메뉴 건너뛰기




Volumn 9, Issue 5, 2005, Pages 431-440

The Sir2 family of protein deacetylases

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; NICOTINAMIDE; RESVERATROL; SILENT INFORMATION REGULATOR PROTEIN 2; SIRTUIN;

EID: 25144496904     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2005.08.010     Document Type: Review
Times cited : (238)

References (69)
  • 1
    • 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
  • 2
    • 0035313756 scopus 로고    scopus 로고
    • Enzymatic activities of Sir2 and chromatin silencing
    • D. Moazed Enzymatic activities of Sir2 and chromatin silencing Curr Opin Cell Biol 13 2001 232 238
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 232-238
    • Moazed, D.1
  • 3
    • 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
  • 4
    • 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
  • 5
    • 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
  • 6
    • 0035871393 scopus 로고    scopus 로고
    • Conversion of a gene-specific repressor to a regional silencer
    • L.N. Rusche, and J. Rine Conversion of a gene-specific repressor to a regional silencer Genes Dev 15 2001 955 967
    • (2001) Genes Dev , vol.15 , pp. 955-967
    • Rusche, L.N.1    Rine, J.2
  • 7
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • M. Kaeberlein, M. McVey, and L. Guarente 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
  • 8
    • 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
  • 9
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • B. Rogina, and S.L. Helfand 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
  • 10
    • 2942564591 scopus 로고    scopus 로고
    • Sirtuins: Sir2-related NAD-dependent protein deacetylases
    • B.J. North, and E. Verdin 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
  • 11
    • 1842610541 scopus 로고    scopus 로고
    • A link between transcription and intermediary metabolism: A role for Sir2 in the control of acetyl-coenzyme a synthetase
    • V.J. Starai, H. Takahashi, J.D. Boeke, and J.C. Escalante-Semerena A link between transcription and intermediary metabolism: a role for Sir2 in the control of acetyl-coenzyme A synthetase Curr Opin Microbiol 7 2004 115 119
    • (2004) Curr Opin Microbiol , vol.7 , pp. 115-119
    • Starai, V.J.1    Takahashi, H.2    Boeke, J.D.3    Escalante-Semerena, J.C.4
  • 12
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • V.J. Starai, I. Celic, R.N. Cole, J.D. Boeke, and J.C. Escalante-Semerena Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine Science 298 2002 2390 2392 This study demonstrated a clear link between sirtuins and the direct control of metabolic pathways regulated by acetyl-CoA synthetase. This was one of first studies to establish non-histone proteins as target substrates of sirtuins.
    • (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
  • 13
    • 0037297590 scopus 로고    scopus 로고
    • Short-chain fatty acid activation by acyl-coenzyme a synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae
    • V.J. Starai, H. Takahashi, J.D. Boeke, and J.C. Escalante-Semerena Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae Genetics 163 2003 545 555
    • (2003) Genetics , vol.163 , pp. 545-555
    • Starai, V.J.1    Takahashi, H.2    Boeke, J.D.3    Escalante-Semerena, J.C.4
  • 15
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • J. Luo, A.Y. Nikolaev, S. Imai, D. Chen, F. Su, A. Shiloh, L. Guarente, and W. Gu 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    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 20
    • 15444377466 scopus 로고    scopus 로고
    • SIRT1 deacetylation and repression of P300 involves lysine residues 1020/1024 within the cell-cycle regulatory domain 1
    • T. Bouras, M. Fu, A.A. Sauve, F. Wang, A.A. Quong, N.D. Perkins, R.T. Hay, W. Gu, and R.G. Pestell SIRT1 deacetylation and repression of P300 involves lysine residues 1020/1024 within the cell-cycle regulatory domain 1 J Biol Chem 280 2005 10264 10276
    • (2005) J Biol Chem , vol.280 , pp. 10264-10276
    • Bouras, T.1    Fu, M.2    Sauve, A.A.3    Wang, F.4    Quong, A.A.5    Perkins, N.D.6    Hay, R.T.7    Gu, W.8    Pestell, R.G.9
  • 21
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • F. Yeung, J.E. Hoberg, C.S. Ramsey, M.D. Keller, D.R. Jones, R.A. Frye, and M.W. Mayo 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    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6    Mayo, M.W.7
  • 22
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • J.T. Rodgers, C. Lerin, W. Haas, S.P. Gygi, B.M. Spiegelman, and P. Puigserver Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1 Nature 434 2005 113 118 This work along with that reported in [23], established SIRT1 as a critical regulator of PGC-1α, a coactivator that regulates cellular metabolism. These results implicate SIRT1 in the basic pathways of energy homeostasis, diabetes and lifespan.
    • (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
  • 23
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}
    • S. Nemoto, M.M. Fergusson, and T. Finkel SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha} J Biol Chem 280 2005 16456 16460
    • (2005) J Biol Chem , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 26
    • 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
    • K.G. Tanner, J. Landry, R. Sternglanz, and J.M. Denu 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 97 2000 14178 14182
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 27
    • 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 USA 98 2001 415 420
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 28
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • S. Imai, C.M. Armstrong, M. Kaeberlein, and L. Guarente 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
  • 29
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: The mechanism of NAD+-dependent deacetylation reactions
    • A.A. Sauve, I. Celic, J. Avalos, H. Deng, J.D. Boeke, and V.L. Schramm 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    Celic, I.2    Avalos, J.3    Deng, H.4    Boeke, J.D.5    Schramm, V.L.6
  • 30
    • 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
    • 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
  • 34
    • 1642580758 scopus 로고    scopus 로고
    • Nicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity
    • C.M. Gallo, D.L. Smith Jr., and J.S. Smith Nicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity Mol Cell Biol 24 2004 1301 1312
    • (2004) Mol Cell Biol , vol.24 , pp. 1301-1312
    • Gallo, C.M.1    Smith Jr., D.L.2    Smith, J.S.3
  • 35
    • 0036194785 scopus 로고    scopus 로고
    • Telomeric and rDNA silencing in Saccharomyces cerevisiae are dependent on a nuclear NAD(+) salvage pathway
    • J.J. Sandmeier, I. Celic, J.D. Boeke, and J.S. Smith 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    Celic, I.2    Boeke, J.D.3    Smith, J.S.4
  • 36
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • R.M. Anderson, K.J. Bitterman, J.G. Wood, O. Medvedik, and D.A. Sinclair Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae Nature 423 2003 181 185 The authors reported evidence that nicotinamide is a cellular inhibitor of ySir2 and that PNC1, a nicotinamidase of the NAD salvage pathway, controls cellular nicotinamide levels and Sir2 activity.
    • (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
  • 37
    • 10944270187 scopus 로고    scopus 로고
    • The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells
    • •], demonstrated that NAD biosynthetic enzymes can regulate SIRT1 function in mammalian cells.
    • (2004) J Biol Chem , vol.279 , pp. 50754-50763
    • Revollo, J.R.1    Grimm, A.A.2    Imai, S.3
  • 38
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • T. Araki, Y. Sasaki, and J. Milbrandt Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration Science 305 2004 1010 1013 In addition to indicating that nuclear NAD biosynthesis can upregulate SIRT1, this work suggested that SIRT1 functions in protecting neuronal cells from injury such as oxidant insult.
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 39
    • 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
  • 40
    • 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, F.J. O'Neill, M.D. Jackson, B. Marshall, E. Verdin, K.R. Foltz, and J.M. Denu 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 The production of O-acetyl-ADP-ribose by sirtuins was shown to be universally conserved among active enzymes from diverse species. Also, this was the first report to show the biological effects of O-acetyl-ADP-ribose by microinjection.
    • (2002) J Biol Chem , vol.277 , pp. 12632-12641
    • Borra, M.T.1    O'Neill, F.J.2    Jackson, M.D.3    Marshall, B.4    Verdin, E.5    Foltz, K.R.6    Denu, J.M.7
  • 41
    • 0037033021 scopus 로고    scopus 로고
    • Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolases
    • L.A. Rafty, M.T. Schmidt, A.L. Perraud, A.M. Scharenberg, and J.M. Denu 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    Schmidt, M.T.2    Perraud, A.L.3    Scharenberg, A.M.4    Denu, J.M.5
  • 42
    • 3343024449 scopus 로고    scopus 로고
    • Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases
    • M.T. Borra, M.R. Langer, J.T. Slama, and J.M. Denu Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases Biochemistry 43 2004 9877 9887 This kinetic study established the complete kinetic mechanism for sirtuin enzymes. Acetyl-peptide substrate analysis provided evidence that the catalytic domains of sirtuins exhibit substrate preferences.
    • (2004) Biochemistry , vol.43 , pp. 9877-9887
    • Borra, M.T.1    Langer, M.R.2    Slama, J.T.3    Denu, J.M.4
  • 43
    • 0036753953 scopus 로고    scopus 로고
    • Structure of a Sir2 enzyme bound to an acetylated p53 peptide
    • J.L. Avalos, I. Celic, S. Muhammad, M.S. Cosgrove, J.D. Boeke, and C. Wolberger Structure of a Sir2 enzyme bound to an acetylated p53 peptide Mol Cell 10 2002 523 535 This binary complex structure was the first to establish the acetyl-peptide binding site within sirtuins.
    • (2002) Mol Cell , vol.10 , pp. 523-535
    • Avalos, J.L.1    Celic, I.2    Muhammad, S.3    Cosgrove, M.S.4    Boeke, J.D.5    Wolberger, C.6
  • 44
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • J. Min, J. Landry, R. Sternglanz, and R.M. Xu Crystal structure of a SIR2 homolog-NAD complex Cell 105 2001 269 279
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 45
    • 15244355745 scopus 로고    scopus 로고
    • Mechanism of sirtuin inhibition by nicotinamide: Altering the NAD(+) cosubstrate specificity of a Sir2 enzyme
    • J.L. Avalos, K.M. Bever, and C. Wolberger Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme Mol Cell 17 2005 855 868
    • (2005) Mol Cell , vol.17 , pp. 855-868
    • Avalos, J.L.1    Bever, K.M.2    Wolberger, C.3
  • 46
    • 1642297558 scopus 로고    scopus 로고
    • Structural basis for the mechanism and regulation of Sir2 enzymes
    • + binding surface, highlighted by nicotinamide bound to the previously described C pocket [44].
    • (2004) Mol Cell , vol.13 , pp. 639-648
    • Avalos, J.L.1    Boeke, J.D.2    Wolberger, C.3
  • 47
    • 2942534101 scopus 로고    scopus 로고
    • Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases
    • K. Zhao, R. Harshaw, X. Chai, and R. Marmorstein Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases Proc Natl Acad Sci USA 101 2004 8563 8568 A ternary complex between HST2, a histone acetyl-peptide and an NAD analog provided additional structural evidence for the mechanism of catalysis by sirtuins.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8563-8568
    • Zhao, K.1    Harshaw, R.2    Chai, X.3    Marmorstein, R.4
  • 48
    • 1842430616 scopus 로고    scopus 로고
    • SIR2: The biochemical mechanism of NAD(+)-dependent protein deacetylation and ADP-ribosyl enzyme intermediates
    • A.A. Sauve, and V.L. Schramm SIR2: the biochemical mechanism of NAD(+)-dependent protein deacetylation and ADP-ribosyl enzyme intermediates Curr Med Chem 11 2004 807 826
    • (2004) Curr Med Chem , vol.11 , pp. 807-826
    • Sauve, A.A.1    Schramm, V.L.2
  • 49
    • 0346435109 scopus 로고    scopus 로고
    • Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
    • M.D. Jackson, M.T. Schmidt, N.J. Oppenheimer, and J.M. Denu Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases J Biol Chem 278 2003 50985 50998 This study provided the molecular insight into the mechanisms of catalysis and of nicotinamide inhibition by sirtuins.
    • (2003) J Biol Chem , vol.278 , pp. 50985-50998
    • Jackson, M.D.1    Schmidt, M.T.2    Oppenheimer, N.J.3    Denu, J.M.4
  • 50
    • 0041571570 scopus 로고    scopus 로고
    • Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
    • A.A. Sauve, and V.L. Schramm Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry Biochemistry 42 2003 9249 9256 This study describes the mechanistic basis for nicotinamide inhibition, and suggested the use of nicotinamide analogs as sirtuin activators.
    • (2003) Biochemistry , vol.42 , pp. 9249-9256
    • Sauve, A.A.1    Schramm, V.L.2
  • 51
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • J.C. Tanny, G.J. Dowd, J. Huang, H. Hilz, and D. Moazed An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing Cell 99 1999 735 745
    • (1999) Cell , vol.99 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 52
    • 0242556798 scopus 로고    scopus 로고
    • A chromosomal SIR2 homologue with both histone NAD-dependent ADP-ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei
    • J.A. Garcia-Salcedo, P. Gijon, D.P. Nolan, P. Tebabi, and E. Pays A chromosomal SIR2 homologue with both histone NAD-dependent ADP- ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei EMBO J 22 2003 5851 5862
    • (2003) EMBO J , vol.22 , pp. 5851-5862
    • Garcia-Salcedo, J.A.1    Gijon, P.2    Nolan, D.P.3    Tebabi, P.4    Pays, E.5
  • 53
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • G. Liszt, E. Ford, M. Kurtev, and L. Guarente Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase J Biol Chem 280 2005 21313 21320
    • (2005) J Biol Chem , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 54
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-O-acetyl ADP ribose and histone peptide
    • K. Zhao, X. Chai, and R. Marmorstein Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-O-acetyl ADP ribose and histone peptide Structure (Camb) 11 2003 1403 1411
    • (2003) Structure (Camb) , vol.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 56
    • 4544243684 scopus 로고    scopus 로고
    • Coenzyme specificity of Sir2 protein deacetylases: Implications for physiological regulation
    • M.T. Schmidt, B.C. Smith, M.D. Jackson, and J.M. Denu Coenzyme 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    Smith, B.C.2    Jackson, M.D.3    Denu, J.M.4
  • 57
    • 0034735990 scopus 로고    scopus 로고
    • Role of NAD(+) in the deacetylase activity of the SIR2-like proteins
    • J. Landry, J.T. Slama, and R. Sternglanz 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    Slama, J.T.2    Sternglanz, R.3
  • 58
    • 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, R.M. Anderson, H.Y. Cohen, M. Latorre-Esteves, and D.A. Sinclair 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
  • 59
    • 13944258164 scopus 로고    scopus 로고
    • Chemical activation of sir2- dependent silencing by relief of nicotinamide inhibition
    • A.A. Sauve, R.D. Moir, V.L. Schramm, and I.M. Willis Chemical activation of sir2- dependent silencing by relief of nicotinamide inhibition Mol Cell 17 2005 595 601 These authors used isonicotinamide as an activator of ySir2 in vitro and in vivo. This work suggests the possibility of developing sirtuin activators that compete for the nicotinamide binding site and relieve endogenous nicotinamide inhibition.
    • (2005) Mol Cell , vol.17 , pp. 595-601
    • Sauve, A.A.1    Moir, R.D.2    Schramm, V.L.3    Willis, I.M.4
  • 61
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • J.G. Wood, B. Rogina, S. Lavu, K. Howitz, S.L. Helfand, M. Tatar, and D. Sinclair Sirtuin activators mimic caloric restriction and delay ageing in metazoans Nature 430 2004 686 689 The authors of this study and that of [60] report the anti-aging effects of resveratrol and suggest that Sir2 proteins are the direct in vivo targets of resveratrol, leading to activation of protein deacetylation.
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3    Howitz, K.4    Helfand, S.L.5    Tatar, M.6    Sinclair, D.7
  • 63
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • M.T. Borra, B.C. Smith, and J.M. Denu Mechanism of human SIRT1 activation by resveratrol J Biol Chem 280 2005 17187 17195 This report provided the mechanistic basis for the apparent activation of SIRT1 by resveratrol, when a variety of both native and fluorescently labeled peptides are employed as substrates.
    • (2005) J Biol Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 64
    • 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, E.D. Chao, H.E. Blackwell, D. Moazed, and S.L. Schreiber 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 Using a chemical genetics approach, these authors identified the molecule sirtinol as an inhibitor of ySir2.
    • (2001) J Biol Chem , vol.276 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 65
    • 0035910031 scopus 로고    scopus 로고
    • Identification of a small molecule inhibitor of Sir2p
    • A. Bedalov, T. Gatbonton, W.P. Irvine, D.E. Gottschling, and J.A. Simon Identification of a small molecule inhibitor of Sir2p Proc Natl Acad Sci USA 98 2001 15113 15118 Using a chemical genetics approach, splitomicin was discovered as an inhibitor of sirtuins.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15113-15118
    • Bedalov, A.1    Gatbonton, T.2    Irvine, W.P.3    Gottschling, D.E.4    Simon, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.