메뉴 건너뛰기




Volumn 6, Issue 3, 2011, Pages

Neuronal sirt3 protects against excitotoxic injury in mouse cortical neuron culture

Author keywords

[No Author keywords available]

Indexed keywords

N METHYL DEXTRO ASPARTIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; REACTIVE OXYGEN METABOLITE; SIRTUIN 3; SMALL INTERFERING RNA; N METHYLASPARTIC ACID; NEUROTOXIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; SIRT3 PROTEIN, MOUSE;

EID: 79952353862     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0014731     Document Type: Article
Times cited : (153)

References (71)
  • 1
    • 0019829662 scopus 로고
    • Relationships among local functional activity, energy metabolism, and blood flow in the central nervous system
    • Sokoloff L, (1981) Relationships among local functional activity, energy metabolism, and blood flow in the central nervous system. Fed Proc 40: 2311-2316.
    • (1981) Fed Proc , vol.40 , pp. 2311-2316
    • Sokoloff, L.1
  • 2
    • 0036043866 scopus 로고    scopus 로고
    • Energetics and oxidative stress in synaptic plasticity and neurodegenerative disorders
    • Mattson MP, Liu D, (2002) Energetics and oxidative stress in synaptic plasticity and neurodegenerative disorders. Neuromolecular Med 2: 215-231.
    • (2002) Neuromolecular Med , vol.2 , pp. 215-231
    • Mattson, M.P.1    Liu, D.2
  • 3
    • 0038043242 scopus 로고    scopus 로고
    • Intra-mitochondrial poly(ADP-ribosylation) contributes to NAD+ depletion and cell death induced by oxidative stress
    • Du L, Zhang X, Han YY, Burke NA, Kochanek PM, et al. (2003) Intra-mitochondrial poly(ADP-ribosylation) contributes to NAD+ depletion and cell death induced by oxidative stress. J Biol Chem 278: 18426-18433.
    • (2003) J Biol Chem , vol.278 , pp. 18426-18433
    • Du, L.1    Zhang, X.2    Han, Y.Y.3    Burke, N.A.4    Kochanek, P.M.5
  • 4
    • 33846404132 scopus 로고    scopus 로고
    • Pyruvate improves recovery after PARP-1-associated energy failure induced by oxidative stress in neonatal rat cerebrocortical slices
    • Zeng J, Yang GY, Ying W, Kelly M, Hirai K, et al. (2007) Pyruvate improves recovery after PARP-1-associated energy failure induced by oxidative stress in neonatal rat cerebrocortical slices. J Cereb Blood Flow Metab 27: 304-315.
    • (2007) J Cereb Blood Flow Metab , vol.27 , pp. 304-315
    • Zeng, J.1    Yang, G.Y.2    Ying, W.3    Kelly, M.4    Hirai, K.5
  • 5
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Araki T, Sasaki Y, Milbrandt J, (2004) Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305: 1010-1013.
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 6
    • 23744474976 scopus 로고    scopus 로고
    • A local mechanism mediates NAD-dependent protection of axon degeneration
    • Wang J, Zhai Q, Chen Y, Lin E, Gu W, et al. (2005) A local mechanism mediates NAD-dependent protection of axon degeneration. J Cell Biol 170: 349-355.
    • (2005) J Cell Biol , vol.170 , pp. 349-355
    • Wang, J.1    Zhai, Q.2    Chen, Y.3    Lin, E.4    Gu, W.5
  • 7
    • 33751095946 scopus 로고    scopus 로고
    • Neuroprotective effects of NU1025, a PARP inhibitor in cerebral ischemia are mediated through reduction in NAD depletion and DNA fragmentation
    • Kaundal RK, Shah KK, Sharma SS, (2006) Neuroprotective effects of NU1025, a PARP inhibitor in cerebral ischemia are mediated through reduction in NAD depletion and DNA fragmentation. Life Sci 79: 2293-2302.
    • (2006) Life Sci , vol.79 , pp. 2293-2302
    • Kaundal, R.K.1    Shah, K.K.2    Sharma, S.S.3
  • 8
    • 34248375793 scopus 로고    scopus 로고
    • Intranasal administration with NAD+ profoundly decreases brain injury in a rat model of transient focal ischemia
    • Ying W, Wei G, Wang D, Wang Q, Tang X, et al. (2007) Intranasal administration with NAD+ profoundly decreases brain injury in a rat model of transient focal ischemia. Front Biosci 12: 2728-2734.
    • (2007) Front Biosci , vol.12 , pp. 2728-2734
    • Ying, W.1    Wei, G.2    Wang, D.3    Wang, Q.4    Tang, X.5
  • 9
    • 57649217303 scopus 로고    scopus 로고
    • Preventing NAD(+) depletion protects neurons against excitotoxicity: bioenergetic effects of mild mitochondrial uncoupling and caloric restriction
    • Liu D, Pitta M, Mattson MP, (2008) Preventing NAD(+) depletion protects neurons against excitotoxicity: bioenergetic effects of mild mitochondrial uncoupling and caloric restriction. Ann N Y Acad Sci 1147: 275-282.
    • (2008) Ann N Y Acad Sci , vol.1147 , pp. 275-282
    • Liu, D.1    Pitta, M.2    Mattson, M.P.3
  • 10
    • 52449091282 scopus 로고    scopus 로고
    • Cellular NAD replenishment confers marked neuroprotection against ischemic cell death: role of enhanced DNA repair
    • Wang S, Xing Z, Vosler PS, Yin H, Li W, et al. (2008) Cellular NAD replenishment confers marked neuroprotection against ischemic cell death: role of enhanced DNA repair. Stroke 39: 2587-2595.
    • (2008) Stroke , vol.39 , pp. 2587-2595
    • Wang, S.1    Xing, Z.2    Vosler, P.S.3    Yin, H.4    Li, W.5
  • 11
    • 77449120223 scopus 로고    scopus 로고
    • Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway
    • Pillai VB, Sundaresan NR, Kim G, Gupta M, Rajamohan SB, et al. (2010) Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway. J Biol Chem 285: 3133-3144.
    • (2010) J Biol Chem , vol.285 , pp. 3133-3144
    • Pillai, V.B.1    Sundaresan, N.R.2    Kim, G.3    Gupta, M.4    Rajamohan, S.B.5
  • 12
    • 79952319919 scopus 로고    scopus 로고
    • Nmnat2 delays axon degeneration in superior cervical ganglia dependent on its NAD synthesis activity
    • Yan T, Feng Y, Zheng J, Ge X, Zhang Y, et al. (2009) Nmnat2 delays axon degeneration in superior cervical ganglia dependent on its NAD synthesis activity. Neurochem Int.
    • (2009) Neurochem Int
    • Yan, T.1    Feng, Y.2    Zheng, J.3    Ge, X.4    Zhang, Y.5
  • 13
    • 0030842946 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia
    • Eliasson MJ, Sampei K, Mandir AS, Hurn PD, Traystman RJ, et al. (1997) Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia. Nat Med 3: 1089-1095.
    • (1997) Nat Med , vol.3 , pp. 1089-1095
    • Eliasson, M.J.1    Sampei, K.2    Mandir, A.S.3    Hurn, P.D.4    Traystman, R.J.5
  • 14
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D, Desnoyers S, D'Silva I, Poirier GG, (1999) Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem J 342: 249-268.
    • (1999) Biochem J , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 15
    • 33845317242 scopus 로고    scopus 로고
    • Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death
    • Yu SW, Andrabi SA, Wang H, Kim NS, Poirier GG, et al. (2006) Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death. Proc Natl Acad Sci U S A 103: 18314-18319.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18314-18319
    • Yu, S.W.1    Andrabi, S.A.2    Wang, H.3    Kim, N.S.4    Poirier, G.G.5
  • 16
    • 65249173918 scopus 로고    scopus 로고
    • Nicotinamide prevents NAD+ depletion and protects neurons against excitotoxicity and cerebral ischemia: NAD+ consumption by SIRT1 may endanger energetically compromised neurons
    • Liu D, Gharavi R, Pitta M, Gleichmann M, Mattson MP, (2009) Nicotinamide prevents NAD+ depletion and protects neurons against excitotoxicity and cerebral ischemia: NAD+ consumption by SIRT1 may endanger energetically compromised neurons. Neuromolecular Med 11: 28-42.
    • (2009) Neuromolecular Med , vol.11 , pp. 28-42
    • Liu, D.1    Gharavi, R.2    Pitta, M.3    Gleichmann, M.4    Mattson, M.P.5
  • 17
    • 0035834146 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death
    • Ying W, Sevigny MB, Chen Y, Swanson RA, (2001) Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death. Proc Natl Acad Sci U S A 98: 12227-12232.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12227-12232
    • Ying, W.1    Sevigny, M.B.2    Chen, Y.3    Swanson, R.A.4
  • 18
    • 0037067317 scopus 로고    scopus 로고
    • Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor
    • Yu SW, Wang H, Poitras MF, Coombs C, Bowers WJ, et al. (2002) Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor. Science 297: 259-263.
    • (2002) Science , vol.297 , pp. 259-263
    • Yu, S.W.1    Wang, H.2    Poitras, M.F.3    Coombs, C.4    Bowers, W.J.5
  • 19
    • 2442624618 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1-mediated cell death in astrocytes requires NAD+ depletion and mitochondrial permeability transition
    • Alano CC, Ying W, Swanson RA, (2004) Poly(ADP-ribose) polymerase-1-mediated cell death in astrocytes requires NAD+ depletion and mitochondrial permeability transition. J Biol Chem 279: 18895-18902.
    • (2004) J Biol Chem , vol.279 , pp. 18895-18902
    • Alano, C.C.1    Ying, W.2    Swanson, R.A.3
  • 20
    • 35848932089 scopus 로고    scopus 로고
    • Differences among cell types in NAD(+) compartmentalization: a comparison of neurons, astrocytes, and cardiac myocytes
    • Alano CC, Tran A, Tao R, Ying W, Karliner JS, et al. (2007) Differences among cell types in NAD(+) compartmentalization: a comparison of neurons, astrocytes, and cardiac myocytes. J Neurosci Res 85: 3378-3385.
    • (2007) J Neurosci Res , vol.85 , pp. 3378-3385
    • Alano, C.C.1    Tran, A.2    Tao, R.3    Ying, W.4    Karliner, J.S.5
  • 21
    • 77649133016 scopus 로고    scopus 로고
    • NAD+ depletion is necessary and sufficient for poly(ADP-ribose) polymerase-1-mediated neuronal death
    • Alano CC, Garnier P, Ying W, Higashi Y, Kauppinen TM, et al. (2010) NAD+ depletion is necessary and sufficient for poly(ADP-ribose) polymerase-1-mediated neuronal death. J Neurosci 30: 2967-2978.
    • (2010) J Neurosci , vol.30 , pp. 2967-2978
    • Alano, C.C.1    Garnier, P.2    Ying, W.3    Higashi, Y.4    Kauppinen, T.M.5
  • 22
    • 78751643428 scopus 로고    scopus 로고
    • Minocycline Protects Cardiac Myocytes Against Simulated Ischemia-Reperfusion Injury by Inhibiting Poly(ADP-ribose) Polymerase-1
    • Tao R, Kim SH, Honbo N, Karliner JS, Alano CC, (2010) Minocycline Protects Cardiac Myocytes Against Simulated Ischemia-Reperfusion Injury by Inhibiting Poly(ADP-ribose) Polymerase-1. J Cardiovasc Pharmacol.
    • (2010) J Cardiovasc Pharmacol
    • Tao, R.1    Kim, S.H.2    Honbo, N.3    Karliner, J.S.4    Alano, C.C.5
  • 23
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye RA, (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273: 793-798.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 24
    • 0024536650 scopus 로고
    • A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA
    • Gottlieb S, Esposito RE, (1989) A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA. Cell 56: 771-776.
    • (1989) Cell , vol.56 , pp. 771-776
    • Gottlieb, S.1    Esposito, R.E.2
  • 25
    • 0029591894 scopus 로고
    • Silencing and heritable domains of gene expression
    • Loo S, Rine J, (1995) Silencing and heritable domains of gene expression. Annu Rev Cell Dev Biol 11: 519-548.
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 519-548
    • Loo, S.1    Rine, J.2
  • 26
    • 0032750220 scopus 로고    scopus 로고
    • Diverse and dynamic functions of the Sir silencing complex
    • Guarente L, (1999) Diverse and dynamic functions of the Sir silencing complex. Nat Genet 23: 281-285.
    • (1999) Nat Genet , vol.23 , pp. 281-285
    • Guarente, L.1
  • 27
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny JC, Dowd GJ, Huang J, Hilz H, Moazed D, (1999) An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99: 735-745.
    • (1999) Cell , vol.99 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 28
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I, (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell 16: 4623-4635.
    • (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
  • 29
    • 0032831936 scopus 로고    scopus 로고
    • Modulation of life-span by histone deacetylase genes in Saccharomyces cerevisiae
    • Kim S, Benguria A, Lai CY, Jazwinski SM, (1999) Modulation of life-span by histone deacetylase genes in Saccharomyces cerevisiae. Mol Biol Cell 10: 3125-3136.
    • (1999) Mol Biol Cell , vol.10 , pp. 3125-3136
    • Kim, S.1    Benguria, A.2    Lai, C.Y.3    Jazwinski, S.M.4
  • 30
    • 0037130175 scopus 로고    scopus 로고
    • Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
    • Lin SJ, Kaeberlein M, Andalis AA, Sturtz LA, Defossez PA, et al. (2002) Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration. Nature 418: 344-348.
    • (2002) Nature , vol.418 , pp. 344-348
    • Lin, S.J.1    Kaeberlein, M.2    Andalis, A.A.3    Sturtz, L.A.4    Defossez, P.A.5
  • 31
    • 30044440497 scopus 로고    scopus 로고
    • Sirt1: a metabolic master switch that modulates lifespan
    • Leibiger IB, Berggren PO, (2006) Sirt1: a metabolic master switch that modulates lifespan. Nat Med 12: 34-36; discussion 36.
    • (2006) Nat Med , vol.12
    • Leibiger, I.B.1    Berggren, P.O.2
  • 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, (2006) Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci U S A 103: 10224-10229.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 33
    • 34547875773 scopus 로고    scopus 로고
    • Sirtuins: critical regulators at the crossroads between cancer and aging
    • Saunders LR, Verdin E, (2007) Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene 26: 5489-5504.
    • (2007) Oncogene , vol.26 , pp. 5489-5504
    • Saunders, L.R.1    Verdin, E.2
  • 34
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling
    • Chen J, Zhou Y, Mueller-Steiner S, Chen LF, Kwon H, et al. (2005) SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling. J Biol Chem 280: 40364-40374.
    • (2005) J Biol Chem , vol.280 , pp. 40364-40374
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3    Chen, L.F.4    Kwon, H.5
  • 35
    • 34447308268 scopus 로고    scopus 로고
    • SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis
    • Kim D, Nguyen MD, Dobbin MM, Fischer A, Sananbenesi F, et al. (2007) SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. EMBO J 26: 3169-3179.
    • (2007) EMBO J , vol.26 , pp. 3169-3179
    • Kim, D.1    Nguyen, M.D.2    Dobbin, M.M.3    Fischer, A.4    Sananbenesi, F.5
  • 36
    • 10744232772 scopus 로고    scopus 로고
    • Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly
    • Rose G, Dato S, Altomare K, Bellizzi D, Garasto S, et al. (2003) Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly. Exp Gerontol 38: 1065-1070.
    • (2003) Exp Gerontol , vol.38 , pp. 1065-1070
    • Rose, G.1    Dato, S.2    Altomare, K.3    Bellizzi, D.4    Garasto, S.5
  • 37
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi T, Wang F, Stieren E, Tong Q, (2005) SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J Biol Chem 280: 13560-13567.
    • (2005) J Biol Chem , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 38
    • 55749084738 scopus 로고    scopus 로고
    • A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • Ahn BH, Kim HS, Song S, Lee IH, Liu J, et al. (2008) A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc Natl Acad Sci U S A 105: 14447-14452.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 14447-14452
    • Ahn, B.H.1    Kim, H.S.2    Song, S.3    Lee, I.H.4    Liu, J.5
  • 39
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows WC, Lee S, Denu JM, (2006) Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc Natl Acad Sci U S A 103: 10230-10235.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 40
    • 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, et al. (2009) Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J Clin Invest 119: 2758-2771.
    • (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
  • 41
    • 0029065517 scopus 로고
    • Potentiated necrosis of cultured cortical neurons by neurotrophins
    • Koh JY, Gwag BJ, Lobner D, Choi DW, (1995) Potentiated necrosis of cultured cortical neurons by neurotrophins. Science 268: 573-575.
    • (1995) Science , vol.268 , pp. 573-575
    • Koh, J.Y.1    Gwag, B.J.2    Lobner, D.3    Choi, D.W.4
  • 42
    • 0031041530 scopus 로고    scopus 로고
    • Slowly triggered excitotoxicity occurs by necrosis in cortical cultures
    • Gwag BJ, Koh JY, DeMaro JA, Ying HS, Jacquin M, et al. (1997) Slowly triggered excitotoxicity occurs by necrosis in cortical cultures. Neuroscience 77: 393-401.
    • (1997) Neuroscience , vol.77 , pp. 393-401
    • Gwag, B.J.1    Koh, J.Y.2    DeMaro, J.A.3    Ying, H.S.4    Jacquin, M.5
  • 43
    • 33748068133 scopus 로고    scopus 로고
    • Blockade of PARP activity attenuates poly(ADP-ribosyl)ation but offers only partial neuroprotection against NMDA-induced cell death in the rat retina
    • Goebel DJ, Winkler BS, (2006) Blockade of PARP activity attenuates poly(ADP-ribosyl)ation but offers only partial neuroprotection against NMDA-induced cell death in the rat retina. J Neurochem 98: 1732-1745.
    • (2006) J Neurochem , vol.98 , pp. 1732-1745
    • Goebel, D.J.1    Winkler, B.S.2
  • 44
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, Sweeney LB, Sturgill JF, Chua KF, Greer PL, et al. (2004) Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 303: 2011-2015.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3    Chua, K.F.4    Greer, P.L.5
  • 46
    • 53549105529 scopus 로고    scopus 로고
    • SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70
    • Sundaresan NR, Samant SA, Pillai VB, Rajamohan SB, Gupta MP, (2008) SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol Cell Biol 28: 6384-6401.
    • (2008) Mol Cell Biol , vol.28 , pp. 6384-6401
    • Sundaresan, N.R.1    Samant, S.A.2    Pillai, V.B.3    Rajamohan, S.B.4    Gupta, M.P.5
  • 47
    • 0035860724 scopus 로고    scopus 로고
    • Intracellular delivery of proteins with a new lipid-mediated delivery system
    • Zelphati O, Wang Y, Kitada S, Reed JC, Felgner PL, et al. (2001) Intracellular delivery of proteins with a new lipid-mediated delivery system. J Biol Chem 276: 35103-35110.
    • (2001) J Biol Chem , vol.276 , pp. 35103-35110
    • Zelphati, O.1    Wang, Y.2    Kitada, S.3    Reed, J.C.4    Felgner, P.L.5
  • 48
    • 37549002891 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
    • Lombard DB, Alt FW, Cheng HL, Bunkenborg J, Streeper RS, et al. (2007) Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol Cell Biol 27: 8807-8814.
    • (2007) Mol Cell Biol , vol.27 , pp. 8807-8814
    • Lombard, D.B.1    Alt, F.W.2    Cheng, H.L.3    Bunkenborg, J.4    Streeper, R.S.5
  • 49
    • 0030597992 scopus 로고    scopus 로고
    • Inhibition of free radical production or free radical scavenging protects from the excitotoxic cell death mediated by glutamate in cultures of cerebellar granule neurons
    • Ciani E, Groneng L, Voltattorni M, Rolseth V, Contestabile A, et al. (1996) Inhibition of free radical production or free radical scavenging protects from the excitotoxic cell death mediated by glutamate in cultures of cerebellar granule neurons. Brain Res 728: 1-6.
    • (1996) Brain Res , vol.728 , pp. 1-6
    • Ciani, E.1    Groneng, L.2    Voltattorni, M.3    Rolseth, V.4    Contestabile, A.5
  • 50
    • 0033061920 scopus 로고    scopus 로고
    • Oxidative stress, mitochondrial function, and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Castilho RF, Ward MW, Nicholls DG, (1999) Oxidative stress, mitochondrial function, and acute glutamate excitotoxicity in cultured cerebellar granule cells. J Neurochem 72: 1394-1401.
    • (1999) J Neurochem , vol.72 , pp. 1394-1401
    • Castilho, R.F.1    Ward, M.W.2    Nicholls, D.G.3
  • 51
    • 0035865259 scopus 로고    scopus 로고
    • Exploration of the role of reactive oxygen species in glutamate neurotoxicity in rat hippocampal neurones in culture
    • Vergun O, Sobolevsky AI, Yelshansky MV, Keelan J, Khodorov BI, et al. (2001) Exploration of the role of reactive oxygen species in glutamate neurotoxicity in rat hippocampal neurones in culture. J Physiol 531: 147-163.
    • (2001) J Physiol , vol.531 , pp. 147-163
    • Vergun, O.1    Sobolevsky, A.I.2    Yelshansky, M.V.3    Keelan, J.4    Khodorov, B.I.5
  • 52
    • 37249047093 scopus 로고    scopus 로고
    • Ca2+-dependent generation of mitochondrial reactive oxygen species serves as a signal for poly(ADP-ribose) polymerase-1 activation during glutamate excitotoxicity
    • Duan Y, Gross RA, Sheu SS, (2007) Ca2+-dependent generation of mitochondrial reactive oxygen species serves as a signal for poly(ADP-ribose) polymerase-1 activation during glutamate excitotoxicity. J Physiol 585: 741-758.
    • (2007) J Physiol , vol.585 , pp. 741-758
    • Duan, Y.1    Gross, R.A.2    Sheu, S.S.3
  • 53
    • 67649800742 scopus 로고    scopus 로고
    • NADPH oxidase is the primary source of superoxide induced by NMDA receptor activation
    • Brennan AM, Suh SW, Won SJ, Narasimhan P, Kauppinen TM, et al. (2009) NADPH oxidase is the primary source of superoxide induced by NMDA receptor activation. Nat Neurosci 12: 857-863.
    • (2009) Nat Neurosci , vol.12 , pp. 857-863
    • Brennan, A.M.1    Suh, S.W.2    Won, S.J.3    Narasimhan, P.4    Kauppinen, T.M.5
  • 54
    • 0034987156 scopus 로고    scopus 로고
    • Effect of poly(ADP-ribose) polymerase inhibitors on the ischemia-reperfusion-induced oxidative cell damage and mitochondrial metabolism in Langendorff heart perfusion system
    • Halmosi R, Berente Z, Osz E, Toth K, Literati-Nagy P, et al. (2001) Effect of poly(ADP-ribose) polymerase inhibitors on the ischemia-reperfusion-induced oxidative cell damage and mitochondrial metabolism in Langendorff heart perfusion system. Mol Pharmacol 59: 1497-1505.
    • (2001) Mol Pharmacol , vol.59 , pp. 1497-1505
    • Halmosi, R.1    Berente, Z.2    Osz, E.3    Toth, K.4    Literati-Nagy, P.5
  • 56
    • 0041573041 scopus 로고    scopus 로고
    • NAD+ repletion prevents PARP-1-induced glycolytic blockade and cell death in cultured mouse astrocytes
    • Ying W, Garnier P, Swanson RA, (2003) NAD+ repletion prevents PARP-1-induced glycolytic blockade and cell death in cultured mouse astrocytes. Biochem Biophys Res Commun 308: 809-813.
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 809-813
    • Ying, W.1    Garnier, P.2    Swanson, R.A.3
  • 57
    • 33745457705 scopus 로고    scopus 로고
    • Minocycline inhibits poly(ADP-ribose) polymerase-1 at nanomolar concentrations
    • Alano CC, Kauppinen TM, Valls AV, Swanson RA, (2006) Minocycline inhibits poly(ADP-ribose) polymerase-1 at nanomolar concentrations. Proc Natl Acad Sci U S A 103: 9685-9690.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9685-9690
    • Alano, C.C.1    Kauppinen, T.M.2    Valls, A.V.3    Swanson, R.A.4
  • 58
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer B, North BJ, Frye RA, Ott M, Verdin E, (2002) The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol 158: 647-657.
    • (2002) J Cell Biol , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 59
    • 34548627517 scopus 로고    scopus 로고
    • Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival
    • Yang H, Yang T, Baur JA, Perez E, Matsui T, et al. (2007) Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival. Cell 130: 1095-1107.
    • (2007) Cell , vol.130 , pp. 1095-1107
    • Yang, H.1    Yang, T.2    Baur, J.A.3    Perez, E.4    Matsui, T.5
  • 60
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz KT, Bitterman KJ, Cohen HY, Lamming DW, Lavu S, et al. (2003) Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425: 191-196.
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1    Bitterman, K.J.2    Cohen, H.Y.3    Lamming, D.W.4    Lavu, S.5
  • 61
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra MT, Smith BC, Denu JM, (2005) Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 280: 17187-17195.
    • (2005) J Biol Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 62
    • 58149339917 scopus 로고    scopus 로고
    • Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity
    • Pfister JA, Ma C, Morrison BE, D'Mello SR, (2008) Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity. PLoS One 3: e4090.
    • (2008) PLoS One , vol.3
    • Pfister, J.A.1    Ma, C.2    Morrison, B.E.3    D'Mello, S.R.4
  • 63
    • 34247271282 scopus 로고    scopus 로고
    • SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress
    • Scher MB, Vaquero A, Reinberg D, (2007) SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev 21: 920-928.
    • (2007) Genes Dev , vol.21 , pp. 920-928
    • Scher, M.B.1    Vaquero, A.2    Reinberg, D.3
  • 64
    • 63749099484 scopus 로고    scopus 로고
    • A new splice variant of the mouse SIRT3 gene encodes the mitochondrial precursor protein
    • Cooper HM, Huang JY, Verdin E, Spelbrink JN, (2009) A new splice variant of the mouse SIRT3 gene encodes the mitochondrial precursor protein. PLoS One 4: e4986.
    • (2009) PLoS One , vol.4
    • Cooper, H.M.1    Huang, J.Y.2    Verdin, E.3    Spelbrink, J.N.4
  • 65
    • 78049299600 scopus 로고    scopus 로고
    • Characterization of murine SIRT3 transcript variants and corresponding protein products
    • Yang Y, Hubbard BP, Sinclair DA, Tong Q, (2010) Characterization of murine SIRT3 transcript variants and corresponding protein products. J Cell Biochem 111: 1051-1058.
    • (2010) J Cell Biochem , vol.111 , pp. 1051-1058
    • Yang, Y.1    Hubbard, B.P.2    Sinclair, D.A.3    Tong, Q.4
  • 66
  • 67
    • 42449132299 scopus 로고    scopus 로고
    • The human SIRT3 protein deacetylase is exclusively mitochondrial
    • Cooper HM, Spelbrink JN, (2008) The human SIRT3 protein deacetylase is exclusively mitochondrial. Biochem J 411: 279-285.
    • (2008) Biochem J , vol.411 , pp. 279-285
    • Cooper, H.M.1    Spelbrink, J.N.2
  • 68
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • Hirschey MD, Shimazu T, Goetzman E, Jing E, Schwer B, et al. (2010) SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 464: 121-125.
    • (2010) Nature , vol.464 , pp. 121-125
    • Hirschey, M.D.1    Shimazu, T.2    Goetzman, E.3    Jing, E.4    Schwer, B.5
  • 69
    • 0036488223 scopus 로고    scopus 로고
    • Mitochondrial permeability transition and calcium dynamics in striatal neurons upon intense NMDA receptor activation
    • Alano CC, Beutner G, Dirksen RT, Gross RA, Sheu SS, (2002) Mitochondrial permeability transition and calcium dynamics in striatal neurons upon intense NMDA receptor activation. J Neurochem 80: 531-538.
    • (2002) J Neurochem , vol.80 , pp. 531-538
    • Alano, C.C.1    Beutner, G.2    Dirksen, R.T.3    Gross, R.A.4    Sheu, S.S.5
  • 70
    • 74049094817 scopus 로고    scopus 로고
    • SIRT3 Is a Mitochondria-Localized Tumor Suppressor Required for Maintenance of Mitochondrial Integrity and Metabolism during Stress
    • Kim HS, Patel K, Muldoon-Jacobs K, Bisht KS, Aykin-Burns N, et al. (2010) SIRT3 Is a Mitochondria-Localized Tumor Suppressor Required for Maintenance of Mitochondrial Integrity and Metabolism during Stress. Cancer Cell 17: 41-52.
    • (2010) Cancer Cell , vol.17 , pp. 41-52
    • Kim, H.S.1    Patel, K.2    Muldoon-Jacobs, K.3    Bisht, K.S.4    Aykin-Burns, N.5
  • 71
    • 34748877230 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone preserves mitochondrial function and prevents oxidative injury in adult rat cardiac myocytes
    • Tao R, Karliner JS, Simonis U, Zheng J, Zhang J, et al. (2007) Pyrroloquinoline quinone preserves mitochondrial function and prevents oxidative injury in adult rat cardiac myocytes. Biochem Biophys Res Commun 363: 257-262.
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 257-262
    • Tao, R.1    Karliner, J.S.2    Simonis, U.3    Zheng, J.4    Zhang, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.