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Volumn 29, Issue 12, 2015, Pages 1316-1325

Structural basis for allosteric, substratedependent stimulation of SIRT1 activity by resveratrol

Author keywords

Histone; Protein deacetylase; Resveratrol; Sirtuins; Structure

Indexed keywords

7 AMINO 4 METHYLCOUMARIN; COUMARIN DERIVATIVE; RESVERATROL; SIRTUIN 1; UNCLASSIFIED DRUG; STILBENE DERIVATIVE;

EID: 84933524839     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.265462.115     Document Type: Article
Times cited : (189)

References (54)
  • 3
    • 77953480631 scopus 로고    scopus 로고
    • Biochemical effects of SIRT1 activators
    • Baur JA. 2010. Biochemical effects of SIRT1 activators. Biochim Biophys Acta 1804: 1626-1634.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1626-1634
    • Baur, J.A.1
  • 6
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra MT, Smith BC, Denu JM. 2005. Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 280: 17187-17195.
    • (2005) J Biol Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 9
    • 84892495970 scopus 로고    scopus 로고
    • Structural and functional analysis of human SIRT1
    • Davenport AM, Huber FM, Hoelz A. 2014. Structural and functional analysis of human SIRT1. J Mol Biol 426: 526-541.
    • (2014) J Mol Biol , vol.426 , pp. 526-541
    • Davenport, A.M.1    Huber, F.M.2    Hoelz, A.3
  • 10
  • 13
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye RA. 2000. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273: 793-798.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 16
    • 79958206937 scopus 로고    scopus 로고
    • Franklin H. Epstein lecture: Sirtuins, aging, and medicine
    • Guarente L. 2011. Franklin H. Epstein lecture: sirtuins, aging, and medicine. N Engl J Med 364: 2235-2244.
    • (2011) N Engl J Med , vol.364 , pp. 2235-2244
    • Guarente, L.1
  • 20
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L. 2000. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 24
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim EJ, Kho JH, Kang MR,UmSJ. 2007. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol Cell 28: 277-290.
    • (2007) Mol Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 27
    • 84870506099 scopus 로고    scopus 로고
    • Resveratrol rescues SIRT1-dependent adult stem cell decline and alleviates progeroid features in laminopathy-based progeria
    • Liu B, Ghosh S, Yang X, Zheng H, Liu X,Wang Z, Jin G, Zheng B, Kennedy BK, Suh Y, et al. 2012. Resveratrol rescues SIRT1-dependent adult stem cell decline and alleviates progeroid features in laminopathy-based progeria. Cell Metab 16: 738-750.
    • (2012) Cell Metab , vol.16 , pp. 738-750
    • Liu, B.1    Ghosh, S.2    Yang, X.3    Zheng, H.4    Liu, X.5    Wang, Z.6    Jin, G.7    Zheng, B.8    Kennedy, B.K.9    Suh, Y.10
  • 31
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min J, Landry J, Sternglanz R, Xu RM. 2001. Crystal structure of a SIR2 homolog-NAD complex. Cell 105: 269-279.
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 34
    • 84888306269 scopus 로고    scopus 로고
    • Crystal structures of Sirt3 complexes with 4′-bromo-resveratrol reveal binding sites and inhibition mechanism
    • Nguyen GT, Gertz M, Steegborn C. 2013. Crystal structures of Sirt3 complexes with 4′-bromo-resveratrol reveal binding sites and inhibition mechanism. Chem Biol 20: 1375-1385.
    • (2013) Chem Biol , vol.20 , pp. 1375-1385
    • Nguyen, G.T.1    Gertz, M.2    Steegborn, C.3
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 84856076413 scopus 로고    scopus 로고
    • SIRT1 contains N-and C-terminal regions that potentiate deacetylase activity
    • Pan M, Yuan H, Brent M, Ding EC, Marmorstein R. 2012. SIRT1 contains N-and C-terminal regions that potentiate deacetylase activity. J Biol Chem 287: 2468-2476.
    • (2012) J Biol Chem , vol.287 , pp. 2468-2476
    • Pan, M.1    Yuan, H.2    Brent, M.3    Ding, E.C.4    Marmorstein, R.5
  • 40
    • 77953289094 scopus 로고    scopus 로고
    • Structural basis for sirtuin function: What we know and what we don't
    • Sanders BD, Jackson B, Marmorstein R. 2010. Structural basis for sirtuin function: what we know and what we don't. Biochim Biophys Acta 1804: 1604-1616.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1604-1616
    • Sanders, B.D.1    Jackson, B.2    Marmorstein, R.3
  • 41
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: The mechanism of NAD+-dependent deacetylation reactions
    • Sauve AA, Celic I, Avalos J, Deng H, Boeke JD, Schramm VL. 2001. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 40: 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
  • 42
    • 13944258164 scopus 로고    scopus 로고
    • Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition
    • Sauve AA, Moir RD, Schramm VL,Willis IM. 2005. Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition. Mol Cell 17: 595-601.
    • (2005) Mol Cell , vol.17 , pp. 595-601
    • Sauve, A.A.1    Moir, R.D.2    Schramm, V.L.3    Willis, I.M.4
  • 45
    • 84891848670 scopus 로고    scopus 로고
    • Small-molecule allosteric activators of sirtuins
    • Sinclair DA, Guarente L. 2014. Small-molecule allosteric activators of sirtuins. Annu Rev Pharmacol Toxicol 54: 363-380.
    • (2014) Annu Rev Pharmacol Toxicol , vol.54 , pp. 363-380
    • Sinclair, D.A.1    Guarente, L.2
  • 47
    • 69249206539 scopus 로고    scopus 로고
    • A continuous microplate assay for sirtuins and nicotinamide-producing enzymes
    • Smith BC, Hallows WC, Denu JM. 2009. A continuous microplate assay for sirtuins and nicotinamide-producing enzymes. Anal Biochem 394: 101-109.
    • (2009) Anal Biochem , vol.394 , pp. 101-109
    • Smith, B.C.1    Hallows, W.C.2    Denu, J.M.3
  • 48
    • 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, Denu JM. 2000. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci 97: 14178-14182.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 49
    • 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
    • Tanny JC, Moazed D. 2001. 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 98: 415-420.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 50
    • 3543038804 scopus 로고    scopus 로고
    • Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions
    • Tanny JC, Kirkpatrick DS, Gerber SA, Gygi SP, Moazed D. 2004. Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions. Mol Cell Biol 24: 6931-6946.
    • (2004) Mol Cell Biol , vol.24 , pp. 6931-6946
    • Tanny, J.C.1    Kirkpatrick, D.S.2    Gerber, S.A.3    Gygi, S.P.4    Moazed, D.5
  • 51
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D. 2004. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell 16: 93-105.
    • (2004) Mol Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 53
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-Oacetyl ADP ribose and histone peptide
    • Zhao K, Chai X, Marmorstein R. 2003. Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-Oacetyl ADP ribose and histone peptide. Structure 11: 1403-1411.
    • (2003) Structure , vol.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.