메뉴 건너뛰기




Volumn 7, Issue 2, 2008, Pages 104-112

Conserved Metabolic Regulatory Functions of Sirtuins

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A SYNTHETASE; GLUCOSE; INSULIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN SUBUNIT; SIRTUIN; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; SIRTUIN 6; SIRTUIN 7; UNCLASSIFIED DRUG;

EID: 38649123072     PISSN: 15504131     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cmet.2007.11.006     Document Type: Review
Times cited : (353)

References (82)
  • 2
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., and Sinclair D.A. Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 423 (2003) 181-185
    • (2003) Nature , vol.423 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 3
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: the in vivo evidence
    • Baur J.A., and Sinclair D.A. Therapeutic potential of resveratrol: the in vivo evidence. Nat. Rev. Drug Discov. 5 (2006) 493-506
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 493-506
    • Baur, J.A.1    Sinclair, D.A.2
  • 5
    • 34247502715 scopus 로고    scopus 로고
    • Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+
    • Belenky P., Racette F.G., Bogan K.L., McClure J.M., Smith J.S., and Brenner C. Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell 129 (2007) 473-484
    • (2007) Cell , vol.129 , pp. 473-484
    • Belenky, P.1    Racette, F.G.2    Bogan, K.L.3    McClure, J.M.4    Smith, J.S.5    Brenner, C.6
  • 6
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman K.J., Anderson R.M., Cohen H.Y., Latorre-Esteves M., and Sinclair D.A. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J. Biol. Chem. 277 (2002) 45099-45107
    • (2002) J. Biol. Chem. , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 7
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G., and Guarente L. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 73 (2004) 417-435
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 8
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: understanding longevity
    • Bordone L., and Guarente L. Calorie restriction, SIRT1 and metabolism: understanding longevity. Nat. Rev. Mol. Cell Biol. 6 (2005) 298-305
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 11
    • 0017699890 scopus 로고
    • Origins of blood acetate in the rat
    • Buckley B.M., and Williamson D.H. Origins of blood acetate in the rat. Biochem. J. 166 (1977) 539-545
    • (1977) Biochem. J. , vol.166 , pp. 539-545
    • Buckley, B.M.1    Williamson, D.H.2
  • 12
    • 28844469898 scopus 로고    scopus 로고
    • Increase in activity during calorie restriction requires Sirt1
    • Chen D., Steele A.D., Lindquist S., and Guarente L. Increase in activity during calorie restriction requires Sirt1. Science 310 (2005) 1641
    • (2005) Science , vol.310 , pp. 1641
    • Chen, D.1    Steele, A.D.2    Lindquist, S.3    Guarente, L.4
  • 13
  • 15
    • 34249846128 scopus 로고    scopus 로고
    • Resveratrol stimulates AMP kinase activity in neurons
    • Dasgupta B., and Milbrandt J. Resveratrol stimulates AMP kinase activity in neurons. Proc. Natl. Acad. Sci. USA 104 (2007) 7217-7222
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7217-7222
    • Dasgupta, B.1    Milbrandt, J.2
  • 16
    • 25144496904 scopus 로고    scopus 로고
    • The Sir 2 family of protein deacetylases
    • Denu J.M. The Sir 2 family of protein deacetylases. Curr. Opin. Chem. Biol. 9 (2005) 431-440
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 431-440
    • Denu, J.M.1
  • 17
    • 0242580872 scopus 로고    scopus 로고
    • Convergence of peroxisome proliferator-activated receptor gamma and Foxo1 signaling pathways
    • Dowell P., Otto T.C., Adi S., and Lane M.D. Convergence of peroxisome proliferator-activated receptor gamma and Foxo1 signaling pathways. J. Biol. Chem. 278 (2003) 45485-45491
    • (2003) J. Biol. Chem. , vol.278 , pp. 45485-45491
    • Dowell, P.1    Otto, T.C.2    Adi, S.3    Lane, M.D.4
  • 18
    • 20144365700 scopus 로고    scopus 로고
    • Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes
    • Frescas D., Valenti L., and Accili D. Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes. J. Biol. Chem. 280 (2005) 20589-20595
    • (2005) J. Biol. Chem. , vol.280 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 19
    • 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 R.A. 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. 260 (1999) 273-279
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 20
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273 (2000) 793-798
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 21
    • 0035815751 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate
    • Fujino T., Kondo J., Ishikawa M., Morikawa K., and Yamamoto T.T. Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate. J. Biol. Chem. 276 (2001) 11420-11426
    • (2001) J. Biol. Chem. , vol.276 , pp. 11420-11426
    • Fujino, T.1    Kondo, J.2    Ishikawa, M.3    Morikawa, K.4    Yamamoto, T.T.5
  • 23
    • 0034626747 scopus 로고    scopus 로고
    • Genetic pathways that regulate ageing in model organisms
    • Guarente L., and Kenyon C. Genetic pathways that regulate ageing in model organisms. Nature 408 (2000) 255-262
    • (2000) Nature , vol.408 , pp. 255-262
    • Guarente, L.1    Kenyon, C.2
  • 24
    • 13944253348 scopus 로고    scopus 로고
    • Calorie restriction--the SIR2 connection
    • Guarente L., and Picard F. Calorie restriction--the SIR2 connection. Cell 120 (2005) 473-482
    • (2005) Cell , vol.120 , pp. 473-482
    • Guarente, L.1    Picard, F.2
  • 25
    • 12244299825 scopus 로고    scopus 로고
    • Caloric restriction increases gluconeogenic and transaminase enzyme activities in mouse liver
    • Hagopian K., Ramsey J.J., and Weindruch R. Caloric restriction increases gluconeogenic and transaminase enzyme activities in mouse liver. Exp. Gerontol. 38 (2003) 267-278
    • (2003) Exp. Gerontol. , vol.38 , pp. 267-278
    • Hagopian, K.1    Ramsey, J.J.2    Weindruch, R.3
  • 27
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows W.C., Lee S., and Denu J.M. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. USA 103 (2006) 10230-10235
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 29
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S., Armstrong C.M., Kaeberlein M., and Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403 (2000) 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 30
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation
    • Jing E., Gesta S., and Kahn C.R. SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab. 6 (2007) 105-114
    • (2007) Cell Metab. , vol.6 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 31
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein M., McVey M., and Guarente L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13 (1999) 2570-2580
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 32
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism
    • Kahn B.B., Alquier T., Carling D., and Hardie D.G. AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab. 1 (2005) 15-25
    • (2005) Cell Metab. , vol.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 33
  • 34
    • 27744518040 scopus 로고    scopus 로고
    • FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction
    • Kitamura Y.I., Kitamura T., Kruse J.P., Raum J.C., Stein R., Gu W., and Accili D. FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction. Cell Metab. 2 (2005) 153-163
    • (2005) Cell Metab. , vol.2 , pp. 153-163
    • Kitamura, Y.I.1    Kitamura, T.2    Kruse, J.P.3    Raum, J.C.4    Stein, R.5    Gu, W.6    Accili, D.7
  • 35
    • 0037312020 scopus 로고    scopus 로고
    • How does calorie restriction work?
    • Koubova J., and Guarente L. How does calorie restriction work?. Genes Dev. 17 (2003) 313-321
    • (2003) Genes Dev. , vol.17 , pp. 313-321
    • Koubova, J.1    Guarente, L.2
  • 39
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • Lin S.J., Defossez P.A., and Guarente L. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289 (2000) 2126-2128
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 41
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin S.J., Ford E., Haigis M., Liszt G., and Guarente L. Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev. 18 (2004) 12-16
    • (2004) Genes Dev. , vol.18 , pp. 12-16
    • Lin, S.J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 43
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • Longo V.D., and Kennedy B.K. Sirtuins in aging and age-related disease. Cell 126 (2006) 257-268
    • (2006) Cell , vol.126 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 44
    • 0034714382 scopus 로고    scopus 로고
    • Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins
    • Luong A., Hannah V.C., Brown M.S., and Goldstein J.L. Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins. J. Biol. Chem. 275 (2000) 26458-26466
    • (2000) J. Biol. Chem. , vol.275 , pp. 26458-26466
    • Luong, A.1    Hannah, V.C.2    Brown, M.S.3    Goldstein, J.L.4
  • 45
    • 0034033586 scopus 로고    scopus 로고
    • Caloric restriction and aging: an update
    • Masoro E.J. Caloric restriction and aging: an update. Exp. Gerontol. 35 (2000) 299-305
    • (2000) Exp. Gerontol. , vol.35 , pp. 299-305
    • Masoro, E.J.1
  • 46
    • 0022343849 scopus 로고
    • Physiological changes in the activities of extramitochondrial acetyl-CoA hydrolase in the liver of rats under various metabolic conditions
    • Matsunaga T., Isohashi F., Nakanishi Y., and Sakamoto Y. Physiological changes in the activities of extramitochondrial acetyl-CoA hydrolase in the liver of rats under various metabolic conditions. Eur. J. Biochem. 152 (1985) 331-336
    • (1985) Eur. J. Biochem. , vol.152 , pp. 331-336
    • Matsunaga, T.1    Isohashi, F.2    Nakanishi, Y.3    Sakamoto, Y.4
  • 47
    • 0002458132 scopus 로고
    • The effects of retarded growth upon the length of life span and upon the ultimate body size
    • McCay C.M., Crowell M.F., and Maynard L.A. The effects of retarded growth upon the length of life span and upon the ultimate body size. J. Nutr. 10 (1935) 63-79
    • (1935) J. Nutr. , vol.10 , pp. 63-79
    • McCay, C.M.1    Crowell, M.F.2    Maynard, L.A.3
  • 48
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., and Horikawa I. Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16 (2005) 4623-4635
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 51
    • 0037192473 scopus 로고    scopus 로고
    • Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway
    • Nemoto S., and Finkel T. Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science 295 (2002) 2450-2452
    • (2002) Science , vol.295 , pp. 2450-2452
    • Nemoto, S.1    Finkel, T.2
  • 52
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead-dependent pathway
    • Nemoto S., Fergusson M.M., and Finkel T. Nutrient availability regulates SIRT1 through a forkhead-dependent pathway. Science 306 (2004) 2105-2108
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 54
    • 2942564591 scopus 로고    scopus 로고
    • Sirtuins: Sir2-related NAD-dependent protein deacetylases
    • North B.J., and Verdin E. Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome Biol. 5 (2004) 224
    • (2004) Genome Biol. , vol.5 , pp. 224
    • North, B.J.1    Verdin, E.2
  • 55
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North B.J., Marshall B.L., Borra M.T., Denu J.M., and Verdin E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11 (2003) 437-444
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 56
    • 0037108799 scopus 로고    scopus 로고
    • SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria
    • Onyango P., Celic I., McCaffery J.M., Boeke J.D., and Feinberg A.P. SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proc. Natl. Acad. Sci. USA 99 (2002) 13653-13658
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13653-13658
    • Onyango, P.1    Celic, I.2    McCaffery, J.M.3    Boeke, J.D.4    Feinberg, A.P.5
  • 58
    • 0032879458 scopus 로고    scopus 로고
    • Controlling caloric consumption: protocols for rodents and rhesus monkeys
    • Pugh T.D., Klopp R.G., and Weindruch R. Controlling caloric consumption: protocols for rodents and rhesus monkeys. Neurobiol. Aging 20 (1999) 157-165
    • (1999) Neurobiol. Aging , vol.20 , pp. 157-165
    • Pugh, T.D.1    Klopp, R.G.2    Weindruch, R.3
  • 59
    • 0032549811 scopus 로고    scopus 로고
    • A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
    • Puigserver P., Wu Z., Park C.W., Graves R., Wright M., and Spiegelman B.M. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92 (1998) 829-839
    • (1998) Cell , vol.92 , pp. 829-839
    • Puigserver, P.1    Wu, Z.2    Park, C.W.3    Graves, R.4    Wright, M.5    Spiegelman, B.M.6
  • 60
    • 34547906123 scopus 로고    scopus 로고
    • Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1
    • Rodgers J.T., and Puigserver P. Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1. Proc. Natl. Acad. Sci. USA 104 (2007) 12861-12866
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12861-12866
    • Rodgers, J.T.1    Puigserver, P.2
  • 61
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers J.T., Lerin C., Haas W., Gygi S.P., Spiegelman B.M., and Puigserver P. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434 (2005) 113-118
    • (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
  • 62
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina B., and Helfand S.L. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. USA 101 (2004) 15998-16003
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 64
    • 34247271282 scopus 로고    scopus 로고
    • SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress
    • Scher M.B., Vaquero A., and Reinberg D. SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 21 (2007) 920-928
    • (2007) Genes Dev. , vol.21 , pp. 920-928
    • Scher, M.B.1    Vaquero, A.2    Reinberg, D.3
  • 65
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer B., North B.J., Frye R.A., Ott M., and Verdin E. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 158 (2002) 647-657
    • (2002) J. Cell Biol. , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 66
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., and Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. USA 103 (2006) 10224-10229
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 67
    • 0016374763 scopus 로고
    • Formation of free acetate by isolated perfused livers from normal, starved and diabetic rats
    • Seufert C.D., Graf M., Janson G., Kuhn A., and Soling H.D. Formation of free acetate by isolated perfused livers from normal, starved and diabetic rats. Biochem. Biophys. Res. Commun. 57 (1974) 901-909
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 901-909
    • Seufert, C.D.1    Graf, M.2    Janson, G.3    Kuhn, A.4    Soling, H.D.5
  • 68
    • 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. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem. 280 (2005) 13560-13567
    • (2005) J. Biol. Chem. , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 71
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • Starai V.J., Celic I., Cole R.N., Boeke J.D., and Escalante-Semerena J.C. Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298 (2002) 2390-2392
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 72
    • 34548857700 scopus 로고    scopus 로고
    • SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B
    • Sun C., Zhang F., Ge X., Yan T., Chen X., Shi X., and Zhai Q. SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B. Cell Metab. 6 (2007) 307-319
    • (2007) Cell Metab. , vol.6 , pp. 307-319
    • Sun, C.1    Zhang, F.2    Ge, X.3    Yan, T.4    Chen, X.5    Shi, X.6    Zhai, Q.7
  • 73
    • 33745557847 scopus 로고    scopus 로고
    • Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription
    • Takahashi H., McCaffery J.M., Irizarry R.A., and Boeke J.D. Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Mol. Cell 23 (2006) 207-217
    • (2006) Mol. Cell , vol.23 , pp. 207-217
    • Takahashi, H.1    McCaffery, J.M.2    Irizarry, R.A.3    Boeke, J.D.4
  • 74
    • 34250365395 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1
    • Tanno M., Sakamoto J., Miura T., Shimamoto K., and Horio Y. Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J. Biol. Chem. 282 (2007) 6823-6832
    • (2007) J. Biol. Chem. , vol.282 , pp. 6823-6832
    • Tanno, M.1    Sakamoto, J.2    Miura, T.3    Shimamoto, K.4    Horio, Y.5
  • 75
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum H.A., and Guarente L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410 (2001) 227-230
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 76
    • 33847080728 scopus 로고    scopus 로고
    • AMP-activated protein kinase in metabolic control and insulin signaling
    • Towler M.C., and Hardie D.G. AMP-activated protein kinase in metabolic control and insulin signaling. Circ. Res. 100 (2007) 328-341
    • (2007) Circ. Res. , vol.100 , pp. 328-341
    • Towler, M.C.1    Hardie, D.G.2
  • 77
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 39 (2005) 359-407
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 80
    • 0035978425 scopus 로고    scopus 로고
    • Production of acetate in the liver and its utilization in peripheral tissues
    • Yamashita H., Kaneyuki T., and Tagawa K. Production of acetate in the liver and its utilization in peripheral tissues. Biochim. Biophys. Acta 1532 (2001) 79-87
    • (2001) Biochim. Biophys. Acta , vol.1532 , pp. 79-87
    • Yamashita, H.1    Kaneyuki, T.2    Tagawa, K.3
  • 82
    • 9344237090 scopus 로고    scopus 로고
    • Distinct pathways of insulin-regulated versus diabetes-regulated gene expression: an in vivo analysis in MIRKO mice
    • Yechoor V.K., Patti M.E., Ueki K., Laustsen P.G., Saccone R., Rauniyar R., and Kahn C.R. Distinct pathways of insulin-regulated versus diabetes-regulated gene expression: an in vivo analysis in MIRKO mice. Proc. Natl. Acad. Sci. USA 101 (2004) 16525-16530
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16525-16530
    • Yechoor, V.K.1    Patti, M.E.2    Ueki, K.3    Laustsen, P.G.4    Saccone, R.5    Rauniyar, R.6    Kahn, C.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.