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Volumn 17, Issue 1, 2012, Pages 28-46

NAD + metabolism and oxidative stress: The golden nucleotide on a crown of thorns

Author keywords

Ageing; NAD+; Oxidative stress; PARP; Sirtuins

Indexed keywords

HYDROGEN PEROXIDE; HYDROXYL RADICAL; KYNURENINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; POLY(ADENOSINE DIPHOSPHATE RIBOSE); REACTIVE OXYGEN METABOLITE; SINGLET OXYGEN; SIRTUIN; SUPEROXIDE;

EID: 84857286276     PISSN: 13510002     EISSN: 17432928     Source Type: Journal    
DOI: 10.1179/1351000212Y.0000000001     Document Type: Review
Times cited : (114)

References (200)
  • 1
    • 0002679866 scopus 로고
    • Relation of nicotinic acid and nicotinic acid amide to canine black tongue
    • Elvehjem C, Madden R, Strong F, Woolley D. Relation of nicotinic acid and nicotinic acid amide to canine black tongue. J Am Chem Soc 1937;59:1767-8.
    • (1937) J Am Chem Soc , vol.59 , pp. 1767-1768
    • Elvehjem, C.1    Madden, R.2    Strong, F.3    Woolley, D.4
  • 2
    • 63849188090 scopus 로고
    • Pellagra-a deficiency disease
    • Elvehjem C. Pellagra-a deficiency disease. Proc Am Philos Soc 1949;93:335-9.
    • (1949) Proc Am Philos Soc , vol.93 , pp. 335-339
    • Elvehjem, C.1
  • 3
    • 14644386887 scopus 로고    scopus 로고
    • Neutral amino acid transport in epithelial cells and its malfunction in Hartnup disorder
    • Broer S, Ja C, Rasko J. Neutral amino acid transport in epithelial cells and its malfunction in Hartnup disorder. Biochem Soc Trans 2005;33:233-6.
    • (2005) Biochem Soc Trans , vol.33 , pp. 233-236
    • Broer, S.1    Ja, C.2    Rasko, J.3
  • 5
    • 0017253138 scopus 로고
    • Topically applied niacinamide in ioniazid-induced pellagra
    • Comaish J, Felix R, McGrath H. Topically applied niacinamide in ioniazid-induced pellagra. Arch Dermatol 1976;112:70-2.
    • (1976) Arch Dermatol , vol.112 , pp. 70-72
    • Comaish, J.1    Felix, R.2    McGrath, H.3
  • 6
    • 34247182736 scopus 로고    scopus 로고
    • Pharmacological targeting of IDO-mediated tolerance for treating autoimmune disease
    • Penberthy WT. Pharmacological targeting of IDO-mediated tolerance for treating autoimmune disease. Curr Drug Metab 2007;8:245-66.
    • (2007) Curr Drug Metab , vol.8 , pp. 245-266
    • Penberthy, W.T.1
  • 7
    • 0025949160 scopus 로고
    • Implications of interferon-induced tryptophan catabolism in cancer, auto-immune diseases and AIDS
    • Brown RR, Ozaki Y, Datta SP, Borden EC, Sondel PM, Malone DG. Implications of interferon-induced tryptophan catabolism in cancer, auto-immune diseases and AIDS. Adv Exp Med Biol 1991;294:425-35.
    • (1991) Adv Exp Med Biol , vol.294 , pp. 425-435
    • Brown, R.R.1    Ozaki, Y.2    Datta, S.P.3    Borden, E.C.4    Sondel, P.M.5    Malone, D.G.6
  • 10
    • 0011863707 scopus 로고
    • Pyridin, der wasserstoffubertragende Bestandteil von Garungsfermenten (Pyridin-Nucleotide)
    • Warburg O, Christian W. Pyridin, der wasserstoffubertragende Bestandteil von Garungsfermenten (Pyridin-Nucleotide). Biochem Z 1936;287:291-328.
    • (1936) Biochem Z , vol.287 , pp. 291-328
    • Warburg, O.1    Christian, W.2
  • 11
    • 52049117617 scopus 로고    scopus 로고
    • Enzymology of mammalian NAD metabolism in health and disease
    • Magni G, Orsomando G, Raffelli N, Ruggieri S. Enzymology of mammalian NAD metabolism in health and disease. Front Biosci 2008;13:6135-54.
    • (2008) Front Biosci , vol.13 , pp. 6135-6154
    • Magni, G.1    Orsomando, G.2    Raffelli, N.3    Ruggieri, S.4
  • 12
    • 84957353129 scopus 로고
    • The participation of inorganic pyrophosphate in the reversible enzymatic synthesis of diphosphopyridine nucleotide
    • Kornberg A. The participation of inorganic pyrophosphate in the reversible enzymatic synthesis of diphosphopyridine nucleotide. J Biol Chem 1948;176:1475-6.
    • (1948) J Biol Chem , vol.176 , pp. 1475-1476
    • Kornberg, A.1
  • 13
    • 0036918074 scopus 로고    scopus 로고
    • Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis
    • Rizzi M, Schindelin H. Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis. Curr Opin Struct Biol 2002;12:709-20.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 709-720
    • Rizzi, M.1    Schindelin, H.2
  • 14
    • 0002160618 scopus 로고
    • Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesising nuclear enzyme
    • Chambon P, Weill J, Mandel P. Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesising nuclear enzyme. Biochem Biophys Res Commun 1963;11: 39-43.
    • (1963) Biochem Biophys Res Commun , vol.11 , pp. 39-43
    • Chambon, P.1    Weill, J.2    Mandel, P.3
  • 15
    • 0014029054 scopus 로고
    • The pyridine nucleotide cycle
    • Gholson RK. The pyridine nucleotide cycle. Nature 1966;212: 933-4.
    • (1966) Nature , vol.212 , pp. 933-934
    • Gholson, R.K.1
  • 16
    • 0016370994 scopus 로고
    • The biosynthesis and turnover of nicotinamide adenine dinucleotide in enucleated culture cells
    • Rechsteiner M, Catanzarite V. The biosynthesis and turnover of nicotinamide adenine dinucleotide in enucleated culture cells. J Cell Physiol 1974;84:409-22.
    • (1974) J Cell Physiol , vol.84 , pp. 409-422
    • Rechsteiner, M.1    Catanzarite, V.2
  • 19
    • 34248357083 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery
    • Khan JA, Forouhar F, Tao X, Tong L. Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery. Expert Opin Ther Targets 2007;11:695-705.
    • (2007) Expert Opin Ther Targets , vol.11 , pp. 695-705
    • Khan, J.A.1    Forouhar, F.2    Tao, X.3    Tong, L.4
  • 20
    • 77953631698 scopus 로고    scopus 로고
    • The secret life of NAD+: An old metabolite controlling new metabolic signaling pathways
    • Houtkooper R, Canto C, Wanders R, Auwerx J. The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways. Endocr Rev 2010;31:194-223.
    • (2010) Endocr Rev , vol.31 , pp. 194-223
    • Houtkooper, R.1    Canto, C.2    Wanders, R.3    Auwerx, J.4
  • 21
    • 55249118587 scopus 로고    scopus 로고
    • Promotion of cellular NAD+ anabolism: Therapeutic potential for oxidative stress in ageing and Alzheimer's disease
    • Braidy N, Guillemin G, Grant R. Promotion of cellular NAD+ anabolism: therapeutic potential for oxidative stress in ageing and Alzheimer's disease. Neurotox Res 2008;13:173-84.
    • (2008) Neurotox Res , vol.13 , pp. 173-184
    • Braidy, N.1    Guillemin, G.2    Grant, R.3
  • 24
    • 0034850590 scopus 로고    scopus 로고
    • Lipopolysaccharide induction of indoleamine 2,3-dioxygenase is mediated dominantly by an IFN-gamma-independent mechanism
    • Fujigaki S, Saito K, Sekikawa K, Tone S, Takikawa O, Fujii H, et al. Lipopolysaccharide induction of indoleamine 2,3-dioxygenase is mediated dominantly by an IFN-gamma-independent mechanism. Eur J Immunol 2001;31:2313-8.
    • (2001) Eur J Immunol , vol.31 , pp. 2313-2318
    • Fujigaki, S.1    Saito, K.2    Sekikawa, K.3    Tone, S.4    Takikawa, O.5    Fujii, H.6
  • 26
    • 34147115208 scopus 로고    scopus 로고
    • HIV-1 inhibits CD4+ T cell proliferation by inducing indoleamine 2,3-dioxygenase in plasmacytoid dendritic cells
    • Boasso A, Herbeuval JP, Hardy AW, Anderson SA, Dolan MJ, Fuchs D, et al. HIV-1 inhibits CD4+ T cell proliferation by inducing indoleamine 2,3-dioxygenase in plasmacytoid dendritic cells. Blood 2006;109:3351-9.
    • (2006) Blood , vol.109 , pp. 3351-3359
    • Boasso, A.1    Herbeuval, J.P.2    Hardy, A.W.3    Anderson, S.A.4    Dolan, M.J.5    Fuchs, D.6
  • 28
    • 0000429092 scopus 로고
    • Reduced triphophopyridinenucleotide requirement for the enzymatic formation of 3-hydroxykynurenine from L-kynurenine
    • De Castro F, Price J, Brown R. Reduced triphophopyridinenucleotide requirement for the enzymatic formation of 3-hydroxykynurenine from L-kynurenine. J Am Chem Soc 1956;78: 2904-5.
    • (1956) J Am Chem Soc , vol.78 , pp. 2904-2905
    • de Castro, F.1    Price, J.2    Brown, R.3
  • 29
    • 0000474008 scopus 로고
    • The kynurenine transaminase of rat kidney
    • Mason M. The kynurenine transaminase of rat kidney. J Biol Chem 1954;211:839-44.
    • (1954) J Biol Chem , vol.211 , pp. 839-844
    • Mason, M.1
  • 30
    • 0004399763 scopus 로고
    • Uber den Abbau von Kynurenin, Oxykynurenin und verwandten Substanzen durch Rattenleberenzym
    • Wiss O, Fuchs H. Uber den Abbau von Kynurenin, Oxykynurenin und verwandten Substanzen durch Rattenleberenzym. Experientia (Basel) 1950;6:472-3.
    • (1950) Experientia (Basel) , vol.6 , pp. 472-473
    • Wiss, O.1    Fuchs, H.2
  • 31
    • 0006210815 scopus 로고
    • 3-Hydroxyanthranilic acid metabolism. IV. Spectrophotometric evidence for the formation of an intermediate
    • Bokman AH, Schweigert BS. 3-Hydroxyanthranilic acid metabolism. IV. Spectrophotometric evidence for the formation of an intermediate. Arch Biochem Biophys 1951;33:270-6.
    • (1951) Arch Biochem Biophys , vol.33 , pp. 270-276
    • Bokman, A.H.1    Schweigert, B.S.2
  • 32
    • 0000515044 scopus 로고
    • Studies with carboxyl-labelled 3-hydroxyanthranilic acid and picolinic acid in vivo and in vitro
    • Mehler A, May F. Studies with carboxyl-labelled 3-hydroxyanthranilic acid and picolinic acid in vivo and in vitro. J Biol Chem 1956;223:449-55.
    • (1956) J Biol Chem , vol.223 , pp. 449-455
    • Mehler, A.1    May, F.2
  • 33
    • 0037066148 scopus 로고    scopus 로고
    • Quinolinate phosphoribosyltransferase: Kinetic mechanism for a type II PRTase
    • Cao H, Pietrak BL, Grubmeyer C. Quinolinate phosphoribosyltransferase: kinetic mechanism for a type II PRTase. Biochemistry 2002;41:3520-8.
    • (2002) Biochemistry , vol.41 , pp. 3520-3528
    • Cao, H.1    Pietrak, B.L.2    Grubmeyer, C.3
  • 34
    • 0023876882 scopus 로고
    • Quinolinic acid effects on amino acid release from the rat cerebral cortex in vitro and in vivo
    • Connick JH, Stone TW. Quinolinic acid effects on amino acid release from the rat cerebral cortex in vitro and in vivo. Br J Pharmacol 1988;93:868-76.
    • (1988) Br J Pharmacol , vol.93 , pp. 868-876
    • Connick, J.H.1    Stone, T.W.2
  • 35
    • 0032441894 scopus 로고    scopus 로고
    • Modulation of N-methyl-D-aspartate receptor function by glycine transport
    • Bergeron R, Meyer TM, Coyle JT, Greene RW. Modulation of N-methyl-D-aspartate receptor function by glycine transport. Proc Natl Acad Sci USA 1998;95:15730-4.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15730-15734
    • Bergeron, R.1    Meyer, T.M.2    Coyle, J.T.3    Greene, R.W.4
  • 37
    • 59449090534 scopus 로고    scopus 로고
    • Age and circadian influences on picolinic acid concentrations in human cerebrospinal fluid
    • Coggan S, Smythe G, Bilgin A, Grant R. Age and circadian influences on picolinic acid concentrations in human cerebrospinal fluid. J Neurochem 2009;108:1220-5.
    • (2009) J Neurochem , vol.108 , pp. 1220-1225
    • Coggan, S.1    Smythe, G.2    Bilgin, A.3    Grant, R.4
  • 38
    • 1042268020 scopus 로고    scopus 로고
    • 3-Hydroxykynurenine and quinolinate: Pathogenic synergism in early grade Huntington's disease?
    • Guidetti P, Schwarcz R. 3-Hydroxykynurenine and quinolinate: pathogenic synergism in early grade Huntington's disease? Adv Exp Med Biol 2003;527:137-45.
    • (2003) Adv Exp Med Biol , vol.527 , pp. 137-145
    • Guidetti, P.1    Schwarcz, R.2
  • 39
    • 17744374079 scopus 로고    scopus 로고
    • 3-Hydroxyanthranilic acid, an L-tryptophan metabolite, induces apoptosis in monocyte-derived cells stimulated by interferon-gamma
    • Morita T, Saito K, Takemura M, Maekawa N, Fujigaki S, Fujii H, et al. 3-Hydroxyanthranilic acid, an L-tryptophan metabolite, induces apoptosis in monocyte-derived cells stimulated by interferon-gamma. Ann Clin Biochem 2001;38:242-51.
    • (2001) Ann Clin Biochem , vol.38 , pp. 242-251
    • Morita, T.1    Saito, K.2    Takemura, M.3    Maekawa, N.4    Fujigaki, S.5    Fujii, H.6
  • 40
    • 35948955851 scopus 로고    scopus 로고
    • Mass spectrometric detection of quinolinic acid in microdissected Alzheimer's disease plaques
    • In: Takai K, (ed.), Elsevier B.V., Amsterdam
    • Guillemin GJ, Brew BJ, Noonan CE, Knight TG, Smythe GA, Cullen KM. Mass spectrometric detection of quinolinic acid in microdissected Alzheimer's disease plaques. In: Takai K, (ed.) International Congress Series. 2007. Elsevier B.V., Amsterdam. p. 404-8.
    • (2007) International Congress Series , pp. 404-408
    • Guillemin, G.J.1    Brew, B.J.2    Noonan, C.E.3    Knight, T.G.4    Smythe, G.A.5    Cullen, K.M.6
  • 41
  • 42
    • 0036378826 scopus 로고    scopus 로고
    • Implications of the kynurenine pathway and quinolinic acid in Alzheimer's disease
    • Guillemin GJ, Brew BJ. Implications of the kynurenine pathway and quinolinic acid in Alzheimer's disease. Redox Rep 2002;7:199-206.
    • (2002) Redox Rep , vol.7 , pp. 199-206
    • Guillemin, G.J.1    Brew, B.J.2
  • 43
    • 35948957337 scopus 로고    scopus 로고
    • Chronic HIV infection leads to an Alzheimer's disease like illness. Involvement of the kynurenine pathway
    • In: Takai K, (ed.), Elsevier B.V., Amsterdam
    • Guillemin GJ, Brew BJ. Chronic HIV infection leads to an Alzheimer's disease like illness. Involvement of the kynurenine pathway. In: Takai K, (ed.) International Congress Series. 2007. Elsevier B.V., Amsterdam. p. 324-34.
    • (2007) International Congress Series , pp. 324-334
    • Guillemin, G.J.1    Brew, B.J.2
  • 44
    • 15844427653 scopus 로고    scopus 로고
    • Involvement of quinolinic acid in AIDS dementia complex
    • Guillemin GJ, Kerr SJ, Brew BJ. Involvement of quinolinic acid in AIDS dementia complex. Neurotox Res 2005;7:103-23.
    • (2005) Neurotox Res , vol.7 , pp. 103-123
    • Guillemin, G.J.1    Kerr, S.J.2    Brew, B.J.3
  • 46
    • 33744781601 scopus 로고    scopus 로고
    • Implications for the kynurenine pathway and quinolinic acid in amyotrophic lateral sclerosis
    • Guillemin G, Meininger V, Brew B. Implications for the kynurenine pathway and quinolinic acid in amyotrophic lateral sclerosis. Neurodegener Dis 2006;2:166-76.
    • (2006) Neurodegener Dis , vol.2 , pp. 166-176
    • Guillemin, G.1    Meininger, V.2    Brew, B.3
  • 47
    • 0035808849 scopus 로고    scopus 로고
    • Kynurenine 3-mono-oxygenase activity and neurotoxic kynureninemetabolites increase in the spinal cord of ratswith experimental allergic encephalomyelitis
    • Chiarugi A, Cozzi A, Ballerini C, Massacesi L, Moroni F. Kynurenine 3-mono-oxygenase activity and neurotoxic kynureninemetabolites increase in the spinal cord of ratswith experimental allergic encephalomyelitis. Neuroscience 2001;102:687-95.
    • (2001) Neuroscience , vol.102 , pp. 687-695
    • Chiarugi, A.1    Cozzi, A.2    Ballerini, C.3    Massacesi, L.4    Moroni, F.5
  • 48
    • 0026043565 scopus 로고
    • Chronic quinolinic acid lesions in rats closely resemble Huntington's disease
    • Beal MF, Ferrante RJ, Swartz KJ, Kowall NW. Chronic quinolinic acid lesions in rats closely resemble Huntington's disease. J Neurosci 1991;11:1649-59.
    • (1991) J Neurosci , vol.11 , pp. 1649-1659
    • Beal, M.F.1    Ferrante, R.J.2    Swartz, K.J.3    Kowall, N.W.4
  • 49
    • 0026554440 scopus 로고
    • Kynurenic acid concentrations are reduced in Huntington's disease cerebral cortex
    • Beal MF, Matson WR, Storey E, Milbury P, Ryan EA, Ogawa T, et al. Kynurenic acid concentrations are reduced in Huntington's disease cerebral cortex. J Neurol Sci 1992;108: 80-7.
    • (1992) J Neurol Sci , vol.108 , pp. 80-87
    • Beal, M.F.1    Matson, W.R.2    Storey, E.3    Milbury, P.4    Ryan, E.A.5    Ogawa, T.6
  • 50
    • 34248335693 scopus 로고    scopus 로고
    • Elevations of endogenous kynurenic acid produce spatial working memory deficits
    • Chess AC, Simoni MK, Alling TE, Bucci DJ. Elevations of endogenous kynurenic acid produce spatial working memory deficits. Schizophrenia Bull 2007;33:797-804.
    • (2007) Schizophrenia Bull , vol.33 , pp. 797-804
    • Chess, A.C.1    Simoni, M.K.2    Alling, T.E.3    Bucci, D.J.4
  • 51
    • 0742323784 scopus 로고    scopus 로고
    • The kynurenine pathway of tryptophan degradation as a drug target
    • Schwarcz R. The kynurenine pathway of tryptophan degradation as a drug target. Curr Opin Pharmacol 2004;4:12-7.
    • (2004) Curr Opin Pharmacol , vol.4 , pp. 12-17
    • Schwarcz, R.1
  • 52
    • 0033998033 scopus 로고    scopus 로고
    • Induction of indolamine 2,3-dioxygenase in primary human macrophages by human immunodeficiency virus type 1 is strain dependent
    • Grant RS, Naif H, Thuruthyil SJ, Nasr N, Littlejohn T, Takikawa O, et al. Induction of indolamine 2,3-dioxygenase in primary human macrophages by human immunodeficiency virus type 1 is strain dependent. J Virol 2000;74:4110-5.
    • (2000) J Virol , vol.74 , pp. 4110-4115
    • Grant, R.S.1    Naif, H.2    Thuruthyil, S.J.3    Nasr, N.4    Littlejohn, T.5    Takikawa, O.6
  • 54
    • 0023013615 scopus 로고
    • Tryptophan degredation in mice initiated by indoleamine 2,3-dioxygenase
    • Takikawa O, Yoshida R, Kido R, Hayaishi O. Tryptophan degredation in mice initiated by indoleamine 2,3-dioxygenase. J Biol Chem 1986;261:3648-53.
    • (1986) J Biol Chem , vol.261 , pp. 3648-3653
    • Takikawa, O.1    Yoshida, R.2    Kido, R.3    Hayaishi, O.4
  • 55
    • 7944224888 scopus 로고    scopus 로고
    • Increased expression of indoleamine 2,3-dioxygenase in murine malaria infection is predominantly localised to the vascular endothelium
    • Hansen AM, Ball HJ, Mitchell AJ, Miu J, Takikawa O, Hunt NH. Increased expression of indoleamine 2,3-dioxygenase in murine malaria infection is predominantly localised to the vascular endothelium. Int J Parasitol 2004;34:1309-19.
    • (2004) Int J Parasitol , vol.34 , pp. 1309-1319
    • Hansen, A.M.1    Ball, H.J.2    Mitchell, A.J.3    Miu, J.4    Takikawa, O.5    Hunt, N.H.6
  • 57
    • 0035995944 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase expression in transplanted NOD Islets prolongs graft surviva; after adoptive transfer of diabetogenic splenocytes
    • Alexander A, Crawford M, Bertera S, Rudert W, Takikawa O, Robbin P, et al. Indoleamine 2,3-dioxygenase expression in transplanted NOD Islets prolongs graft surviva; after adoptive transfer of diabetogenic splenocytes. Diabetes 2002;51:356-65.
    • (2002) Diabetes , vol.51 , pp. 356-365
    • Alexander, A.1    Crawford, M.2    Bertera, S.3    Rudert, W.4    Takikawa, O.5    Robbin, P.6
  • 59
    • 0142137237 scopus 로고    scopus 로고
    • Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase
    • Uyttenhove C, Pilotte L, Theate I, Stroobant V, Colau D, Parmentier N, et al. Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Nat Med 2003;9:1269-74.
    • (2003) Nat Med , vol.9 , pp. 1269-1274
    • Uyttenhove, C.1    Pilotte, L.2    Theate, I.3    Stroobant, V.4    Colau, D.5    Parmentier, N.6
  • 60
  • 61
    • 0033485301 scopus 로고    scopus 로고
    • Evidence for increased de novo synthesis of NAD in immuneactivated RAW264.7 macrophages: A self-protective mechanism?
    • Grant RS, Passey R, Matanovic G, Smythe G, Kapoor V. Evidence for increased de novo synthesis of NAD in immuneactivated RAW264.7 macrophages: a self-protective mechanism? Arch Biochem Biophys 1999;372:1-7.
    • (1999) Arch Biochem Biophys , vol.372 , pp. 1-7
    • Grant, R.S.1    Passey, R.2    Matanovic, G.3    Smythe, G.4    Kapoor, V.5
  • 62
    • 0033915898 scopus 로고    scopus 로고
    • IDO induction in IFN-gamma activated astroglia: A role in improving cell viability during oxidative stress
    • Grant RS, Naif H, Espinosa M, Kapoor V. IDO induction in IFN-gamma activated astroglia: a role in improving cell viability during oxidative stress. Redox Rep 2000;5:101-4.
    • (2000) Redox Rep , vol.5 , pp. 101-104
    • Grant, R.S.1    Naif, H.2    Espinosa, M.3    Kapoor, V.4
  • 63
    • 0042762821 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase activity in IFN-gamma stimulated astroglioma cells decreases intracellular NAD levels
    • Grant R, Kapoor V. Inhibition of indoleamine 2,3-dioxygenase activity in IFN-gamma stimulated astroglioma cells decreases intracellular NAD levels. Biochem Pharmacol 2003;66:1033-6.
    • (2003) Biochem Pharmacol , vol.66 , pp. 1033-1036
    • Grant, R.1    Kapoor, V.2
  • 66
    • 33745817828 scopus 로고    scopus 로고
    • Molecular basis for inhibition of human NMPRTase, a novel target for anticancer agents
    • Khan JA, Tao X, Tong L. Molecular basis for inhibition of human NMPRTase, a novel target for anticancer agents. Nat Struct Mol Biol 2006;13:582-8.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 582-588
    • Khan, J.A.1    Tao, X.2    Tong, L.3
  • 67
    • 0039301347 scopus 로고    scopus 로고
    • Kinetic mechanism of nicotinic acid phosphoribosyltransferase: Implications for energy coupling
    • Gross J, Rajavel M, Grubmeyer C. Kinetic mechanism of nicotinic acid phosphoribosyltransferase: implications for energy coupling. Biochem 1998;37:4189-99.
    • (1998) Biochem , vol.37 , pp. 4189-4199
    • Gross, J.1    Rajavel, M.2    Grubmeyer, C.3
  • 68
    • 2342550554 scopus 로고    scopus 로고
    • Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Priess-Handler independent route to NAD+ in fungi and humans
    • Bieganowski P, Brenner C. Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Priess-Handler independent route to NAD+ in fungi and humans. Cell 2004;117:495-502.
    • (2004) Cell , vol.117 , pp. 495-502
    • Bieganowski, P.1    Brenner, C.2
  • 69
    • 0033766731 scopus 로고    scopus 로고
    • Tiazofurine ICN Pharmaceuticals
    • Grifantini M. Tiazofurine ICN Pharmaceuticals. Curr Opin Invest Drugs 2000;1:257-62.
    • (2000) Curr Opin Invest Drugs , vol.1 , pp. 257-262
    • Grifantini, M.1
  • 70
    • 0141538207 scopus 로고    scopus 로고
    • Nicotinamide offers multiple protective mechanisms in stroke as a precursor for NAD+, as a PARP inhibitor and by partial restoration of mitochondrial function
    • Klaidman L, Morales M, Kem S, Yang J, Chang M, Adams J, Jr. Nicotinamide offers multiple protective mechanisms in stroke as a precursor for NAD+, as a PARP inhibitor and by partial restoration of mitochondrial function. Pharmacology 2003;69:150-7.
    • (2003) Pharmacology , vol.69 , pp. 150-157
    • Klaidman, L.1    Morales, M.2    Kem, S.3    Yang, J.4    Chang, M.5    Adams Jr., J.6
  • 71
    • 33646021946 scopus 로고    scopus 로고
    • Facilitation of glutamate release by nicotine involves the activation of Ca2+/calmodulin signaling pathway in rat prefrontal cortex nerve terminals
    • Wang B, Liao W, Chang C, Wang S. Facilitation of glutamate release by nicotine involves the activation of Ca2+/calmodulin signaling pathway in rat prefrontal cortex nerve terminals. Synapse 2006;59:491-501.
    • (2006) Synapse , vol.59 , pp. 491-501
    • Wang, B.1    Liao, W.2    Chang, C.3    Wang, S.4
  • 72
    • 34247502715 scopus 로고    scopus 로고
    • Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+
    • Belenky P, Racette F, Bogan KL, McClure J, Smith J, Brenner C. Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell 2005;129:473-84.
    • (2005) Cell , vol.129 , pp. 473-484
    • Belenky, P.1    Racette, F.2    Bogan, K.L.3    McClure, J.4    Smith, J.5    Brenner, C.6
  • 75
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D. Aging: a theory based on free radical and radiation chemistry. J Gerontol 1956;11:298-300.
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 76
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Bechman K, Ames B. The free radical theory of aging matures. Physiol Rev 1998;78:547-81.
    • (1998) Physiol Rev , vol.78 , pp. 547-581
    • Bechman, K.1    Ames, B.2
  • 77
    • 79952158836 scopus 로고    scopus 로고
    • Comparative studies of oxidative stress and mitochondrial function in aging
    • Shi Y, Buffenstein R, Pulliam D, Van R. Comparative studies of oxidative stress and mitochondrial function in aging. Integr Comp Biol 2010;50:869-79.
    • (2010) Integr Comp Biol , vol.50 , pp. 869-879
    • Shi, Y.1    Buffenstein, R.2    Pulliam, D.3    Van, R.4
  • 78
    • 79251497324 scopus 로고    scopus 로고
    • Oxidative stress action in cellular aging
    • OliveiraM, Schoffen J. Oxidative stress action in cellular aging. Braz Arch Biol Tech 2010;53:1333-42.
    • (2010) Braz Arch Biol Tech , vol.53 , pp. 1333-1342
    • Oliveira, M.1    Schoffen, J.2
  • 79
    • 50949112045 scopus 로고    scopus 로고
    • The oxidative stress theory of aging:Embattled or invincible? Insights from non-traditional model organisms
    • Buffenstein R, Edrey Y, Yang T, Mele J. The oxidative stress theory of aging:embattled or invincible? Insights from non-traditional model organisms. AGE 2008;30:99-109.
    • (2008) AGE , vol.30 , pp. 99-109
    • Buffenstein, R.1    Edrey, Y.2    Yang, T.3    Mele, J.4
  • 80
    • 2542612966 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and independent components of aging
    • Koc A, Gasch A, Rutherford J, Kim H, Gladyshev V. Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and independent components of aging. Proc Natl Acad Sci 2004;101:7999-8004.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 7999-8004
    • Koc, A.1    Gasch, A.2    Rutherford, J.3    Kim, H.4    Gladyshev, V.5
  • 81
    • 0036182865 scopus 로고    scopus 로고
    • Aging in fungi: Role of mitochondria in Podospora anserina
    • Osiewacz H. Aging in fungi: role of mitochondria in Podospora anserina. Mech Ageing Dev 2002;123:755-64.
    • (2002) Mech Ageing Dev , vol.123 , pp. 755-764
    • Osiewacz, H.1
  • 82
    • 0034676493 scopus 로고    scopus 로고
    • Effects of antioxidant enzymes in molecular control of reactive oxygen species toxicology
    • Mates JM. Effects of antioxidant enzymes in molecular control of reactive oxygen species toxicology. Toxicology 2000;153: 83-104.
    • (2000) Toxicology , vol.153 , pp. 83-104
    • Mates, J.M.1
  • 83
    • 0013686380 scopus 로고    scopus 로고
    • β-Amyloid and oxidative stress in the pathogenesis of Alzheimer's disease
    • In: Basu T, Temple N, Garg M, (eds.), Oxford: CABI Publishing
    • Martin R, Chan C, Veurink G, Laws S, Croft K, Dharmarajan A. β-Amyloid and oxidative stress in the pathogenesis of Alzheimer's disease. In: Basu T, Temple N, Garg M, (eds.) Antioxidants in human health and disease. Oxford: CABI Publishing; 1999.
    • (1999) Antioxidants in human health and disease
    • Martin, R.1    Chan, C.2    Veurink, G.3    Laws, S.4    Croft, K.5    Dharmarajan, A.6
  • 84
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • DrogeW. Free radicals in the physiological control of cell function. Physiol Rev 2002;82:47-95.
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Droge, W.1
  • 85
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy M. How mitochondria produce reactive oxygen species. Biochem J 2009;417:1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.1
  • 87
    • 0028659210 scopus 로고
    • Active oxygen mechanisms of UV inflammation
    • Pentland A. Active oxygen mechanisms of UV inflammation. Adv Exp Med Biol 1994;366:87-97.
    • (1994) Adv Exp Med Biol , vol.366 , pp. 87-97
    • Pentland, A.1
  • 88
    • 0028882439 scopus 로고
    • Association between criteria air pollutants and asthma
    • Koren H. Association between criteria air pollutants and asthma. Environ Health Perspect 1995;103:235-42.
    • (1995) Environ Health Perspect , vol.103 , pp. 235-242
    • Koren, H.1
  • 89
    • 0031695866 scopus 로고    scopus 로고
    • Role of oxygen radical and lipid peroxidation in indomethacin-induced gastric mucosal injury
    • Naito Y, Yoshikawa M, Yoshida A, Kondo M. Role of oxygen radical and lipid peroxidation in indomethacin-induced gastric mucosal injury. Dig Dis Sci 1998;43: 30S-4S.
    • (1998) Dig Dis Sci , vol.43
    • Naito, Y.1    Yoshikawa, M.2    Yoshida, A.3    Kondo, M.4
  • 90
    • 0035020198 scopus 로고    scopus 로고
    • Evaluation of UV-induced superoxide radical generation potential of some common antibiotics
    • Rav R, Mehrotra S, Shanker U, Babu G, Joshi P, Hanss R. Evaluation of UV-induced superoxide radical generation potential of some common antibiotics. Drug Chem Toxicol 2001;24: 191-200.
    • (2001) Drug Chem Toxicol , vol.24 , pp. 191-200
    • Rav, R.1    Mehrotra, S.2    Shanker, U.3    Babu, G.4    Joshi, P.5    Hanss, R.6
  • 91
    • 0035816351 scopus 로고    scopus 로고
    • Release of dopamine by perfusion with 1-methyl-4-phenylpyridinium ion (MPP(+) into the striatum is associated with hydroxyl free radical production generation
    • Obata T, Yamanaka Y, Kinemuchi H, Oreland L. Release of dopamine by perfusion with 1-methyl-4-phenylpyridinium ion (MPP(+) into the striatum is associated with hydroxyl free radical production generation. Brain Res 2001;906:170-5.
    • (2001) Brain Res , vol.906 , pp. 170-175
    • Obata, T.1    Yamanaka, Y.2    Kinemuchi, H.3    Oreland, L.4
  • 92
    • 0036867895 scopus 로고    scopus 로고
    • Oxidation of biological systems: Oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification
    • Kohen R, Nyska A. Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification. Toxicol Pathol 2001;30:620-50.
    • (2001) Toxicol Pathol , vol.30 , pp. 620-650
    • Kohen, R.1    Nyska, A.2
  • 94
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals
    • Davis K. Protein damage and degradation by oxygen radicals. J Biol Chem 1987;262:9895-901.
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davis, K.1
  • 95
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidised proteins in mammalian cells
    • Grune T, Reinheckei T, Davies K. Degradation of oxidised proteins in mammalian cells. FASEB J 1997;11:526-34.
    • (1997) FASEB J , vol.11 , pp. 526-534
    • Grune, T.1    Reinheckei, T.2    Davies, K.3
  • 96
    • 1842788079 scopus 로고    scopus 로고
    • Cerebrospinal fluid levels of free 3-nitrotyrosine are not elevated in the majority of patients with amyotrophic lateral sclerosis or Alzheimer's disease
    • Ryberg H, Soderling AS, Davidsson P, Blennow K, Caidahl K, Persson LI. Cerebrospinal fluid levels of free 3-nitrotyrosine are not elevated in the majority of patients with amyotrophic lateral sclerosis or Alzheimer's disease. Neurochem Int 2004;45:57-62.
    • (2004) Neurochem Int , vol.45 , pp. 57-62
    • Ryberg, H.1    Soderling, A.S.2    Davidsson, P.3    Blennow, K.4    Caidahl, K.5    Persson, L.I.6
  • 97
    • 0026773281 scopus 로고
    • Oxygen radicals as key mediators in neurological disease: Fact or fiction?
    • Halliwell B. Oxygen radicals as key mediators in neurological disease: Fact or fiction? Ann Neurol 1992;32:S10-15.
    • (1992) Ann Neurol , vol.32
    • Halliwell, B.1
  • 98
    • 0034796353 scopus 로고    scopus 로고
    • Role of free radicals in the neurodegenerative diseases: Therapeutic implications for antioxidant treatment
    • Halliwell B. Role of free radicals in the neurodegenerative diseases: therapeutic implications for antioxidant treatment. Drugs Aging 2001;18:685-716.
    • (2001) Drugs Aging , vol.18 , pp. 685-716
    • Halliwell, B.1
  • 99
    • 0035319295 scopus 로고    scopus 로고
    • Accumulation of 8-oxo-2′-deoxyguanosine and increased expression of hMTH1 protein in brain tumors
    • Iida T, Furuta A, Kawashima M, Nishida J, Nakabeppu Y, Iwaki T. Accumulation of 8-oxo-2′-deoxyguanosine and increased expression of hMTH1 protein in brain tumors. Neuro-oncol 2001;3:73-81.
    • (2001) Neuro-oncol , vol.3 , pp. 73-81
    • Iida, T.1    Furuta, A.2    Kawashima, M.3    Nishida, J.4    Nakabeppu, Y.5    Iwaki, T.6
  • 100
    • 39049195244 scopus 로고    scopus 로고
    • Constitutive histone H2AX phosphorylation on Ser-139 in cells untreated by genotoxic agents is cell-cycle phase specific and attenuated by scavenging reactive oxygen species
    • Huang X, Tanaka T, Kurose A, Traganos F, Darzynkiewicz Z. Constitutive histone H2AX phosphorylation on Ser-139 in cells untreated by genotoxic agents is cell-cycle phase specific and attenuated by scavenging reactive oxygen species. Int J Oncol 2006;29:495-501.
    • (2006) Int J Oncol , vol.29 , pp. 495-501
    • Huang, X.1    Tanaka, T.2    Kurose, A.3    Traganos, F.4    Darzynkiewicz, Z.5
  • 101
    • 34548417690 scopus 로고    scopus 로고
    • Cytometry of ATM activation and histone H2AX phosphorylation to estimate extent of DNA damage induced by exogenous agents
    • Tanaka T, Huang X, Halicka H, Zhao H, Traganos F, Albino A, et al. Cytometry of ATM activation and histone H2AX phosphorylation to estimate extent of DNA damage induced by exogenous agents. Cytometry A 2007;71:648-61.
    • (2007) Cytometry A , vol.71 , pp. 648-661
    • Tanaka, T.1    Huang, X.2    Halicka, H.3    Zhao, H.4    Traganos, F.5    Albino, A.6
  • 102
    • 65649083341 scopus 로고
    • The rate of DNA damage and ageing
    • In: Emerit I, Button C, (eds.), Basel, Switzerland: Birhauser Verlag
    • Miquel M. The rate of DNA damage and ageing. In: Emerit I, Button C, (eds.) Free radicals in ageing. Basel, Switzerland: Birhauser Verlag; 1992.
    • (1992) Free radicals in ageing
    • Miquel, M.1
  • 103
    • 0037166274 scopus 로고    scopus 로고
    • Manipulation of nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels
    • Anderson RM, Bitterman KJ, Wood JG. Manipulation of nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J Biol Chem 2002;277:18881-90.
    • (2002) J Biol Chem , vol.277 , pp. 18881-18890
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3
  • 104
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: Where are we today and where are we going?
    • Hassa P, Haenni S, Elser M, Hottiger M. Nuclear ADP-ribosylation reactions in mammalian cells: Where are we today and where are we going? Microbiol Mol Biol Rev 2006;70:789-829.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 789-829
    • Hassa, P.1    Haenni, S.2    Elser, M.3    Hottiger, M.4
  • 105
    • 0028176627 scopus 로고
    • Glucose-6-phosphate dehydrogenase: A 'housekeeping' enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress
    • Kletzein R, Harris P, Foellmi L. Glucose-6-phosphate dehydrogenase: a 'housekeeping' enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress. FASEB J 1994;8:174-81.
    • (1994) FASEB J , vol.8 , pp. 174-181
    • Kletzein, R.1    Harris, P.2    Foellmi, L.3
  • 108
    • 17044456631 scopus 로고
    • The role of of Ca2+ in the regulation of intramitochondrial energy production in heart
    • McCormack J, Denton R. The role of of Ca2+ in the regulation of intramitochondrial energy production in heart. Biomed Biochim Acta 1987;46:S487-92.
    • (1987) Biomed Biochim Acta , vol.46
    • McCormack, J.1    Denton, R.2
  • 109
    • 0033532508 scopus 로고    scopus 로고
    • Modulation of cytochrome c-mediated extramitochondrial NADH oxidation by contact site density
    • Marzulli D, La Piana G, Fransvea E, Lofrumento N. Modulation of cytochrome c-mediated extramitochondrial NADH oxidation by contact site density. Biochem Biophys Res Commun 1999;259:325-30.
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 325-330
    • Marzulli, D.1    la Piana, G.2    Fransvea, E.3    Lofrumento, N.4
  • 110
    • 0032546461 scopus 로고    scopus 로고
    • Mitochondrial membrane potential supported by exogenous cytochrome c oxidation mimics the early stages of apoptosis
    • La Piana G, Fransvea E, Marzulli D, Lofrumento N. Mitochondrial membrane potential supported by exogenous cytochrome c oxidation mimics the early stages of apoptosis. Biochem Biophys Res Commun 1998;246:556-61.
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 556-561
    • la Piana, G.1    Fransvea, E.2    Marzulli, D.3    Lofrumento, N.4
  • 111
    • 0038449141 scopus 로고    scopus 로고
    • PARP-1, a determinant of cell survival in response to DNA damage
    • Bouchard V, Rouleau M, Poirier GG. PARP-1, a determinant of cell survival in response to DNA damage. Exp Hematol 2003;31:446-54.
    • (2003) Exp Hematol , vol.31 , pp. 446-454
    • Bouchard, V.1    Rouleau, M.2    Poirier, G.G.3
  • 112
    • 65649133017 scopus 로고    scopus 로고
    • Enzymes in poly(ADP-Ribose) metabolism
    • In: Burkle A, (ed.), New York: Springer-Landes Bioscience
    • Meyer R, Meyer-Ficca M, Jacobsen E, Jacobsen M. Enzymes in poly(ADP-Ribose) metabolism. In: Burkle A, (ed.) Poly(ADP-Ribosyl)ation. New York: Springer-Landes Bioscience; 2006.
    • (2006) Poly(ADP-Ribosyl)ation
    • Meyer, R.1    Meyer-Ficca, M.2    Jacobsen, E.3    Jacobsen, M.4
  • 113
    • 0031930117 scopus 로고    scopus 로고
    • Murine glial cells regenerate NAD, after peroxide-induced depletion, using either nicotinic acid, nicotinamide, or quinolinic acid as substrates
    • Grant RS, Kapoor V. Murine glial cells regenerate NAD, after peroxide-induced depletion, using either nicotinic acid, nicotinamide, or quinolinic acid as substrates. J Neurochem 1998;70:1759-63.
    • (1998) J Neurochem , vol.70 , pp. 1759-1763
    • Grant, R.S.1    Kapoor, V.2
  • 115
    • 34247195332 scopus 로고    scopus 로고
    • + and NADH in brain functions, brain diseases and brain aging
    • + and NADH in brain functions, brain diseases and brain aging. Front Biosci 2007;12:1863-88.
    • (2007) Front Biosci , vol.12 , pp. 1863-1888
    • Ying, W.1
  • 116
    • 0020479802 scopus 로고
    • DNA fragmentation and NAD depletion. Their relation to the turnover of endogenous mono(ADP-ribosyl) and poly(ADP-ribosyl) proteins
    • Wielckens K, Schmidt A, George E, Bredehorst R, Hilz H. DNA fragmentation and NAD depletion. Their relation to the turnover of endogenous mono(ADP-ribosyl) and poly(ADP-ribosyl) proteins. J Biol Chem 1982;257:12872-77.
    • (1982) J Biol Chem , vol.257 , pp. 12872-12877
    • Wielckens, K.1    Schmidt, A.2    George, E.3    Bredehorst, R.4    Hilz, H.5
  • 118
    • 0028294246 scopus 로고
    • Nitric oxide activation of poly (ADP-ribose) synthetase in neurotoxicity
    • Zhang J, Dawson VL, Dawson TM, Snyder SH. Nitric oxide activation of poly (ADP-ribose) synthetase in neurotoxicity. Science 1994;263:687-9.
    • (1994) Science , vol.263 , pp. 687-689
    • Zhang, J.1    Dawson, V.L.2    Dawson, T.M.3    Snyder, S.H.4
  • 120
    • 0037713529 scopus 로고    scopus 로고
    • Apoptosis inducing factor and PARP mediated injury in the MPTP mouse model of Parkinson's disease
    • Wang H, Schimoji M, Yu SW, Dawson TM, Dawson VL. Apoptosis inducing factor and PARP mediated injury in the MPTP mouse model of Parkinson's disease. Ann NY Acad Sci 2003;991:132-9.
    • (2003) Ann NY Acad Sci , vol.991 , pp. 132-139
    • Wang, H.1    Schimoji, M.2    Yu, S.W.3    Dawson, T.M.4    Dawson, V.L.5
  • 121
    • 0032901904 scopus 로고    scopus 로고
    • Increased poly(ADP-ribosyl)ation of nuclear proteins in Azheimer's Disease
    • Love S, Barber R, Wilcock GK. Increased poly(ADP-ribosyl)ation of nuclear proteins in Azheimer's Disease. Brain 1999;122: 247-53.
    • (1999) Brain , vol.122 , pp. 247-253
    • Love, S.1    Barber, R.2    Wilcock, G.K.3
  • 122
    • 4143130089 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation inhibitors: Promising drug candidates for a wide variety of pathophysiologic conditions
    • Beneke S, Diefenbach J, Burkle A. Poly(ADP-ribosyl)ation inhibitors: promising drug candidates for a wide variety of pathophysiologic conditions. Int J Cancer 2004;111:813-8.
    • (2004) Int J Cancer , vol.111 , pp. 813-818
    • Beneke, S.1    Diefenbach, J.2    Burkle, A.3
  • 123
    • 25444463296 scopus 로고    scopus 로고
    • +
    • +. Febs J 2005;272:4576-89.
    • (2005) Febs J , vol.272 , pp. 4576-4589
    • Burkle, A.1
  • 124
    • 0027081044 scopus 로고
    • Poly(ADP-ribose) polymerase activity in mononuclear cell lines of 13 mammalian species correlates with species specific lifespan
    • Grube K, Burkle A. Poly(ADP-ribose) polymerase activity in mononuclear cell lines of 13 mammalian species correlates with species specific lifespan. Proc Nat Acad Sci USA 1992;89:11759-63.
    • (1992) Proc Nat Acad Sci USA , vol.89 , pp. 11759-11763
    • Grube, K.1    Burkle, A.2
  • 125
    • 40849135481 scopus 로고    scopus 로고
    • The Sirtuin family: Therapeutic targets to treat diseases of aging
    • Milne J, Denu JM. The Sirtuin family: therapeutic targets to treat diseases of aging. Curr Pharm Des 2008;12:11-7.
    • (2008) Curr Pharm Des , vol.12 , pp. 11-17
    • Milne, J.1    Denu, J.M.2
  • 126
    • 33845327501 scopus 로고    scopus 로고
    • SIRT1: Linking adaptive cellular responses to aging-associated changes in organismal physiology
    • Anastasiou D, Krek W. SIRT1: linking adaptive cellular responses to aging-associated changes in organismal physiology. Physiology (Bethesda) 2006;21:404-10.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 404-410
    • Anastasiou, D.1    Krek, W.2
  • 128
    • 33244486764 scopus 로고    scopus 로고
    • Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic beta cells
    • Bordone L, Motta MC, Picard F. 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
  • 129
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionary conserved and nonconserved cellular localisations and functions of human SIRT proteins
    • Michishita E, Park J, Burneskis J, Barrett J, Horikawa I. Evolutionary conserved and nonconserved cellular localisations and functions of human SIRT proteins. Mol Biol Chem 2005;16:4623-35.
    • (2005) Mol Biol Chem , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.2    Burneskis, J.3    Barrett, J.4    Horikawa, I.5
  • 130
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation
    • Jing E, Gesta S, Kahn C. SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab 2007;6:105-14.
    • (2007) Cell Metab , vol.6 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.3
  • 131
  • 132
    • 67349276169 scopus 로고    scopus 로고
    • AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
    • Canto C, Gerhart-Hines Z, Feige J, Lagouge M, Noriega L, Milne J, et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 2009;458: 1056-60.
    • (2009) Nature , vol.458 , pp. 1056-1060
    • Canto, C.1    Gerhart-Hines, Z.2    Feige, J.3    Lagouge, M.4    Noriega, L.5    Milne, J.6
  • 133
    • 43049121395 scopus 로고    scopus 로고
    • Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt
    • Fuclo M, Cen Y, Zhao P, Hoffman E, McBurney M, Sauve A, et al. Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt. Dev Cell 2008;14:661-73.
    • (2008) Dev Cell , vol.14 , pp. 661-673
    • Fuclo, M.1    Cen, Y.2    Zhao, P.3    Hoffman, E.4    McBurney, M.5    Sauve, A.6
  • 134
    • 44649119816 scopus 로고    scopus 로고
    • Transcriptional targets of sirtuins in the coordination of mammalian physiology
    • Fiege J, Auwerx J. Transcriptional targets of sirtuins in the coordination of mammalian physiology. Curr Opin Cell Biol 2008;20:303-9.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 303-309
    • Fiege, J.1    Auwerx, J.2
  • 135
    • 12844271254 scopus 로고    scopus 로고
    • The emerging therapeutic potential of sirtuin-interacting drugs: From cell death to lifespan extension
    • Porcu M, Chiarugi A. The emerging therapeutic potential of sirtuin-interacting drugs: from cell death to lifespan extension. Trends Pharmacol Sci 2005;26:94-103.
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 94-103
    • Porcu, M.1    Chiarugi, A.2
  • 136
    • 0041829415 scopus 로고    scopus 로고
    • Proteomics-based identification of differentially expressed genes in human gliomas: Down-regulation of SIRT2 gene
    • Hiratsuka M, Inoue T, Toda T, Kimura N, Shirayoshi Y, Kamitani H, et al. Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene. Biochem Biophys Res Commun 2003;309:558-66.
    • (2003) Biochem Biophys Res Commun , vol.309 , pp. 558-566
    • Hiratsuka, M.1    Inoue, T.2    Toda, T.3    Kimura, N.4    Shirayoshi, Y.5    Kamitani, H.6
  • 137
    • 33847053144 scopus 로고    scopus 로고
    • SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress
    • Inoue T, Hiratsuka M, Osaki M, Yamada H, Kishimoto I, Yamaguchi S, et al. SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress. Oncogene 2007;26:945-57.
    • (2007) Oncogene , vol.26 , pp. 945-957
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Yamada, H.4    Kishimoto, I.5    Yamaguchi, S.6
  • 138
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating α-tubulin
    • Li W, Zhang B, Tang J, Cao Q, Wu Y, Wu C, et al. Sirtuin2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating α-tubulin. J Neurosci 2007;27:2606-16.
    • (2007) J Neurosci , vol.27 , pp. 2606-2616
    • Li, W.1    Zhang, B.2    Tang, J.3    Cao, Q.4    Wu, Y.5    Wu, C.6
  • 139
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G, Guarente L. The Sir2 family of protein deacetylases. Annu Rev Biochem 2004;73:417-35.
    • (2004) Annu Rev Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 140
    • 48349144852 scopus 로고    scopus 로고
    • Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending lifespan
    • Pearson K, Baur J, Lewis K, Peshkin L, Price N, Labinskyy N, et al. Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending lifespan. Cell Metab 2008;8:157-68.
    • (2008) Cell Metab , vol.8 , pp. 157-168
    • Pearson, K.1    Baur, J.2    Lewis, K.3    Peshkin, L.4    Price, N.5    Labinskyy, N.6
  • 141
    • 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, Rodgers JT, et al. SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. Embo J 2007;26:3169-79.
    • (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    Rodgers, J.T.6
  • 142
    • 22744450382 scopus 로고    scopus 로고
    • Toward a unified theory of calorie restriction and longevity regulation
    • Sinclair D. Toward a unified theory of calorie restriction and longevity regulation. Mech Ageing Dev 2005;126:987-1002.
    • (2005) Mech Ageing Dev , vol.126 , pp. 987-1002
    • Sinclair, D.1
  • 144
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • Lin SJ, Guarente L. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr Opin Cell Biol 2003;15:241-6.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 145
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, amitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi T, Wang F, Stieren E, TongQ. SIRT3, amitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J Biol Chem 2005;280:13560-67.
    • (2005) J Biol Chem , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 146
    • 55749084738 scopus 로고    scopus 로고
    • A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • Ahn B, Kim H, Song S, Lee I, Liu J, Vassilopoulos A, et al. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. PNAS 2008;105:14447-52.
    • (2008) PNAS , vol.105 , pp. 14447-14452
    • Ahn, B.1    Kim, H.2    Song, S.3    Lee, I.4    Liu, J.5    Vassilopoulos, A.6
  • 147
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • Anderson RM, Bitterman KJ, Wood JG. Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 2003;423:181-5.
    • (2003) Nature , vol.423 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3
  • 148
    • 33748316536 scopus 로고    scopus 로고
    • SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic β cells
    • Haigis M, Mostoslavsky R, Haigis K, Fahie K, Christodoulou D, Murphy A, et al. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic β cells. Cell 2006;126:941-54.
    • (2006) Cell , vol.126 , pp. 941-954
    • Haigis, M.1    Mostoslavsky, R.2    Haigis, K.3    Fahie, K.4    Christodoulou, D.5    Murphy, A.6
  • 149
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa T, Lomb D, Haigis M, 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.2    Haigis, M.3    Guarente, L.4
  • 150
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt G, Ford E, Kurtev M, Guarente L. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J Biol Chem 2005;280:21313-20.
    • (2005) J Biol Chem , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 151
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky R, Chua K, Lombard D, Pang W, Fischer M, Gellon L, et al. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 2006;124: 315-29.
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1    Chua, K.2    Lombard, D.3    Pang, W.4    Fischer, M.5    Gellon, L.6
  • 152
    • 33744466971 scopus 로고    scopus 로고
    • Mammalian Sirt2 homolog SIRT7 is an activator of RNApolymerase I transcription
    • Ford E, Voit R, Liszt G, Magin C, Grummt I, Guarente L. Mammalian Sirt2 homolog SIRT7 is an activator of RNApolymerase I transcription. Genes Dev 2006;20:1075-80.
    • (2006) Genes Dev , vol.20 , pp. 1075-1080
    • Ford, E.1    Voit, R.2    Liszt, G.3    Magin, C.4    Grummt, I.5    Guarente, L.6
  • 153
    • 0042671307 scopus 로고    scopus 로고
    • Epigenetic silencing of RNApolymerase I transcription
    • Grummt I, Pikaard C. Epigenetic silencing of RNApolymerase I transcription. Nat Rev Mol Cell Biol 2003;4:641-9.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 641-649
    • Grummt, I.1    Pikaard, C.2
  • 154
    • 64049090625 scopus 로고    scopus 로고
    • Sirt7-dependent inhibition of cell growth and proliferation might be instrumental to mediate tissue integrity during aging
    • Vakhrusheva O, Braeuer D, Liu Z, Braun T, Bober E. Sirt7-dependent inhibition of cell growth and proliferation might be instrumental to mediate tissue integrity during aging. J Physiol Pharmacol 2008;59:201-12.
    • (2008) J Physiol Pharmacol , vol.59 , pp. 201-212
    • Vakhrusheva, O.1    Braeuer, D.2    Liu, Z.3    Braun, T.4    Bober, E.5
  • 155
    • 0041589716 scopus 로고    scopus 로고
    • Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked?
    • Zhang J. Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked? Bioessays 2003;25:808-14.
    • (2003) Bioessays , vol.25 , pp. 808-814
    • Zhang, J.1
  • 156
    • 0035831080 scopus 로고    scopus 로고
    • Pathophysiological relevance of mitochondria in NAD+ metabolism
    • de Lisa F, Ziegler M. Pathophysiological relevance of mitochondria in NAD+ metabolism. FEBS Lett 2001;492:4-8.
    • (2001) FEBS Lett , vol.492 , pp. 4-8
    • de Lisa, F.1    Ziegler, M.2
  • 159
    • 0034843930 scopus 로고    scopus 로고
    • Is ischemia involved in the pathogenesis of cerebral malaria?
    • Sanni LA, Rae C, Maitland A, Stocker R, Hunt N. Is ischemia involved in the pathogenesis of cerebral malaria? Am J Pathol 2001;159:1105-12.
    • (2001) Am J Pathol , vol.159 , pp. 1105-1112
    • Sanni, L.A.1    Rae, C.2    Maitland, A.3    Stocker, R.4    Hunt, N.5
  • 160
    • 0035933809 scopus 로고    scopus 로고
    • In vivo role of NAD(P)H: Quinone oxidoreductase 1 (NQO1) in the regulation of intracellular redox state and accumulation of abdominal adipose tissue
    • Gaikwad A, Long DI, Stringer J, Jaiswal A. In vivo role of NAD(P)H: quinone oxidoreductase 1 (NQO1) in the regulation of intracellular redox state and accumulation of abdominal adipose tissue. J Biol Chem 2001;276:22559-64.
    • (2001) J Biol Chem , vol.276 , pp. 22559-22564
    • Gaikwad, A.1    Long, D.I.2    Stringer, J.3    Jaiswal, A.4
  • 161
    • 33750867930 scopus 로고    scopus 로고
    • Metabolic effects of aldose reductase inhibition during low-flow ischemia and reperfusion
    • Ramasamy R, Trueblood N, Schaefer S. Metabolic effects of aldose reductase inhibition during low-flow ischemia and reperfusion. Am J Physiol 1998;275:H195-203.
    • (1998) Am J Physiol , vol.275
    • Ramasamy, R.1    Trueblood, N.2    Schaefer, S.3
  • 162
    • 84857291670 scopus 로고    scopus 로고
    • Pyruvate improves redox status and decreases indicators of hepatic apoptosis during hemorrhagic shock in swine
    • Mongan P, Capacchione J, West S, Karaian J, Dubois D, Keneally R, et al. Pyruvate improves redox status and decreases indicators of hepatic apoptosis during hemorrhagic shock in swine. Am J Physiol Heart Circ Physiol 2002;384: 143-53.
    • (2002) Am J Physiol Heart Circ Physiol , vol.384 , pp. 143-153
    • Mongan, P.1    Capacchione, J.2    West, S.3    Karaian, J.4    Dubois, D.5    Keneally, R.6
  • 163
    • 0034544579 scopus 로고    scopus 로고
    • + linked glycerol phosphate dehydrogenase has normal pancreatic beta cell function but abnormal metabolite pattern in skeletal muscle
    • + linked glycerol phosphate dehydrogenase has normal pancreatic beta cell function but abnormal metabolite pattern in skeletal muscle. Arch Biochem Biophys 2000;384:143-53.
    • (2000) Arch Biochem Biophys , vol.384 , pp. 143-153
    • MacDonald, M.1    Marshall, L.2
  • 164
    • 0035831109 scopus 로고    scopus 로고
    • Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis
    • Schweiger M, Hennig K, Lerner F, Niere M, Hirsch-Kauffmann M, Specht T, et al. Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis. FEBS Lett 2001;492:95-100.
    • (2001) FEBS Lett , vol.492 , pp. 95-100
    • Schweiger, M.1    Hennig, K.2    Lerner, F.3    Niere, M.4    Hirsch-Kauffmann, M.5    Specht, T.6
  • 165
    • 34247278118 scopus 로고    scopus 로고
    • Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1
    • Berger F, Lau C, Ziegler M. Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1. Proc Natl Acad Sci USA 2007;104:3765-70.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3765-3770
    • Berger, F.1    Lau, C.2    Ziegler, M.3
  • 168
    • 84864405038 scopus 로고    scopus 로고
    • NAD: Metabolism and Regulatory Functions
    • In: Burkle A, (ed.), Georgetown, TX: Landes Bioscience
    • Ziegler M. NAD: Metabolism and Regulatory Functions. In: Burkle A, (ed.) Poly(ADP-ribosyl)ation. Georgetown, TX: Landes Bioscience; 2006.
    • (2006) Poly(ADP-ribosyl)ation
    • Ziegler, M.1
  • 170
    • 4243098426 scopus 로고    scopus 로고
    • NAD to the rescue
    • Bedalov A, Simon DA. NAD to the rescue. Sci Mag 2004;305: 954-8.
    • (2004) Sci Mag , vol.305 , pp. 954-958
    • Bedalov, A.1    Simon, D.A.2
  • 171
    • 0037012844 scopus 로고    scopus 로고
    • Axonal self-destruction and neurodegeneration
    • Raff MC, Whitemore AV, Finn JT. Axonal self-destruction and neurodegeneration. Science 2002;296:868-71.
    • (2002) Science , vol.296 , pp. 868-871
    • Raff, M.C.1    Whitemore, A.V.2    Finn, J.T.3
  • 172
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Arraki T, Sasaki A, Milbrandt J. Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 2004;305:1010-3.
    • (2004) Science , vol.305 , pp. 1010-1013
    • Arraki, T.1    Sasaki, A.2    Milbrandt, J.3
  • 173
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin M, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 2006;443:787-95.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.1    Beal, M.F.2
  • 174
    • 23844531504 scopus 로고    scopus 로고
    • Poly(ADPribose) polymerase-1 activation in a primate model of multiple sclerosis
    • Kauppinen TM, Suh SW, Genain C, Swanson RA. Poly(ADPribose) polymerase-1 activation in a primate model of multiple sclerosis. J Neurosci Res 2005;81:190-8.
    • (2005) J Neurosci Res , vol.81 , pp. 190-198
    • Kauppinen, T.M.1    Suh, S.W.2    Genain, C.3    Swanson, R.A.4
  • 175
    • 0030581308 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase inhibitors protect against MPTPinduced depletions of striatal dopamine and cortical noradrenaline in C57B1/6 mice
    • Cosi C, Colpaert F, Koek W, Degryse A, Marien M. Poly (ADP-ribose) polymerase inhibitors protect against MPTPinduced depletions of striatal dopamine and cortical noradrenaline in C57B1/6 mice. Brain Res 1996;729:264-9.
    • (1996) Brain Res , vol.729 , pp. 264-269
    • Cosi, C.1    Colpaert, F.2    Koek, W.3    Degryse, A.4    Marien, M.5
  • 176
    • 0034843077 scopus 로고    scopus 로고
    • The role of kynurenines in the production of neuronal death, and the neuroprotective effect of purines
    • Stone TW, Behan WM, Jones PA, Darlington LG, Smith RA. The role of kynurenines in the production of neuronal death, and the neuroprotective effect of purines. J Alzheimers Dis 2001;3:355-66.
    • (2001) J Alzheimers Dis , vol.3 , pp. 355-366
    • Stone, T.W.1    Behan, W.M.2    Jones, P.A.3    Darlington, L.G.4    Smith, R.A.5
  • 177
    • 0035123904 scopus 로고    scopus 로고
    • Kynurenines in the CNS: From endogenous obscurity to therapeutic importance
    • StoneTW. Kynurenines in the CNS: from endogenous obscurity to therapeutic importance. Prog Neurobiol 2001;64:185-218.
    • (2001) Prog Neurobiol , vol.64 , pp. 185-218
    • Stone, T.W.1
  • 178
    • 0036690151 scopus 로고    scopus 로고
    • Endogenous kynurenines as targets for drug discovery and development
    • Stone TW, Darlington LG. Endogenous kynurenines as targets for drug discovery and development. Nat Rev Drug Discov 2002;1:609-20.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 609-620
    • Stone, T.W.1    Darlington, L.G.2
  • 179
    • 0035834146 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death
    • YingW, Sevigny MB, Chen Y, Swanson RA. Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death. Proc Natl Acad Sci USA 2001;98:12227-32.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12227-12232
    • Ying, W.1    Sevigny, M.B.2    Chen, Y.3    Swanson, R.A.4
  • 180
    • 0022634961 scopus 로고
    • Metabolic consequences of DNA damage: DNA damage induces alterations in glucose metabolism by activation of Poly(ADP-ribose) polymerase
    • Berger SJ, Sudar DC, Berger NA. Metabolic consequences of DNA damage: DNA damage induces alterations in glucose metabolism by activation of Poly(ADP-ribose) polymerase. Biochem Biophys Res Commun 1986;134:227-32.
    • (1986) Biochem Biophys Res Commun , vol.134 , pp. 227-232
    • Berger, S.J.1    Sudar, D.C.2    Berger, N.A.3
  • 181
    • 79955591489 scopus 로고    scopus 로고
    • Age related changes in NAD+ metabolism, oxidative stress and Sirt1 activity in Wistar Rats
    • Braidy N, Guillemin G, Mansour H, Chan-Ling T, Poljak A, Grant R. Age related changes in NAD+ metabolism, oxidative stress and Sirt1 activity in Wistar Rats. PLOSONE 2011;6: e19194.
    • (2011) PLOSONE , vol.6
    • Braidy, N.1    Guillemin, G.2    Mansour, H.3    Chan-Ling, T.4    Poljak, A.5    Grant, R.6
  • 182
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • Bordone L, Guarente L. Calorie restriction, SIRT1 and metabolism: understanding longevity. Nat Rev Mol Cell Biol 2005;6: 298-305.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 183
    • 19944433088 scopus 로고    scopus 로고
    • A novel VTNR enhancer within the SIRT3 gene, a human homologue of SIR2 is associated with survival at oldest ages
    • Bellizzi D, Rose G, Cavalcante P, Covello G, Dato S, De Rango F, et al. A novel VTNR enhancer within the SIRT3 gene, a human homologue of SIR2 is associated with survival at oldest ages. Genomics 2005;85:258-63.
    • (2005) Genomics , vol.85 , pp. 258-263
    • Bellizzi, D.1    Rose, G.2    Cavalcante, P.3    Covello, G.4    Dato, S.5    de Rango, F.6
  • 184
    • 33845399894 scopus 로고    scopus 로고
    • Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha
    • Lagouge M, Argmann C, Gerhart-Hines Z, Meziane H, Lerin C, Daussin F, et al. Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha. Cell 2006;127:1109-22.
    • (2006) Cell , vol.127 , pp. 1109-1122
    • Lagouge, M.1    Argmann, C.2    Gerhart-Hines, Z.3    Meziane, H.4    Lerin, C.5    Daussin, F.6
  • 186
    • 3843101621 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 regulates both the exonuclease and helicase activities of the Werner syndrome protein
    • von Kobbe C, Harrigan J, Schreiber V, Stiegler P, Piotrowski J, Dawut L, et al. Poly(ADP-ribose) polymerase 1 regulates both the exonuclease and helicase activities of the Werner syndrome protein. Nucleic Acids Res 2004;32:4003-14.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4003-4014
    • von Kobbe, C.1    Harrigan, J.2    Schreiber, V.3    Stiegler, P.4    Piotrowski, J.5    Dawut, L.6
  • 188
    • 62149128630 scopus 로고    scopus 로고
    • The importance of NAD in multiple sclerosis
    • PenberthyWT, Tsunoda I. The importance of NAD in multiple sclerosis. Curr Pharm Des 2009;15:64-99.
    • (2009) Curr Pharm Des , vol.15 , pp. 64-99
    • Penberthy, W.T.1    Tsunoda, I.2
  • 189
    • 2442624618 scopus 로고    scopus 로고
    • + depletion and mitochondrial permeability transition
    • + depletion and mitochondrial permeability transition. J Biol Chem 2004;279:18895-902.
    • (2004) J Biol Chem , vol.279 , pp. 18895-18902
    • Alano, C.C.1    Ying, W.2    Swanson, R.A.3
  • 190
    • 30044443515 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sirt2 deacetylase activity
    • Pillai JB, Isbatan A, Imai SI, Gupta MP. Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sirt2 deacetylase activity. J Biol Chem 2005;280:43121-30.
    • (2005) J Biol Chem , vol.280 , pp. 43121-43130
    • Pillai, J.B.1    Isbatan, A.2    Imai, S.I.3    Gupta, M.P.4
  • 191
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra MT, Smith BC, Denu JM. Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 2005;280:17187-95.
    • (2005) J Biol Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 192
    • 34249846128 scopus 로고    scopus 로고
    • Resveratrol stimulates AMP kinase activity in neurons
    • Dasgupta B, Milbrandt J. Resveratrol stimulates AMP kinase activity in neurons. Proc Natl Acad Sci USA 2007;104: 7217-22.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7217-7222
    • Dasgupta, B.1    Milbrandt, J.2
  • 193
    • 74549166483 scopus 로고    scopus 로고
    • Neuroprotective effects of naturally occurring polyphenols on quinolinic-acid induced excitotoxicity in human neurons
    • Braidy N, Grant R, Adams S, Guillemin G. Neuroprotective effects of naturally occurring polyphenols on quinolinic-acid induced excitotoxicity in human neurons. FEBS J 2010;277: 368-82.
    • (2010) FEBS J , vol.277 , pp. 368-382
    • Braidy, N.1    Grant, R.2    Adams, S.3    Guillemin, G.4
  • 194
    • 34247520466 scopus 로고    scopus 로고
    • Vitamins and aging: Pathways to NAD+ synthesis
    • Denu JM. Vitamins and aging: pathways to NAD+ synthesis. Cell 2007;129:453-4.
    • (2007) Cell , vol.129 , pp. 453-454
    • Denu, J.M.1
  • 195
    • 0021680811 scopus 로고
    • Protein-diet-induced elevation of 5-phosphoribosyl 1-disphosphate concentrations in mouse liver associated with increased syntheses of various nucleotides and the possible involvement of glucagon
    • Chikenji T, Asai T, Tatibana M. Protein-diet-induced elevation of 5-phosphoribosyl 1-disphosphate concentrations in mouse liver associated with increased syntheses of various nucleotides and the possible involvement of glucagon. Biochim Biophys Acta 1984;802:274-81.
    • (1984) Biochim Biophys Acta , vol.802 , pp. 274-281
    • Chikenji, T.1    Asai, T.2    Tatibana, M.3
  • 199
    • 33744509311 scopus 로고    scopus 로고
    • Regulation of intracellular levels of NAD: A novel role for CD38
    • Aksoy P, White T, Thompson M, Chini E. Regulation of intracellular levels of NAD: a novel role for CD38. Biochem Biophys Res Commun 2006;345:1386-92.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 1386-1392
    • Aksoy, P.1    White, T.2    Thompson, M.3    Chini, E.4
  • 200
    • 12344320413 scopus 로고    scopus 로고
    • Tankyrase 1 as a target for telomere-directed molecular cancer therapeutics
    • Seimiya H, Muramatsu Y, Ohishi T, Tsuruo T. Tankyrase 1 as a target for telomere-directed molecular cancer therapeutics. Cancer Cell 2005;7:25-37.
    • (2005) Cancer Cell , vol.7 , pp. 25-37
    • Seimiya, H.1    Muramatsu, Y.2    Ohishi, T.3    Tsuruo, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.