메뉴 건너뛰기




Volumn 27, Issue 5, 2013, Pages 345-352

Targeting Sirtuin-1 in Huntington's disease: Rationale and current status

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN DERIVED NEUROTROPHIC FACTOR; BRAIN DERIVED NEUROTROPHIC FACTOR RECEPTOR; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NUCLEAR RESPIRATORY FACTOR 1; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; RESVERATROL; SIRTUIN 1; SOMATOMEDIN C; TRANSCRIPTION FACTOR FKHRL1; UNCOUPLING PROTEIN 1;

EID: 84878573777     PISSN: 11727047     EISSN: 11791934     Source Type: Journal    
DOI: 10.1007/s40263-013-0055-0     Document Type: Article
Times cited : (38)

References (87)
  • 1
    • 0027480960 scopus 로고
    • The Huntington's Disease Collaborative Research Group. A Novel Gene Containing A Trinucleotide Repeat That Is Expanded and Unstable on Huntington's Disease Chromosomes
    • The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell. 1993;72(6):971-83.
    • (1993) Cell. , vol.72 , Issue.6 , pp. 971-983
  • 2
    • 1842477303 scopus 로고    scopus 로고
    • A new model for prediction of the age of onset and penetrance for Huntington's disease based on CAG length
    • 15025718 10.1111/j.1399-0004.2004.00241.x 1:STN:280: DC%2BD2c7msVertg%3D%3D
    • Langbehn DR, Brinkman RR, Falush D, Paulsen JS, Hayden MR. A new model for prediction of the age of onset and penetrance for Huntington's disease based on CAG length. Clin Genet. 2004;65(4):267-77.
    • (2004) Clin Genet , vol.65 , Issue.4 , pp. 267-277
    • Langbehn, D.R.1    Brinkman, R.R.2    Falush, D.3    Paulsen, J.S.4    Hayden, M.R.5
  • 3
    • 78049522766 scopus 로고    scopus 로고
    • Huntington's disease
    • 21036268 10.1016/S0140-6736(10)61989-7 1:STN:280:DC%2BC3cbjsVCltw%3D%3D
    • Hoppitt T, Calvert M, Pall H, Rickards H, Sackley C. Huntington's disease. Lancet. 2010;376(9751):1463-4.
    • (2010) Lancet , vol.376 , Issue.9751 , pp. 1463-1464
    • Hoppitt, T.1    Calvert, M.2    Pall, H.3    Rickards, H.4    Sackley, C.5
  • 4
    • 78650031174 scopus 로고    scopus 로고
    • Huntington's disease: From molecular pathogenesis to clinical treatment
    • 21163446 10.1016/S1474-4422(10)70245-3 1:CAS:528:DC%2BC3cXhsFCru7bM
    • Ross CA, Tabrizi SJ. Huntington's disease: from molecular pathogenesis to clinical treatment. Lancet Neurol. 2011;10(1):83-98.
    • (2011) Lancet Neurol , vol.10 , Issue.1 , pp. 83-98
    • Ross, C.A.1    Tabrizi, S.J.2
  • 5
    • 12144288251 scopus 로고    scopus 로고
    • Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset
    • 14993615 10.1073/pnas.0308679101 1:CAS:528:DC%2BD2cXisFWmsbg%3D
    • Wexler NS, Lorimer J, Porter J, Gomez F, Moskowitz C, Shackell E, et al. Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset. Proc Natl Acad Sci USA. 2004;101(10):3498- 503.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.10 , pp. 3498-3503
    • Wexler, N.S.1    Lorimer, J.2    Porter, J.3    Gomez, F.4    Moskowitz, C.5    Shackell, E.6
  • 6
    • 57649187103 scopus 로고    scopus 로고
    • Mitochondria and Huntington's disease pathogenesis: Insight from genetic and chemical models
    • 19076457 10.1196/annals.1427.018 1:CAS:528:DC%2BD1MXhsVaqu7Y%3D
    • Browne SE. Mitochondria and Huntington's disease pathogenesis: insight from genetic and chemical models. Ann N Y Acad Sci. 2008;1147:358-82.
    • (2008) Ann N y Acad Sci , vol.1147 , pp. 358-382
    • Browne, S.E.1
  • 7
    • 0029875381 scopus 로고    scopus 로고
    • Mitochondrial defect in Huntington's disease caudate nucleus
    • 8602759 10.1002/ana.410390317 1:CAS:528:DyaK28XisFyrsbo%3D
    • Gu M, Gash MT, Mann VM, Javoy-Agid F, Cooper JM, Schapira AH. Mitochondrial defect in Huntington's disease caudate nucleus. Ann Neurol. 1996;39(3):385-9.
    • (1996) Ann Neurol , vol.39 , Issue.3 , pp. 385-389
    • Gu, M.1    Gash, M.T.2    Mann, V.M.3    Javoy-Agid, F.4    Cooper, J.M.5    Schapira, A.H.6
  • 8
    • 0025078573 scopus 로고
    • Mitochondrial function and parental sex effect in Huntington's disease
    • 1975918 10.1016/0140-6736(90)92242-A 1:STN:280:DyaK3czns1yrtQ%3D%3D
    • Mann VM, Cooper JM, Javoy-Agid F, Agid Y, Jenner P, Schapira AH. Mitochondrial function and parental sex effect in Huntington's disease. Lancet. 1990;336(8717):749.
    • (1990) Lancet , vol.336 , Issue.8717 , pp. 749
    • Mann, V.M.1    Cooper, J.M.2    Javoy-Agid, F.3    Agid, Y.4    Jenner, P.5    Schapira, A.H.6
  • 9
    • 84873446708 scopus 로고    scopus 로고
    • Defective mitochondrial disulfide relay system, altered mitochondrial morphology and function in Huntington's disease
    • 23197653 10.1093/hmg/dds503 1:CAS:528:DC%2BC3sXhvV2qtbY%3D
    • Napoli E, Wong S, Hung C, Ross-Inta C, Bomdica P, Giulivi C. Defective mitochondrial disulfide relay system, altered mitochondrial morphology and function in Huntington's disease. Hum Mol Genet. 2013;22(5):989-1004.
    • (2013) Hum Mol Genet , vol.22 , Issue.5 , pp. 989-1004
    • Napoli, E.1    Wong, S.2    Hung, C.3    Ross-Inta, C.4    Bomdica, P.5    Giulivi, C.6
  • 10
    • 44449131447 scopus 로고    scopus 로고
    • Huntington's disease: From pathology and genetics to potential therapies
    • 18466116 10.1042/BJ20071619 1:CAS:528:DC%2BD1cXlvVWmsbw%3D
    • Imarisio S, Carmichael J, Korolchuk V, Chen CW, Saiki S, Rose C, et al. Huntington's disease: from pathology and genetics to potential therapies. Biochem J. 2008;412(2):191-209.
    • (2008) Biochem J. , vol.412 , Issue.2 , pp. 191-209
    • Imarisio, S.1    Carmichael, J.2    Korolchuk, V.3    Chen, C.W.4    Saiki, S.5    Rose, C.6
  • 11
    • 33750437278 scopus 로고    scopus 로고
    • Thermoregulatory and metabolic defects in Huntington's disease transgenic mice implicate PGC-1alpha in Huntington's disease neurodegeneration
    • 17055784 10.1016/j.cmet.2006.10.004 1:CAS:528:DC%2BD28Xht1aksrnP
    • Weydt P, Pineda VV, Torrence AE, Libby RT, Satterfield TF, Lazarowski ER, et al. Thermoregulatory and metabolic defects in Huntington's disease transgenic mice implicate PGC-1alpha in Huntington's disease neurodegeneration. Cell Metab. 2006;4(5):349-62.
    • (2006) Cell Metab , vol.4 , Issue.5 , pp. 349-362
    • Weydt, P.1    Pineda, V.V.2    Torrence, A.E.3    Libby, R.T.4    Satterfield, T.F.5    Lazarowski, E.R.6
  • 12
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • 17018277 10.1016/j.cell.2006.09.015 1:CAS:528:DC%2BD28XhtFSitr%2FP
    • Cui L, Jeong H, Borovecki F, Parkhurst CN, Tanese N, Krainc D. Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell. 2006;127(1):59-69.
    • (2006) Cell , vol.127 , Issue.1 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 13
    • 77954424574 scopus 로고    scopus 로고
    • Mitochondrial matters of the brain: The role in Huntington's disease
    • 20480217 10.1007/s10863-010-9290-y 1:CAS:528:DC%2BC3cXotVWjtLk%3D
    • Turner C, Schapira AH. Mitochondrial matters of the brain: the role in Huntington's disease. J Bioenerg Biomembr. 2010;42(3):193-8.
    • (2010) J Bioenerg Biomembr , vol.42 , Issue.3 , pp. 193-198
    • Turner, C.1    Schapira, A.H.2
  • 14
    • 77954426618 scopus 로고    scopus 로고
    • Mitochondrial bioenergetics and dynamics in Huntington's disease: Tripartite synapses and selective striatal degeneration
    • 20454921 10.1007/s10863-010-9287-6 1:CAS:528:DC%2BC3cXotVWjtLc%3D
    • Oliveira JM. Mitochondrial bioenergetics and dynamics in Huntington's disease: tripartite synapses and selective striatal degeneration. J Bioenerg Biomembr. 2010;42(3):227-34.
    • (2010) J Bioenerg Biomembr , vol.42 , Issue.3 , pp. 227-234
    • Oliveira, J.M.1
  • 15
    • 70349422148 scopus 로고    scopus 로고
    • Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease
    • 19622387 10.1016/j.brainresbull.2009.07.010 1:CAS:528:DC%2BD1MXht1WqtbfN
    • Quintanilla RA, Johnson GV. Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease. Brain Res Bull. 2009;80(4-5):242-7.
    • (2009) Brain Res Bull , vol.80 , Issue.4-5 , pp. 242-247
    • Quintanilla, R.A.1    Johnson, G.V.2
  • 16
    • 38449118776 scopus 로고    scopus 로고
    • Mitochondria and neurodegeneration
    • (discussion 92-6)
    • Beal MF. Mitochondria and neurodegeneration. Novartis Found Symp. 2007;287:183-92 (discussion 92-6).
    • (2007) Novartis Found Symp , vol.287 , pp. 183-192
    • Beal, M.F.1
  • 17
    • 79551518229 scopus 로고    scopus 로고
    • Energy deficit in Huntington disease: Why it matters
    • 21285522 10.1172/JCI45691 1:CAS:528:DC%2BC3MXhsl2rtbc%3D
    • Mochel F, Haller RG. Energy deficit in Huntington disease: why it matters. J Clin Invest. 2011;121(2):493-9.
    • (2011) J Clin Invest , vol.121 , Issue.2 , pp. 493-499
    • Mochel, F.1    Haller, R.G.2
  • 18
    • 84878573949 scopus 로고    scopus 로고
    • Mitochondrial-associated metabolic changes and neurodegeneration in Huntington's disease - from clinical features to the bench Curr Drug Targets
    • Rosenstock TR, Duarte AI. Rego AC. Curr Drug Targets: Mitochondrial-associated metabolic changes and neurodegeneration in Huntington's disease - from clinical features to the bench; 2010.
    • (2010) Rego AC
    • Rosenstock, T.R.1    Duarte, A.I.2
  • 19
    • 33947675275 scopus 로고    scopus 로고
    • Oxidative damage in Huntington's disease pathogenesis
    • 17034350 10.1089/ars.2006.8.2061 1:CAS:528:DC%2BD28XhtVKntbzN
    • Browne SE, Beal MF. Oxidative damage in Huntington's disease pathogenesis. Antioxid Redox Signal. 2006;8(11-12):2061-73.
    • (2006) Antioxid Redox Signal , vol.8 , Issue.11-12 , pp. 2061-2073
    • Browne, S.E.1    Beal, M.F.2
  • 20
    • 37549005157 scopus 로고    scopus 로고
    • Oxidative DNA damage estimated by plasma 8-hydroxydeoxyguanosine (8-OHdG): Influence of 4,4′-methylenebis (2-chloroaniline) exposure and smoking
    • 17951971 10.1539/joh.49.389 1:CAS:528:DC%2BD2sXht1CltrzM
    • Chen HI, Liou SH, Ho SF, Wu KY, Sun CW, Chen MF, et al. Oxidative DNA damage estimated by plasma 8-hydroxydeoxyguanosine (8-OHdG): influence of 4,4′-methylenebis (2-chloroaniline) exposure and smoking. J Occup Health. 2007;49(5):389-98.
    • (2007) J Occup Health , vol.49 , Issue.5 , pp. 389-398
    • Chen, H.I.1    Liou, S.H.2    Ho, S.F.3    Wu, K.Y.4    Sun, C.W.5    Chen, M.F.6
  • 21
    • 48449091060 scopus 로고    scopus 로고
    • Proteomic and oxidative stress analysis in human brain samples of Huntington disease
    • 18588971 10.1016/j.freeradbiomed.2008.05.014 1:CAS:528: DC%2BD1cXpslWrs7s%3D
    • Sorolla MA, Reverter-Branchat G, Tamarit J, Ferrer I, Ros J, Cabiscol E. Proteomic and oxidative stress analysis in human brain samples of Huntington disease. Free Radic Biol Med. 2008;45(5):667-78.
    • (2008) Free Radic Biol Med , vol.45 , Issue.5 , pp. 667-678
    • Sorolla, M.A.1    Reverter-Branchat, G.2    Tamarit, J.3    Ferrer, I.4    Ros, J.5    Cabiscol, E.6
  • 22
    • 0034915234 scopus 로고    scopus 로고
    • Comparative analysis of superoxide dismutase activity between acute pharmacological models and a transgenic mouse model of Huntington's disease
    • 11495354 10.1023/A:1010911417383 1:CAS:528:DC%2BD3MXlslSgtbg%3D
    • Santamaria A, Perez-Severiano F, Rodriguez-Martinez E, Maldonado PD, Pedraza-Chaverri J, Rios C, et al. Comparative analysis of superoxide dismutase activity between acute pharmacological models and a transgenic mouse model of Huntington's disease. Neurochem Res. 2001;26(4):419-24.
    • (2001) Neurochem Res , vol.26 , Issue.4 , pp. 419-424
    • Santamaria, A.1    Perez-Severiano, F.2    Rodriguez-Martinez, E.3    Maldonado, P.D.4    Pedraza-Chaverri, J.5    Rios, C.6
  • 23
    • 26844558334 scopus 로고    scopus 로고
    • Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS
    • 16224023 10.1126/science.1117728 1:CAS:528:DC%2BD2MXhtV2hurvO
    • Nisoli E, Tonello C, Cardile A, Cozzi V, Bracale R, Tedesco L, et al. Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS. Science. 2005;310(5746):314-7.
    • (2005) Science , vol.310 , Issue.5746 , pp. 314-317
    • Nisoli, E.1    Tonello, C.2    Cardile, A.3    Cozzi, V.4    Bracale, R.5    Tedesco, L.6
  • 24
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction
    • 17079682 10.1101/gad.1467506 1:CAS:528:DC%2BD28XhtFynu7bJ
    • Haigis MC, Guarente LP. Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction. Genes Dev. 2006;20(21):2913-21.
    • (2006) Genes Dev , vol.20 , Issue.21 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 25
    • 84859977895 scopus 로고    scopus 로고
    • Sirtuins mediate mammalian metabolic responses to nutrient availability
    • 22249520 10.1038/nrendo.2011.225 1:CAS:528:DC%2BC38XlvFWiu74%3D
    • Chalkiadaki A, Guarente L. Sirtuins mediate mammalian metabolic responses to nutrient availability. Nat Rev Endocrinol. 2012;8(5):287-96.
    • (2012) Nat Rev Endocrinol , vol.8 , Issue.5 , pp. 287-296
    • Chalkiadaki, A.1    Guarente, L.2
  • 26
    • 84882835206 scopus 로고    scopus 로고
    • Dietary restriction and aging in rodents: A current view on its molecular mechanisms
    • 22396859
    • Shimokawa I, Trindade LS. Dietary restriction and aging in rodents: a current view on its molecular mechanisms. Aging Dis. 2010;1(2):89-107.
    • (2010) Aging Dis , vol.1 , Issue.2 , pp. 89-107
    • Shimokawa, I.1    Trindade, L.S.2
  • 27
    • 69849107217 scopus 로고    scopus 로고
    • Caloric restriction, SIRT1 and longevity
    • 19713122 10.1016/j.tem.2009.03.008 1:CAS:528:DC%2BD1MXhtFantbbL
    • Canto C, Auwerx J. Caloric restriction, SIRT1 and longevity. Trends Endocrinol Metab. 2009;20(7):325-31.
    • (2009) Trends Endocrinol Metab , vol.20 , Issue.7 , pp. 325-331
    • Canto, C.1    Auwerx, J.2
  • 28
    • 75949098771 scopus 로고    scopus 로고
    • Could Sirt1-mediated epigenetic effects contribute to the longevity response to dietary restriction and be mimicked by other dietary interventions?
    • 10.1007/s11357-009-9104-5 1:CAS:528:DC%2BC3cXpslCmuw%3D%3D
    • Wakeling LA, Ions LJ, Ford D. Could Sirt1-mediated epigenetic effects contribute to the longevity response to dietary restriction and be mimicked by other dietary interventions? Age (Dordr). 2009;31(4):327-41.
    • (2009) Age (Dordr) , vol.31 , Issue.4 , pp. 327-341
    • Wakeling, L.A.1    Ions, L.J.2    Ford, D.3
  • 29
    • 42749086593 scopus 로고    scopus 로고
    • OutFOXOing disease and disability: The therapeutic potential of targeting FoxO proteins
    • 18403263 10.1016/j.molmed.2008.03.002 1:CAS:528:DC%2BD1cXls12qsrY%3D
    • Maiese K, Chong ZZ, Shang YC. OutFOXOing disease and disability: the therapeutic potential of targeting FoxO proteins. Trends Mol Med. 2008;14(5):219-27.
    • (2008) Trends Mol Med , vol.14 , Issue.5 , pp. 219-227
    • Maiese, K.1    Chong, Z.Z.2    Shang, Y.C.3
  • 30
    • 46349096040 scopus 로고    scopus 로고
    • Sirt1 protects against oxidative stress-induced renal tubular cell apoptosis by the bidirectional regulation of catalase expression
    • 18485895 10.1016/j.bbrc.2008.04.176 1:CAS:528:DC%2BD1cXmvFeku70%3D
    • Hasegawa K, Wakino S, Yoshioka K, Tatematsu S, Hara Y, Minakuchi H, et al. Sirt1 protects against oxidative stress-induced renal tubular cell apoptosis by the bidirectional regulation of catalase expression. Biochem Biophys Res Commun. 2008;372(1):51-6.
    • (2008) Biochem Biophys Res Commun , vol.372 , Issue.1 , pp. 51-56
    • Hasegawa, K.1    Wakino, S.2    Yoshioka, K.3    Tatematsu, S.4    Hara, Y.5    Minakuchi, H.6
  • 31
    • 49949091740 scopus 로고    scopus 로고
    • Enhanced tolerance against early and late apoptotic oxidative stress in mammalian neurons through nicotinamidase and sirtuin mediated pathways
    • 18691073 10.2174/156720208785425666 1:CAS:528:DC%2BD1cXhtV2htLzP
    • Chong ZZ, Maiese K. Enhanced tolerance against early and late apoptotic oxidative stress in mammalian neurons through nicotinamidase and sirtuin mediated pathways. Curr Neurovasc Res. 2008;5(3):159-70.
    • (2008) Curr Neurovasc Res , vol.5 , Issue.3 , pp. 159-170
    • Chong, Z.Z.1    Maiese, K.2
  • 32
    • 77950901103 scopus 로고    scopus 로고
    • Induction of manganese superoxide dismutase by nuclear translocation and activation of SIRT1 promotes cell survival in chronic heart failure
    • 20089851 10.1074/jbc.M109.090266 1:CAS:528:DC%2BC3cXisl2jt74%3D
    • Tanno M, Kuno A, Yano T, Miura T, Hisahara S, Ishikawa S, et al. Induction of manganese superoxide dismutase by nuclear translocation and activation of SIRT1 promotes cell survival in chronic heart failure. J Biol Chem. 2010;285(11):8375-82.
    • (2010) J Biol Chem , vol.285 , Issue.11 , pp. 8375-8382
    • Tanno, M.1    Kuno, A.2    Yano, T.3    Miura, T.4    Hisahara, S.5    Ishikawa, S.6
  • 33
    • 84863923855 scopus 로고    scopus 로고
    • PGC-1alpha rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function
    • 142ra97
    • Tsunemi T, Ashe TD, Morrison BE, Soriano KR, Au J, Roque RA, et al. PGC-1alpha rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function. Sci Transl Med. 2012;4(142):142ra97.
    • (2012) Sci Transl Med. , vol.4 , pp. 142
    • Tsunemi, T.1    Ashe, T.D.2    Morrison, B.E.3    Soriano, K.R.4    Au, J.5    Roque, R.A.6
  • 34
    • 84870918556 scopus 로고    scopus 로고
    • PPARGC1A/PGC-1alpha, TFEB and enhanced proteostasis in Huntington disease: Defining regulatory linkages between energy production and protein-organelle quality control
    • 22932698 10.4161/auto.21862
    • La Spada AR. PPARGC1A/PGC-1alpha, TFEB and enhanced proteostasis in Huntington disease: defining regulatory linkages between energy production and protein-organelle quality control. Autophagy. 2012;8(12):1845-7.
    • (2012) Autophagy , vol.8 , Issue.12 , pp. 1845-1847
    • La Spada, A.R.1
  • 35
    • 54049158932 scopus 로고    scopus 로고
    • Brain SIRT1: Anatomical distribution and regulation by energy availability
    • 18829956 10.1523/JNEUROSCI.3257-08.2008 1:CAS:528:DC%2BD1cXht1ChsLjF
    • Ramadori G, Lee CE, Bookout AL, Lee S, Williams KW, Anderson J, et al. Brain SIRT1: anatomical distribution and regulation by energy availability. J Neurosci. 2008;28(40):9989-96.
    • (2008) J Neurosci , vol.28 , Issue.40 , pp. 9989-9996
    • Ramadori, G.1    Lee, C.E.2    Bookout, A.L.3    Lee, S.4    Williams, K.W.5    Anderson, J.6
  • 36
    • 0023340731 scopus 로고
    • Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae
    • 3297920 1:STN:280:DyaL2s3kvVSnsw%3D%3D
    • Rine J, Herskowitz I. Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae. Genetics. 1987;116(1):9-22.
    • (1987) Genetics , vol.116 , Issue.1 , pp. 9-22
    • Rine, J.1    Herskowitz, I.2
  • 37
    • 84867418514 scopus 로고    scopus 로고
    • Sirtuins, aging, and metabolism
    • 22114328 10.1101/sqb.2011.76.010629 1:CAS:528:DC%2BC38Xht1ChsbjI
    • Guarente L. Sirtuins, aging, and metabolism. Cold Spring Harb Symp Quant Biol. 2011;76:81-90.
    • (2011) Cold Spring Harb Symp Quant Biol , vol.76 , pp. 81-90
    • Guarente, L.1
  • 38
    • 79958206937 scopus 로고    scopus 로고
    • Epstein lecture: Sirtuins, aging, and medicine
    • 21651395 10.1056/NEJMra1100831 1:CAS:528:DC%2BC3MXnsV2ns7o%3D
    • Guarente L, Franklin H. Epstein lecture: sirtuins, aging, and medicine. N Engl J Med. 2011;364(23):2235-44.
    • (2011) N Engl J Med , vol.364 , Issue.23 , pp. 2235-2244
    • Guarente, L.1    Franklin, H.2
  • 39
    • 79952806932 scopus 로고    scopus 로고
    • Sirtuins at a glance
    • 21378304 10.1242/jcs.081067 1:CAS:528:DC%2BC3MXkvVOrtbY%3D
    • Nakagawa T, Guarente L. Sirtuins at a glance. J Cell Sci. 2011;124(Pt 6):833-8.
    • (2011) J Cell Sci , vol.124 , Issue.PART 6 , pp. 833-838
    • Nakagawa, T.1    Guarente, L.2
  • 40
    • 34250365395 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1
    • 17197703 10.1074/jbc.M609554200 1:CAS:528:DC%2BD2sXitVCitLk%3D
    • Tanno M, Sakamoto J, Miura T, Shimamoto K, Horio Y. Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J Biol Chem. 2007;282(9):6823-32.
    • (2007) J Biol Chem , vol.282 , Issue.9 , pp. 6823-6832
    • Tanno, M.1    Sakamoto, J.2    Miura, T.3    Shimamoto, K.4    Horio, Y.5
  • 41
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • 20078221 10.1146/annurev.pathol.4.110807.092250 1:CAS:528: DC%2BC3cXivFekt7c%3D
    • Haigis MC, Sinclair DA. Mammalian sirtuins: biological insights and disease relevance. Annu Rev Pathol. 2010;5:253-95.
    • (2010) Annu Rev Pathol , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 42
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • 15310905 10.1126/science.1098014 1:CAS:528:DC%2BD2cXmsVGmsbc%3D
    • Araki T, Sasaki Y, Milbrandt J. Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science. 2004;305(5686):1010-3.
    • (2004) Science , vol.305 , Issue.5686 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 43
    • 80055085693 scopus 로고    scopus 로고
    • Role of sirtuins and calorie restriction in neuroprotection: Implications in Alzheimer's and Parkinson's diseases
    • 21902666 10.2174/138161211798072526 1:CAS:528:DC%2BC38XjtVGhsQ%3D%3D
    • Srivastava S, Haigis MC. Role of sirtuins and calorie restriction in neuroprotection: implications in Alzheimer's and Parkinson's diseases. Curr Pharm Des. 2011;17(31):3418-33.
    • (2011) Curr Pharm des , vol.17 , Issue.31 , pp. 3418-3433
    • Srivastava, S.1    Haigis, M.C.2
  • 44
    • 77955046461 scopus 로고    scopus 로고
    • SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10
    • 20655472 10.1016/j.cell.2010.06.020 1:CAS:528:DC%2BC3cXpsVahsrw%3D
    • Donmez G, Wang D, Cohen DE, Guarente L. SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10. Cell. 2010;142(2):320-32.
    • (2010) Cell , vol.142 , Issue.2 , pp. 320-332
    • Donmez, G.1    Wang, D.2    Cohen, D.E.3    Guarente, L.4
  • 45
    • 77955670715 scopus 로고    scopus 로고
    • The molecular genetics of sirtuins: Association with human longevity and age-related diseases
    • 21537393 1:CAS:528:DC%2BC3cXptFagsLY%3D
    • Polito L, Kehoe PG, Forloni G, Albani D. The molecular genetics of sirtuins: association with human longevity and age-related diseases. Int J Mol Epidemiol Genet. 2010;1(3):214-25.
    • (2010) Int J Mol Epidemiol Genet , vol.1 , Issue.3 , pp. 214-225
    • Polito, L.1    Kehoe, P.G.2    Forloni, G.3    Albani, D.4
  • 46
    • 77953421120 scopus 로고    scopus 로고
    • The role of Sirt1: At the crossroad between promotion of longevity and protection against Alzheimer's disease neuropathology
    • 19945548 10.1016/j.bbapap.2009.11.015 1:CAS:528:DC%2BC3cXntlaltbc%3D
    • Wang J, Fivecoat H, Ho L, Pan Y, Ling E, Pasinetti GM. The role of Sirt1: at the crossroad between promotion of longevity and protection against Alzheimer's disease neuropathology. Biochim Biophys Acta. 2010;1804(8):1690-4.
    • (2010) Biochim Biophys Acta , vol.1804 , Issue.8 , pp. 1690-1694
    • Wang, J.1    Fivecoat, H.2    Ho, L.3    Pan, Y.4    Ling, E.5    Pasinetti, G.M.6
  • 47
    • 34447308268 scopus 로고    scopus 로고
    • SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis
    • 17581637 10.1038/sj.emboj.7601758 1:CAS:528:DC%2BD2sXnsFejt7k%3D
    • Kim D, Nguyen MD, Dobbin MM, Fischer A, Sananbenesi F, Rodgers JT, et al. SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. EMBO J. 2007;26(13):3169-79.
    • (2007) EMBO J , vol.26 , Issue.13 , pp. 3169-3179
    • Kim, D.1    Nguyen, M.D.2    Dobbin, M.M.3    Fischer, A.4    Sananbenesi, F.5    Rodgers, J.T.6
  • 48
    • 84855929223 scopus 로고    scopus 로고
    • SIRT1 protects against alpha-synuclein aggregation by activating molecular chaperones
    • 22219275 10.1523/JNEUROSCI.3442-11.2012 1:CAS:528:DC%2BC38XovV2nuw%3D%3D
    • Donmez G, Arun A, Chung CY, McLean PJ, Lindquist S, Guarente L. SIRT1 protects against alpha-synuclein aggregation by activating molecular chaperones. J Neurosci. 2012;32(1):124-32.
    • (2012) J Neurosci , vol.32 , Issue.1 , pp. 124-132
    • Donmez, G.1    Arun, A.2    Chung, C.Y.3    McLean, P.J.4    Lindquist, S.5    Guarente, L.6
  • 49
    • 84855544817 scopus 로고    scopus 로고
    • Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets
    • 10.1038/nm.2558 1:CAS:528:DC%2BC3MXhs1eitr%2FL
    • Jiang M, Wang J, Fu J, Du L, Jeong H, West T, et al. Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets. Nat Med. 2012;18(1):153-8.
    • (2012) Nat Med , vol.18 , Issue.1 , pp. 153-158
    • Jiang, M.1    Wang, J.2    Fu, J.3    Du, L.4    Jeong, H.5    West, T.6
  • 50
    • 84855563516 scopus 로고    scopus 로고
    • Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway
    • 10.1038/nm.2559 1:CAS:528:DC%2BC3MXhs1eisb3M
    • Jeong H, Cohen DE, Cui L, Supinski A, Savas JN, Mazzulli JR, et al. Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway. Nat Med. 2012;18(1):159-65.
    • (2012) Nat Med , vol.18 , Issue.1 , pp. 159-165
    • Jeong, H.1    Cohen, D.E.2    Cui, L.3    Supinski, A.4    Savas, J.N.5    Mazzulli, J.R.6
  • 51
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • 15793589 10.1038/ng1534 1:CAS:528:DC%2BD2MXislCmu7w%3D
    • Parker JA, Arango M, Abderrahmane S, Lambert E, Tourette C, Catoire H, et al. Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nat Genet. 2005;37(4):349-50.
    • (2005) Nat Genet , vol.37 , Issue.4 , pp. 349-350
    • Parker, J.A.1    Arango, M.2    Abderrahmane, S.3    Lambert, E.4    Tourette, C.5    Catoire, H.6
  • 52
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • 18762557 10.1093/hmg/ddn273 1:CAS:528:DC%2BD1cXhtlGisrfF
    • Pallos J, Bodai L, Lukacsovich T, Purcell JM, Steffan JS, Thompson LM, et al. Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum Mol Genet. 2008;17(23):3767-75.
    • (2008) Hum Mol Genet , vol.17 , Issue.23 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3    Purcell, J.M.4    Steffan, J.S.5    Thompson, L.M.6
  • 53
    • 80053168829 scopus 로고    scopus 로고
    • Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila
    • 21938067 10.1038/nature10296 1:CAS:528:DC%2BC3MXht1WltLfK
    • Burnett C, Valentini S, Cabreiro F, Goss M, Somogyvari M, Piper MD, et al. Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila. Nature. 2011;477(7365):482-5.
    • (2011) Nature , vol.477 , Issue.7365 , pp. 482-485
    • Burnett, C.1    Valentini, S.2    Cabreiro, F.3    Goss, M.4    Somogyvari, M.5    Piper, M.D.6
  • 54
    • 84855544817 scopus 로고    scopus 로고
    • Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets
    • 10.1038/nm.2558 1:CAS:528:DC%2BC3MXhs1eitr%2FL
    • Jiang M, Wang J, Fu J, Du L, Jeong H, West T, et al. Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets. Nat Med. 2012;18(1):153-8.
    • (2012) Nat Med , vol.18 , Issue.1 , pp. 153-158
    • Jiang, M.1    Wang, J.2    Fu, J.3    Du, L.4    Jeong, H.5    West, T.6
  • 55
    • 84855563516 scopus 로고    scopus 로고
    • Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway
    • 22179316 10.1038/nm.2559
    • Jeong H, Cohen DE, Cui L, Supinski A, Savas JN, Mazzulli JR, et al. Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway. Nat Med. 2011;18(1):159-65.
    • (2011) Nat Med , vol.18 , Issue.1 , pp. 159-165
    • Jeong, H.1    Cohen, D.E.2    Cui, L.3    Supinski, A.4    Savas, J.N.5    Mazzulli, J.R.6
  • 56
    • 20444456571 scopus 로고    scopus 로고
    • Progressive loss of BDNF in a mouse model of Huntington's disease and rescue by BDNF delivery
    • 15967378 10.1016/j.phrs.2005.01.001 1:CAS:528:DC%2BD2MXlsFCksro%3D
    • Zuccato C, Liber D, Ramos C, Tarditi A, Rigamonti D, Tartari M, et al. Progressive loss of BDNF in a mouse model of Huntington's disease and rescue by BDNF delivery. Pharmacol Res. 2005;52(2):133-9.
    • (2005) Pharmacol Res , vol.52 , Issue.2 , pp. 133-139
    • Zuccato, C.1    Liber, D.2    Ramos, C.3    Tarditi, A.4    Rigamonti, D.5    Tartari, M.6
  • 57
    • 0035919701 scopus 로고    scopus 로고
    • Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease
    • 11408619 10.1126/science.1059581 1:CAS:528:DC%2BD3MXlsFGjtr0%3D
    • Zuccato C, Ciammola A, Rigamonti D, Leavitt BR, Goffredo D, Conti L, et al. Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease. Science. 2001;293(5529):493-8.
    • (2001) Science , vol.293 , Issue.5529 , pp. 493-498
    • Zuccato, C.1    Ciammola, A.2    Rigamonti, D.3    Leavitt, B.R.4    Goffredo, D.5    Conti, L.6
  • 58
    • 34047130812 scopus 로고    scopus 로고
    • Role of brain-derived neurotrophic factor in Huntington's disease
    • 17379385 10.1016/j.pneurobio.2007.01.003 1:CAS:528:DC%2BD2sXjvFGqtL0%3D
    • Zuccato C, Cattaneo E. Role of brain-derived neurotrophic factor in Huntington's disease. Prog Neurobiol. 2007;81(5-6):294-330.
    • (2007) Prog Neurobiol , vol.81 , Issue.5-6 , pp. 294-330
    • Zuccato, C.1    Cattaneo, E.2
  • 59
    • 78049525220 scopus 로고    scopus 로고
    • BDNF overexpression in the forebrain rescues Huntington's disease phenotypes in YAC128 mice
    • 21048129 10.1523/JNEUROSCI.1637-10.2010 1:CAS:528:DC%2BC3cXhsVGqtbvK
    • Xie Y, Hayden MR, Xu B. BDNF overexpression in the forebrain rescues Huntington's disease phenotypes in YAC128 mice. J Neurosci. 2010;30(44):14708- 18.
    • (2010) J Neurosci , vol.30 , Issue.44 , pp. 14708-14718
    • Xie, Y.1    Hayden, M.R.2    Xu, B.3
  • 60
    • 80053613635 scopus 로고    scopus 로고
    • Conditional BDNF release under pathological conditions improves Huntington's disease pathology by delaying neuronal dysfunction
    • 21985529 10.1186/1750-1326-6-71 1:CAS:528:DC%2BC3MXhs1Oht7bL
    • Giralt A, Carreton O, Lao-Peregrin C, Martin ED, Alberch J. Conditional BDNF release under pathological conditions improves Huntington's disease pathology by delaying neuronal dysfunction. Mol Neurodegener. 2011;6(1):71.
    • (2011) Mol Neurodegener , vol.6 , Issue.1 , pp. 71
    • Giralt, A.1    Carreton, O.2    Lao-Peregrin, C.3    Martin, E.D.4    Alberch, J.5
  • 61
    • 0037418339 scopus 로고    scopus 로고
    • Dietary restriction normalizes glucose metabolism and BDNF levels, slows disease progression, and increases survival in huntingtin mutant mice
    • 12589027 10.1073/pnas.0536856100 1:CAS:528:DC%2BD3sXitVaiur0%3D
    • Duan W, Guo Z, Jiang H, Ware M, Li XJ, Mattson MP. Dietary restriction normalizes glucose metabolism and BDNF levels, slows disease progression, and increases survival in huntingtin mutant mice. Proc Natl Acad Sci USA. 2003;100(5):2911-6.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.5 , pp. 2911-2916
    • Duan, W.1    Guo, Z.2    Jiang, H.3    Ware, M.4    Li, X.J.5    Mattson, M.P.6
  • 62
    • 43649106471 scopus 로고    scopus 로고
    • Sertraline slows disease progression and increases neurogenesis in N171-82Q mouse model of Huntington's disease
    • 18403212 10.1016/j.nbd.2008.01.015 1:CAS:528:DC%2BD1cXmtlSiu7w%3D
    • Duan W, Peng Q, Masuda N, Ford E, Tryggestad E, Ladenheim B, et al. Sertraline slows disease progression and increases neurogenesis in N171-82Q mouse model of Huntington's disease. Neurobiol Dis. 2008;30(3):312-22.
    • (2008) Neurobiol Dis , vol.30 , Issue.3 , pp. 312-322
    • Duan, W.1    Peng, Q.2    Masuda, N.3    Ford, E.4    Tryggestad, E.5    Ladenheim, B.6
  • 63
    • 39249084415 scopus 로고    scopus 로고
    • The antidepressant sertraline improves the phenotype, promotes neurogenesis and increases BDNF levels in the R6/2 Huntington's disease mouse model
    • 18096160 10.1016/j.expneurol.2007.10.015 1:CAS:528:DC%2BD1cXisVWis7k%3D
    • Peng Q, Masuda N, Jiang M, Li Q, Zhao M, Ross CA, et al. The antidepressant sertraline improves the phenotype, promotes neurogenesis and increases BDNF levels in the R6/2 Huntington's disease mouse model. Exp Neurol. 2008;210(1):154-63.
    • (2008) Exp Neurol , vol.210 , Issue.1 , pp. 154-163
    • Peng, Q.1    Masuda, N.2    Jiang, M.3    Li, Q.4    Zhao, M.5    Ross, C.A.6
  • 64
    • 0037562083 scopus 로고    scopus 로고
    • Reversal of behavioral and metabolic abnormalities, and insulin resistance syndrome, by dietary restriction in mice deficient in brain-derived neurotrophic factor
    • 12746306 10.1210/en.2002-0113 1:CAS:528:DC%2BD3sXktFehu7w%3D
    • Duan W, Guo Z, Jiang H, Ware M, Mattson MP. Reversal of behavioral and metabolic abnormalities, and insulin resistance syndrome, by dietary restriction in mice deficient in brain-derived neurotrophic factor. Endocrinology. 2003;144(6):2446-53.
    • (2003) Endocrinology , vol.144 , Issue.6 , pp. 2446-2453
    • Duan, W.1    Guo, Z.2    Jiang, H.3    Ware, M.4    Mattson, M.P.5
  • 65
    • 52449086907 scopus 로고    scopus 로고
    • The insulin paradox: Aging, proteotoxicity and neurodegeneration
    • 18769445 10.1038/nrn2474 1:CAS:528:DC%2BD1cXhtFeit7fM
    • Cohen E, Dillin A. The insulin paradox: aging, proteotoxicity and neurodegeneration. Nat Rev Neurosci. 2008;9(10):759-67.
    • (2008) Nat Rev Neurosci , vol.9 , Issue.10 , pp. 759-767
    • Cohen, E.1    Dillin, A.2
  • 66
    • 42649140573 scopus 로고    scopus 로고
    • The insulin-regulated CREB coactivator TORC promotes stress resistance in Drosophila
    • 18460334 10.1016/j.cmet.2008.02.010 1:CAS:528:DC%2BD1cXmtFeiuro%3D
    • Wang B, Goode J, Best J, Meltzer J, Schilman PE, Chen J, et al. The insulin-regulated CREB coactivator TORC promotes stress resistance in Drosophila. Cell Metab. 2008;7(5):434-44.
    • (2008) Cell Metab , vol.7 , Issue.5 , pp. 434-444
    • Wang, B.1    Goode, J.2    Best, J.3    Meltzer, J.4    Schilman, P.E.5    Chen, J.6
  • 67
    • 0035883151 scopus 로고    scopus 로고
    • NF-kappaB signaling pathways in mammalian and insect innate immunity
    • 11562344 10.1101/gad.909001 1:CAS:528:DC%2BD3MXnsV2hs7o%3D
    • Silverman N, Maniatis T. NF-kappaB signaling pathways in mammalian and insect innate immunity. Genes Dev. 2001;15(18):2321-42.
    • (2001) Genes Dev , vol.15 , Issue.18 , pp. 2321-2342
    • Silverman, N.1    Maniatis, T.2
  • 68
    • 77955660387 scopus 로고    scopus 로고
    • Resveratrol protects against peripheral deficits in a mouse model of Huntington's disease
    • 20561979 10.1016/j.expneurol.2010.05.006 1:CAS:528:DC%2BC3cXhtVersrzE
    • Ho DJ, Calingasan NY, Wille E, Dumont M, Beal MF. Resveratrol protects against peripheral deficits in a mouse model of Huntington's disease. Exp Neurol. 2010;225(1):74-84.
    • (2010) Exp Neurol , vol.225 , Issue.1 , pp. 74-84
    • Ho, D.J.1    Calingasan, N.Y.2    Wille, E.3    Dumont, M.4    Beal, M.F.5
  • 69
    • 33751072349 scopus 로고    scopus 로고
    • Resveratrol improves health and survival of mice on a high-calorie diet
    • 17086191 10.1038/nature05354 1:CAS:528:DC%2BD28Xht1Sgtb3I
    • Baur JA, Pearson KJ, Price NL, Jamieson HA, Lerin C, Kalra A, et al. Resveratrol improves health and survival of mice on a high-calorie diet. Nature. 2006;444(7117):337-42.
    • (2006) Nature , vol.444 , Issue.7117 , pp. 337-342
    • Baur, J.A.1    Pearson, K.J.2    Price, N.L.3    Jamieson, H.A.4    Lerin, C.5    Kalra, A.6
  • 70
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: The in vivo evidence
    • 16732220 10.1038/nrd2060 1:CAS:528:DC%2BD28XlsV2jur8%3D
    • Baur JA, Sinclair DA. Therapeutic potential of resveratrol: the in vivo evidence. Nat Rev Drug Discov. 2006;5(6):493-506.
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.6 , pp. 493-506
    • Baur, J.A.1    Sinclair, D.A.2
  • 71
    • 33748310632 scopus 로고    scopus 로고
    • Effect of resveratrol on 3-nitropropionic acid-induced biochemical and behavioural changes: Possible neuroprotective mechanisms
    • 16940769 10.1097/00008877-200609000-00014 1:CAS:528:DC%2BD28XoslOnt7k%3D
    • Kumar P, Padi SS, Naidu PS, Kumar A. Effect of resveratrol on 3-nitropropionic acid-induced biochemical and behavioural changes: possible neuroprotective mechanisms. Behav Pharmacol. 2006;17(5-6):485-92.
    • (2006) Behav Pharmacol , vol.17 , Issue.5-6 , pp. 485-492
    • Kumar, P.1    Padi, S.S.2    Naidu, P.S.3    Kumar, A.4
  • 72
    • 78650525484 scopus 로고    scopus 로고
    • ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington's disease
    • 20952447 10.1093/hmg/ddq460 1:CAS:528:DC%2BC3cXhs1WgtbrN
    • Maher P, Dargusch R, Bodai L, Gerard PE, Purcell JM, Marsh JL. ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington's disease. Hum Mol Genet. 2011;20(2):261-70.
    • (2011) Hum Mol Genet , vol.20 , Issue.2 , pp. 261-270
    • Maher, P.1    Dargusch, R.2    Bodai, L.3    Gerard, P.E.4    Purcell, J.M.5    Marsh, J.L.6
  • 73
    • 84855334376 scopus 로고    scopus 로고
    • Resveratrol in human cancer chemoprevention-choosing the 'right' dose
    • 22218912 10.1002/mnfr.201100400 1:CAS:528:DC%2BC38XotFOk
    • Scott E, Steward WP, Gescher AJ, Brown K. Resveratrol in human cancer chemoprevention-choosing the 'right' dose. Mol Nutr Food Res. 2012;56(1):7-13.
    • (2012) Mol Nutr Food Res , vol.56 , Issue.1 , pp. 7-13
    • Scott, E.1    Steward, W.P.2    Gescher, A.J.3    Brown, K.4
  • 74
    • 84859551307 scopus 로고    scopus 로고
    • Dose-dependent effect of resveratrol on bladder cancer cells: Chemoprevention and oxidative stress
    • 22386766 10.1016/j.maturitas.2012.02.004 1:CAS:528:DC%2BC38XltlamsL0%3D
    • Stocco B, Toledo K, Salvador M, Paulo M, Koyama N, Torqueti Toloi MR. Dose-dependent effect of resveratrol on bladder cancer cells: chemoprevention and oxidative stress. Maturitas. 2012;72(1):72-8.
    • (2012) Maturitas , vol.72 , Issue.1 , pp. 72-78
    • Stocco, B.1    Toledo, K.2    Salvador, M.3    Paulo, M.4    Koyama, N.5    Torqueti Toloi, M.R.6
  • 75
    • 84860477354 scopus 로고    scopus 로고
    • SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function
    • 22560220 10.1016/j.cmet.2012.04.003 1:CAS:528:DC%2BC38XmsVCit7w%3D
    • Price NL, Gomes AP, Ling AJ, Duarte FV, Martin-Montalvo A, North BJ, et al. SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function. Cell Metab. 2012;15(5):675-90.
    • (2012) Cell Metab , vol.15 , Issue.5 , pp. 675-690
    • Price, N.L.1    Gomes, A.P.2    Ling, A.J.3    Duarte, F.V.4    Martin-Montalvo, A.5    North, B.J.6
  • 76
    • 84855689149 scopus 로고    scopus 로고
    • Repeated resveratrol administration confers lasting protection against neuronal damage but induces dose-related alterations of behavioral impairments after global ischemia
    • 22146698 10.1097/FBP.0b013e32834eafa3 1:CAS:528:DC%2BC38Xmt1aquw%3D%3D
    • Girbovan C, Morin L, Plamondon H. Repeated resveratrol administration confers lasting protection against neuronal damage but induces dose-related alterations of behavioral impairments after global ischemia. Behav Pharmacol. 2012;23(1):1-13.
    • (2012) Behav Pharmacol , vol.23 , Issue.1 , pp. 1-13
    • Girbovan, C.1    Morin, L.2    Plamondon, H.3
  • 77
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • 18046409 10.1038/nature06261 1:CAS:528:DC%2BD2sXhtlKmtbrM
    • Milne JC, Lambert PD, Schenk S, Carney DP, Smith JJ, Gagne DJ, et al. Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature. 2007;450(7170):712-6.
    • (2007) Nature , vol.450 , Issue.7170 , pp. 712-716
    • Milne, J.C.1    Lambert, P.D.2    Schenk, S.3    Carney, D.P.4    Smith, J.J.5    Gagne, D.J.6
  • 78
    • 77950246109 scopus 로고    scopus 로고
    • SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
    • 20061378 10.1074/jbc.M109.088682 1:CAS:528:DC%2BC3cXisl2jtr0%3D
    • Pacholec M, Bleasdale JE, Chrunyk B, Cunningham D, Flynn D, Garofalo RS, et al. SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1. J Biol Chem. 2010;285(11):8340-51.
    • (2010) J Biol Chem , vol.285 , Issue.11 , pp. 8340-8351
    • Pacholec, M.1    Bleasdale, J.E.2    Chrunyk, B.3    Cunningham, D.4    Flynn, D.5    Garofalo, R.S.6
  • 79
    • 78349291479 scopus 로고    scopus 로고
    • Nicotinamide improves motor deficits and upregulates PGC-1alpha and BDNF gene expression in a mouse model of Huntington's disease
    • 20736066 10.1016/j.nbd.2010.08.017 1:CAS:528:DC%2BC3cXhsVWqsLbK
    • Hathorn T, Snyder-Keller A, Messer A. Nicotinamide improves motor deficits and upregulates PGC-1alpha and BDNF gene expression in a mouse model of Huntington's disease. Neurobiol Dis. 2011;41(1):43-50.
    • (2011) Neurobiol Dis , vol.41 , Issue.1 , pp. 43-50
    • Hathorn, T.1    Snyder-Keller, A.2    Messer, A.3
  • 80
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • 18827828 10.1038/nrd2681 1:CAS:528:DC%2BD1cXhtFOlu7rK
    • Kazantsev AG, Thompson LM. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat Rev Drug Discov. 2008;7(10):854-68.
    • (2008) Nat Rev Drug Discov , vol.7 , Issue.10 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 81
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • 11483616 10.1074/jbc.M106779200 1:CAS:528:DC%2BD3MXnvVentbk%3D
    • Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL. Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J Biol Chem. 2001;276(42):38837-43.
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 82
    • 28144438533 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of sirtinol analogues as class III histone/protein deacetylase (Sirtuin) inhibitors
    • 16302818 10.1021/jm050100l 1:CAS:528:DC%2BD2MXhtFKgsLbM
    • Mai A, Massa S, Lavu S, Pezzi R, Simeoni S, Ragno R, et al. Design, synthesis, and biological evaluation of sirtinol analogues as class III histone/protein deacetylase (Sirtuin) inhibitors. J Med Chem. 2005;48(24):7789-95.
    • (2005) J Med Chem , vol.48 , Issue.24 , pp. 7789-7795
    • Mai, A.1    Massa, S.2    Lavu, S.3    Pezzi, R.4    Simeoni, S.5    Ragno, R.6
  • 83
    • 29144501185 scopus 로고    scopus 로고
    • Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1
    • 16335928 10.1021/jm050522v 1:CAS:528:DC%2BD2MXhtFyqsb3N
    • Napper AD, Hixon J, McDonagh T, Keavey K, Pons JF, Barker J, et al. Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1. J Med Chem. 2005;48(25):8045-54.
    • (2005) J Med Chem , vol.48 , Issue.25 , pp. 8045-8054
    • Napper, A.D.1    Hixon, J.2    McDonagh, T.3    Keavey, K.4    Pons, J.F.5    Barker, J.6
  • 84
    • 35548936745 scopus 로고    scopus 로고
    • Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins)
    • 17628866 10.1002/cmdc.200700003 1:CAS:528:DC%2BD2sXhtF2qtb3N
    • Trapp J, Meier R, Hongwiset D, Kassack MU, Sippl W, Jung M. Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins). ChemMedChem. 2007;2(10):1419-31.
    • (2007) ChemMedChem , vol.2 , Issue.10 , pp. 1419-1431
    • Trapp, J.1    Meier, R.2    Hongwiset, D.3    Kassack, M.U.4    Sippl, W.5    Jung, M.6
  • 85
    • 84871706585 scopus 로고    scopus 로고
    • The sirtuin 2 inhibitor AK-7 is neuroprotective in Huntington's disease mouse models
    • 23200855 10.1016/j.celrep.2012.11.001 1:CAS:528:DC%2BC3sXlt1yjsw%3D%3D
    • Chopra V, Quinti L, Kim J, Vollor L, Narayanan KL, Edgerly C, et al. The sirtuin 2 inhibitor AK-7 is neuroprotective in Huntington's disease mouse models. Cell Rep. 2012;2(6):1492-7.
    • (2012) Cell Rep , vol.2 , Issue.6 , pp. 1492-1497
    • Chopra, V.1    Quinti, L.2    Kim, J.3    Vollor, L.4    Narayanan, K.L.5    Edgerly, C.6
  • 86
    • 80054123174 scopus 로고    scopus 로고
    • Protective effects and mechanisms of sirtuins in the nervous system
    • 21930182 10.1016/j.pneurobio.2011.09.001 1:CAS:528:DC%2BC3MXhsVSkt7rE
    • Zhang F, Wang S, Gan L, Vosler PS, Gao Y, Zigmond MJ, et al. Protective effects and mechanisms of sirtuins in the nervous system. Prog Neurobiol. 2011;95(3):373-95.
    • (2011) Prog Neurobiol , vol.95 , Issue.3 , pp. 373-395
    • Zhang, F.1    Wang, S.2    Gan, L.3    Vosler, P.S.4    Gao, Y.5    Zigmond, M.J.6
  • 87
    • 84874709843 scopus 로고    scopus 로고
    • SIRT1 and SIRT2: Emerging targets in neurodegeneration
    • Donmez G, Outeiro TF. SIRT1 and SIRT2: emerging targets in neurodegeneration. EMBO Mol Med. 2013;5(3):344-52.
    • (2013) EMBO Mol Med. , vol.5 , Issue.3 , pp. 344-352
    • Donmez, G.1    Outeiro, T.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.