cited : (11)

References (79)
  • 1
    • 20044386668 scopus 로고    scopus 로고
    • Calorie restriction may be neuroprotective in AD and PD
    • Love R. Calorie restriction may be neuroprotective in AD and PD. Lancet Neurol 2005; 4:84.
    • (2005) Lancet Neurol , vol.4 , pp. 84
    • Love, R.1
  • 3
    • 50249094970 scopus 로고    scopus 로고
    • The mitochondrial free radical theory of ageing-where do we stand?
    • Gruber J, Schaffer S, Halliwell B. The mitochondrial free radical theory of ageing-where do we stand? Front Biosci 2008; 13:6554-6579.
    • (2008) Front Biosci , vol.13 , pp. 6554-6579
    • Gruber, J.1    Schaffer, S.2    Halliwell, B.3
  • 4
    • 34548150187 scopus 로고    scopus 로고
    • The role of nuclear architecture in genomic instability and ageing
    • Oberdoerffer P, Sinclair DA. The role of nuclear architecture in genomic instability and ageing. Nat Rev Mol Cell Biol 2007; 8:692-702.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 692-702
    • Oberdoerffer, P.1    Sinclair, D.A.2
  • 5
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim SC, Sprung R, Chen Y et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 2006; 23:607-618.
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3
  • 6
    • 0024656069 scopus 로고
    • The effect of retarded growth upon the length of life span and upon the ultimate body size. 1935
    • discussion 72
    • McCay CM, Crowell MF, Maynard LA. The effect of retarded growth upon the length of life span and upon the ultimate body size. 1935. Nutrition 1989; 5:155-171; discussion 72.
    • (1989) Nutrition , vol.5 , pp. 155-171
    • McCay, C.M.1    Crowell, M.F.2    Maynard, L.A.3
  • 7
    • 0029848121 scopus 로고    scopus 로고
    • The evolution of the anti-aging action of dietary restriction: A hypothesis
    • Masoro EJ, Austad SN. The evolution of the anti-aging action of dietary restriction: a hypothesis. J Gerontol A Biol Sci Med Sci 1996; 51:B387-B391.
    • (1996) J Gerontol A Biol Sci Med Sci , vol.51
    • Masoro, E.J.1    Austad, S.N.2
  • 8
    • 0034033586 scopus 로고    scopus 로고
    • Caloric restriction and aging: An update
    • Masoro EJ. Caloric restriction and aging: an update. Exp Gerontol 2000; 35:299-305.
    • (2000) Exp Gerontol , vol.35 , pp. 299-305
    • Masoro, E.J.1
  • 9
    • 0031549576 scopus 로고    scopus 로고
    • Seminars in medicine of the Beth Israel Deaconess Medical Center. Caloric intake and aging
    • Weindruch R, Sohal RS. Seminars in medicine of the Beth Israel Deaconess Medical Center. Caloric intake and aging. N Engl J Med 1997; 337:986-994.
    • (1997) N Engl J Med , vol.337 , pp. 986-994
    • Weindruch, R.1    Sohal, R.S.2
  • 10
    • 0022517746 scopus 로고
    • The retardation of aging in mice by dietary restriction: Longevity, cancer, immunity and lifetime energy intake
    • Weindruch R, Walford RL, Fligiel S et al. The retardation of aging in mice by dietary restriction: longevity, cancer, immunity and lifetime energy intake. J Nutr 1986; 116:641-654.
    • (1986) J Nutr , vol.116 , pp. 641-654
    • Weindruch, R.1    Walford, R.L.2    Fligiel, S.3
  • 11
    • 0028345369 scopus 로고
    • How diet influences the aging process of the rat
    • Yu BP. How diet influences the aging process of the rat. Proc Soc Exp Biol Med 1994; 205:97-105.
    • (1994) Proc Soc Exp Biol Med , vol.205 , pp. 97-105
    • Yu, B.P.1
  • 12
    • 0029108666 scopus 로고
    • Diet restriction in rhesus monkeys lowers fasting and glucose-stimulated glucoregulatory end points
    • Lane MA, Ball SS, Ingram DK et al. Diet restriction in rhesus monkeys lowers fasting and glucose-stimulated glucoregulatory end points. Am J Physiol 1995; 268:E941-E948.
    • (1995) Am J Physiol , vol.268
    • Lane, M.A.1    Ball, S.S.2    Ingram, D.K.3
  • 13
    • 14844293962 scopus 로고    scopus 로고
    • The role ofinsulin and IGF-1 signaling in longevity
    • Katic M, Kahn CR. The role ofinsulin and IGF-1 signaling in longevity. Cell Mol Life Sci 2005; 62:320-343.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 320-343
    • Katic, M.1    Kahn, C.R.2
  • 14
    • 0029994960 scopus 로고    scopus 로고
    • Calorie restriction lowers body temperature in rhesus monkeys, consistent with a postulated anti-aging mechanism in rodents
    • Lane MA, Baer DJ, Rumpler WV et al. Calorie restriction lowers body temperature in rhesus monkeys, consistent with a postulated anti-aging mechanism in rodents. Proc Natl Acad Sci USA 1996; 93:4159-4164.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4159-4164
    • Lane, M.A.1    Baer, D.J.2    Rumpler, W.V.3
  • 15
    • 0029052573 scopus 로고
    • Slowing ageing by caloric restriction
    • Roth GS, Ingram DK, Lane MA. Slowing ageing by caloric restriction. Nat Med 1995; 1:414-1415.
    • (1995) Nat Med , vol.1 , pp. 414-1415
    • Roth, G.S.1    Ingram, D.K.2    Lane, M.A.3
  • 16
    • 0036584681 scopus 로고    scopus 로고
    • Effects of diet restriction on life span and age-related changes in dogs
    • Kealy RD, Lawler DF, Ballam JM et al. Effects of diet restriction on life span and age-related changes in dogs. J Am Vet Med Assoc 2002; 220:1315-1320.
    • (2002) J Am Vet Med Assoc , vol.220 , pp. 1315-1320
    • Kealy, R.D.1    Lawler, D.F.2    Ballam, J.M.3
  • 17
    • 0015352143 scopus 로고
    • Lifetime effects of winter supplemental feed level and age at first parturition on range beef cows
    • Pinney DO, Stephens DF, Pope LS. Lifetime effects of winter supplemental feed level and age at first parturition on range beef cows. J Anim Sci 1972; 34:1067-1074.
    • (1972) J Anim Sci , vol.34 , pp. 1067-1074
    • Pinney, D.O.1    Stephens, D.F.2    Pope, L.S.3
  • 18
  • 19
    • 4444281969 scopus 로고    scopus 로고
    • Aging in rhesus monkeys: Relevance to human health interventions
    • Roth GS, Mattison JA, Ottinger MA, et al. Aging in rhesus monkeys: relevance to human health interventions. Science 2004; 305:1423-1426.
    • (2004) Science , vol.305 , pp. 1423-1426
    • Roth, G.S.1    Mattison, J.A.2    Ottinger, M.A.3
  • 21
    • 0141720388 scopus 로고    scopus 로고
    • Calorie restriction and aging: Review of the literature and implications for studies in humans
    • Heilbronn LK, Ravussin E. Calorie restriction and aging: review of the literature and implications for studies in humans. Am J Clin Nutr 2003; 78:361-369.
    • (2003) Am J Clin Nutr , vol.78 , pp. 361-369
    • Heilbronn, L.K.1    Ravussin, E.2
  • 22
    • 27744495078 scopus 로고    scopus 로고
    • Caloric restriction and caloric restriction mimetics: Current status and promise for the future
    • Roth GS. Caloric restriction and caloric restriction mimetics: current status and promise for the future. J Am Geriatr Soc 2005; 53:S280-S283.
    • (2005) J Am Geriatr Soc , vol.53
    • Roth, G.S.1
  • 23
    • 32244436937 scopus 로고    scopus 로고
    • Caloric restriction mimetics: The next phase
    • Roth GS, Lane MA, Ingram DK. Caloric restriction mimetics: the next phase. Ann NY Acad Sci 2005; 1057:365-371.
    • (2005) Ann NY Acad Sci , vol.1057 , pp. 365-371
    • Roth, G.S.1    Lane, M.A.2    Ingram, D.K.3
  • 24
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye RA. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 1999; 260:273-279.
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 25
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye RA. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 2000; 273:793-798.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 26
    • 33644875936 scopus 로고    scopus 로고
    • Cloning, chromosomal characterization and mapping of the NAD-dependent histone deacetylases gene sirtuin 1
    • Voelter-Mahlknecht S, Mahlknecht U. Cloning, chromosomal characterization and mapping of the NAD-dependent histone deacetylases gene sirtuin 1. Int J Mol Med 2006; 17:59-67.
    • (2006) Int J Mol Med , vol.17 , pp. 59-67
    • Voelter-Mahlknecht, S.1    Mahlknecht, U.2
  • 27
    • 0034705129 scopus 로고    scopus 로고
    • The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
    • Landry J, Sutton A, Tafrov ST et al. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci USA 2000; 97:5807-5811.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5807-5811
    • Landry, J.1    Sutton, A.2    Tafrov, S.T.3
  • 28
    • 0034687694 scopus 로고    scopus 로고
    • Silent information regulator 2 family of NAD- dependent histone/ protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose
    • Tanner KG, Landry J, Sternglanz R et al. Silent information regulator 2 family of NAD- dependent histone/ protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci USA 2000; 97:14178-14182.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3
  • 29
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • Michan S, Sinclair D. Sirtuins in mammals: insights into their biological function. Biochem J 2007; 404:1-13.
    • (2007) Biochem J , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 30
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • Longo VD, Kennedy BK. Sirtuins in aging and age-related disease. Cell 2006; 126:257-268.
    • (2006) Cell , vol.126 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 31
    • 13944253348 scopus 로고    scopus 로고
    • Calorie restriction-the SIR2 connection
    • Guarente L, Picard F. Calorie restriction-the SIR2 connection. Cell 2005; 120:473-482.
    • (2005) Cell , vol.120 , pp. 473-482
    • Guarente, L.1    Picard, F.2
  • 32
    • 34547875773 scopus 로고    scopus 로고
    • Sirtuins: Critical regulators at the crossroads between cancer and aging
    • Saunders LR, Verdin E. Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene 2007; 26:5489-5504.
    • (2007) Oncogene , vol.26 , pp. 5489-5504
    • Saunders, L.R.1    Verdin, E.2
  • 33
    • 36249016246 scopus 로고    scopus 로고
    • A therapeutic role for sirtuins in diseases of aging?
    • Westphal CH, Dipp MA, Guarente L. A therapeutic role for sirtuins in diseases of aging? Trends Biochem Sci 2007; 32:555-560.
    • (2007) Trends Biochem Sci , vol.32 , pp. 555-560
    • Westphal, C.H.1    Dipp, M.A.2    Guarente, L.3
  • 34
    • 64749103641 scopus 로고    scopus 로고
    • Chromosomal characterization and localization ofthe NAD+-dependent histone deacetylase gene sirtuin 1 in the mouse
    • Mahlknecht U, Voelter-Mahlknecht S. Chromosomal characterization and localization ofthe NAD+-dependent histone deacetylase gene sirtuin 1 in the mouse. Int J Mol Med 2009; 23:245-252.
    • (2009) Int J Mol Med , vol.23 , pp. 245-252
    • Mahlknecht, U.1    Voelter-Mahlknecht, S.2
  • 35
    • 33748331132 scopus 로고    scopus 로고
    • Progressive loss of SIRT1 with cell cycle withdrawal
    • Sasaki T, Maier B, Bartke A et al. Progressive loss of SIRT1 with cell cycle withdrawal. Aging Cell 2006; 5:413-422.
    • (2006) Aging Cell , vol.5 , pp. 413-422
    • Sasaki, T.1    Maier, B.2    Bartke, A.3
  • 36
    • 33748948208 scopus 로고    scopus 로고
    • DeltaNp63alpha overexpression induces downregulation of Sirt1 and an accelerated aging phenotype in the mouse
    • Sommer M, Poliak N, Upadhyay S et al. DeltaNp63alpha overexpression induces downregulation of Sirt1 and an accelerated aging phenotype in the mouse. Cell Cycle 2006; 5:2005-2011.
    • (2006) Cell Cycle , vol.5 , pp. 2005-2011
    • Sommer, M.1    Poliak, N.2    Upadhyay, S.3
  • 37
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, Miller C, Bitterman KJ et al. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 2004; 305:390-392.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3
  • 38
    • 28844469898 scopus 로고    scopus 로고
    • Increase in activity during calorie restriction requires Sirt1
    • Chen D, Steele AD, Lindquist S et al. Increase in activity during calorie restriction requires Sirt1. Science 2005; 310:1641.
    • (2005) Science , vol.310 , pp. 1641
    • Chen, D.1    Steele, A.D.2    Lindquist, S.3
  • 39
    • 36248975293 scopus 로고    scopus 로고
    • SIRT1 transgenic mice show phenotypes resembling calorie restriction
    • Bordone L, Cohen D, Robinson A et al. SIRT1 transgenic mice show phenotypes resembling calorie restriction. Aging Cell 2007; 6:759-767.
    • (2007) Aging Cell , vol.6 , pp. 759-767
    • Bordone, L.1    Cohen, D.2    Robinson, A.3
  • 40
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers JT, Lerin C, Haas W et al. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 2005; 434:113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3
  • 41
    • 33845399894 scopus 로고    scopus 로고
    • Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha
    • Lagouge M, Argmann C, Gerhart-Hines Z et al. Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha. Cell 2006; 127:1109-1122.
    • (2006) Cell , vol.127 , pp. 1109-1122
    • Lagouge, M.1    Argmann, C.2    Gerhart-Hines, Z.3
  • 42
    • 49649128985 scopus 로고    scopus 로고
    • Mitochondrial biogenesis and healthy aging
    • Lopez-Lluch G, Irusta PM, Navas P et al. Mitochondrial biogenesis and healthy aging. Exp Gerontol 2008; 43:813-819.
    • (2008) Exp Gerontol , vol.43 , pp. 813-819
    • Lopez-Lluch, G.1    Irusta, P.M.2    Navas, P.3
  • 43
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Araki T, Sasaki Y, Milbrandt J. Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 2004; 305:1010-1013.
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 44
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, Sweeney LB, Sturgill JF et al. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 2004; 303:2011-2015.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3
  • 45
    • 34447308268 scopus 로고    scopus 로고
    • SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis
    • Kim D, Nguyen MD, Dobbin MM et al. SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. EMBO J 2007; 26:3169-3179.
    • (2007) EMBO J , vol.26 , pp. 3169-3179
    • Kim, D.1    Nguyen, M.D.2    Dobbin, M.M.3
  • 46
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz KT, Bitterman KJ, Cohen HY et al. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 2003; 425:191-196.
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1    Bitterman, K.J.2    Cohen, H.Y.3
  • 47
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • Wood JG, Rogina B, Lavu S et al. Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 2004; 430:686-689.
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3
  • 48
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra MT, Smith BC, Denu JM. Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 2005; 280:17187-17195.
    • (2005) J Biol Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 49
    • 45849137875 scopus 로고    scopus 로고
    • SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6kl signaling in human diploid fibroblasts
    • Huang J, Gan Q, Han L et al. SIRT1 overexpression antagonizes cellular senescence with activated ERK/ S6kl signaling in human diploid fibroblasts. PLoS ONE 2008; 3:el710.
    • (2008) PLoS ONE , vol.3
    • Huang, J.1    Gan, Q.2    Han, L.3
  • 50
    • 33751072349 scopus 로고    scopus 로고
    • Resveratrol improves health and survival of mice on a high-calorie diet
    • Baur JA, Pearson KJ, Price NL et al. Resveratrol improves health and survival of mice on a high-calorie diet. Nature 2006; 444:337-342.
    • (2006) Nature , vol.444 , pp. 337-342
    • Baur, J.A.1    Pearson, K.J.2    Price, N.L.3
  • 51
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne JC, Lambert PD, Schenk S, et al. Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 2007; 450:712-716.
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1    Lambert, P.D.2    Schenk, S.3
  • 52
    • 35349011597 scopus 로고    scopus 로고
    • Sirt1 modulates premature senescence-like phenotype in human endothelial cells
    • Ota H, Akishita M, Eto M et al. Sirt1 modulates premature senescence-like phenotype in human endothelial cells. J Mol Cell Cardiol 2007; 43:571-579.
    • (2007) J Mol Cell Cardiol , vol.43 , pp. 571-579
    • Ota, H.1    Akishita, M.2    Eto, M.3
  • 53
    • 30544445468 scopus 로고    scopus 로고
    • Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells
    • Ota H, Tokunaga E, Chang K et al. Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells. Oncogene 2006; 25:176-185.
    • (2006) Oncogene , vol.25 , pp. 176-185
    • Ota, H.1    Tokunaga, E.2    Chang, K.3
  • 54
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang F, Nguyen M, Qin FX et al. SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 2007; 6:505-514.
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3
  • 55
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT et al. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 2003; 11:437-444.
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3
  • 56
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation
    • Jing E, Gesta S, Kahn CR. SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab 2007; 6:105-114.
    • (2007) Cell Metab , vol.6 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 57
    • 33644643513 scopus 로고    scopus 로고
    • FISH-mapping and genomic organization of the NAD-dependent histone deacetylase gene, Sirtuin 2 (Sirt2)
    • Voelter-Mahlknecht S, Ho AD, Mahlknecht U. FISH-mapping and genomic organization of the NAD-dependent histone deacetylase gene, Sirtuin 2 (Sirt2). Int J Oncol 2005; 27:1187-1196.
    • (2005) Int J Oncol , vol.27 , pp. 1187-1196
    • Voelter-Mahlknecht, S.1    Ho, A.D.2    Mahlknecht, U.3
  • 58
    • 24944559665 scopus 로고    scopus 로고
    • HST2 mediates SIR2-independent life-span extension by calorie restriction
    • Lamming DW, Latorre-Esteves M, Medvedik O et al. HST2 mediates SIR2-independent life-span extension by calorie restriction. Science 2005; 309:1861-1864.
    • (2005) Science , vol.309 , pp. 1861-1864
    • Lamming, D.W.1    Latorre-Esteves, M.2    Medvedik, O.3
  • 59
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease
    • Outeiro TF, Kontopoulos E, Altmann SM et al. Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 2007; 317:516-519.
    • (2007) Science , vol.317 , pp. 516-519
    • Outeiro, T.F.1    Kontopoulos, E.2    Altmann, S.M.3
  • 60
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E, Park JY, Burneskis JM, et al. Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell 2005; 16:4623-4635.
    • (2005) Mol Biol Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3
  • 61
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer B, Bunkenborg J, Verdin RO et al. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci USA 2006; 103:10224-10229.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3
  • 62
    • 1542494461 scopus 로고    scopus 로고
    • Cloning and structural characterization of the human histone deacetylase 6 gene
    • Voelter-Mahlknecht S, Mahlknecht U. Cloning and structural characterization of the human histone deacetylase 6 gene. Int J Mol Med 2003; 12:87-93.
    • (2003) Int J Mol Med , vol.12 , pp. 87-93
    • Voelter-Mahlknecht, S.1    Mahlknecht, U.2
  • 63
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3 a mitochondrial sirtuin deacetylase regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi T, Wang F, Stieren E et al. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J Biol Chem 2005; 280:13560-13567.
    • (2005) J Biol Chem , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3
  • 64
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows WC, Lee S, Denu JM. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc Natl Acad Sci USA 2006; 103:10230-10235.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 65
    • 19944433088 scopus 로고    scopus 로고
    • A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages
    • Bellizzi D, Rose G, Cavalcante P, et al. A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages. Genomics 2005; 85:258-263.
    • (2005) Genomics , vol.85 , pp. 258-263
    • Bellizzi, D.1    Rose, G.2    Cavalcante, P.3
  • 66
    • 10744232772 scopus 로고    scopus 로고
    • Variability of the SIRT3 gene, human silent information regulator Sir2 homologue and survivorship in the elderly
    • Rose G, Dato S, Altomare K et al. Variability of the SIRT3 gene, human silent information regulator Sir2 homologue and survivorship in the elderly. Exp Gerontol 2003; 38:1065-1070.
    • (2003) Exp Gerontol , vol.38 , pp. 1065-1070
    • Rose, G.1    Dato, S.2    Altomare, K.3
  • 67
    • 33748316536 scopus 로고    scopus 로고
    • SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells
    • Haigis MC, Mostoslavsky R, Haigis KM et al. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 2006; 126:941-954.
    • (2006) Cell , vol.126 , pp. 941-954
    • Haigis, M.C.1    Mostoslavsky, R.2    Haigis, K.M.3
  • 68
    • 64549123882 scopus 로고    scopus 로고
    • Fluorescence in situ hybridization and chromosomal organization of the sirtuin 4 gene (Sirt4) in the mouse
    • Mahlknecht U, Voelter-Mahlknecht S. Fluorescence in situ hybridization and chromosomal organization of the sirtuin 4 gene (Sirt4) in the mouse. Biochem Biophys Res Commun 2009; 382:685-690.
    • (2009) Biochem Biophys Res Commun , vol.382 , pp. 685-690
    • Mahlknecht, U.1    Voelter-Mahlknecht, S.2
  • 69
    • 36349030394 scopus 로고    scopus 로고
    • Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase
    • Aiuja N, Schwer B, Carobbio S et al. Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase. J Biol Chem 2007; 282:33583-33592.
    • (2007) J Biol Chem , vol.282 , pp. 33583-33592
    • Aiuja, N.1    Schwer, B.2    Carobbio, S.3
  • 70
    • 33847635635 scopus 로고    scopus 로고
    • Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin
    • Sdrnetz A, Min J, Antoshenko T et al. Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin. Structure 2007; 15:377-389.
    • (2007) Structure , vol.15 , pp. 377-389
    • Sdrnetz, A.1    Min, J.2    Antoshenko, T.3
  • 71
    • 50149103440 scopus 로고    scopus 로고
    • Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
    • Schlicker C, Gertz M, Papatheodorou P et al. Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J Mol Biol 2008; 382:790-801.
    • (2008) J Mol Biol , vol.382 , pp. 790-801
    • Schlicker, C.1    Gertz, M.2    Papatheodorou, P.3
  • 72
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa T, Lomb DJ, Haigis MC et al. SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 2009; 137:560-570.
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3
  • 73
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt G, Ford E, Kurtev M et al. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J Biol Chem 2005; 280:21313-21320.
    • (2005) J Biol Chem , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3
  • 74
    • 39049184073 scopus 로고    scopus 로고
    • Chromosomal organization and fluorescence in situ hybridization of the human Sirtuin 6 gene
    • Mahlknecht U, Ho AD, Voelter-Mahlknecht S. Chromosomal organization and fluorescence in situ hybridization of the human Sirtuin 6 gene. Int J Oncol 2006; 28:447-456.
    • (2006) Int J Oncol , vol.28 , pp. 447-456
    • Mahlknecht, U.1    Ho, A.D.2    Voelter-Mahlknecht, S.3
  • 75
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky R, Chua KF, Lombard DB et al. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 2006; 124:315-329.
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1    Chua, K.F.2    Lombard, D.B.3
  • 76
    • 13944249618 scopus 로고    scopus 로고
    • DNA repair, genome stability and aging
    • Lombard DB, Chua KF, Mostoslavsky R et al. DNA repair, genome stability and aging. Cell 2005; 120:497-512.
    • (2005) Cell , vol.120 , pp. 497-512
    • Lombard, D.B.1    Chua, K.F.2    Mostoslavsky, R.3
  • 77
    • 33744466971 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase i transcription
    • Ford E, Voit R, Liszt G et al. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev 2006; 20:1075-1080.
    • (2006) Genes Dev , vol.20 , pp. 1075-1080
    • Ford, E.1    Voit, R.2    Liszt, G.3
  • 78
    • 33744735005 scopus 로고    scopus 로고
    • Fluorescence in situ hybridization and chromosomal organization of the human Sirtuin 7 gene
    • Voelter-Mahlknecht S, Letzel S, Mahlknecht U. Fluorescence in situ hybridization and chromosomal organization of the human Sirtuin 7 gene. Int J Oncol 2006; 28:899-908.
    • (2006) Int J Oncol , vol.28 , pp. 899-908
    • Voelter-Mahlknecht, S.1    Letzel, S.2    Mahlknecht, U.3
  • 79
    • 41449083867 scopus 로고    scopus 로고
    • Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice
    • Vakhrusheva O, Smolka C, Gajawada P et al. Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ Res 2008; 102:703-710.
    • (2008) Circ Res , vol.102 , pp. 703-710
    • Vakhrusheva, O.1    Smolka, C.2    Gajawada, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.