메뉴 건너뛰기




Volumn 19, Issue 32, 2013, Pages 5663-5677

Insulin resistance, oxidative stress and cardiovascular complications: Role of sirtuins

Author keywords

Acetylation; Cardiovascular complications; Diabetes; Insulin resistance; Mitochondria; Oxidative stress; SIRT; Sirtuins

Indexed keywords

HISTONE; NONHISTONE PROTEIN; SIRTUIN; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; SIRTUIN 6; SIRTUIN 7;

EID: 84884230262     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/13816128113199990372     Document Type: Review
Times cited : (34)

References (222)
  • 1
    • 82955247909 scopus 로고    scopus 로고
    • IDF Diabetes Atlas: Global estimates of the prevalence of diabetes for 2011 and 2030
    • David RW, Guariguata L, Weil C, Shaw J. IDF Diabetes Atlas: Global estimates of the prevalence of diabetes for 2011 and 2030. Diabetes Res Clin Pract 2011; 94: 311-21.
    • (2011) Diabetes Res Clin Pract , vol.94 , pp. 311-321
    • David, R.W.1    Guariguata, L.2    Weil, C.3    Shaw, J.4
  • 2
    • 0035856980 scopus 로고    scopus 로고
    • Biology of diabetic complications
    • Brownlee M. Biology of diabetic complications. Nature 2001; 414: 813-20.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 3
    • 34249328873 scopus 로고    scopus 로고
    • Biomarkers of susceptibility to type 1 diabetes with special reference to the Indian population
    • Mehra NK, Kumar N, Kaur G, Kanga U, Tandon N. Biomarkers of susceptibility to type 1 diabetes with special reference to the Indian population. Indian J Med Res 2007; 321-44.
    • (2007) Indian J Med Res , pp. 321-344
    • Mehra, N.K.1    Kumar, N.2    Kaur, G.3    Kanga, U.4    Tandon, N.5
  • 4
    • 79551640972 scopus 로고    scopus 로고
    • Preventing type 2 diabetes mellitus: Room for residual risk reduction after lifestyle changes?
    • Athyros VG, Tziomalos K, Karagiannis A, Mikhailidis DP. Preventing type 2 diabetes mellitus: room for residual risk reduction after lifestyle changes? Curr Pharm Des 2010; 16(34): 3939-47.
    • (2010) Curr Pharm Des , vol.16 , Issue.34 , pp. 3939-3947
    • Athyros, V.G.1    Tziomalos, K.2    Karagiannis, A.3    Mikhailidis, D.P.4
  • 5
    • 0037283601 scopus 로고    scopus 로고
    • The relative contributions of insulin resistance and betacell dysfunction to the pathophysiology of type 2 diabetes
    • Kahan SE. The relative contributions of insulin resistance and betacell dysfunction to the pathophysiology of type 2 diabetes. Diabetologia 2003; 46: 3-19.
    • (2003) Diabetologia , vol.46 , pp. 3-19
    • Kahan, S.E.1
  • 6
    • 79953763364 scopus 로고    scopus 로고
    • Signaling of reactive oxygen and nitrogen species in diabetes mellitus
    • Afanas'ev I. Signaling of reactive oxygen and nitrogen species in diabetes mellitus. Oxid Med Cell Longev 2010; 3(6): 361-73.
    • (2010) Oxid Med Cell Longev , vol.3 , Issue.6 , pp. 361-373
    • Afanas'ev, I.1
  • 7
    • 34347352169 scopus 로고    scopus 로고
    • Diabetic cardiomyopathy revisited
    • Boudina S. Abel ED. Diabetic cardiomyopathy revisited. Circulation 2007; 115: 3213-23.
    • (2007) Circulation , vol.115 , pp. 3213-3223
    • Boudina, S.1    Abel, E.D.2
  • 8
    • 30044435707 scopus 로고    scopus 로고
    • Early detection of diabetic cardiomyopathy: Usefulness of tissue Doppler imaging
    • Di Bonito P, Moio N, Cavuto L, et al. Early detection of diabetic cardiomyopathy: usefulness of tissue Doppler imaging. Diabet Med 2005; 22: 1720-25
    • (2005) Diabet Med , vol.22 , pp. 1720-1725
    • Di Bonito, P.1    Moio, N.2    Cavuto, L.3
  • 9
    • 37849047917 scopus 로고    scopus 로고
    • Insulin-resistant cardiomyopathy clinical evidence, mechanisms, and treatment options
    • Witteles RM, Fowler MB. Insulin-resistant cardiomyopathy clinical evidence, mechanisms, and treatment options. J Am Coll Cardiol 2008; 51(2): 27-9.
    • (2008) J Am Coll Cardiol , vol.51 , Issue.2 , pp. 27-29
    • Witteles, R.M.1    Fowler, M.B.2
  • 10
    • 33846826589 scopus 로고    scopus 로고
    • Post-translational protein modifications in type 1 diabetes: Role for the repair enzyme protein-L-isoaspartate (D-aspartate) O-methyltransferase?
    • Wägner AM, Cloos P, Bergholdt R, et al. Post-translational protein modifications in type 1 diabetes: role for the repair enzyme protein-L-isoaspartate (D-aspartate) O-methyltransferase? Diabetologia 2007; 50(3): 676-81.
    • (2007) Diabetologia , vol.50 , Issue.3 , pp. 676-681
    • Wägner, A.M.1    Cloos, P.2    Bergholdt, R.3
  • 11
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • Christopher TW, Tsodikova GS, Gatto GJ, Chemie A. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew. Chem. Int. Ed 2005; 44: 7342-72.
    • (2005) Angew. Chem. Int. Ed , vol.44 , pp. 7342-7372
    • Christopher, T.W.1    Tsodikova, G.S.2    Gatto, G.J.3    Chemie, A.4
  • 12
    • 84865299042 scopus 로고    scopus 로고
    • Protein acetylation mechanisms in the regulation of insulin and insulin-like growth factor 1 signalling
    • Pirola L, Zerzaihi O, Vidal H, Solari F. Protein acetylation mechanisms in the regulation of insulin and insulin-like growth factor 1 signalling. Mol Cell Endocrinol.2012; 1-10.
    • (2012) Mol Cell Endocrinol , pp. 1-10
    • Pirola, L.1    Zerzaihi, O.2    Vidal, H.3    Solari, F.4
  • 13
    • 77955707062 scopus 로고    scopus 로고
    • Potential role of sirtuin as a therapeutic target for neurodegenerative diseases
    • Han SH. Potential role of sirtuin as a therapeutic target for neurodegenerative diseases. J Clin Neurol 2009; 5(3): 120-5.
    • (2009) J Clin Neurol , vol.5 , Issue.3 , pp. 120-125
    • Han, S.H.1
  • 14
    • 53249121556 scopus 로고    scopus 로고
    • Sirtuins-novel therapeutic targets to treat age-associated diseases
    • Lavu S, Boss O, Elliott PJ, Lambert PD. Sirtuins-novel therapeutic targets to treat age-associated diseases. Nat Rev Drug Discov 2009; 7: 841-54.
    • (2009) Nat Rev Drug Discov , vol.7 , pp. 841-854
    • Lavu, S.1    Boss, O.2    Elliott, P.J.3    Lambert, P.D.4
  • 15
    • 70350441907 scopus 로고    scopus 로고
    • The role of sirtuins in the control of metabolic homeostasis
    • Yu J, Auwerx J. The role of sirtuins in the control of metabolic homeostasis. Ann N Y Acad Sci 2009; 19: 10-9.
    • (2009) Ann N Y Acad Sci , vol.19 , pp. 10-19
    • Yu, J.1    Auwerx, J.2
  • 17
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and non-conserved cellular localizations and functions of human SIRT proteins
    • Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I. Evolutionarily conserved and non-conserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell 2005; 16: 4623-35.
    • (2005) Mol Biol Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 18
    • 34548150187 scopus 로고    scopus 로고
    • The role of nuclear architecture in genomic instability and ageing
    • Oberdoerffer P, Sinclair DA. The role of nuclear architecture in genomic instability and ageing. Nat Rev Mol Cell Biol 2007; 8: 692-702.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 692-702
    • Oberdoerffer, P.1    Sinclair, D.A.2
  • 19
    • 36249016246 scopus 로고    scopus 로고
    • A therapeutic role for sirtuins in diseases of aging?
    • Westphal CH, Dipp MA, Guarente L. A therapeutic role for sirtuins in diseases of aging? Trends Biochem Sci 2007; 32: 555-60.
    • (2007) Trends Biochem Sci , vol.32 , pp. 555-560
    • Westphal, C.H.1    Dipp, M.A.2    Guarente, L.3
  • 21
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction
    • 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
  • 22
    • 84859977895 scopus 로고    scopus 로고
    • Sirtuins mediate mammalian metabolic responses to nutrient availability
    • 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
  • 23
    • 79952806932 scopus 로고    scopus 로고
    • Sirtuins at a glance
    • Nakagawa T, Guarente L. Sirtuins at a glance, J Cell Sci 2011; 124: 833-8.
    • (2011) J Cell Sci , vol.124 , pp. 833-838
    • Nakagawa, T.1    Guarente, L.2
  • 24
    • 77951217683 scopus 로고    scopus 로고
    • SIRT1 regulates auto acetylation and histone acetyltransferase activity of TIP60
    • Wang J, Chen J. SIRT1 regulates auto acetylation and histone acetyltransferase activity of TIP60. J Bio Chem 2010; 285 (15): 11458-11464.
    • (2010) J Bio Chem , vol.285 , Issue.15 , pp. 11458-11464
    • Wang, J.1    Chen, J.2
  • 25
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E, Pearson M, Faretta M, et al. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO 2002; 21 (10): 2383-96.
    • (2002) EMBO , vol.21 , Issue.10 , pp. 2383-2396
    • Langley, E.1    Pearson, M.2    Faretta, M.3
  • 26
    • 3042750643 scopus 로고    scopus 로고
    • Silent information regulator 2 potentiates Foxo 1-mediated transcription through its deacetylase activity
    • Daitoku H, Hatta M, Matsuzaki H, et al. Silent information regulator 2 potentiates Foxo 1-mediated transcription through its deacetylase activity. Proc Natl Acad Sci 2004; 101(27): 10042-7.
    • (2004) Proc Natl Acad Sci , vol.101 , Issue.27 , pp. 10042-10047
    • Daitoku, H.1    Hatta, M.2    Matsuzaki, H.3
  • 27
    • 16344384026 scopus 로고    scopus 로고
    • Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation
    • Yang Y, Hou H, Haller EM, Nicosia SV, Bai W. Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation. EMBO 2005; 24(5): 1021-32.
    • (2005) EMBO , vol.24 , Issue.5 , pp. 1021-1032
    • Yang, Y.1    Hou, H.2    Haller, E.M.3    Nicosia, S.V.4    Bai, W.5
  • 28
    • 70349633646 scopus 로고    scopus 로고
    • TIMP3 Is Reduced in Atherosclerotic Plaques From Subjects With Type 2 Diabetes and Increased by SIRT1
    • Cardellini M, Menghini R, Martelli E, et al. TIMP3 Is Reduced in Atherosclerotic Plaques From Subjects With Type 2 Diabetes and Increased by SIRT1. Diabetes 2009; 58(10): 2396-401.
    • (2009) Diabetes , vol.58 , Issue.10 , pp. 2396-2401
    • Cardellini, M.1    Menghini, R.2    Martelli, E.3
  • 29
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • Motta MC, Divecha N, Lemieux M, et al. Mammalian SIRT1 represses forkhead transcription factors. Cell 2004; 116(4): 551-63.
    • (2004) Cell , vol.116 , Issue.4 , pp. 551-563
    • Motta, M.C.1    Divecha, N.2    Lemieux, M.3
  • 30
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai SI, et al. Negative control of p53 by Sir2α promotes cell survival under stress. Cell 2001; 107(2): 137-48.
    • (2001) Cell , vol.107 , Issue.2 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.I.3
  • 31
    • 3142548829 scopus 로고    scopus 로고
    • Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10
    • Bae NS, Swanson MJ, Vassilev A, Howard BH. Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10. J Bio 2004; 135(6): 695-700.
    • (2004) J Bio , vol.135 , Issue.6 , pp. 695-700
    • Bae, N.S.1    Swanson, M.J.2    Vassilev, A.3    Howard, B.H.4
  • 32
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer B, Bunkenborg J, Verdin RO, Andersen JS, Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci 2006; 103(27): 10224-9.
    • (2006) Proc Natl Acad Sci , vol.103 , Issue.27 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 33
    • 79952117379 scopus 로고    scopus 로고
    • Calorie restriction on insulin resistance and expression of SIRT1 and SIRT4 in rats
    • Chen YR, Fang SR, Fu YC, Zhou XH, Xu MY, Xu WC. Calorie restriction on insulin resistance and expression of SIRT1 and SIRT4 in rats. Biochem Cell Biol 2010; 88(4): 715-22.
    • (2010) Biochem Cell Biol , vol.88 , Issue.4 , pp. 715-722
    • Chen, Y.R.1    Fang, S.R.2    Fu, Y.C.3    Zhou, X.H.4    Xu, M.Y.5    Xu, W.C.6
  • 34
    • 10044262126 scopus 로고    scopus 로고
    • The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60
    • Patel JH, Du Y, Ard PG, et al. The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60. Mol Cell Bio 2004; 24: 10826-34.
    • (2004) Mol Cell Bio , vol.24 , pp. 10826-10834
    • Patel, J.H.1    Du, Y.2    Ard, P.G.3
  • 35
    • 62149130110 scopus 로고    scopus 로고
    • Cellular regulation of SIRT1
    • Milner J. Cellular regulation of SIRT1. Curr Pharm Des 2009; 15(1): 39-44.
    • (2009) Curr Pharm Des , vol.15 , Issue.1 , pp. 39-44
    • Milner, J.1
  • 36
    • 80055085693 scopus 로고    scopus 로고
    • Role of sirtuins and calorie restriction in neuroprotection: Implications in Alzheimer's and Parkinson's diseases
    • 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
  • 38
    • 77958523925 scopus 로고    scopus 로고
    • NAD 1-dependent histone deacetylases (sirtuins) as novel therapeutictargets
    • Uciechowska U, Sippl W, Jung M. NAD 1-dependent histone deacetylases (sirtuins) as novel therapeutictargets. Med Res Rev 2009; 30(6): 861-89.
    • (2009) Med Res Rev , vol.30 , Issue.6 , pp. 861-889
    • Uciechowska, U.1    Sippl, W.2    Jung, M.3
  • 39
    • 77953240381 scopus 로고    scopus 로고
    • Sirtuins
    • Lin S. Sirtuins. Biochim Biophys Acta 2010; 1804: 1565-6.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1565-1566
    • Lin, S.1
  • 40
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 2003; 11: 437-44.
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 41
    • 2342496712 scopus 로고    scopus 로고
    • FoxOs at the crossroads of cellular metabolism, differentiation, and transformation
    • Accili D, Arden KC. FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell 2004; 117: 421-6.
    • (2004) Cell , vol.117 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 42
    • 0036629251 scopus 로고    scopus 로고
    • Cell cycle and death control: Long live Forkheads
    • Burgering BM, Kops GJ. Cell cycle and death control: long live Forkheads. Trends Biochem Sci 2002; 27: 352-60.
    • (2002) Trends Biochem Sci , vol.27 , pp. 352-360
    • Burgering, B.M.1    Kops, G.J.2
  • 43
    • 27844497945 scopus 로고    scopus 로고
    • FOXO transcription factors at the interface between longevity and tumor suppression
    • Greer E, Brunet A. FOXO transcription factors at the interface between longevity and tumor suppression. Oncogene 2005; 24: 7410-25.
    • (2005) Oncogene , vol.24 , pp. 7410-7425
    • Greer, E.1    Brunet, A.2
  • 44
    • 13944269223 scopus 로고    scopus 로고
    • The plasticity of aging: Insights from long-lived mutants
    • Kenyon C. The plasticity of aging: insights from long-lived mutants. Cell 2005; 120: 449-60.
    • (2005) Cell , vol.120 , pp. 449-460
    • Kenyon, C.1
  • 46
    • 42349085704 scopus 로고    scopus 로고
    • Sirt1 contributes critically to the redox-dependent fate of neural progenitors
    • Prozorovski T, Topphoff SU, Glumm R, et al. Sirt1 contributes critically to the redox-dependent fate of neural progenitors. Nat. Cell Biol 2008; 10: 385-94.
    • (2008) Nat. Cell Biol , vol.10 , pp. 385-394
    • Prozorovski, T.1    Topphoff, S.U.2    Glumm, R.3
  • 47
    • 28644447272 scopus 로고    scopus 로고
    • The antioxidant functions of the p53 tumor suppressor
    • Sablina AA, Budanov AV, Ilyinskaya GV, et al. The antioxidant functions of the p53 tumor suppressor. Nat. Med 2005; 11: 1306-13.
    • (2005) Nat. Med , vol.11 , pp. 1306-1313
    • Sablina, A.A.1    Budanov, A.V.2    Ilyinskaya, G.V.3
  • 48
    • 79961180595 scopus 로고    scopus 로고
    • p53, oxidative stress and aging
    • Liu D, Xu Y. p53, oxidative stress and aging. Antioxid Redox Signal 2011; 15(6): 1669-78.
    • (2011) Antioxid Redox Signal , vol.15 , Issue.6 , pp. 1669-1678
    • Liu, D.1    Xu, Y.2
  • 49
    • 39749087530 scopus 로고    scopus 로고
    • SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization
    • Han MK, Song EK, Guo Y, Ou X, Mantel C, Broxmeyer HE. SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization. Cell Stem Cell 2008; 2: 241-51.
    • (2008) Cell Stem Cell , vol.2 , pp. 241-251
    • Han, M.K.1    Song, E.K.2    Guo, Y.3    Ou, X.4    Mantel, C.5    Broxmeyer, H.E.6
  • 50
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2 (SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, Dessain SK, Ng EE, et al. hSIR2 (SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 2001; 107: 149-59.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng, E.E.3
  • 51
    • 77449121720 scopus 로고    scopus 로고
    • SIRT1 confers protection against UVB and H2O2-induced cell death via modulation of p53 and JNK in cultured skin keratinocytes
    • Cao C, Lu S, Kivlin R, Wallin B, Card E, Bagdasarian A, et al. SIRT1 confers protection against UVB and H2O2-induced cell death via modulation of p53 and JNK in cultured skin keratinocytes. J Cell Mol Med 2009; 13(9B): 3632-43.
    • (2009) J Cell Mol Med , vol.13 , Issue.9 B , pp. 3632-3643
    • Cao, C.1    Lu, S.2    Kivlin, R.3    Wallin, B.4    Card, E.5    Bagdasarian, A.6
  • 52
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • Cheng HL, Mostoslavsky R, Saito S, Manis JP, Gu YS, Patel P, et al. Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc. Natl. Acad. Sci 2003; 100(19): 10794-9.
    • (2003) Proc. Natl. Acad. Sci , vol.100 , Issue.19 , pp. 10794-10799
    • Cheng, H.L.1    Mostoslavsky, R.2    Saito, S.3    Manis, J.P.4    Gu, Y.S.5    Patel, P.6
  • 53
    • 33745166337 scopus 로고    scopus 로고
    • Silent information regulator 2 (SIRT1) attenuates oxidative stress-induced mesangial cell apoptosis via p53 deacetylation
    • Kume S, Haneda M, Kanasaki K. et al. Silent information regulator 2 (SIRT1) attenuates oxidative stress-induced mesangial cell apoptosis via p53 deacetylation. Free Radic. Biol. Med 2006; 40: 2175-82.
    • (2006) Free Radic. Biol. Med , vol.40 , pp. 2175-2182
    • Kume, S.1    Haneda, M.2    Kanasaki, K.3
  • 54
    • 33748200050 scopus 로고    scopus 로고
    • Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage
    • Wang C, Chen L, Hou X, et al. Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. Nat Cell Biol 2006; 8(9): 1025-31.
    • (2006) Nat Cell Biol , vol.8 , Issue.9 , pp. 1025-1031
    • Wang, C.1    Chen, L.2    Hou, X.3
  • 55
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, Sweeney LB, Sturgill JF, et al. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 2004; 303: 2011-5.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3
  • 56
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang F, Nguyen M, Qin FX, Tong Q. SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 2007; 6: 505-14.
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 57
    • 66149163230 scopus 로고    scopus 로고
    • A "FOXO" in sight: Targeting Foxo proteins from conception to cancer
    • Maiese K, Chong ZZ, Shang YC, Hou J. A "FOXO" in sight: targeting Foxo proteins from conception to cancer. Med Res Rev 2009; 29: 395-418.
    • (2009) Med Res Rev , vol.29 , pp. 395-418
    • Maiese, K.1    Chong, Z.Z.2    Shang, Y.C.3    Hou, J.4
  • 58
    • 46349096040 scopus 로고    scopus 로고
    • Sirt1 protects against oxidative stress-induced renal tubular cell apoptosis by the bidirectional regulation of catalase expression
    • Hasegawa K, Wakino S, Yoshioka K, 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: 51-6.
    • (2008) Biochem Biophys Res Commun , vol.372 , pp. 51-56
    • Hasegawa, K.1    Wakino, S.2    Yoshioka, K.3
  • 59
    • 80051534214 scopus 로고    scopus 로고
    • Erythropoietin employs cell longevity pathways of SIRT1 to foster endothelial vascular integrity during oxidant stress
    • Hou J, Wang S, Shang YC, et al. Erythropoietin employs cell longevity pathways of SIRT1 to foster endothelial vascular integrity during oxidant stress. Curr Neurovasc Res 2011; 8: 220-35.
    • (2011) Curr Neurovasc Res , vol.8 , pp. 220-235
    • Hou, J.1    Wang, S.2    Shang, Y.C.3
  • 60
    • 0037136563 scopus 로고    scopus 로고
    • Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress
    • Kops GJ, Dansen TB, Polderman PE, et al. Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress. Nature 2002; 419: 316-21.
    • (2002) Nature , vol.419 , pp. 316-321
    • Kops, G.J.1    Dansen, T.B.2    Polderman, P.E.3
  • 61
    • 34249669270 scopus 로고    scopus 로고
    • Sirt1 regulates aging and resistance to oxidative stress in the heart
    • Alcendor RR, Gao S, Zhai P, et al. Sirt1 regulates aging and resistance to oxidative stress in the heart. Circ Res 2007; 100: 1512-21
    • (2007) Circ Res , vol.100 , pp. 1512-1521
    • Alcendor, R.R.1    Gao, S.2    Zhai, P.3
  • 62
    • 78650691023 scopus 로고    scopus 로고
    • Deacetylation of FoxO by Sirt1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes
    • Hariharan N, Maejima Y, Nakae J, et al. Deacetylation of FoxO by Sirt1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes. Circ Res 2010; 107: 1470-82.
    • (2010) Circ Res , vol.107 , pp. 1470-1482
    • Hariharan, N.1    Maejima, Y.2    Nakae, J.3
  • 63
    • 79953152333 scopus 로고    scopus 로고
    • FoxO1 mediates an auto feedback loop regulating SIRT1 expression
    • Xiong S, Salazar G, Patrushev N, Alexander RW. FoxO1 mediates an auto feedback loop regulating SIRT1 expression. J Biol Chem 2011; 286: 5289-99.
    • (2011) J Biol Chem , vol.286 , pp. 5289-5299
    • Xiong, S.1    Salazar, G.2    Patrushev, N.3    Alexander, R.W.4
  • 64
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead dependent pathway
    • Nemoto S, Fergusson MM, Finkel T. Nutrient availability regulates SIRT1 through a forkhead dependent pathway. Science 2004; 306: 2105-8.
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 65
    • 70349208608 scopus 로고    scopus 로고
    • Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a dependent antioxidant defense mechanisms in mice
    • Sundaresan NR, Gupta M, Kim G, Rajamohan SB, Isbatan A, Gupta MP. Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a dependent antioxidant defense mechanisms in mice. J. Clin. Invest 2009; 119: 2758-71.
    • (2009) J. Clin. Invest , vol.119 , pp. 2758-2771
    • Sundaresan, N.R.1    Gupta, M.2    Kim, G.3    Rajamohan, S.B.4    Isbatan, A.5    Gupta, M.P.6
  • 66
    • 51449083112 scopus 로고    scopus 로고
    • SIRT3 interacts with the daf-16 homolog FOXO3a in themitochondria, as well as increases FOXO3a dependent gene expression
    • Jacobs KM, Pennington JD, Bisht KS, et al. SIRT3 interacts with the daf-16 homolog FOXO3a in themitochondria, as well as increases FOXO3a dependent gene expression. Int. J. Biol. Sci 2008; 4: 291-9.
    • (2008) Int. J. Biol. Sci , vol.4 , pp. 291-299
    • Jacobs, K.M.1    Pennington, J.D.2    Bisht, K.S.3
  • 68
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxiainducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum EM, Chen R, Alexander MS, et al. Regulation of hypoxiainducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1. Science 2009; 324: 1289-93.
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3
  • 69
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxiainducible factor 1alpha
    • Lim JH, Lee YM, Chun YS, Chen J, Kim JE, Park JW. Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxiainducible factor 1alpha. Mol. Cell 38: 864-878; 2010.
    • (2010) Mol. Cell , vol.38 , pp. 864-878
    • Lim, J.H.1    Lee, Y.M.2    Chun, Y.S.3    Chen, J.4    Kim, J.E.5    Park, J.W.6
  • 70
    • 74549142287 scopus 로고    scopus 로고
    • The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1alpha
    • Zhong L, D'Urso A, Toiber D, et al. The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1alpha. Cell 2010; 140: 280-93.
    • (2010) Cell , vol.140 , pp. 280-293
    • Zhong, L.1    D'Urso, A.2    Toiber, D.3
  • 71
    • 74249092946 scopus 로고    scopus 로고
    • NF-kappaB-induced oxidative stress contributes to mitochondrial and cardiac dysfunction in type II diabetes
    • Mariappan N, Elks CM, Sriramula S, et al. NF-kappaB-induced oxidative stress contributes to mitochondrial and cardiac dysfunction in type II diabetes. Cardiovasc res 2010; 85(3): 473-83.
    • (2010) Cardiovasc res , vol.85 , Issue.3 , pp. 473-483
    • Mariappan, N.1    Elks, C.M.2    Sriramula, S.3
  • 72
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-jBdependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, Hoberg JE, Ramsey CS, et al. Modulation of NF-jBdependent transcription and cell survival by the SIRT1 deacetylase. EMBO 2004; 23(12): 2369-80.
    • (2004) EMBO , vol.23 , Issue.12 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3
  • 73
    • 78649738291 scopus 로고    scopus 로고
    • SIRT2 regulates NF-kB-dependent gene expression through deacetylation of p65 Lys310
    • Rothgiesser KM, Erener S, Waibel S, Lüscher B, Hottiger MO. SIRT2 regulates NF-kB-dependent gene expression through deacetylation of p65 Lys310. J Cell Sci 2010; 123: 4251-8.
    • (2010) J Cell Sci , vol.123 , pp. 4251-4258
    • Rothgiesser, K.M.1    Erener, S.2    Waibel, S.3    Lüscher, B.4    Hottiger, M.O.5
  • 74
    • 58149086403 scopus 로고    scopus 로고
    • When Sirtuins and NF-κB Collide
    • Gioacchino N, When Sirtuins and NF-κB Collide. Cell 2009; 136: 19-21.
    • (2009) Cell , vol.136 , pp. 19-21
    • Gioacchino, N.1
  • 75
    • 26644471251 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial biogenesis: A key to long-term regulation of cellular metabolism
    • Clementi E, Nisoli E. Nitric oxide and mitochondrial biogenesis: a key to long-term regulation of cellular metabolism. Comp Biochem Physiol A Mol Integr Physiol 2005; 142: 102-10.
    • (2005) Comp Biochem Physiol A Mol Integr Physiol , vol.142 , pp. 102-110
    • Clementi, E.1    Nisoli, E.2
  • 76
    • 35549008884 scopus 로고    scopus 로고
    • SIRT1 promotes endothelium-dependent vascu-lar relaxation by activating endothelial nitric oxide synthase
    • Mattagajasingh I, Kim CS, Naqvi A, et al. SIRT1 promotes endothelium-dependent vascu-lar relaxation by activating endothelial nitric oxide synthase. Proc. Natl. Acad. Sci 2007; 104: 14855-60.
    • (2007) Proc. Natl. Acad. Sci , vol.104 , pp. 14855-14860
    • Mattagajasingh, I.1    Kim, C.S.2    Naqvi, A.3
  • 77
    • 79953225194 scopus 로고    scopus 로고
    • Acetylation-Deacetylation of the Transcription Factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its Transcriptional Activity and Nucleo-cytoplasmic Localization
    • Yumiko K, LaKisha G, Melanie T, Jianqi Y, Ifeanyi JA. Acetylation-Deacetylation of the Transcription Factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its Transcriptional Activity and Nucleo-cytoplasmic Localization. J Biol Chem 2011; 286(9): 7629-40.
    • (2011) J Biol Chem , vol.286 , Issue.9 , pp. 7629-7640
    • Yumiko, K.1    LaKisha, G.2    Melanie, T.3    Jianqi, Y.4    Ifeanyi, J.A.5
  • 78
    • 84864277111 scopus 로고    scopus 로고
    • Attenuation of insulin resistance, metabolic syndrome and hepatic oxidative stress by resveratrol in fructose-fed rats
    • Bagul PK, Middela H, Matapally S, et al. Attenuation of insulin resistance, metabolic syndrome and hepatic oxidative stress by resveratrol in fructose-fed rats. Pharmacol Res 2012; 66: 260-8.
    • (2012) Pharmacol Res , vol.66 , pp. 260-268
    • Bagul, P.K.1    Middela, H.2    Matapally, S.3
  • 79
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel T, Deng CX, Mostoslavsky R. Recent progress in the biology and physiology of sirtuins. Nature 2009; 460(7255): 587-91.
    • (2009) Nature , vol.460 , Issue.7255 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 80
    • 41549136422 scopus 로고    scopus 로고
    • Paths of convergence: Sirtuins in aging and neurodegeneration
    • Gan L, Mucke L. Paths of convergence: sirtuins in aging and neurodegeneration. Neuron 2008; 58 (1):10-4.
    • (2008) Neuron , vol.58 , Issue.1 , pp. 10-14
    • Gan, L.1    Mucke, L.2
  • 81
    • 0038268180 scopus 로고    scopus 로고
    • HSF-1 interacts with Ral-binding protein 1 in a stress-responsive, multiprotein complex with HSP90 in vivo
    • Hu Y, Mivechi NF. HSF-1 interacts with Ral-binding protein 1 in a stress-responsive, multiprotein complex with HSP90 in vivo. J Biol Chem 2003; 278: 17299-306.
    • (2003) J Biol Chem , vol.278 , pp. 17299-17306
    • Hu, Y.1    Mivechi, N.F.2
  • 83
    • 67649333085 scopus 로고    scopus 로고
    • DeubiKuitylation: A novel DUB enzymatic activity for the DNA repair protein, Ku70
    • Rathaus M, Lerrer B, Cohen HY. DeubiKuitylation: a novel DUB enzymatic activity for the DNA repair protein, Ku70. Cell Cycle 2009; 8: 1843-52.
    • (2009) Cell Cycle , vol.8 , pp. 1843-1852
    • Rathaus, M.1    Lerrer, B.2    Cohen, H.Y.3
  • 84
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, Miller C, Bitterman KJ, et al, Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 2004; 305: 390-2.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3
  • 85
    • 79551514834 scopus 로고    scopus 로고
    • SIRT1 inhibits angiotensin II-induced vascular smooth muscle cell hypertrophy
    • Li Li, Gao P, Zhang H. SIRT1 inhibits angiotensin II-induced vascular smooth muscle cell hypertrophy. Acta Biochim Biophys Sin 2011, 43: 103-9
    • (2011) Acta Biochim Biophys Sin , vol.43 , pp. 103-109
    • Li, L.1    Gao, P.2    Zhang, H.3
  • 86
    • 80052142793 scopus 로고    scopus 로고
    • Restriction of Advanced Glycation End Products Improves Insulin Resistance in Human Type 2 Diabetes Potential role of AGER1 and SIRT1
    • Uribarri J, Cai W, Ramdas M. Restriction of Advanced Glycation End Products Improves Insulin Resistance in Human Type 2 Diabetes Potential role of AGER1 and SIRT1. Diabetes Care July 2011; 34: 1610-6.
    • (2011) Diabetes Care July , vol.34 , pp. 1610-1616
    • Uribarri, J.1    Cai, W.2    Ramdas, M.3
  • 87
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao S, Xu W, Jiang W et al. Regulation of cellular metabolism by protein lysine acetylation. Science 2010; 327: 1000-4.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3
  • 88
    • 37549002891 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT3 regulates global mito-chondrial lysine acetylation
    • Lombard D, Alt W, Cheng L, et al. Mammalian Sir2 homolog SIRT3 regulates global mito-chondrial lysine acetylation. Mol Cell Biol 2007; 27: 8807-14.
    • (2007) Mol Cell Biol , vol.27 , pp. 8807-8814
    • Lombard, D.1    Alt, W.2    Cheng, L.3
  • 89
    • 84884270949 scopus 로고    scopus 로고
    • Superoxide levels and mitochondrial function are regulated by SIRT3
    • Jacobs KM, Gius D. Superoxide levels and mitochondrial function are regulated by SIRT3. Free Radic Biol Med 2007; 43: S156.
    • (2007) Free Radic Biol Med , vol.43
    • Jacobs, K.M.1    Gius, D.2
  • 90
    • 77956173286 scopus 로고    scopus 로고
    • SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity
    • Bao J, Scott I, Lu Z, et al. SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity. Free Radic. Biol. Med 2010; 49: 1230-7.
    • (2010) Free Radic. Biol. Med , vol.49 , pp. 1230-1237
    • Bao, J.1    Scott, I.2    Lu, Z.3
  • 91
    • 55749084738 scopus 로고    scopus 로고
    • Role for the mitochondrial deacetylase Sirt3in regulating energy homeostasis
    • Ahn BH, Kim HS, Song S, et al. Role for the mitochondrial deacetylase Sirt3in regulating energy homeostasis. Proc. Natl. Acad. Sci 2008; 105: 14447-52.
    • (2008) Proc. Natl. Acad. Sci , vol.105 , pp. 14447-14452
    • Ahn, B.H.1    Kim, H.S.2    Song, S.3
  • 92
    • 75349111140 scopus 로고    scopus 로고
    • Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria
    • Cimen H, Han MJ, Yang Y, Tong Q, Koc H, Koc EC. Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry 2010; 49: 304-11.
    • (2010) Biochemistry , vol.49 , pp. 304-311
    • Cimen, H.1    Han, M.J.2    Yang, Y.3    Tong, Q.4    Koc, H.5    Koc, E.C.6
  • 93
    • 78649509214 scopus 로고    scopus 로고
    • SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production
    • Shimazu T, Hirschey D, Hua L, et al. SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production. Cell Metab 2010; 12: 654-61.
    • (2010) Cell Metab , vol.12 , pp. 654-661
    • Shimazu, T.1    Hirschey, D.2    Hua, L.3
  • 94
    • 77957777952 scopus 로고    scopus 로고
    • Mitochondrial HMG-CoA synthase partially contributes to antioxidant protection in the kidney of strokeprone spontaneously hypertensive rats
    • Yi W, Fu P, Fan Z, et al. Mitochondrial HMG-CoA synthase partially contributes to antioxidant protection in the kidney of strokeprone spontaneously hypertensive rats. Nutrition 2010; 26: 1176-80.
    • (2010) Nutrition , vol.26 , pp. 1176-1180
    • Yi, W.1    Fu, P.2    Fan, Z.3
  • 95
    • 80051716282 scopus 로고    scopus 로고
    • Succinate dehydrogenase is a direct target of sirtuin 3 531 deacetylase activity
    • Finley W, Haas W, Desquiret-Dumas V, et al. Succinate dehydrogenase is a direct target of sirtuin 3 531 deacetylase activity. PLoS 2011; 6: e23295.
    • (2011) PLoS , vol.6
    • Finley, W.1    Haas, W.2    Desquiret-Dumas, V.3
  • 96
    • 79959819034 scopus 로고    scopus 로고
    • SirT3 suppresses hypoxia 497 inducible factor 1alpha and tumor growth by inhibiting mitochondrial ROS pro-498 duction
    • Bell E, Emerling M, Ricoult S, Guarente L. SirT3 suppresses hypoxia 497 inducible factor 1alpha and tumor growth by inhibiting mitochondrial ROS pro-498 duction. Oncogene 2011; 30: 2986-96.
    • (2011) Oncogene , vol.30 , pp. 2986-2996
    • Bell, E.1    Emerling, M.2    Ricoult, S.3    Guarente, L.4
  • 97
    • 80052291180 scopus 로고    scopus 로고
    • Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production
    • Jing E, Emanuelli B, Hirschey M, et al. Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production PNAS 2011; 108: 14608-13.
    • (2011) PNAS , vol.108 , pp. 14608-14613
    • Jing, E.1    Emanuelli, B.2    Hirschey, M.3
  • 98
    • 79952266729 scopus 로고    scopus 로고
    • Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy
    • Hafner V, Dai J, Gomes A, et al. Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy. Aging 2010; 2: 914-23.
    • (2010) Aging , vol.2 , pp. 914-923
    • Hafner, V.1    Dai, J.2    Gomes, A.3
  • 101
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a Mitochondrial Sirtuin Deacetylase, Regulates Mitochondrial Function and Thermogenesis in Brown Adipocytes
    • Tong S, Wang F, Stieren E, Tong Q. SIRT3, a Mitochondrial Sirtuin Deacetylase, Regulates Mitochondrial Function and Thermogenesis in Brown Adipocytes. The J Bio Chem 2005; 280: 13560-7.
    • (2005) The J Bio Chem , vol.280 , pp. 13560-13567
    • Tong, S.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 102
    • 77955347446 scopus 로고    scopus 로고
    • Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis
    • Kong X, Wang R, Xue Y, et al. Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis. PLoS One 2010; 5: e11707.
    • (2010) PLoS One , vol.5
    • Kong, X.1    Wang, R.2    Xue, Y.3
  • 103
    • 79951887419 scopus 로고    scopus 로고
    • Forkhead box O as a sensor, mediator, and regulator of redox signaling
    • de Keizer L, Burgering M, Dansen B. Forkhead box O as a sensor, mediator, and regulator of redox signaling. Antioxid. Redox Signal 2011; 14: 1093-106.
    • (2011) Antioxid. Redox Signal , vol.14 , pp. 1093-1106
    • de Keizer, L.1    Burgering, M.2    Dansen, B.3
  • 104
    • 77952940043 scopus 로고    scopus 로고
    • Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1alpha in skeletal muscle
    • Palacios M, Carmona J, Michan S, et al. Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1alpha in skeletal muscle. Aging 2009; 1: 771-83.
    • (2009) Aging , vol.1 , pp. 771-783
    • Palacios, M.1    Carmona, J.2    Michan, S.3
  • 105
    • 78651468722 scopus 로고    scopus 로고
    • Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
    • Someya S, Yu W, Hallows WC, et al. Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 2010; 143: 802-12.
    • (2010) Cell , vol.143 , pp. 802-812
    • Someya, S.1    Yu, W.2    Hallows, W.C.3
  • 106
    • 74049094817 scopus 로고    scopus 로고
    • SIRT3 is a mitochondrialocalized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress
    • Kim HS, Patel K, Muldoon JK, et al. SIRT3 is a mitochondrialocalized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress. Cancer Cell 2010; 17(1): 41-52.
    • (2010) Cancer Cell , vol.17 , Issue.1 , pp. 41-52
    • Kim, H.S.1    Patel, K.2    Muldoon, J.K.3
  • 107
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim SC, Sprung R, Chen Y, et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 2006; 23: 607-18.
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3
  • 108
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3 mediated SOD2 activation
    • Qiu, X, Brown K, Hirschey MD, Verdin E, Chen D. Calorie restriction reduces oxidative stress by SIRT3 mediated SOD2 activation. Cell Metab 2010; 12: 662-7.
    • (2010) Cell Metab , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 109
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and coregulates major cellular functions
    • Choudhary C, Kumar C, Gnad F, et al. Lysine acetylation targets protein complexes and coregulates major cellular functions. Science 2009; 325: 834-40.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3
  • 110
    • 78650248160 scopus 로고    scopus 로고
    • Sirt3-mediated deacetylation of evolutionarily conserved lysine-122 regulates MnSOD activity in response to stress
    • Tao R, Coleman MC, Pennington JD, et al. Sirt3-mediated deacetylation of evolutionarily conserved lysine-122 regulates MnSOD activity in response to stress. Mol Cell 2010; 40: 893-904.
    • (2010) Mol Cell , vol.40 , pp. 893-904
    • Tao, R.1    Coleman, M.C.2    Pennington, J.D.3
  • 111
    • 79957979314 scopus 로고    scopus 로고
    • Tumor suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • Chen Y, Zhang J, Lin Y, et al. Tumor suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep 2011; 12: 534-41.
    • (2011) EMBO Rep , vol.12 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3
  • 112
    • 84855433458 scopus 로고    scopus 로고
    • The role of sirtuins in modulating redox stressors
    • Webster BR, Lu Z, Sack MN, Scott I. The role of sirtuins in modulating redox stressors. Free Radic Biol Med 2012; 52(2): 281-90.
    • (2012) Free Radic Biol Med , vol.52 , Issue.2 , pp. 281-290
    • Webster, B.R.1    Lu, Z.2    Sack, M.N.3    Scott, I.4
  • 113
    • 77955347446 scopus 로고    scopus 로고
    • Sirtuin 3, a New Target of PGC-1a, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis
    • Kong X, Wang R, Xue Y. Sirtuin 3, a New Target of PGC-1a, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis. PLoS ONE 2010; 5(7): e11707
    • (2010) PLoS ONE , vol.5 , Issue.7
    • Kong, X.1    Wang, R.2    Xue, Y.3
  • 114
    • 33748316536 scopus 로고    scopus 로고
    • SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells
    • Haigis MC, Mostoslavsky R, Haigis KM, et al. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 2006; 126: 941-54.
    • (2006) Cell , vol.126 , pp. 941-954
    • Haigis, M.C.1    Mostoslavsky, R.2    Haigis, K.M.3
  • 115
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa T, Lomb DJ, Haigis MC, Guarente L. SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 2009; 137: 560-70.
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 116
    • 78651468707 scopus 로고    scopus 로고
    • Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
    • Hallows WC, Yu W, Smith BC, et al. Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction. Mol. Cell 2011; 41: 139-49.
    • (2011) Mol. Cell , vol.41 , pp. 139-149
    • Hallows, W.C.1    Yu, W.2    Smith, B.C.3
  • 117
    • 79959363092 scopus 로고    scopus 로고
    • SIRT6 promotes DNA repair under stress by activating PARP1
    • Zhiyong M, Christopher H, Xiao T, et al. SIRT6 promotes DNA repair under stress by activating PARP1. Science 2011; 332: 1443-6.
    • (2011) Science , vol.332 , pp. 1443-1446
    • Zhiyong, M.1    Christopher, H.2    Xiao, T.3
  • 118
    • 41449083867 scopus 로고    scopus 로고
    • Sirt7 Increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice
    • Olesya V, Christian S, Praveen G, et al. Sirt7 Increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ Res 2008; 102: 703-10.
    • (2008) Circ Res , vol.102 , pp. 703-710
    • Olesya, V.1    Christian, S.2    Praveen, G.3
  • 119
    • 34447569485 scopus 로고    scopus 로고
    • Nocturnal free fatty acids are uniquely elevated in the longitudinal development of diet-induced insulin resistance and hyperinsulinemia
    • Kim SP, Catalano KJ, Hsu IR, Chiu J, Richey JM, Bergman RN. Nocturnal free fatty acids are uniquely elevated in the longitudinal development of diet-induced insulin resistance and hyperinsulinemia. Am J Physiol Endocrinol Metab 2007; 292: E1590-8.
    • (2007) Am J Physiol Endocrinol Metab , vol.292
    • Kim, S.P.1    Catalano, K.J.2    Hsu, I.R.3    Chiu, J.4    Richey, J.M.5    Bergman, R.N.6
  • 120
    • 80052678652 scopus 로고    scopus 로고
    • Molecular mechanisms of insulin resistance in type 2 diabetes mellitus
    • Saini V. Molecular mechanisms of insulin resistance in type 2 diabetes mellitus. World J Diabetes 2010; 1(3): 68-75.
    • (2010) World J Diabetes , vol.1 , Issue.3 , pp. 68-75
    • Saini, V.1
  • 121
    • 33244486764 scopus 로고    scopus 로고
    • Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic beta cells
    • Bordone L, Motta MC, Picard F et al. Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic beta cells. PLoS Biol 2006; 4: e31.
    • (2006) PLoS Biol , vol.4
    • Bordone, L.1    Motta, M.C.2    Picard, F.3
  • 122
    • 27744518040 scopus 로고    scopus 로고
    • FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction
    • Kitamura YI, Kitamura T, Kruse JP, et al. FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction. Cell. Metab 2005; 2: 153-63.
    • (2005) Cell. Metab , vol.2 , pp. 153-163
    • Kitamura, Y.I.1    Kitamura, T.2    Kruse, J.P.3
  • 123
    • 38349112898 scopus 로고    scopus 로고
    • Age-associated loss of sirt1-mediated enhancement of glucose stimulated insulin secretion in beta cell-specific Sirt1-overexpressing (BesTO) mice
    • Ramsey KM, Mills KF, Satoh A, Imai S. Age-associated loss of sirt1-mediated enhancement of glucose stimulated insulin secretion in beta cell-specific Sirt1-overexpressing (BesTO) mice. Aging Cell 2008; 7: 78-88.
    • (2008) Aging Cell , vol.7 , pp. 78-88
    • Ramsey, K.M.1    Mills, K.F.2    Satoh, A.3    Imai, S.4
  • 124
    • 25144454432 scopus 로고    scopus 로고
    • Increased dosage of mammalian sir2 in pancreatic beta cells enhances glucosestimulated insulin secretion in mice
    • Moynihan KA, Grimm AA, Plueger MM, et al. Increased dosage of mammalian sir2 in pancreatic beta cells enhances glucosestimulated insulin secretion in mice. Cell Metab 2005; 2: 105-17.
    • (2005) Cell Metab , vol.2 , pp. 105-117
    • Moynihan, K.A.1    Grimm, A.A.2    Plueger, M.M.3
  • 125
    • 34548857700 scopus 로고    scopus 로고
    • SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B
    • Sun C, Zhang F, Ge X, et al. SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B. Cell. Metab 2007; 6: 307-19.
    • (2007) Cell. Metab , vol.6 , pp. 307-319
    • Sun, C.1    Zhang, F.2    Ge, X.3
  • 126
    • 0029762957 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B interacts with the activated insulin receptor
    • Seely BL, Staubs PA, Reichart DR, et al. Protein tyrosine phosphatase 1B interacts with the activated insulin receptor. Diabetes 1996; 45: 1379-85.
    • (1996) Diabetes , vol.45 , pp. 1379-1385
    • Seely, B.L.1    Staubs, P.A.2    Reichart, D.R.3
  • 127
    • 0034635374 scopus 로고    scopus 로고
    • Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein
    • Goldstein BJ, Kowalczyk AB, White MF, Harbeck M. Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein. J Biol Chem 2000; 275: 4283-9.
    • (2000) J Biol Chem , vol.275 , pp. 4283-4289
    • Goldstein, B.J.1    Kowalczyk, A.B.2    White, M.F.3    Harbeck, M.4
  • 128
    • 0032496150 scopus 로고    scopus 로고
    • Dynamics of insulin signaling in 3T3-L1 adipocytes. Differential compartmentalization and trafficking of insulin receptor substrate (IRS)-1 and IRS-2
    • Inoue G, Cheatham B, Emkey R. Kahn CR. Dynamics of insulin signaling in 3T3-L1 adipocytes. Differential compartmentalization and trafficking of insulin receptor substrate (IRS)-1 and IRS-2. J Biol Chem 1998: 273: 11548-55.
    • (1998) J Biol Chem , vol.273 , pp. 11548-11555
    • Inoue, G.1    Cheatham, B.2    Emkey, R.3    Kahn, C.R.4
  • 129
    • 36348974168 scopus 로고    scopus 로고
    • The direct involvement of SIRT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation
    • Zhang J. The direct involvement of SIRT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation. J Biol Chem 2007; 282: 34356-64.
    • (2007) J Biol Chem , vol.282 , pp. 34356-34364
    • Zhang, J.1
  • 130
    • 61749095297 scopus 로고    scopus 로고
    • SIRT 1 exerts antiinflammatory effects and improves insulin sensitivity in adipocytes
    • Yoshizaki T, Milne JC, Imamura T, et al. SIRT 1 exerts antiinflammatory effects and improves insulin sensitivity in adipocytes. Mol Cell Biol 2009; 29: 1363-74.
    • (2009) Mol Cell Biol , vol.29 , pp. 1363-1374
    • Yoshizaki, T.1    Milne, J.C.2    Imamura, T.3
  • 131
    • 0036092239 scopus 로고    scopus 로고
    • Banting, Dysregulation of fatty acid me in the etiology of type 2 diabetes
    • McGarry JD. Banting, Dysregulation of fatty acid me in the etiology of type 2 diabetes. Diabetes 2002; 51: 7-18.
    • (2002) Diabetes , vol.51 , pp. 7-18
    • McGarry, J.D.1
  • 132
    • 0035149738 scopus 로고    scopus 로고
    • Prolonged inhibition of muscle carnitine palmitoyltransferase-1 promotes intramyocellular lipid accumulation and insulin resistance in rats
    • Dobbins RL, Szczepaniak LS, Bentley B, Esser V, Myhill J, McGarry JD. Prolonged inhibition of muscle carnitine palmitoyltransferase-1 promotes intramyocellular lipid accumulation and insulin resistance in rats. Diabetes 2001; 50: 123-30.
    • (2001) Diabetes , vol.50 , pp. 123-130
    • Dobbins, R.L.1    Szczepaniak, L.S.2    Bentley, B.3    Esser, V.4    Myhill, J.5    McGarry, J.D.6
  • 134
    • 0033927667 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance
    • Shulman GI. Cellular mechanisms of insulin resistance. J. Clin. Invest 2000; 106: 171-6.
    • (2000) J. Clin. Invest , vol.106 , pp. 171-176
    • Shulman, G.I.1
  • 135
    • 0023868703 scopus 로고
    • Carbohydrate and lipid metabolism of skeletal muscle in type 2 diabetic patients
    • Falholt K, Jensen I, Lindkaer JS, et al. Carbohydrate and lipid metabolism of skeletal muscle in type 2 diabetic patients. Diabet Med 1988; 5: 27-31.
    • (1988) Diabet Med , vol.5 , pp. 27-31
    • Falholt, K.1    Jensen, I.2    Lindkaer, J.S.3
  • 136
    • 0030969532 scopus 로고    scopus 로고
    • Skeletal muscle triglyceride levels are inversely related to insulin action
    • Pan DA, Lillioja S, Kriketos AD, et al. Skeletal muscle triglyceride levels are inversely related to insulin action. Diabetes 1997; 46: 983-8.
    • (1997) Diabetes , vol.46 , pp. 983-988
    • Pan, D.A.1    Lillioja, S.2    Kriketos, A.D.3
  • 137
    • 0033007207 scopus 로고    scopus 로고
    • Measurement of intracellular triglyceride stores by H spectroscopy: Validation in vivo
    • Szczepaniak LS, Babcock EE, Schick F, et al. Measurement of intracellular triglyceride stores by H spectroscopy: validation in vivo. Am J Physiol 1999; 276: E977-89.
    • (1999) Am J Physiol , vol.276
    • Szczepaniak, L.S.1    Babcock, E.E.2    Schick, F.3
  • 138
    • 0035083842 scopus 로고    scopus 로고
    • Nonalcoholic steatohepatitis: Definition and pathology
    • Brunt EM. Nonalcoholic steatohepatitis: definition and pathology. Semin. Liver Dis 2001; 21(1): 3-16.
    • (2001) Semin Liver Dis , vol.21 , Issue.1 , pp. 3-16
    • Brunt, E.M.1
  • 139
    • 0033947158 scopus 로고    scopus 로고
    • Ability of insulin to modulate hepatic glucose production aging rats is impaired by fat accumulation
    • Gupta G, Cases JA, She L, et al. Ability of insulin to modulate hepatic glucose production aging rats is impaired by fat accumulation. Am J Physiol Endocrinol Metab 2000; 278: E985-91.
    • (2000) Am J Physiol Endocrinol Metab , vol.278
    • Gupta, G.1    Cases, J.A.2    She, L.3
  • 140
    • 0033958461 scopus 로고    scopus 로고
    • Decrease in triglyceride accumulation in tissues by restricted diet and improvement of diabetes in O Long-Evans Tokushima fatty rats, a non-insulindependent diabetes model
    • Man ZW, Hirashima T, Mori, S, Kawano K. Decrease in triglyceride accumulation in tissues by restricted diet and improvement of diabetes in O Long-Evans Tokushima fatty rats, a non-insulindependent diabetes model. Metabolism 2000; 49: 108-14.
    • (2000) Metabolism , vol.49 , pp. 108-114
    • Man, Z.W.1    Hirashima, T.2    Mori, S.3    Kawano, K.4
  • 141
    • 0342314436 scopus 로고    scopus 로고
    • Hepatic fat content and insulin action on free fatty acids and glucose metabolism rather than insulin absorption are associated with insulin requirements during insulin therapy in type 2 diabetic patients
    • Ryysy L, Hakkinen AM, Goto T, et al. Hepatic fat content and insulin action on free fatty acids and glucose metabolism rather than insulin absorption are associated with insulin requirements during insulin therapy in type 2 diabetic patients. Diabetes 2000; 49: 749-58.
    • (2000) Diabetes , vol.49 , pp. 749-758
    • Ryysy, L.1    Hakkinen, A.M.2    Goto, T.3
  • 142
    • 0034830055 scopus 로고    scopus 로고
    • The effect of dietary polyunsaturated fatty acid on insulin sensitivity and lipid metabolism in Otsuka Long-Evans Tokushima Fatty (OLETF) rats
    • Sasagawa T, Ishii K, Hasuda K, Kubota M, Ota Y, Okita M. The effect of dietary polyunsaturated fatty acid on insulin sensitivity and lipid metabolism in Otsuka Long-Evans Tokushima Fatty (OLETF) rats. Prostaglandins Leukot. Essent Fatty Acids 2001; 64: 181-7.
    • (2001) Prostaglandins Leukot. Essent Fatty Acids , vol.64 , pp. 181-187
    • Sasagawa, T.1    Ishii, K.2    Hasuda, K.3    Kubota, M.4    Ota, Y.5    Okita, M.6
  • 143
    • 0036312905 scopus 로고    scopus 로고
    • Fat accumulation in the liver is associated with defects in insulin suppression of glucose production and serum free fatty acids independent of obesity in normal men
    • Lindroos SA, Vehkavaara S, Hakkinen AM, et al. Fat accumulation in the liver is associated with defects in insulin suppression of glucose production and serum free fatty acids independent of obesity in normal men. J Clin Endocrinol Metab 2002; 87: 3023-8.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 3023-3028
    • Lindroos, S.A.1    Vehkavaara, S.2    Hakkinen, A.M.3
  • 145
    • 3042681042 scopus 로고    scopus 로고
    • SIRT 1 promotes fat mobilization in white adipocytes by repressing PPARγ
    • Picard F, Kurtev M, Chung N, et al. SIRT 1 promotes fat mobilization in white adipocytes by repressing PPARγ. Nature 2004; 429: 771-6.
    • (2004) Nature , vol.429 , pp. 771-776
    • Picard, F.1    Kurtev, M.2    Chung, N.3
  • 146
    • 37549052177 scopus 로고    scopus 로고
    • Identification of a domain within peroxisome proliferator activated receptor gamma regulating expression of a group of genes containing fibroblast growth factor 21 that are selectively repressed by SIRT1 in adipocytes
    • Wang H, Qiang L, Farmer SR. Identification of a domain within peroxisome proliferator activated receptor gamma regulating expression of a group of genes containing fibroblast growth factor 21 that are selectively repressed by SIRT1 in adipocytes. Mol Cell Biol 2008; 28: 188-200.
    • (2008) Mol Cell Biol , vol.28 , pp. 188-200
    • Wang, H.1    Qiang, L.2    Farmer, S.R.3
  • 147
    • 0242580872 scopus 로고    scopus 로고
    • Convergence of peroxisome proliferator activated receptor gamma and Foxo1 signaling pathways
    • Dowell P, Otto TC, Adi S, Lane MD. Convergence of peroxisome proliferator activated receptor gamma and Foxo1 signaling pathways. J Biol Chem 2003; 278: 45485-491.
    • (2003) J Biol Chem , vol.278 , pp. 45485-45491
    • Dowell, P.1    Otto, T.C.2    Adi, S.3    Lane, M.D.4
  • 148
    • 34547135428 scopus 로고    scopus 로고
    • Role of FoxO1 in FFA-induced oxidative stress in adipocytes
    • Subauste AR, Burant CF. Role of FoxO1 in FFA-induced oxidative stress in adipocytes. Am J Physiol Endocrinol Metab 2007; 293: e159-64.
    • (2007) Am J Physiol Endocrinol Metab , vol.293
    • Subauste, A.R.1    Burant, C.F.2
  • 149
    • 33845985335 scopus 로고    scopus 로고
    • SIRT1 regulates adiponectin gene expression through Foxo1 C/enhancer binding protein alpha transcriptional complex
    • Qiao L, Shao J. SIRT1 regulates adiponectin gene expression through Foxo1 C/enhancer binding protein alpha transcriptional complex. J Biol Chem 2006; 281: 39915-24.
    • (2006) J Biol Chem , vol.281 , pp. 39915-39924
    • Qiao, L.1    Shao, J.2
  • 151
    • 80555146753 scopus 로고    scopus 로고
    • Hepatic SIRT1 deficiency in mice impairs mTorc2/Akt signaling and results in hyperglycemia, oxidative damage, and insulin resistance
    • Rui HW, Kim HS, Xiao C, Xu X, Gavrilova O, Deng C. Hepatic SIRT1 deficiency in mice impairs mTorc2/Akt signaling and results in hyperglycemia, oxidative damage, and insulin resistance, J Clin Invest 2011; 121(11): 4477-90.
    • (2011) J Clin Invest , vol.121 , Issue.11 , pp. 4477-4490
    • Rui, H.W.1    Kim, H.S.2    Xiao, C.3    Xu, X.4    Gavrilova, O.5    Deng, C.6
  • 152
    • 50649112638 scopus 로고    scopus 로고
    • SIRT1 regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase
    • Hou X, Xu S, Maitland-Toolan KA, et al. SIRT1 regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase. J Biol Chem 2008; 283: 20015-26.
    • (2008) J Biol Chem , vol.283 , pp. 20015-20026
    • Hou, X.1    Xu, S.2    Maitland-Toolan, K.A.3
  • 153
    • 0043244921 scopus 로고    scopus 로고
    • SIR2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • Fulco M, Schiltz RL, Iezzi S, King MT, et al. SIR2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell 2003; 12: 51-62.
    • (2003) Mol Cell , vol.12 , pp. 51-62
    • Fulco, M.1    Schiltz, R.L.2    Iezzi, S.3    King, M.T.4
  • 154
    • 15444377466 scopus 로고    scopus 로고
    • SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1
    • Bouras T, Fu M, Sauve AA, et al. SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1. J Biol Chem 2005; 280: 10264-76.
    • (2005) J Biol Chem , vol.280 , pp. 10264-10276
    • Bouras, T.1    Fu, M.2    Sauve, A.A.3
  • 155
    • 0035957375 scopus 로고    scopus 로고
    • Restoration of insulin sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcription coactivator PGC-1
    • Michael LF, Wu Z, Cheatham RB, et al. Restoration of insulin sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcription coactivator PGC-1. Proc. Natl Acad Sci 2001; 98: 3820-5.
    • (2001) Proc. Natl Acad Sci , vol.98 , pp. 3820-3825
    • Michael, L.F.1    Wu, Z.2    Cheatham, R.B.3
  • 156
    • 34247259630 scopus 로고    scopus 로고
    • Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC-1 alpha
    • Gerhart-Hines Z, Rodgers JT, Bare O, et al. Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC-1 alpha. EMBO 2007; 26(7): 1913-23.
    • (2007) EMBO , vol.26 , Issue.7 , pp. 1913-1923
    • Gerhart-Hines, Z.1    Rodgers, J.T.2    Bare, O.3
  • 157
    • 79955661493 scopus 로고    scopus 로고
    • Hepatic overexpression of SIRT1 in mice attenuates endoplasmic reticulum stress and insulin resistance in the liver
    • Li Y, Xu S, Giles A, Nakamura K. Hepatic overexpression of SIRT1 in mice attenuates endoplasmic reticulum stress and insulin resistance in the liver. FASEB J 2011; 25: 1664-79.
    • (2011) FASEB J , vol.25 , pp. 1664-1679
    • Li, Y.1    Xu, S.2    Giles, A.3    Nakamura, K.4
  • 158
    • 84861712572 scopus 로고    scopus 로고
    • SIRT1 attenuates palmitateinduced endoplasmic reticulum stress and insulin resistance in HepG2 cells via induction of oxygen-regulated protein 150
    • Jung TW, Lee KT, Lee MW, Ka KH. SIRT1 attenuates palmitateinduced endoplasmic reticulum stress and insulin resistance in HepG2 cells via induction of oxygen-regulated protein 150. Biochem Biophys Res Commun 2012; 422: 229-32.
    • (2012) Biochem Biophys Res Commun , vol.422 , pp. 229-232
    • Jung, T.W.1    Lee, K.T.2    Lee, M.W.3    Ka, K.H.4
  • 159
    • 64049089450 scopus 로고    scopus 로고
    • SIRT2 Suppresses Adipocyte Differentiation by Deacetylating FOXO1 and Enhancing FOXO1's Repressive Interaction with PPAR-γ
    • Wang F, Tong Q. SIRT2 Suppresses Adipocyte Differentiation by Deacetylating FOXO1 and Enhancing FOXO1's Repressive Interaction with PPAR-γ, Mol Bio Cell 2009; 20: 801-8.
    • (2009) Mol Bio Cell , vol.20 , pp. 801-808
    • Wang, F.1    Tong, Q.2
  • 160
    • 80052291180 scopus 로고    scopus 로고
    • Sirtuin-3 (SIRT3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production
    • Jinga E, Emanuellia B, Hirscheyb MD, et al. Sirtuin-3 (SIRT3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. Proc Natl Acad Sci, 2011; 108(35): 14608-13.
    • (2011) Proc Natl Acad Sci , vol.108 , Issue.35 , pp. 14608-14613
    • Jinga, E.1    Emanuellia, B.2    Hirscheyb, M.D.3
  • 161
    • 82455212901 scopus 로고    scopus 로고
    • SIRT3 Deficiency and Mitochondrial Protein Hyperacetylation Accelerate the Development of the Metabolic Syndrome
    • Hirschey MD, Shimazu T, Jing E, et al. SIRT3 Deficiency and Mitochondrial Protein Hyperacetylation Accelerate the Development of the Metabolic Syndrome, Molecular Cell 2011; 44: 1-14.
    • (2011) Molecular Cell , vol.44 , pp. 1-14
    • Hirschey, M.D.1    Shimazu, T.2    Jing, E.3
  • 162
    • 77957762687 scopus 로고    scopus 로고
    • SIRT4 Regulates Fatty Acid Oxidation and Mitochondrial Gene Expression in Liver and Muscle Cells
    • Nasrin N, Wu X, Fortier E, et al. SIRT4 Regulates Fatty Acid Oxidation and Mitochondrial Gene Expression in Liver and Muscle Cells. J Bio Chem 2010; 285(42): 31995-2002
    • (2010) J Bio Chem , vol.285 , Issue.42 , pp. 31995-32002
    • Nasrin, N.1    Wu, X.2    Fortier, E.3
  • 163
    • 33748199578 scopus 로고    scopus 로고
    • Insulin secretion: SIRT4 gets in on the act
    • Argmann C, Auwerx J. Insulin secretion: SIRT4 gets in on the act. Cell 2006; 126(5): 837-9.
    • (2006) Cell , vol.126 , Issue.5 , pp. 837-839
    • Argmann, C.1    Auwerx, J.2
  • 164
    • 36349030394 scopus 로고    scopus 로고
    • Regulation Of Insulin Secretion By Sirt4, A Mitochondrial ADP-Ribosyltransferase
    • Ahuja N, Schwer B, Carobbio S, et al. Regulation Of Insulin Secretion By Sirt4, A Mitochondrial ADP-Ribosyltransferase, J Bio Chem 2007; 282: 33583-92.
    • (2007) J Bio Chem , vol.282 , pp. 33583-33592
    • Ahuja, N.1    Schwer, B.2    Carobbio, S.3
  • 165
    • 78449248442 scopus 로고    scopus 로고
    • SIRT6 Deficiency Results in Severe Hypoglycemia by Enhancing Both Basal and Insulin-stimulated Glucose Uptake in Mice
    • Xiao C, Kim HS, Lahusen T, SIRT6 Deficiency Results in Severe Hypoglycemia by Enhancing Both Basal and Insulin-stimulated Glucose Uptake in Mice. JBiol Chem 2010; 285(47): 36776-84.
    • (2010) J Biol Chem , vol.285 , Issue.47 , pp. 36776-36784
    • Xiao, C.1    Kim, H.S.2    Lahusen, T.3
  • 166
    • 84858000209 scopus 로고    scopus 로고
    • The sirtuin SIRT6 regulates lifespan in male mice
    • Kanfi Y, Naiman S, Amir G, et al. The sirtuin SIRT6 regulates lifespan in male mice. Nature 2012; 05: 3-6.
    • (2012) Nature , vol.5 , pp. 3-6
    • Kanfi, Y.1    Naiman, S.2    Amir, G.3
  • 167
    • 0028961110 scopus 로고
    • Diabetes and cardiovascular disease. The "common soil" hypothesis
    • Stern MP. Diabetes and cardiovascular disease. The "common soil" hypothesis. Diabetes 1995; 44: 369-74.
    • (1995) Diabetes , vol.44 , pp. 369-374
    • Stern, M.P.1
  • 168
    • 0035140346 scopus 로고    scopus 로고
    • Protection against oxidative stress-induced insulin resistance in rat L6 muscle cells by micro molar concentrations of lipoic acid
    • Maddux BA, See W, Lawrence JC, Goldfine AL, Goldfine ID, Evans JL. Protection against oxidative stress-induced insulin resistance in rat L6 muscle cells by micro molar concentrations of lipoic acid. Diabetes 2001; 50: 404-10.
    • (2001) Diabetes , vol.50 , pp. 404-410
    • Maddux, B.A.1    See, W.2    Lawrence, J.C.3    Goldfine, A.L.4    Goldfine, I.D.5    Evans, J.L.6
  • 169
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of alpha-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • Tretter L, Adam-Vizi V. Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of alpha-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. J Neurosci 2000; 20: 8972-79.
    • (2000) J Neurosci , vol.20 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 170
    • 0031683542 scopus 로고    scopus 로고
    • Pro-longed oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes
    • Rudich A, Tirosh A, Potashnik R, Hemi R, Kanety H, Bashan N. Pro-longed oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes. Diabetes 1998; 47: 1562-9.
    • (1998) Diabetes , vol.47 , pp. 1562-1569
    • Rudich, A.1    Tirosh, A.2    Potashnik, R.3    Hemi, R.4    Kanety, H.5    Bashan, N.6
  • 171
    • 0042804808 scopus 로고    scopus 로고
    • Increased glucose uptake promotes oxidative stress and PKC delta activation in adipocytes of obese, insulin-resistant mice
    • Talior I, Yarkoni M, Bashan N, Fielman EH. Increased glucose uptake promotes oxidative stress and PKC delta activation in adipocytes of obese, insulin-resistant mice. Am J Physiol 2003; 285: E295-302.
    • (2003) Am J Physiol , vol.285
    • Talior, I.1    Yarkoni, M.2    Bashan, N.3    Fielman, E.H.4
  • 172
    • 0032840875 scopus 로고    scopus 로고
    • Oral administration of RACalpha-lipoic acid modulates insulin sensitivity in patients with type-2 diabetes mellitus: A placebo-controlled pilot trial
    • Jacob S, Ruus P, Hermann R, et al. Oral administration of RACalpha-lipoic acid modulates insulin sensitivity in patients with type-2 diabetes mellitus: a placebo-controlled pilot trial. Free Radic Biol Med 1999; 27: 309-14.
    • (1999) Free Radic Biol Med , vol.27 , pp. 309-314
    • Jacob, S.1    Ruus, P.2    Hermann, R.3
  • 173
    • 0029742327 scopus 로고    scopus 로고
    • The antioxidant alpha-lipoic acid enhances insulin-stimulated glucose metabolism in insulinresistant rat skeletal muscle
    • Jacob S, Streeper RS, Fogt DL, et al. The antioxidant alpha-lipoic acid enhances insulin-stimulated glucose metabolism in insulinresistant rat skeletal muscle. Diabetes 1996; 45: 1024-1029.
    • (1996) Diabetes , vol.45 , pp. 1024-1029
    • Jacob, S.1    Streeper, R.S.2    Fogt, D.L.3
  • 174
    • 0036182681 scopus 로고    scopus 로고
    • Prevention of hypertension, insulin resistance and oxidative stress by a-lipoic acid
    • Midaoui A, Champlain J. Prevention of hypertension, insulin resistance and oxidative stress by a-lipoic acid. Hypertension 2002; 39: 303-7.
    • (2002) Hypertension , vol.39 , pp. 303-307
    • Midaoui, A.1    Champlain, J.2
  • 175
    • 0037154310 scopus 로고    scopus 로고
    • Antioxidative properties of acetylsalicylic acid on vascular tissues from normotensive and spontaneously hypertensive rats
    • Wu R, Lamontagne D, Champlain J. Antioxidative properties of acetylsalicylic acid on vascular tissues from normotensive and spontaneously hypertensive rats. Circulation 2002; 105: 387-92.
    • (2002) Circulation , vol.105 , pp. 387-392
    • Wu, R.1    Lamontagne, D.2    Champlain, J.3
  • 176
    • 0036628762 scopus 로고    scopus 로고
    • Prevention of hypertension, hyperglycemia and vascular oxidative stress by aspirin treatment in chronically glucose-fed rats
    • Midaoui A, Wu R, Champlain J. Prevention of hypertension, hyperglycemia and vascular oxidative stress by aspirin treatment in chronically glucose-fed rats. J Hypertens 2002; 20: 1407-12.
    • (2002) J Hypertens , vol.20 , pp. 1407-1412
    • Midaoui, A.1    Wu, R.2    Champlain, J.3
  • 177
    • 33744946526 scopus 로고    scopus 로고
    • Resveratrol, a red wine antioxidant, possesses an insulin-like effect in streptozotocin-induced diabetic rats
    • Su H, Hung L, Chen J. Resveratrol, a red wine antioxidant, possesses an insulin-like effect in streptozotocin-induced diabetic rats. Am J Physiol Endocrinol Metab 2006; 290: E1339-46.
    • (2006) Am J Physiol Endocrinol Metab , vol.290
    • Su, H.1    Hung, L.2    Chen, J.3
  • 178
    • 0030042738 scopus 로고    scopus 로고
    • Oxidative stress and insulin action. Is there a relationship?
    • Paolisso, G., Giugliano, D. Oxidative stress and insulin action. Is there a relationship? Diabetologia 1996; 39: 357-63.
    • (1996) Diabetologia , vol.39 , pp. 357-363
    • Paolisso, G.1    Giugliano, D.2
  • 179
    • 0042093769 scopus 로고    scopus 로고
    • New insights on oxidative stress and diabetic complications may lead to a 'causal' antioxidant therapy
    • Ceriello, A. New insights on oxidative stress and diabetic complications may lead to a 'causal' antioxidant therapy. Diabetes Care 2003; 26: 1589-96.
    • (2003) Diabetes Care , vol.26 , pp. 1589-1596
    • Ceriello, A.1
  • 180
    • 80054084256 scopus 로고    scopus 로고
    • Ectopic fat storage, insulin resistance, and hypertension
    • Sironi AM, Sicari R, Folli F, Gastaldelli A. Ectopic fat storage, insulin resistance, and hypertension. Curr Pharm Des 2011; 17(28): 3074-80.
    • (2011) Curr Pharm Des , vol.17 , Issue.28 , pp. 3074-3080
    • Sironi, A.M.1    Sicari, R.2    Folli, F.3    Gastaldelli, A.4
  • 181
    • 0029933643 scopus 로고    scopus 로고
    • The cellular and molecular mechanisms of diabetic complications
    • King GL, Brownlee M. The cellular and molecular mechanisms of diabetic complications. Endocrinol Metab Clin North Am 1996; 25: 255-70.
    • (1996) Endocrinol Metab Clin North Am , vol.25 , pp. 255-270
    • King, G.L.1    Brownlee, M.2
  • 182
    • 0030871260 scopus 로고    scopus 로고
    • Vascular dysfunction in diabetes mellitus
    • Fenner E, King GL, Vascular dysfunction in diabetes mellitus. Lancet 1997; 350 (1): 9-13.
    • (1997) Lancet , vol.350 , Issue.1 , pp. 9-13
    • Fenner, E.1    King, G.L.2
  • 183
    • 0027465289 scopus 로고
    • The role of oxygen radicals in human disease, with particular reference to the vascular system
    • Halliwell B. The role of oxygen radicals in human disease, with particular reference to the vascular system. Haemostasis 1993; 23(1): 118-26.
    • (1993) Haemostasis , vol.23 , Issue.1 , pp. 118-126
    • Halliwell, B.1
  • 184
    • 0028897751 scopus 로고
    • Diabetes mellitus, hypertension, and cardiovascular disease: Which role for oxidative stress?
    • Giugliano D, Ceriello A, Paolisso G. Diabetes mellitus, hypertension, and cardiovascular disease: which role for oxidative stress? Metabolism 1995; 44: 363-8.
    • (1995) Metabolism , vol.44 , pp. 363-368
    • Giugliano, D.1    Ceriello, A.2    Paolisso, G.3
  • 185
    • 0030797118 scopus 로고    scopus 로고
    • Antioxidant status in patients with uncomplicated insulin-dependent and noninsulindependent diabetes mellitus
    • Maxwell SRJ, Thomason H, Sandler D et al. Antioxidant status in patients with uncomplicated insulin-dependent and noninsulindependent diabetes mellitus. Eur J Clin Invest 1997; 27: 484-90.
    • (1997) Eur J Clin Invest , vol.27 , pp. 484-490
    • Maxwell, S.R.J.1    Thomason, H.2    Sandler, D.3
  • 187
    • 0030743527 scopus 로고    scopus 로고
    • Relationships between plasma measures of oxidative stress and metabolic control in NIDDM
    • Zadeh NJ, Rahimi A, Sarmadi TJ. Relationships between plasma measures of oxidative stress and metabolic control in NIDDM. Diabetologia 1997; 40: 647-53.
    • (1997) Diabetologia , vol.40 , pp. 647-653
    • Zadeh, N.J.1    Rahimi, A.2    Sarmadi, T.J.3
  • 189
    • 0028274304 scopus 로고
    • Free radicals in diabetic endothelial cell dysfunction
    • Tesfamariam B Free radicals in diabetic endothelial cell dysfunction. Free Radic Biol Med 1994; 16: 383-91.
    • (1994) Free Radic Biol Med , vol.16 , pp. 383-391
    • Tesfamariam, B.1
  • 190
    • 0028845524 scopus 로고
    • Treatment of symptomatic diabetic peripheral neuropathy with the antioxidant lipoic acid. A 3-week multicenter randomized controlled trial (ALADIN Study)
    • Ziegler D, Hanefeld M, Ruhnau KJ, et al. Treatment of symptomatic diabetic peripheral neuropathy with the antioxidant lipoic acid. A 3-week multicenter randomized controlled trial (ALADIN Study). Diabetologia 1995; 38: 1425-33.
    • (1995) Diabetologia , vol.38 , pp. 1425-1433
    • Ziegler, D.1    Hanefeld, M.2    Ruhnau, K.J.3
  • 192
    • 44449114217 scopus 로고    scopus 로고
    • Advanced glycation end products and insulin resistance
    • Unoki H, Yamagishi S. Advanced glycation end products and insulin resistance. Curr Pharm Des 2008; 14(10): 987-9.
    • (2008) Curr Pharm Des , vol.14 , Issue.10 , pp. 987-989
    • Unoki, H.1    Yamagishi, S.2
  • 193
    • 0030358424 scopus 로고    scopus 로고
    • Dissection of protein kinase cascades that mediate cellular response to cytokines and cellular stress
    • Cohen P. Dissection of protein kinase cascades that mediate cellular response to cytokines and cellular stress. Adv Pharmacol 1996; 36: 15-27.
    • (1996) Adv Pharmacol , vol.36 , pp. 15-27
    • Cohen, P.1
  • 194
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • Kyriakis JM, Avruch J. Sounding the alarm: protein kinase cascades activated by stress and inflammation. J Biol Chem 1996; 271: 24313-6.
    • (1996) J Biol Chem , vol.271 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 195
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • Adler V, Yin Z, Tew KD, Ronai Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene 1999; 18: 6104-11.
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 196
    • 0038314460 scopus 로고    scopus 로고
    • Oligofructose protects against the hypertriglyceridemia and prooxidative effects of a high fructose diet in rats
    • Busserolles J, Gueux E, Rock E, Demigne C, Mazur A, Rayssiguier Y. Oligofructose protects against the hypertriglyceridemia and prooxidative effects of a high fructose diet in rats. J Nutr 2003; 133: 1903-8.
    • (2003) J Nutr , vol.133 , pp. 1903-1908
    • Busserolles, J.1    Gueux, E.2    Rock, E.3    Demigne, C.4    Mazur, A.5    Rayssiguier, Y.6
  • 197
    • 13444282663 scopus 로고    scopus 로고
    • Effect of taurine on biomarkers of oxidative stress in tissues of fructose-fed insulin-resistant rats
    • Nandhini AT, Thirunavukkarasu V, Ravichandran MK, Anuradha CV. Effect of taurine on biomarkers of oxidative stress in tissues of fructose-fed insulin-resistant rats. SingaporeMed. J 2005; 46: 82-7.
    • (2005) SingaporeMed. J , vol.46 , pp. 82-87
    • Nandhini, A.T.1    Thirunavukkarasu, V.2    Ravichandran, M.K.3    Anuradha, C.V.4
  • 198
    • 37549054120 scopus 로고    scopus 로고
    • Conjugated linoleic acid and car-diac health: Oxidative stress and energetic metabolism in standard and sucrose-rich diets
    • Diniz YS, Santos PP, Assalin HB, et al. Conjugated linoleic acid and car-diac health: Oxidative stress and energetic metabolism in standard and sucrose-rich diets. Eur. J. Pharmacol 2008; 579: 318-25.
    • (2008) Eur. J. Pharmacol , vol.579 , pp. 318-325
    • Diniz, Y.S.1    Santos, P.P.2    Assalin, H.B.3
  • 199
    • 16244384612 scopus 로고    scopus 로고
    • Cardiac lipids and antioxidant status in high fructose rats and the effect of alpha-lipoic acid
    • Thirunavukkarasu V, Anitha Nandhini AT, Anuradha CV. Cardiac lipids and antioxidant status in high fructose rats and the effect of alpha-lipoic acid. Nutr Metab Cardiovasc Dis 2004; 14: 351-7.
    • (2004) Nutr Metab Cardiovasc Dis , vol.14 , pp. 351-357
    • Thirunavukkarasu, V.1    Anitha Nandhini, A.T.2    Anuradha, C.V.3
  • 201
    • 0027717694 scopus 로고
    • Free radical effects on myocardial membrane microviscosity
    • Coetzee IH, Lochner A. Free radical effects on myocardial membrane microviscosity. Cardioscience 1993; 4: 205-15.
    • (1993) Cardioscience , vol.4 , pp. 205-215
    • Coetzee, I.H.1    Lochner, A.2
  • 202
    • 0037019963 scopus 로고    scopus 로고
    • Decreasing cellular hydrogen peroxide with cata-lase mimics the effects of hypoxia on the sensitivity of the Ltype Ca2+ channel to beta-adrenergic receptor stimulation in cardiac myocytes
    • Hool LC, Arthur PG. Decreasing cellular hydrogen peroxide with cata-lase mimics the effects of hypoxia on the sensitivity of the Ltype Ca2+ channel to beta-adrenergic receptor stimulation in cardiac myocytes. Circ Res 2002; 91: 601-9.
    • (2002) Circ Res , vol.91 , pp. 601-609
    • Hool, L.C.1    Arthur, P.G.2
  • 203
    • 1942521160 scopus 로고    scopus 로고
    • H2O2 regulates recombinant Ca2+ channel alpha1C subunits but does not mediate their sensitivity to acute hypoxia
    • Hudasek K, Brown ST, Fearon IM. H2O2 regulates recombinant Ca2+ channel alpha1C subunits but does not mediate their sensitivity to acute hypoxia. Biochem. Biophys. Res. Commun 2004; 318: 135-41.
    • (2004) Biochem. Biophys. Res. Commun , vol.318 , pp. 135-141
    • Hudasek, K.1    Brown, S.T.2    Fearon, I.M.3
  • 204
    • 0033986996 scopus 로고    scopus 로고
    • Diabetes-induced metabolic abnormalities in myocardium: Effect of antioxidant therapy
    • Kowluru RA, Engerman RL, Kern TS. Diabetes-induced metabolic abnormalities in myocardium: Effect of antioxidant therapy. Free Radic Res 2000; 32: 67-74.
    • (2000) Free Radic Res , vol.32 , pp. 67-74
    • Kowluru, R.A.1    Engerman, R.L.2    Kern, T.S.3
  • 206
    • 34249037557 scopus 로고    scopus 로고
    • Oxygen free radicals in the failing myocardium
    • Tomomi I, Hisojuki J. Oxygen free radicals in the failing myocardium. Circulation Res 1999; 85: 357-63
    • (1999) Circulation Res , vol.85 , pp. 357-363
    • Tomomi, I.1    Hisojuki, J.2
  • 207
    • 0033672337 scopus 로고    scopus 로고
    • Antioxidant pyruvate inhibits cardiac formation of reactive oxygen species
    • Bassege E, Sommer O, Schwemmar M, Bunger R. Antioxidant pyruvate inhibits cardiac formation of reactive oxygen species. Am J Physiol 2000; 279: H2431-8.
    • (2000) Am J Physiol , vol.279
    • Bassege, E.1    Sommer, O.2    Schwemmar, M.3    Bunger, R.4
  • 208
    • 17544379019 scopus 로고    scopus 로고
    • Direct evidence of increased hydroxyl radical in the failing myocardium
    • Tomomi I, Tsutsui H, Kingugaw S. Direct evidence of increased hydroxyl radical in the failing myocardium. Circ Res 2000; 186: 152-7.
    • (2000) Circ Res , vol.186 , pp. 152-157
    • Tomomi, I.1    Tsutsui, H.2    Kingugaw, S.3
  • 209
    • 65649098380 scopus 로고    scopus 로고
    • Energy metabolism in the normal and in the diabetic heart
    • Barsotti A, Giannoni A, Di Napoli P, Emdin M. Energy metabolism in the normal and in the diabetic heart. Curr Pharm Des 2009; 15(8): 836-40.
    • (2009) Curr Pharm Des , vol.15 , Issue.8 , pp. 836-840
    • Barsotti, A.1    Giannoni, A.2    Di Napoli, P.3    Emdin, M.4
  • 210
    • 57349195531 scopus 로고    scopus 로고
    • Optimization of cardiac metabolism in diabetes mellitus
    • Vitale C, Collin P. Optimization of cardiac metabolism in diabetes mellitus. Curr Pharm Des 2008; 14(25): 2537-50.
    • (2008) Curr Pharm Des , vol.14 , Issue.25 , pp. 2537-2550
    • Vitale, C.1    Collin, P.2
  • 211
    • 0032191856 scopus 로고    scopus 로고
    • Insulin action and insulin resistance: Diseases involving defects in insulin receptors, signal transduction, and the glucose transport effector system
    • Hunter SJ, Garvey WT. Insulin action and insulin resistance: diseases involving defects in insulin receptors, signal transduction, and the glucose transport effector system. Am J Med 1998; 105: 331-45.
    • (1998) Am J Med , vol.105 , pp. 331-345
    • Hunter, S.J.1    Garvey, W.T.2
  • 212
    • 0028433421 scopus 로고
    • Role of insulin resistance and hyperinsulinemia in development of hypertension and atherosclerosis
    • Sowers JR, Sowers PS, Peuler JD. Role of insulin resistance and hyperinsulinemia in development of hypertension and atherosclerosis. J Lab Clin Med 1994; 123: 647-52.
    • (1994) J Lab Clin Med , vol.123 , pp. 647-652
    • Sowers, J.R.1    Sowers, P.S.2    Peuler, J.D.3
  • 213
    • 0030025673 scopus 로고    scopus 로고
    • Hypertension and associated metabolic abnormalities the role of insulin resistance and the sympathoadrenal system
    • Reaven GM, Lithell H, Landsberg L. Hypertension and associated metabolic abnormalities the role of insulin resistance and the sympathoadrenal system. N Engl J Med 1996; 334: 374-81.
    • (1996) N Engl J Med , vol.334 , pp. 374-381
    • Reaven, G.M.1    Lithell, H.2    Landsberg, L.3
  • 214
    • 61449230001 scopus 로고    scopus 로고
    • Abnormal insulin signaling: Early detection of silent coronary artery disease erectile dysfunction?
    • Potenza MA, Montagnani M. Abnormal insulin signaling: early detection of silent coronary artery disease erectile dysfunction? Curr Pharm Des 2008; 14(35): 3737-48.
    • (2008) Curr Pharm Des , vol.14 , Issue.35 , pp. 3737-3748
    • Potenza, M.A.1    Montagnani, M.2
  • 215
    • 21044443182 scopus 로고    scopus 로고
    • Diabetic vascular complications: Pathophysiology, biochemical basis and potential therapeutic strategy
    • Yamagishi S, Imaizumi T. Diabetic vascular complications: pathophysiology, biochemical basis and potential therapeutic strategy. Curr Pharm Des 2005; 11(18): 2279-99.
    • (2005) Curr Pharm Des , vol.11 , Issue.18 , pp. 2279-2299
    • Yamagishi, S.1    Imaizumi, T.2
  • 216
    • 0021928037 scopus 로고
    • Insulin as a growth factor
    • Hill DJ, Milner RD. Insulin as a growth factor. Pediatr Res 1985; 19: 879-86.
    • (1985) Pediatr Res , vol.19 , pp. 879-886
    • Hill, D.J.1    Milner, R.D.2
  • 217
    • 0027336865 scopus 로고
    • Insulin-like growth factor-I induces hypertrophy with enhanced expression of muscle specific genes in cultured rat cardiomyocytes
    • Ito H, Hiroe M, Hirata Y, et al. Insulin-like growth factor-I induces hypertrophy with enhanced expression of muscle specific genes in cultured rat cardiomyocytes. Circulation 1993; 87: 1715-21.
    • (1993) Circulation , vol.87 , pp. 1715-1721
    • Ito, H.1    Hiroe, M.2    Hirata, Y.3
  • 218
    • 78149409465 scopus 로고    scopus 로고
    • Mitochondrial biogenesis in the metabolic syndrome and cardiovascular disease
    • Ren J, Pulakat L, Whaley-Connell A, Sowers JR. Mitochondrial biogenesis in the metabolic syndrome and cardiovascular disease. J Mol Med 2010; 88: 993-1001.
    • (2010) J Mol Med , vol.88 , pp. 993-1001
    • Ren, J.1    Pulakat, L.2    Whaley-Connell, A.3    Sowers, J.R.4
  • 219
    • 0022639077 scopus 로고
    • Superoxide dismutase plus catalase improve contractile function in the canine model of the "stunned myocardium"
    • Przyklenk K, Kloner RA. Superoxide dismutase plus catalase improve contractile function in the canine model of the "stunned myocardium". Circ Res 1986; 58: 148-56.
    • (1986) Circ Res , vol.58 , pp. 148-156
    • Przyklenk, K.1    Kloner, R.A.2
  • 220
    • 33646519886 scopus 로고    scopus 로고
    • Cardiac overexpression of catalase rescues cardiac contractile dysfunction induced by insulin resistance: Role of oxidative stress, protein carbonyl formation and insulin sensitivity
    • Dong F, Fang CX, Yang X, Zhang X, Lopez FL, Ren J. Cardiac overexpression of catalase rescues cardiac contractile dysfunction induced by insulin resistance: Role of oxidative stress, protein carbonyl formation and insulin sensitivity. Diabetologia 2006; 49: 1421-33.
    • (2006) Diabetologia , vol.49 , pp. 1421-1433
    • Dong, F.1    Fang, C.X.2    Yang, X.3    Zhang, X.4    Lopez, F.L.5    Ren, J.6
  • 222
    • 78349299491 scopus 로고    scopus 로고
    • Surprising sirtuin crosstalk in the heart
    • Schug TT, Li X. Surprising sirtuin crosstalk in the heart. Aging 2010; 2(3): 129-32.
    • (2010) Aging , vol.2 , Issue.3 , pp. 129-132
    • Schug, T.T.1    Li, X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.