메뉴 건너뛰기




Volumn 26, Issue 2, 2005, Pages 94-103

The emerging therapeutic potential of sirtuin-interacting drugs: From cell death to lifespan extension

Author keywords

[No Author keywords available]

Indexed keywords

3,6,3',4' TETRAHYDROXYFLAVONE; 5,7,3',4',5' PENTAHYDROXYFLAVONE; A 3; BUTEIN; CARBAMIDONICOTINAMIDE ADENINE DINUCLEOTIDE; COUMARIN DERIVATIVE; DIHYDROCOUMARIN; DNA DIRECTED RNA POLYMERASE; ENZYME ACTIVATOR; FISTEIN; FLAVONE DERIVATIVE; HYDROLASE INHIBITOR; ISOLIQUIRITIGENIN; LUTEOLIN; M 15; NICOTINAMIDE; PICEATANNOL; PYRAN DERIVATIVE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; RESVERATROL; RIBOSOME DNA; SIRTINOL; SIRTUIN; SIRTUIN ACTIVATOR; SIRTUIN INHIBITOR; SPLITOMICIN; UNCLASSIFIED DRUG;

EID: 12844271254     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2004.12.009     Document Type: Review
Times cited : (171)

References (79)
  • 1
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • T. Jenuwein, and C.D. Allis Translating the histone code Science 293 2001 1074 1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 2
    • 2642531973 scopus 로고    scopus 로고
    • Epigenetics in human disease and prospects for epigenetic therapy
    • G. Egger Epigenetics in human disease and prospects for epigenetic therapy Nature 429 2004 457 463
    • (2004) Nature , vol.429 , pp. 457-463
    • Egger, G.1
  • 3
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • T. Kouzarides Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19 2000 1176 1179
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 4
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • R.W. Johnstone Histone-deacetylase inhibitors: novel drugs for the treatment of cancer Nat. Rev. Drug Discov. 1 2002 287 299
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 5
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • C.M. Grozinger, and S.L. Schreiber Deacetylase enzymes: biological functions and the use of small-molecule inhibitors Chem. Biol. 9 2002 3 16
    • (2002) Chem. Biol. , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 6
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • L. Guarente Sir2 links chromatin silencing, metabolism, and aging Genes Dev. 14 2000 1021 1026
    • (2000) Genes Dev. , vol.14 , pp. 1021-1026
    • Guarente, L.1
  • 7
    • 0035861202 scopus 로고    scopus 로고
    • The molecular biology of the SIR proteins
    • S.M. Gasser, and M.M. Cockell The molecular biology of the SIR proteins Gene 279 2001 1 16
    • (2001) Gene , vol.279 , pp. 1-16
    • Gasser, S.M.1    Cockell, M.M.2
  • 8
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • G. Blander, and L. Guarente 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
  • 9
    • 2642573581 scopus 로고    scopus 로고
    • Diversity in the Sir2 family of protein deacetylases
    • S.W. Buck Diversity in the Sir2 family of protein deacetylases J. Leukoc. Biol. 75 2004 939 950
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 939-950
    • Buck, S.W.1
  • 10
    • 4344590155 scopus 로고    scopus 로고
    • Small molecules that regulate lifespan: Evidence for xenohormesis
    • D.W. Lamming Small molecules that regulate lifespan: evidence for xenohormesis Mol. Microbiol. 53 2004 1003 1009
    • (2004) Mol. Microbiol. , vol.53 , pp. 1003-1009
    • Lamming, D.W.1
  • 11
    • 0035910031 scopus 로고    scopus 로고
    • Identification of a small molecule inhibitor of Sir2p
    • A. Bedalov Identification of a small molecule inhibitor of Sir2p Proc. Natl. Acad. Sci. U. S. A. 98 2001 15113 15118
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 15113-15118
    • Bedalov, A.1
  • 12
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • K.J. Bitterman 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
  • 13
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • R.M. Anderson 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
  • 14
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • M.C. Motta Mammalian SIRT1 represses forkhead transcription factors Cell 116 2004 551 563
    • (2004) Cell , vol.116 , pp. 551-563
    • Motta, M.C.1
  • 15
    • 0037123767 scopus 로고    scopus 로고
    • Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases
    • D. Robyr Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases Cell 109 2002 437 446
    • (2002) Cell , vol.109 , pp. 437-446
    • Robyr, D.1
  • 16
    • 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
    • R.A. Frye 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
  • 17
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • R.A. Frye 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
  • 18
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • S. Imai 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
  • 19
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • M. Fulco Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state Mol. Cell 12 2003 51 62
    • (2003) Mol. Cell , vol.12 , pp. 51-62
    • Fulco, M.1
  • 20
    • 0037359584 scopus 로고    scopus 로고
    • The absence of SIR2alpha protein has no effect on global gene silencing in mouse embryonic stem cells
    • M.W. McBurney The absence of SIR2alpha protein has no effect on global gene silencing in mouse embryonic stem cells Mol. Cancer Res. 1 2003 402 409
    • (2003) Mol. Cancer Res. , vol.1 , pp. 402-409
    • McBurney, M.W.1
  • 21
    • 0037207475 scopus 로고    scopus 로고
    • The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis
    • M.W. McBurney The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis Mol. Cell. Biol. 23 2003 38 54
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 38-54
    • McBurney, M.W.1
  • 22
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • H.L. Cheng Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice Proc. Natl. Acad. Sci. U. S. A. 100 2003 10794 10799
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10794-10799
    • Cheng, H.L.1
  • 23
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • B.J. North 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
  • 24
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • B. Schwer 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
  • 25
    • 0037108799 scopus 로고    scopus 로고
    • SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria
    • P. Onyango SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria Proc. Natl. Acad. Sci. U. S. A. 99 2002 13653 13658
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13653-13658
    • Onyango, P.1
  • 26
    • 0034705129 scopus 로고    scopus 로고
    • The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
    • J. Landry The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases Proc. Natl. Acad. Sci. U. S. A. 97 2000 5807 5811
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5807-5811
    • Landry, J.1
  • 27
    • 12944283150 scopus 로고    scopus 로고
    • A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family
    • J.S. Smith A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family Proc. Natl. Acad. Sci. U. S. A. 97 2000 6658 6663
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6658-6663
    • Smith, J.S.1
  • 28
    • 0034735990 scopus 로고    scopus 로고
    • Role of NAD(+) in the deacetylase activity of the SIR2-like proteins
    • J. Landry Role of NAD(+) in the deacetylase activity of the SIR2-like proteins Biochem. Biophys. Res. Commun. 278 2000 685 690
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 685-690
    • Landry, J.1
  • 29
    • 0035895275 scopus 로고    scopus 로고
    • Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product
    • J.C. Tanny, and D. Moazed Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product Proc. Natl. Acad. Sci. U. S. A. 98 2001 415 420
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 30
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: The mechanism of NAD+-dependent deacetylation reactions
    • A.A. Sauve Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions Biochemistry 40 2001 15456 15463
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1
  • 31
    • 0037166269 scopus 로고    scopus 로고
    • Structural identification of 2′- and 3′-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases
    • M.D. Jackson, and J.M. Denu Structural identification of 2′- and 3′-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases J. Biol. Chem. 277 2002 18535 18544
    • (2002) J. Biol. Chem. , vol.277 , pp. 18535-18544
    • Jackson, M.D.1    Denu, J.M.2
  • 32
    • 0037066738 scopus 로고    scopus 로고
    • Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases
    • M.T. Borra Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases J. Biol. Chem. 277 2002 12632 12641
    • (2002) J. Biol. Chem. , vol.277 , pp. 12632-12641
    • Borra, M.T.1
  • 33
    • 0037072885 scopus 로고    scopus 로고
    • Structural basis for the NAD-dependent deacetylase mechanism of Sir2
    • J.H. Chang Structural basis for the NAD-dependent deacetylase mechanism of Sir2 J. Biol. Chem. 277 2002 34489 34498
    • (2002) J. Biol. Chem. , vol.277 , pp. 34489-34498
    • Chang, J.H.1
  • 34
    • 2942534101 scopus 로고    scopus 로고
    • Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases
    • K. Zhao Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases Proc. Natl. Acad. Sci. U. S. A. 101 2004 8563 8568
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8563-8568
    • Zhao, K.1
  • 35
    • 3343024449 scopus 로고    scopus 로고
    • Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases
    • M.T. Borra Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases Biochemistry 43 2004 9877 9887
    • (2004) Biochemistry , vol.43 , pp. 9877-9887
    • Borra, M.T.1
  • 36
    • 0346435109 scopus 로고    scopus 로고
    • Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
    • M.D. Jackson Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases J. Biol. Chem. 278 2003 50985 50998
    • (2003) J. Biol. Chem. , vol.278 , pp. 50985-50998
    • Jackson, M.D.1
  • 37
    • 1642297558 scopus 로고    scopus 로고
    • Structural basis for the mechanism and regulation of Sir2 enzymes
    • J.L. Avalos Structural basis for the mechanism and regulation of Sir2 enzymes Mol. Cell 13 2004 639 648
    • (2004) Mol. Cell , vol.13 , pp. 639-648
    • Avalos, J.L.1
  • 38
    • 0345731468 scopus 로고    scopus 로고
    • Yeast life-span extension by calorie restriction is independent of NAD fluctuation
    • R.M. Anderson Yeast life-span extension by calorie restriction is independent of NAD fluctuation Science 302 2003 2124 2126
    • (2003) Science , vol.302 , pp. 2124-2126
    • Anderson, R.M.1
  • 39
    • 4544243684 scopus 로고    scopus 로고
    • Co-enzyme specificity of Sir2 protein deacetylases: Implications for physiological regulation
    • M.T. Schmidt Co-enzyme specificity of Sir2 protein deacetylases: implications for physiological regulation J. Biol. Chem. 279 2004 40122 40129
    • (2004) J. Biol. Chem. , vol.279 , pp. 40122-40129
    • Schmidt, M.T.1
  • 40
    • 0028897013 scopus 로고
    • Mutation in the silencing gene SIR4 can delay aging in S. cerevisiae
    • B.K. Kennedy Mutation in the silencing gene SIR4 can delay aging in S. cerevisiae Cell 80 1995 485 496
    • (1995) Cell , vol.80 , pp. 485-496
    • Kennedy, B.K.1
  • 41
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • M. Kaeberlein 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
  • 42
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • H.A. Tissenbaum, and L. Guarente 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
  • 43
    • 0037312020 scopus 로고    scopus 로고
    • How does calorie restriction work?
    • J. Koubova, and L. Guarente 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
  • 44
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • S.J. Lin 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
  • 45
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay aging in metazoans
    • J.G. Wood Sirtuin activators mimic caloric restriction and delay aging in metazoans Nature 430 2004 686 689
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1
  • 46
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • S.J. Lin, and L. Guarente Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease Curr. Opin. Cell Biol. 15 2003 241 246
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 47
    • 0037221445 scopus 로고    scopus 로고
    • Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases
    • J.M. Denu Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases Trends Biochem. Sci. 28 2003 41 48
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 41-48
    • Denu, J.M.1
  • 48
    • 0036194785 scopus 로고    scopus 로고
    • Telomeric and rDNA silencing in Saccharomyces cerevisiae are dependent on a nuclear NAD(+) salvage pathway
    • J.J. Sandmeier Telomeric and rDNA silencing in Saccharomyces cerevisiae are dependent on a nuclear NAD(+) salvage pathway Genetics 160 2002 877 889
    • (2002) Genetics , vol.160 , pp. 877-889
    • Sandmeier, J.J.1
  • 49
    • 0037166274 scopus 로고    scopus 로고
    • Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels
    • R.M. Anderson Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels J. Biol. Chem. 277 2002 18881 18890
    • (2002) J. Biol. Chem. , vol.277 , pp. 18881-18890
    • Anderson, R.M.1
  • 50
    • 0037130175 scopus 로고    scopus 로고
    • Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
    • S.J. Lin Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration Nature 418 2002 344 348
    • (2002) Nature , vol.418 , pp. 344-348
    • Lin, S.J.1
  • 51
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • T. Araki Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration Science 305 2004 1010 1013
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1
  • 52
    • 10944270187 scopus 로고    scopus 로고
    • The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells
    • (in press)
    • Revollo, J.R. et al. The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J. Biol. Chem. (in press)
    • J. Biol. Chem.
    • Revollo, J.R.1
  • 53
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • S.J. Lin 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
  • 54
    • 0036499892 scopus 로고    scopus 로고
    • PARP-1: Killer or conspirator? the suicide hypothesis revisited
    • A. Chiarugi PARP-1: killer or conspirator? The suicide hypothesis revisited Trends Pharmacol. Sci. 23 2002 122 129
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 122-129
    • Chiarugi, A.1
  • 55
    • 0041589716 scopus 로고    scopus 로고
    • Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked?
    • J. Zhang Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked? BioEssays 25 2003 808 814
    • (2003) BioEssays , vol.25 , pp. 808-814
    • Zhang, J.1
  • 56
    • 1542346420 scopus 로고    scopus 로고
    • The new life of a centenarian: Signalling functions of NAD(P)
    • F. Berger The new life of a centenarian: signalling functions of NAD(P) Trends Biochem. Sci. 29 2004 111 118
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 111-118
    • Berger, F.1
  • 57
    • 0035868764 scopus 로고    scopus 로고
    • Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription
    • V. Muth Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription EMBO J. 20 2001 1353 1362
    • (2001) EMBO J. , vol.20 , pp. 1353-1362
    • Muth, V.1
  • 58
    • 0242322010 scopus 로고    scopus 로고
    • Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression
    • T. Senawong Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression J. Biol. Chem. 278 2003 43041 43050
    • (2003) J. Biol. Chem. , vol.278 , pp. 43041-43050
    • Senawong, T.1
  • 59
    • 0036898253 scopus 로고    scopus 로고
    • Acetylation inactivates the transcriptional repressor BCL6
    • O.R. Bereshchenko Acetylation inactivates the transcriptional repressor BCL6 Nat. Genet. 32 2002 606 613
    • (2002) Nat. Genet. , vol.32 , pp. 606-613
    • Bereshchenko, O.R.1
  • 60
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • J. Luo Negative control of p53 by Sir2alpha promotes cell survival under stress Cell 107 2001 137 148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 61
    • 0035913903 scopus 로고    scopus 로고
    • HSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • H. Vaziri hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase Cell 107 2001 149 159
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 62
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • E. Langley Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence EMBO J. 21 2002 2383 2396
    • (2002) EMBO J. , vol.21 , pp. 2383-2396
    • Langley, E.1
  • 63
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • A. Brunet Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase Science 303 2004 2011 2015
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1
  • 64
    • 3042750643 scopus 로고    scopus 로고
    • Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity
    • H. Daitoku Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity Proc. Natl. Acad. Sci. U. S. A. 101 2004 10042 10047
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10042-10047
    • Daitoku, H.1
  • 65
    • 4143050290 scopus 로고    scopus 로고
    • The interaction between FOXO and SIRT1: Tipping the balance towards survival
    • M.E. Giannakou, and L. Partridge The interaction between FOXO and SIRT1: tipping the balance towards survival Trends Cell Biol. 14 2004 408 412
    • (2004) Trends Cell Biol. , vol.14 , pp. 408-412
    • Giannakou, M.E.1    Partridge, L.2
  • 66
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • F. Yeung Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase EMBO J. 23 2004 2369 2380
    • (2004) EMBO J. , vol.23 , pp. 2369-2380
    • Yeung, F.1
  • 67
    • 3042681042 scopus 로고    scopus 로고
    • Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma
    • F. Picard Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma Nature 429 2004 771 776
    • (2004) Nature , vol.429 , pp. 771-776
    • Picard, F.1
  • 68
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • H.Y. Cohen Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase Science 305 2004 390 392
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1
  • 69
    • 3142548829 scopus 로고    scopus 로고
    • Human histone deacetylase SIRT2 Interacts with the homeobox transcription factor HOXA10
    • N.S. Bae Human histone deacetylase SIRT2 Interacts with the homeobox transcription factor HOXA10 J. Biochem. (Tokyo) 135 2004 695 700
    • (2004) J. Biochem. (Tokyo) , vol.135 , pp. 695-700
    • Bae, N.S.1
  • 70
    • 0037033021 scopus 로고    scopus 로고
    • Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolases
    • L.A. Rafty Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolases J. Biol. Chem. 277 2002 47114 47122
    • (2002) J. Biol. Chem. , vol.277 , pp. 47114-47122
    • Rafty, L.A.1
  • 71
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • K.T. Howitz Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan Nature 425 2003 191 196
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1
  • 72
    • 0033637140 scopus 로고    scopus 로고
    • The effects of plant flavonoids on mammalian cells: Implications for inflammation, heart disease, and cancer
    • E. Middleton Jr The effects of plant flavonoids on mammalian cells: implications for inflammation, heart disease, and cancer Pharmacol. Rev. 52 2000 673 751
    • (2000) Pharmacol. Rev. , vol.52 , pp. 673-751
    • Middleton Jr., E.1
  • 73
    • 8844247034 scopus 로고    scopus 로고
    • Silent information regulator 2α, a longevity factor and Class III histone deacetylase, is an essential endogenous apoptosis inhibitor in cardiac myocytes
    • R.R. Alcendor Silent information regulator 2α, a longevity factor and Class III histone deacetylase, is an essential endogenous apoptosis inhibitor in cardiac myocytes Circ. Res 95 2004 971 980
    • (2004) Circ. Res , vol.95 , pp. 971-980
    • Alcendor, R.R.1
  • 74
    • 0037237959 scopus 로고    scopus 로고
    • Calorie restriction in rhesus monkeys
    • J.A. Mattison Calorie restriction in rhesus monkeys Exp. Gerontol. 38 2003 35 46
    • (2003) Exp. Gerontol. , vol.38 , pp. 35-46
    • Mattison, J.A.1
  • 75
    • 0037011958 scopus 로고    scopus 로고
    • P53 mutant mice that display early ageing-associated phenotypes
    • S.D. Tyner p53 mutant mice that display early ageing-associated phenotypes Nature 415 2002 45 53
    • (2002) Nature , vol.415 , pp. 45-53
    • Tyner, S.D.1
  • 76
    • 12144286529 scopus 로고    scopus 로고
    • Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis
    • H.Y. Cohen Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis Mol. Cell 13 2004 627 638
    • (2004) Mol. Cell , vol.13 , pp. 627-638
    • Cohen, H.Y.1
  • 77
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • C.M. Grozinger Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening J. Biol. Chem. 276 2001 38837 38843
    • (2001) J. Biol. Chem. , vol.276 , pp. 38837-38843
    • Grozinger, C.M.1
  • 78
    • 0346101749 scopus 로고    scopus 로고
    • Identification of selective inhibitors of NAD+-dependent deacetylases using phenotypic screens in yeast
    • M. Hirao Identification of selective inhibitors of NAD+-dependent deacetylases using phenotypic screens in yeast J. Biol. Chem. 278 2003 52773 52782
    • (2003) J. Biol. Chem. , vol.278 , pp. 52773-52782
    • Hirao, M.1
  • 79
    • 2342614837 scopus 로고    scopus 로고
    • Inhibitors of Sir2: Evaluation of splitomicin analogues
    • J. Posakony Inhibitors of Sir2: evaluation of splitomicin analogues J. Med. Chem. 47 2004 2635 2644
    • (2004) J. Med. Chem. , vol.47 , pp. 2635-2644
    • Posakony, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.