메뉴 건너뛰기




Volumn 39, Issue , 2014, Pages 86-107

Oxidative stress, mitochondrial dysfunction and the mitochondria theory of aging

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE;

EID: 84904624833     PISSN: 00741132     EISSN: 16623800     Source Type: Book Series    
DOI: 10.1159/000358901     Document Type: Article
Times cited : (88)

References (266)
  • 1
    • 67649866121 scopus 로고    scopus 로고
    • Mitochondria and reactive oxygen species
    • Kowaltowski AJ, et al: Mitochondria and reactive oxygen species. Free Radic Biol Med 2009; 47: 333-343.
    • (2009) Free Radic Biol Med , vol.47 , pp. 333-343
    • Kowaltowski, A.J.1
  • 2
    • 0035782650 scopus 로고    scopus 로고
    • Reactive oxygen species and mitochondrial diseases
    • Kirkinezos IG, Moraes CT: Reactive oxygen species and mitochondrial diseases. Semin Cell Dev Biol 2001; 12: 449-457.
    • (2001) Semin Cell Dev Biol , vol.12 , pp. 449-457
    • Kirkinezos, I.G.1    Moraes, C.T.2
  • 3
    • 2642565930 scopus 로고    scopus 로고
    • Hydroxyl-radical production in physiological reactions. A novel function of peroxidase
    • Chen SX, Schopfer P: Hydroxyl-radical production in physiological reactions. A novel function of peroxidase. Eur J Biochem 1999; 260: 726-735.
    • (1999) Eur J Biochem , vol.260 , pp. 726-735
    • Chen, S.X.1    Schopfer, P.2
  • 4
    • 70449715463 scopus 로고    scopus 로고
    • Reactive oxygen species and peroxisomes: Struggling for balance
    • Bonekamp NA, et al: Reactive oxygen species and peroxisomes: struggling for balance. Biofactors 2009; 35: 346-355.
    • (2009) Biofactors , vol.35 , pp. 346-355
    • Bonekamp, N.A.1
  • 5
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard K, Krause KH: The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 2007; 87: 245-313.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 7
    • 0035750172 scopus 로고    scopus 로고
    • Toxic metals and oxidative stress. I. Mechanisms involved in metal-induced oxidative damage
    • Ercal N, Gurer-Orhan H, Aykin-Burns N: Toxic metals and oxidative stress. I. Mechanisms involved in metal-induced oxidative damage. Curr Top Med Chem 2001; 1: 529-539.
    • (2001) Curr Top Med Chem , vol.1 , pp. 529-539
    • Ercal, N.1    Gurer-Orhan, H.2    Aykin-Burns, N.3
  • 9
    • 0034096271 scopus 로고    scopus 로고
    • Mechanisms of anti-cancer agents: Emphasis on oxidative stress and electron transfer
    • Kovacic P, Osuna JA Jr: Mechanisms of anti-cancer agents: emphasis on oxidative stress and electron transfer. Curr Pharm Des 2000; 6: 277-309.
    • (2000) Curr Pharm des , vol.6 , pp. 277-309
    • Kovacic, P.1    Osuna Jr., J.A.2
  • 10
    • 67649641505 scopus 로고    scopus 로고
    • Role of oxidative stress in cadmium toxicity and carcinogenesis
    • Liu J, Qu W, Kadiiska MB: Role of oxidative stress in cadmium toxicity and carcinogenesis. Toxicol Appl Pharmacol 2009; 238: 209-214.
    • (2009) Toxicol Appl Pharmacol , vol.238 , pp. 209-214
    • Liu, J.1    Qu, W.2    Kadiiska, M.B.3
  • 11
    • 47949103112 scopus 로고    scopus 로고
    • Cellular effects of long wavelength UV light (UVA) in mammalian cells
    • McMillan TJ, et al: Cellular effects of long wavelength UV light (UVA) in mammalian cells. J Pharm Pharmacol 2008; 60: 969-976.
    • (2008) J Pharm Pharmacol , vol.60 , pp. 969-976
    • McMillan, T.J.1
  • 13
    • 60749131956 scopus 로고    scopus 로고
    • Radiation chemistry comes before radiation biology
    • O'Neill P, Wardman P: Radiation chemistry comes before radiation biology. Int J Radiat Biol 2009; 85: 9-25.
    • (2009) Int J Radiat Biol , vol.85 , pp. 9-25
    • O'neill, P.1    Wardman, P.2
  • 14
    • 34347379422 scopus 로고    scopus 로고
    • Hypoxia-induced reactive oxygen species formation in skeletal muscle
    • Clanton TL: Hypoxia-induced reactive oxygen species formation in skeletal muscle. J Appl Physiol (1985) 2007; 102: 2379-2388.
    • (2007) J Appl Physiol (1985) , vol.102 , pp. 2379-2388
    • Clanton, T.L.1
  • 15
    • 64149087422 scopus 로고    scopus 로고
    • Therapeutic strategies by modulating oxygen stress in cancer and inflammation
    • Fang J, Seki T, Maeda H: Therapeutic strategies by modulating oxygen stress in cancer and inflammation. Adv Drug Deliv Rev 2009; 61: 290-302.
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 290-302
    • Fang, J.1    Seki, T.2    Maeda, H.3
  • 16
    • 28544448737 scopus 로고    scopus 로고
    • Reactive oxygen species amplify glucose signalling in renal cells cultured under high glucose and in diabetic kidney
    • Ha H, Lee HB: Reactive oxygen species amplify glucose signalling in renal cells cultured under high glucose and in diabetic kidney. Nephrology (Carlton) 2005; 10(suppl):S7-S10.
    • (2005) Nephrology (Carlton) , vol.10 , Issue.SUPPL.
    • Ha, H.1    Lee, H.B.2
  • 17
    • 8544224992 scopus 로고    scopus 로고
    • Metal-induced oxidative stress and signal transduction
    • Leonard SS, Harris GK, Shi X: Metal-induced oxidative stress and signal transduction. Free Radic Biol Med 2004; 37: 1921-1942.
    • (2004) Free Radic Biol Med , vol.37 , pp. 1921-1942
    • Leonard, S.S.1    Harris, G.K.2    Shi, X.3
  • 18
    • 78649906789 scopus 로고    scopus 로고
    • Environmentally induced oxidative stress in aquatic animals
    • Lushchak VI: Environmentally induced oxidative stress in aquatic animals. Aquat Toxicol 2011; 101: 13-30.
    • (2011) Aquat Toxicol , vol.101 , pp. 13-30
    • Lushchak, V.I.1
  • 19
    • 77955035878 scopus 로고    scopus 로고
    • Reactive oxygen species in TNFalpha-induced signaling and cell death
    • Morgan MJ, Liu ZG: Reactive oxygen species in TNFalpha-induced signaling and cell death. Mol Cells 2010; 30: 1-12.
    • (2010) Mol Cells , vol.30 , pp. 1-12
    • Morgan, M.J.1    Liu, Z.G.2
  • 20
    • 0031987938 scopus 로고    scopus 로고
    • Anthracyclinederived chemotherapeutics in apoptosis and free radical cytotoxicity
    • Muller I, Niethammer D, Bruchelt G: Anthracyclinederived chemotherapeutics in apoptosis and free radical cytotoxicity. Int J Mol Med 1998; 1: 491-494.
    • (1998) Int J Mol Med , vol.1 , pp. 491-494
    • Muller, I.1    Niethammer, D.2    Bruchelt, G.3
  • 21
    • 33749986298 scopus 로고    scopus 로고
    • Free radicals and antioxidants in normal physiological functions and human disease
    • Valko M, et al: Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 2007; 39: 44-84.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 44-84
    • Valko, M.1
  • 23
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel T: Signal transduction by reactive oxygen species. J Cell Biol 2011; 194: 7-15.
    • (2011) J Cell Biol , vol.194 , pp. 7-15
    • Finkel, T.1
  • 24
    • 33847620225 scopus 로고    scopus 로고
    • Aging: A revisited theory based on free radicals generated by NOX family NADPH oxidases
    • Krause KH: Aging: a revisited theory based on free radicals generated by NOX family NADPH oxidases. Exp Gerontol 2007; 42: 256-262.
    • (2007) Exp Gerontol , vol.42 , pp. 256-262
    • Krause, K.H.1
  • 25
    • 84866432422 scopus 로고    scopus 로고
    • Reactive oxygen species: From health to disease
    • Brieger K, et al: Reactive oxygen species: from health to disease. Swiss Med Wkly 2012; 142:w13659.
    • (2012) Swiss Med Wkly , vol.142
    • Brieger, K.1
  • 26
    • 80053337585 scopus 로고    scopus 로고
    • Clinical review: Oxygen as a signaling molecule
    • Bartz RR, Piantadosi CA: Clinical review: oxygen as a signaling molecule. Crit Care 2010; 14: 234.
    • (2010) Crit Care , vol.14 , pp. 234
    • Bartz, R.R.1    Piantadosi, C.A.2
  • 27
    • 0034011261 scopus 로고    scopus 로고
    • Oxyradicals and DNA damage
    • Marnett LJ: Oxyradicals and DNA damage. Carcinogenesis 2000; 21: 361-370.
    • (2000) Carcinogenesis , vol.21 , pp. 361-370
    • Marnett, L.J.1
  • 28
    • 84875185107 scopus 로고    scopus 로고
    • DNA base damage by reactive oxygen species, oxidizing agents, and UV radiation
    • Cadet J, Wagner JR: DNA base damage by reactive oxygen species, oxidizing agents, and UV radiation. Cold Spring Harb Perspect Biol 2013; 5:a012559.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Cadet, J.1    Wagner, J.R.2
  • 29
    • 0036591855 scopus 로고    scopus 로고
    • Free radical-induced damage to DNA: Mechanisms and measurement
    • Dizdaroglu M, et al: Free radical-induced damage to DNA: mechanisms and measurement. Free Radic Biol Med 2002; 32: 1102-1115.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1102-1115
    • Dizdaroglu, M.1
  • 30
    • 34248541922 scopus 로고    scopus 로고
    • Life and death: Metabolic rate, membrane composition, and life span of animals
    • Hulbert AJ, et al: Life and death: metabolic rate, membrane composition, and life span of animals. Physiol Rev 2007; 87: 1175-1213.
    • (2007) Physiol Rev , vol.87 , pp. 1175-1213
    • Hulbert, A.J.1
  • 31
    • 80053629048 scopus 로고    scopus 로고
    • Molecular and structural antioxidant defenses against oxidative stress in animals
    • Pamplona R, Costantini D: Molecular and structural antioxidant defenses against oxidative stress in animals. Am J Physiol Regul Integr Comp Physiol 2011; 301:R843-R863.
    • (2011) Am J Physiol Regul Integr Comp Physiol , vol.301
    • Pamplona, R.1    Costantini, D.2
  • 32
    • 84860716543 scopus 로고    scopus 로고
    • Repair of persistent strand breaks in the mitochondrial genome
    • Sykora P, Wilson DM 3rd, Bohr VA: Repair of persistent strand breaks in the mitochondrial genome. Mech Ageing Dev 2012; 133: 169-175.
    • (2012) Mech Ageing Dev , vol.133 , pp. 169-175
    • Sykora, P.1    Wilson III, D.M.2    Bohr, V.A.3
  • 33
    • 58149350129 scopus 로고    scopus 로고
    • The proteasome and its role in the degradation of oxidized proteins
    • Jung T, Grune T: The proteasome and its role in the degradation of oxidized proteins. IUBMB Life 2008; 60: 743-752.
    • (2008) IUBMB Life , vol.60 , pp. 743-752
    • Jung, T.1    Grune, T.2
  • 34
    • 42649129672 scopus 로고    scopus 로고
    • MtDNA mutations, functional decline and turnover of mitochondria in aging
    • Pang CY, Ma YS, Wei YU: MtDNA mutations, functional decline and turnover of mitochondria in aging. Front Biosci 2008; 13: 3661-3675.
    • (2008) Front Biosci , vol.13 , pp. 3661-3675
    • Pang, C.Y.1    Ma, Y.S.2    Wei, Y.U.3
  • 35
    • 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
  • 36
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman KB, Ames BN: The free radical theory of aging matures. Physiol Rev 1998; 78: 547-581.
    • (1998) Physiol Rev , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 37
    • 0036628724 scopus 로고    scopus 로고
    • Role of oxidative stress and protein oxidation in the aging process
    • Sohal RS: Role of oxidative stress and protein oxidation in the aging process. Free Radic Biol Med 2002; 33: 37-44.
    • (2002) Free Radic Biol Med , vol.33 , pp. 37-44
    • Sohal, R.S.1
  • 38
    • 0024541837 scopus 로고
    • Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases
    • Linnane AW, et al: Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases. Lancet 1989; 1: 642-645.
    • (1989) Lancet , vol.1 , pp. 642-645
    • Linnane, A.W.1
  • 39
    • 0019160038 scopus 로고
    • Mitochondrial role in cell aging
    • Miquel J, et al: Mitochondrial role in cell aging. Exp Gerontol 1980; 15: 575-591.
    • (1980) Exp Gerontol , vol.15 , pp. 575-591
    • Miquel, J.1
  • 40
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame M, Rua D, Greenberg ML: The biosynthesis and functional role of cardiolipin. Prog Lipid Res 2000; 39: 257-288.
    • (2000) Prog Lipid Res , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 41
    • 84896778365 scopus 로고    scopus 로고
    • Age-related changes in mitochondrial membrane composition of Nothobranchius rachovii
    • Lucas-Sanchez A, et al: Age-related changes in mitochondrial membrane composition of Nothobranchius rachovii . J Gerontol A Biol Sci Med Sci 2014; 69: 142-151.
    • (2014) J Gerontol A Biol Sci Med Sci , vol.69 , pp. 142-151
    • Lucas-Sanchez, A.1
  • 42
    • 84862980210 scopus 로고    scopus 로고
    • Age-related changes in mitochondrial membrane composition of rainbow trout (Oncorhynchus mykiss) heart and brain
    • Almaida-Pagan PF, et al: Age-related changes in mitochondrial membrane composition of rainbow trout (Oncorhynchus mykiss) heart and brain. Comp Biochem Physiol B Biochem Mol Biol 2012; 163: 129-137.
    • (2012) Comp Biochem Physiol B Biochem Mol Biol , vol.163 , pp. 129-137
    • Almaida-Pagan, P.F.1
  • 43
    • 0026707798 scopus 로고
    • Effect of age-related lipid peroxidation on membrane fluidity and phospholipase A2: Modulation by dietary restriction
    • Yu BP, Suescun EA, Yang SY: Effect of age-related lipid peroxidation on membrane fluidity and phospholipase A2: modulation by dietary restriction. Mech Ageing Dev 1992; 65: 17-33.
    • (1992) Mech Ageing Dev , vol.65 , pp. 17-33
    • Yu, B.P.1    Suescun, E.A.2    Yang, S.Y.3
  • 44
    • 0030915483 scopus 로고    scopus 로고
    • Mitochondrial decay in hepatocytes from old rats: Membrane potential declines, heterogeneity and oxidants increase
    • Hagen TM, et al: Mitochondrial decay in hepatocytes from old rats: membrane potential declines, heterogeneity and oxidants increase. Proc Natl Acad Sci USA 1997; 94: 3064-3069.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3064-3069
    • Hagen, T.M.1
  • 45
    • 52949106861 scopus 로고    scopus 로고
    • Membrane phospholipids, lipoxidative damage and molecular integrity: A causal role in aging and longevity
    • Pamplona R: Membrane phospholipids, lipoxidative damage and molecular integrity: a causal role in aging and longevity. Biochim Biophys Acta 2008; 1777: 1249-1262.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1249-1262
    • Pamplona, R.1
  • 46
    • 0034891121 scopus 로고    scopus 로고
    • Lipid peroxidation in aging and age-dependent diseases
    • Spiteller G: Lipid peroxidation in aging and age-dependent diseases. Exp Gerontol 2001; 36: 1425-1457.
    • (2001) Exp Gerontol , vol.36 , pp. 1425-1457
    • Spiteller, G.1
  • 47
    • 2342577555 scopus 로고    scopus 로고
    • Modification of the longevity-related degree of fatty acid unsaturation modulates oxidative damage to proteins and mitochondrial DNA in liver and brain
    • Pamplona R, et al: Modification of the longevity-related degree of fatty acid unsaturation modulates oxidative damage to proteins and mitochondrial DNA in liver and brain. Exp Gerontol 2004; 39: 725-733.
    • (2004) Exp Gerontol , vol.39 , pp. 725-733
    • Pamplona, R.1
  • 48
    • 0346731073 scopus 로고    scopus 로고
    • Maillard reaction products in tissue proteins: New products and new perspectives
    • Thorpe SR, Baynes JW: Maillard reaction products in tissue proteins: new products and new perspectives. Amino Acids 2003; 25: 275-281.
    • (2003) Amino Acids , vol.25 , pp. 275-281
    • Thorpe, S.R.1    Baynes, J.W.2
  • 49
    • 69949091187 scopus 로고    scopus 로고
    • Response to the increase of oxidative stress and mutation of mitochondrial DNA in aging
    • Ma YS, et al: Response to the increase of oxidative stress and mutation of mitochondrial DNA in aging. Biochim Biophys Acta 2009; 1790: 1021-1029.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1021-1029
    • Ma, Y.S.1
  • 50
    • 33744972513 scopus 로고    scopus 로고
    • Mitochondrial protein oxidation and degradation in response to oxidative stress and aging
    • Bulteau AL, Szweda LI, Friguet B: Mitochondrial protein oxidation and degradation in response to oxidative stress and aging. Exp Gerontol 2006; 41: 653-657.
    • (2006) Exp Gerontol , vol.41 , pp. 653-657
    • Bulteau, A.L.1    Szweda, L.I.2    Friguet, B.3
  • 51
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett BS, Stadtman ER: Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 1997; 272: 20313-20316.
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 52
    • 0033120863 scopus 로고    scopus 로고
    • Fe-S proteins in sensing and regulatory functions
    • Beinert H, Kiley PJ: Fe-S proteins in sensing and regulatory functions. Curr Opin Chem Biol 1999; 3: 152-157.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 152-157
    • Beinert, H.1    Kiley, P.J.2
  • 53
    • 67549136242 scopus 로고    scopus 로고
    • Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect
    • Veatch JR, et al: Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect. Cell 2009; 137: 1247-1258.
    • (2009) Cell , vol.137 , pp. 1247-1258
    • Veatch, J.R.1
  • 54
    • 0036790385 scopus 로고    scopus 로고
    • Oxidative stress, mitochondrial DNA mutation, and impairment of antioxidant enzymes in aging
    • Wei YH, Lee HC: Oxidative stress, mitochondrial DNA mutation, and impairment of antioxidant enzymes in aging. Exp Biol Med (Maywood) 2002; 227: 671-682.
    • (2002) Exp Biol Med (Maywood) , vol.227 , pp. 671-682
    • Wei, Y.H.1    Lee, H.C.2
  • 55
    • 79959450877 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in disease and aging
    • Park CB, Larsson NG: Mitochondrial DNA mutations in disease and aging. J Cell Biol 2011; 193: 809-818.
    • (2011) J Cell Biol , vol.193 , pp. 809-818
    • Park, C.B.1    Larsson, N.G.2
  • 56
    • 0003097634 scopus 로고    scopus 로고
    • Protein degradation in mitochondria: Implications for oxidative stress, aging and disease: A novel etiological classification of mitochondrial proteolytic disorders
    • Bota DA, Davies KJ: Protein degradation in mitochondria: implications for oxidative stress, aging and disease: a novel etiological classification of mitochondrial proteolytic disorders. Mitochondrion 2001; 1: 33-49.
    • (2001) Mitochondrion , vol.1 , pp. 33-49
    • Bota, D.A.1    Davies, K.J.2
  • 57
    • 77954490419 scopus 로고    scopus 로고
    • Oxidized mitochondrial protein degradation and repair in aging and oxidative stress
    • Ugarte N, Petropoulos I, Friguet B: Oxidized mitochondrial protein degradation and repair in aging and oxidative stress. Antioxid Redox Signal 2010; 13: 539-549.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 539-549
    • Ugarte, N.1    Petropoulos, I.2    Friguet, B.3
  • 58
    • 58949084649 scopus 로고    scopus 로고
    • Base excision repair of oxidative DNA damage and association with cancer and aging
    • Maynard S, et al: Base excision repair of oxidative DNA damage and association with cancer and aging. Carcinogenesis 2009; 30: 2-10.
    • (2009) Carcinogenesis , vol.30 , pp. 2-10
    • Maynard, S.1
  • 59
    • 84860704002 scopus 로고    scopus 로고
    • Oxidative genome damage and its repair: Implications in aging and neurodegenerative diseases
    • Hegde ML, et al: Oxidative genome damage and its repair: implications in aging and neurodegenerative diseases. Mech Ageing Dev 2012; 133: 157-168.
    • (2012) Mech Ageing Dev , vol.133 , pp. 157-168
    • Hegde, M.L.1
  • 60
    • 33644992894 scopus 로고    scopus 로고
    • Mitochondrial DNA maintenance and bioenergetics
    • Stuart JA, Brown MF: Mitochondrial DNA maintenance and bioenergetics. Biochim Biophys Acta 2006; 1757: 79-89.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 79-89
    • Stuart, J.A.1    Brown, M.F.2
  • 62
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters JJ: Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res 2005; 8: 3-5.
    • (2005) Rejuvenation Res , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 63
    • 79959354999 scopus 로고    scopus 로고
    • Mitochondria and the autophagy-inflammation-cell death axis in organismal aging
    • Green DR, Galluzzi L, Kroemer G: Mitochondria and the autophagy-inflammation-cell death axis in organismal aging. Science 2011; 333: 1109-1112.
    • (2011) Science , vol.333 , pp. 1109-1112
    • Green, D.R.1    Galluzzi, L.2    Kroemer, G.3
  • 65
    • 79955945927 scopus 로고    scopus 로고
    • Mitochondrial autophagy in neural function, neurodegenerative disease, neuron cell death, and aging
    • Batlevi Y, La Spada AR: Mitochondrial autophagy in neural function, neurodegenerative disease, neuron cell death, and aging. Neurobiol Dis 2011; 43: 46-51.
    • (2011) Neurobiol Dis , vol.43 , pp. 46-51
    • Batlevi, Y.1    La Spada, A.R.2
  • 66
    • 34548655310 scopus 로고    scopus 로고
    • Highly resistant macromolecular components and low rate of generation of endogenous damage: Two key traits of longevity
    • Pamplona R, Barja G: Highly resistant macromolecular components and low rate of generation of endogenous damage: two key traits of longevity. Ageing Res Rev 2007; 6: 189-210.
    • (2007) Ageing Res Rev , vol.6 , pp. 189-210
    • Pamplona, R.1    Barja, G.2
  • 67
    • 0036236733 scopus 로고    scopus 로고
    • Membrane fatty acid unsaturation, protection against oxidative stress, and maximum life span: A homeoviscous-longevity adaptation?
    • Pamplona R, Barja G, Portero-Otin M: Membrane fatty acid unsaturation, protection against oxidative stress, and maximum life span: a homeoviscous-longevity adaptation? Ann NY Acad Sci 2002; 959: 475-490.
    • (2002) Ann NY Acad Sci , vol.959 , pp. 475-490
    • Pamplona, R.1    Barja, G.2    Portero-Otin, M.3
  • 68
    • 33646704229 scopus 로고    scopus 로고
    • Is the mitochondrial free radical theory of aging intact?
    • Sanz A, Pamplona R, Barja G: Is the mitochondrial free radical theory of aging intact? Antioxid Redox Signal 2006; 8: 582-599.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 582-599
    • Sanz, A.1    Pamplona, R.2    Barja, G.3
  • 69
    • 84867756222 scopus 로고    scopus 로고
    • Mitochondria and organismal longevity
    • Hwang AB, Jeong DE, Lee SJ: Mitochondria and organismal longevity. Curr Genomics 2012; 13: 519-532.
    • (2012) Curr Genomics , vol.13 , pp. 519-532
    • Hwang, A.B.1    Jeong, D.E.2    Lee, S.J.3
  • 70
    • 0032947552 scopus 로고    scopus 로고
    • Interorganelle signaling is a determinant of longevity in Saccharomyces cerevisiae
    • Kirchman PA, et al: Interorganelle signaling is a determinant of longevity in Saccharomyces cerevisiae . Genetics 1999; 152: 179-190.
    • (1999) Genetics , vol.152 , pp. 179-190
    • Kirchman, P.A.1
  • 71
    • 0035515923 scopus 로고    scopus 로고
    • Mitochondrial electron transport is a key determinant of life span in Caenorhabditis elegans
    • Feng J, Bussiere F, Hekimi S: Mitochondrial electron transport is a key determinant of life span in Caenorhabditis elegans . Dev Cell 2001; 1: 633-644.
    • (2001) Dev Cell , vol.1 , pp. 633-644
    • Feng, J.1    Bussiere, F.2    Hekimi, S.3
  • 72
    • 0037228016 scopus 로고    scopus 로고
    • A systematic RNAi screen identifies a critical role for mitochondria in C. Elegans longevity
    • Lee SS, et al: A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity. Nat Genet 2003; 33: 40-48.
    • (2003) Nat Genet , vol.33 , pp. 40-48
    • Lee, S.S.1
  • 73
    • 26944501617 scopus 로고    scopus 로고
    • Evolutionary conservation of the clk- 1-dependent mechanism of longevity: Loss of mclk1 increases cellular fitness and lifespan in mice
    • Liu X, et al: Evolutionary conservation of the clk- 1-dependent mechanism of longevity: loss of mclk1 increases cellular fitness and lifespan in mice. Genes Dev 2005; 19: 2424-2434.
    • (2005) Genes Dev , vol.19 , pp. 2424-2434
    • Liu, X.1
  • 74
    • 33847304164 scopus 로고    scopus 로고
    • Increased longevity and refractoriness to Ca 2+ -dependent neurodegeneration in Surf1 knockout mice
    • Dell'agnello C, et al: Increased longevity and refractoriness to Ca 2+ -dependent neurodegeneration in Surf1 knockout mice. Hum Mol Genet 2007; 16: 431-444.
    • (2007) Hum Mol Genet , vol.16 , pp. 431-444
    • Dell'agnello, C.1
  • 75
    • 70349782312 scopus 로고    scopus 로고
    • Extension of Drosophila life span by RNAi of the mitochondrial respiratory chain
    • Copeland JM, et al: Extension of Drosophila life span by RNAi of the mitochondrial respiratory chain. Curr Biol 2009; 19: 1591-1598.
    • (2009) Curr Biol , vol.19 , pp. 1591-1598
    • Copeland, J.M.1
  • 76
    • 77956241785 scopus 로고    scopus 로고
    • Two modes of mitochondrial dysfunction lead independently to lifespan extension in Caenorhabditis elegans
    • Yang W, Hekimi S: Two modes of mitochondrial dysfunction lead independently to lifespan extension in Caenorhabditis elegans . Aging Cell 2010; 9: 433-447.
    • (2010) Aging Cell , vol.9 , pp. 433-447
    • Yang, W.1    Hekimi, S.2
  • 77
    • 0037147103 scopus 로고    scopus 로고
    • Rates of behavior and aging specified by mitochondrial function during development
    • Dillin A, et al: Rates of behavior and aging specified by mitochondrial function during development. Science 2002; 298: 2398-2401.
    • (2002) Science , vol.298 , pp. 2398-2401
    • Dillin, A.1
  • 78
    • 0033529032 scopus 로고    scopus 로고
    • Apparent uncoupling of energy production and consumption in long-lived Clk mutants of Caenorhabditis elegans
    • Braeckman BP, et al: Apparent uncoupling of energy production and consumption in long-lived Clk mutants of Caenorhabditis elegans . Curr Biol 1999; 9: 493-496.
    • (1999) Curr Biol , vol.9 , pp. 493-496
    • Braeckman, B.P.1
  • 79
    • 2642580016 scopus 로고    scopus 로고
    • Premature ageing in mice expressing defective mitochondrial DNA polymerase
    • Trifunovic A, et al: Premature ageing in mice expressing defective mitochondrial DNA polymerase. Nature 2004; 429: 417-423.
    • (2004) Nature , vol.429 , pp. 417-423
    • Trifunovic, A.1
  • 80
    • 22344456832 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
    • Kujoth GC, et al: Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging. Science 2005; 309: 481-484.
    • (2005) Science , vol.309 , pp. 481-484
    • Kujoth, G.C.1
  • 81
    • 41349087783 scopus 로고    scopus 로고
    • DNA deletions and clonal mutations drive premature aging in mitochondrial mutator mice
    • Vermulst M, et al: DNA deletions and clonal mutations drive premature aging in mitochondrial mutator mice. Nat Genet 2008; 40: 392-394.
    • (2008) Nat Genet , vol.40 , pp. 392-394
    • Vermulst, M.1
  • 82
    • 2342520175 scopus 로고    scopus 로고
    • Deficiencies in mouse Myh and Ogg1 result in tumor predisposition and G to T mutations in codon12 of the K-ras oncogene in lung tumors
    • Xie Y, et al: Deficiencies in mouse Myh and Ogg1 result in tumor predisposition and G to T mutations in codon12 of the K-ras oncogene in lung tumors. Cancer Res 2004; 64: 3096-3102.
    • (2004) Cancer Res , vol.64 , pp. 3096-3102
    • Xie, Y.1
  • 83
    • 13244277942 scopus 로고    scopus 로고
    • CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life
    • Elchuri S, et al: CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life. Oncogene 2005; 24: 367-380.
    • (2005) Oncogene , vol.24 , pp. 367-380
    • Elchuri, S.1
  • 84
    • 0024547664 scopus 로고
    • Null mutation of copper/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity
    • Phillips JP, et al: Null mutation of copper/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity. Proc Natl Acad Sci USA 1989; 86: 2761-2765.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2761-2765
    • Phillips, J.P.1
  • 85
    • 84859483420 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress caused by Sod2 deficiency promotes cellular senescence and aging phenotypes in the skin
    • Velarde MC, et al: Mitochondrial oxidative stress caused by Sod2 deficiency promotes cellular senescence and aging phenotypes in the skin. Aging (Albany NY) 2012; 4: 3-12.
    • (2012) Aging (Albany NY) , vol.4 , pp. 3-12
    • Velarde, M.C.1
  • 86
    • 0034284973 scopus 로고    scopus 로고
    • Extension of life-span with superoxide dismutase/catalase mimetics
    • Melov S, et al: Extension of life-span with superoxide dismutase/catalase mimetics. Science 2000; 289: 1567-1569.
    • (2000) Science , vol.289 , pp. 1567-1569
    • Melov, S.1
  • 87
    • 84879409744 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants and metabolic modulators as pharmacological interventions to slow ageing
    • Gruber J, et al: Mitochondria-targeted antioxidants and metabolic modulators as pharmacological interventions to slow ageing. Biotechnol Adv 2013; 31: 563-592.
    • (2013) Biotechnol Adv , vol.31 , pp. 563-592
    • Gruber, J.1
  • 88
    • 0028220114 scopus 로고
    • Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • Orr WC, Sohal RS: Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster . Science 1994; 263: 1128-1130.
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 89
    • 21144434217 scopus 로고    scopus 로고
    • Extension of murine life span by overexpression of catalase targeted to mitochondria
    • Schriner SE, et al: Extension of murine life span by overexpression of catalase targeted to mitochondria. Science 2005; 308: 1909-1911.
    • (2005) Science , vol.308 , pp. 1909-1911
    • Schriner, S.E.1
  • 90
    • 78649497300 scopus 로고    scopus 로고
    • Targeted expression of catalase to mitochondria prevents age-associated reductions in mitochondrial function and insulin resistance
    • Lee HY, et al: Targeted expression of catalase to mitochondria prevents age-associated reductions in mitochondrial function and insulin resistance. Cell Metab 2010; 12: 668-674.
    • (2010) Cell Metab , vol.12 , pp. 668-674
    • Lee, H.Y.1
  • 91
    • 78049434938 scopus 로고    scopus 로고
    • Age-dependent cardiomyopathy in mitochondrial mutator mice is attenuated by overexpression of catalase targeted to mitochondria
    • Dai DF, et al: Age-dependent cardiomyopathy in mitochondrial mutator mice is attenuated by overexpression of catalase targeted to mitochondria. Aging Cell 2010; 9: 536-544.
    • (2010) Aging Cell , vol.9 , pp. 536-544
    • Dai, D.F.1
  • 92
    • 1842544684 scopus 로고    scopus 로고
    • Effects of short-and mediumterm calorie restriction on muscle mitochondrial proton leak and reactive oxygen species production
    • Bevilacqua L, et al: Effects of short-and mediumterm calorie restriction on muscle mitochondrial proton leak and reactive oxygen species production. Am J Physiol Endocrinol Metab 2004; 286: E852-E861.
    • (2004) Am J Physiol Endocrinol Metab , vol.286
    • Bevilacqua, L.1
  • 93
    • 0035403165 scopus 로고    scopus 로고
    • Caloric restriction decreases mitochondrial free radical generation at complex i and lowers oxidative damage to mitochondrial DNA in the rat heart
    • Gredilla R, et al: Caloric restriction decreases mitochondrial free radical generation at complex I and lowers oxidative damage to mitochondrial DNA in the rat heart. FASEB J 2001; 15: 1589-1591.
    • (2001) FASEB J , vol.15 , pp. 1589-1591
    • Gredilla, R.1
  • 94
    • 13844256455 scopus 로고    scopus 로고
    • Protein restriction without strong caloric restriction decreases mitochondrial oxygen radical production and oxidative DNA damage in rat liver
    • Sanz A, Caro P, Barja G: Protein restriction without strong caloric restriction decreases mitochondrial oxygen radical production and oxidative DNA damage in rat liver. J Bioenerg Biomembr 2004; 36: 545-552.
    • (2004) J Bioenerg Biomembr , vol.36 , pp. 545-552
    • Sanz, A.1    Caro, P.2    Barja, G.3
  • 95
    • 0033581704 scopus 로고    scopus 로고
    • The p66shc adaptor protein controls oxidative stress response and life span in mammals
    • Migliaccio E, et al: The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 1999; 402: 309-313.
    • (1999) Nature , vol.402 , pp. 309-313
    • Migliaccio, E.1
  • 96
    • 22744447211 scopus 로고    scopus 로고
    • Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis
    • Giorgio M, et al: Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 2005; 122: 221-233.
    • (2005) Cell , vol.122 , pp. 221-233
    • Giorgio, M.1
  • 97
    • 0037192473 scopus 로고    scopus 로고
    • Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway
    • Nemoto S, Finkel T: Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science 2002; 295: 2450-2452.
    • (2002) Science , vol.295 , pp. 2450-2452
    • Nemoto, S.1    Finkel, T.2
  • 98
    • 0041885207 scopus 로고    scopus 로고
    • Linking oxidative stress and genetics of aging with p66Shc signaling and forkhead transcription factors
    • Purdom S, Chen QM: Linking oxidative stress and genetics of aging with p66Shc signaling and forkhead transcription factors. Biogerontology 2003; 4: 181-191.
    • (2003) Biogerontology , vol.4 , pp. 181-191
    • Purdom, S.1    Chen, Q.M.2
  • 99
    • 77953806512 scopus 로고    scopus 로고
    • Oxidative stress-dependent p66Shc phosphorylation in skin fibroblasts of children with mitochondrial disorders
    • Lebiedzinska M, et al: Oxidative stress-dependent p66Shc phosphorylation in skin fibroblasts of children with mitochondrial disorders. Biochim Biophys Acta 2010; 1797: 952-960.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 952-960
    • Lebiedzinska, M.1
  • 100
    • 37549002891 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
    • Lombard DB, et al: Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol Cell Biol 2007; 27: 8807-8814.
    • (2007) Mol Cell Biol , vol.27 , pp. 8807-8814
    • Lombard, D.B.1
  • 101
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • Qiu X, et al: Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab 2010; 12: 662-667.
    • (2010) Cell Metab , vol.12 , pp. 662-667
    • Qiu, X.1
  • 102
    • 78650248160 scopus 로고    scopus 로고
    • Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress
    • Tao R, et al: Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress. Mol Cell 2010; 40: 893-904.
    • (2010) Mol Cell , vol.40 , pp. 893-904
    • Tao, R.1
  • 103
    • 80052291180 scopus 로고    scopus 로고
    • Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production
    • Jing E, et al: Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. Proc Natl Acad Sci USA 2011; 108: 14608-14613.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14608-14613
    • Jing, E.1
  • 104
    • 78651468722 scopus 로고    scopus 로고
    • Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
    • Someya S, et al: Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 2010; 143: 802-812.
    • (2010) Cell , vol.143 , pp. 802-812
    • Someya, S.1
  • 105
    • 79953210362 scopus 로고    scopus 로고
    • Regulation of PGC-1alpha, a nodal regulator of mitochondrial biogenesis
    • Fernandez-Marcos PJ, Auwerx J: Regulation of PGC-1alpha, a nodal regulator of mitochondrial biogenesis. Am J Clin Nutr 2011; 93: 884S-890S.
    • (2011) Am J Clin Nutr , vol.93
    • Fernandez-Marcos, P.J.1    Auwerx, J.2
  • 106
    • 80455143200 scopus 로고    scopus 로고
    • Modulation of longevity and tissue homeostasis by the Drosophila PGC-1 homolog
    • Rera M, et al: Modulation of longevity and tissue homeostasis by the Drosophila PGC-1 homolog. Cell Metab 2011; 14: 623-634.
    • (2011) Cell Metab , vol.14 , pp. 623-634
    • Rera, M.1
  • 107
    • 39149086121 scopus 로고    scopus 로고
    • Stems cells and the pathways to aging and cancer
    • Rossi DJ, Jamieson CH, Weissman IL: Stems cells and the pathways to aging and cancer. Cell 2008; 132: 681-696.
    • (2008) Cell , vol.132 , pp. 681-696
    • Rossi, D.J.1    Jamieson, C.H.2    Weissman, I.L.3
  • 108
    • 33745614062 scopus 로고    scopus 로고
    • Stem cells, ageing and the quest for immortality
    • Rando TA: Stem cells, ageing and the quest for immortality. Nature 2006; 441: 1080-1086.
    • (2006) Nature , vol.441 , pp. 1080-1086
    • Rando, T.A.1
  • 109
    • 84870290830 scopus 로고    scopus 로고
    • Redox regulation of stem/ progenitor cells and bone marrow iche
    • Urao N, Ushio-Fukai M: Redox regulation of stem/ progenitor cells and bone marrow iche. Free Radic Biol Med 2013; 54: 26-39.
    • (2013) Free Radic Biol Med , vol.54 , pp. 26-39
    • Urao, N.1    Ushio-Fukai, M.2
  • 110
    • 80052930073 scopus 로고    scopus 로고
    • Accumulation of oxidative DNA damage restricts the self-renewal capacity of human hematopoietic stem cells
    • Yahata T, et al: Accumulation of oxidative DNA damage restricts the self-renewal capacity of human hematopoietic stem cells. Blood 2011; 118: 2941-2950.
    • (2011) Blood , vol.118 , pp. 2941-2950
    • Yahata, T.1
  • 111
    • 69049087814 scopus 로고    scopus 로고
    • Mitochondrial functionality in reproduction: From gonads and gametes to embryos and embryonic stem cells
    • Ramalho-Santos J, et al: Mitochondrial functionality in reproduction: from gonads and gametes to embryos and embryonic stem cells. Hum Reprod Update 2009; 15: 553-572.
    • (2009) Hum Reprod Update , vol.15 , pp. 553-572
    • Ramalho-Santos, J.1
  • 112
    • 84867905197 scopus 로고    scopus 로고
    • Mitochondrial superoxide production negatively regulates neural progenitor proliferation and cerebral cortical development
    • Hou Y, et al: Mitochondrial superoxide production negatively regulates neural progenitor proliferation and cerebral cortical development. Stem Cells 2012; 30: 2535-2547.
    • (2012) Stem Cells , vol.30 , pp. 2535-2547
    • Hou, Y.1
  • 113
    • 84873243518 scopus 로고    scopus 로고
    • Selective impairment on the proliferation of neural progenitor cells by oxidative phosphorylation disruption
    • Lee Y, et al: Selective impairment on the proliferation of neural progenitor cells by oxidative phosphorylation disruption. Neurosci Lett 2013; 535: 134-139.
    • (2013) Neurosci Lett , vol.535 , pp. 134-139
    • Lee, Y.1
  • 114
    • 49249086654 scopus 로고    scopus 로고
    • Coordinated changes of mitochondrial biogenesis and antioxidant enzymes during osteogenic differentiation of human mesenchymal stem cells
    • Chen CT, et al: Coordinated changes of mitochondrial biogenesis and antioxidant enzymes during osteogenic differentiation of human mesenchymal stem cells. Stem Cells 2008; 26: 960-968.
    • (2008) Stem Cells , vol.26 , pp. 960-968
    • Chen, C.T.1
  • 115
    • 84876694073 scopus 로고    scopus 로고
    • Ketamine enhances human neural stem cell proliferation and induces neuronal apoptosis via reactive oxygen species-mediated mitochondrial pathway
    • Bai X, et al: Ketamine enhances human neural stem cell proliferation and induces neuronal apoptosis via reactive oxygen species-mediated mitochondrial pathway. Anesth Analg 2013; 116: 869-880.
    • (2013) Anesth Analg , vol.116 , pp. 869-880
    • Bai, X.1
  • 116
    • 84869830820 scopus 로고    scopus 로고
    • N-acetylcysteine protects induced pluripotent stem cells from in vitro stress: Impact on differentiation outcome
    • Berniakovich I, Laricchia-Robbio L, Izpisua Belmonte JC: N-acetylcysteine protects induced pluripotent stem cells from in vitro stress: impact on differentiation outcome. Int J Dev Biol 2012; 56: 729-735.
    • (2012) Int J Dev Biol , vol.56 , pp. 729-735
    • Berniakovich, I.1    Laricchia-Robbio, L.2    Izpisua Belmonte, J.C.3
  • 117
    • 33749187336 scopus 로고    scopus 로고
    • Increased 'vigilance' of antioxidant mechanisms in neural stem cells potentiates their capability to resist oxidative stress
    • Madhavan L, Ourednik V, Ourednik J: Increased 'vigilance' of antioxidant mechanisms in neural stem cells potentiates their capability to resist oxidative stress. Stem Cells 2006; 24: 2110-2119.
    • (2006) Stem Cells , vol.24 , pp. 2110-2119
    • Madhavan, L.1    Ourednik, V.2    Ourednik, J.3
  • 118
    • 35548936968 scopus 로고    scopus 로고
    • A low level of reactive oxygen species selects for primitive hematopoietic stem cells that may reside in the low-oxygenic niche
    • Jang YY, Sharkis SJ: A low level of reactive oxygen species selects for primitive hematopoietic stem cells that may reside in the low-oxygenic niche. Blood 2007; 110: 3056-3063.
    • (2007) Blood , vol.110 , pp. 3056-3063
    • Jang, Y.Y.1    Sharkis, S.J.2
  • 119
    • 84879559313 scopus 로고    scopus 로고
    • Cord blood-derived CD34+ hematopoietic cells with low mitochondrial mass are enriched in hematopoietic repopulating stem cell function
    • Romero-Moya D, et al: Cord blood-derived CD34+ hematopoietic cells with low mitochondrial mass are enriched in hematopoietic repopulating stem cell function. Haematologica 2013; 98: 1022-1029.
    • (2013) Haematologica , vol.98 , pp. 1022-1029
    • Romero-Moya, D.1
  • 120
    • 55049083950 scopus 로고    scopus 로고
    • Stem cells, phenotypic inversion, and differentiation
    • Siggins RW, et al: Stem cells, phenotypic inversion, and differentiation. Int J Clin Exp Med 2008; 1: 2-21.
    • (2008) Int J Clin Exp Med , vol.1 , pp. 2-21
    • Siggins, R.W.1
  • 121
    • 33747875396 scopus 로고    scopus 로고
    • Dynamic changes in mitochondrial biogenesis and antioxidant enzymes during the spontaneous differentiation of human embryonic stem cells
    • Cho YM, et al: Dynamic changes in mitochondrial biogenesis and antioxidant enzymes during the spontaneous differentiation of human embryonic stem cells. Biochem Biophys Res Commun 2006; 348: 1472-1478.
    • (2006) Biochem Biophys Res Commun , vol.348 , pp. 1472-1478
    • Cho, Y.M.1
  • 122
    • 13744262804 scopus 로고    scopus 로고
    • Derivation and characterization of new human embryonic stem cell lines: SNUhES1, SNUhES2, and SNUhES3
    • Oh SK, et al: Derivation and characterization of new human embryonic stem cell lines: SNUhES1, SNUhES2, and SNUhES3. Stem Cells 2005; 23: 211-219.
    • (2005) Stem Cells , vol.23 , pp. 211-219
    • Oh, S.K.1
  • 123
    • 16244366793 scopus 로고    scopus 로고
    • The impact of mitochondrial genetics on male infertility
    • St John JC, Jokhi RP, Barratt CL: The impact of mitochondrial genetics on male infertility. Int J Androl 2005; 28: 65-73.
    • (2005) Int J Androl , vol.28 , pp. 65-73
    • St John, J.C.1    Jokhi, R.P.2    Barratt, C.L.3
  • 124
    • 27744563079 scopus 로고    scopus 로고
    • The expression of mitochondrial DNA transcription factors during early cardiomyocyte in vitro differentiation from human embryonic stem cells
    • St John JC, et al: The expression of mitochondrial DNA transcription factors during early cardiomyocyte in vitro differentiation from human embryonic stem cells. Cloning Stem Cells 2005; 7: 141-153.
    • (2005) Cloning Stem Cells , vol.7 , pp. 141-153
    • St John, J.C.1
  • 125
    • 33846501510 scopus 로고    scopus 로고
    • Mitochondrial oxidative metabolism is required for the cardiac differentiation of stem cells
    • Chung S, et al: Mitochondrial oxidative metabolism is required for the cardiac differentiation of stem cells. Nat Clin Pract Cardiovasc Med 2007; 4(suppl 1):S60-S67.
    • (2007) Nat Clin Pract Cardiovasc Med , vol.4 , Issue.SUPPL. 1
    • Chung, S.1
  • 126
    • 40949088547 scopus 로고    scopus 로고
    • Downregulation of multiple stress defense mechanisms during differentiation of human embryonic stem cells
    • Saretzki G, et al: Downregulation of multiple stress defense mechanisms during differentiation of human embryonic stem cells. Stem Cells 2008; 26: 455-464.
    • (2008) Stem Cells , vol.26 , pp. 455-464
    • Saretzki, G.1
  • 127
    • 22544446192 scopus 로고    scopus 로고
    • Characterization of mitochondrial and extra-mitochondrial oxygen consuming reactions in human hematopoietic stem cells. Novel evidence of the occurrence of NAD(P)H oxidase activity
    • Piccoli C, et al: Characterization of mitochondrial and extra-mitochondrial oxygen consuming reactions in human hematopoietic stem cells. Novel evidence of the occurrence of NAD(P)H oxidase activity. J Biol Chem 2005; 280: 26467-26476.
    • (2005) J Biol Chem , vol.280 , pp. 26467-26476
    • Piccoli, C.1
  • 128
    • 7244250309 scopus 로고    scopus 로고
    • Regulation of oxidative stress by ATM is required for self-renewal of haematopoietic stem cells
    • Ito K, et al: Regulation of oxidative stress by ATM is required for self-renewal of haematopoietic stem cells. Nature 2004; 431: 997-1002.
    • (2004) Nature , vol.431 , pp. 997-1002
    • Ito, K.1
  • 129
    • 79955778862 scopus 로고    scopus 로고
    • Telomerase reverse transcriptase protects ATM-deficient hematopoietic stem cells from ROS-induced apoptosis through a telomere-independent mechanism
    • Nitta E, et al: Telomerase reverse transcriptase protects ATM-deficient hematopoietic stem cells from ROS-induced apoptosis through a telomere-independent mechanism. Blood 2011; 117: 4169-4180.
    • (2011) Blood , vol.117 , pp. 4169-4180
    • Nitta, E.1
  • 130
    • 78650302424 scopus 로고    scopus 로고
    • ROS-mediated amplification of AKT/mTOR signalling pathway leads to myeloproliferative syndrome in Foxo3 -/- mice
    • Yalcin S, et al: ROS-mediated amplification of AKT/mTOR signalling pathway leads to myeloproliferative syndrome in Foxo3 -/- mice. EMBO J 2010; 29: 4118-4131.
    • (2010) EMBO J , vol.29 , pp. 4118-4131
    • Yalcin, S.1
  • 131
    • 33846419112 scopus 로고    scopus 로고
    • FoxOs are critical mediators of hematopoietic stem cell resistance to physiologic oxidative stress
    • Tothova Z, et al: FoxOs are critical mediators of hematopoietic stem cell resistance to physiologic oxidative stress. Cell 2007; 128: 325-339.
    • (2007) Cell , vol.128 , pp. 325-339
    • Tothova, Z.1
  • 132
    • 84866876832 scopus 로고    scopus 로고
    • Mouse hematopoietic cell-targeted STAT3 deletion: Stem/progenitor cell defects, mitochondrial dysfunction, ROS overproduction, and a rapid aging-like phenotype
    • Mantel C, et al: Mouse hematopoietic cell-targeted STAT3 deletion: stem/progenitor cell defects, mitochondrial dysfunction, ROS overproduction, and a rapid aging-like phenotype. Blood 2012; 120: 2589-2599.
    • (2012) Blood , vol.120 , pp. 2589-2599
    • Mantel, C.1
  • 133
    • 79551515518 scopus 로고    scopus 로고
    • FIP200, an essential component of mammalian autophagy is indispensible for fetal hematopoiesis
    • Liu F, Guan JL: FIP200, an essential component of mammalian autophagy is indispensible for fetal hematopoiesis. Autophagy 2011; 7: 229-230.
    • (2011) Autophagy , vol.7 , pp. 229-230
    • Liu, F.1    Guan, J.L.2
  • 134
    • 84876893671 scopus 로고    scopus 로고
    • FIP200 is required for maintenance and differentiation of postnatal neural stem cells
    • Wang C, et al: FIP200 is required for maintenance and differentiation of postnatal neural stem cells. Nat Neurosci 2013; 16: 532-542.
    • (2013) Nat Neurosci , vol.16 , pp. 532-542
    • Wang, C.1
  • 135
    • 79960327664 scopus 로고    scopus 로고
    • Mitochondrial peptidase IMMP2L mutation causes early onset of age-associated disorders and impairs adult stem cell self-renewal
    • George SK, et al: Mitochondrial peptidase IMMP2L mutation causes early onset of age-associated disorders and impairs adult stem cell self-renewal. Aging Cell 2011; 10: 584-594.
    • (2011) Aging Cell , vol.10 , pp. 584-594
    • George, S.K.1
  • 136
    • 53349091768 scopus 로고    scopus 로고
    • TSC-mTOR maintains quiescence and function of hematopoietic stem cells by repressing mitochondrial biogenesis and reactive oxygen species
    • Chen C, et al: TSC-mTOR maintains quiescence and function of hematopoietic stem cells by repressing mitochondrial biogenesis and reactive oxygen species. J Exp Med 2008; 205: 2397-2408.
    • (2008) J Exp Med , vol.205 , pp. 2397-2408
    • Chen, C.1
  • 137
    • 65949113818 scopus 로고    scopus 로고
    • The axis of mTOR-mitochondria- ROS and stemness of the hematopoietic stem cells
    • Chen C, et al: The axis of mTOR-mitochondria- ROS and stemness of the hematopoietic stem cells. Cell Cycle 2009; 8: 1158-1160.
    • (2009) Cell Cycle , vol.8 , pp. 1158-1160
    • Chen, C.1
  • 138
    • 84866054806 scopus 로고    scopus 로고
    • MTOR inhibition prevents epithelial stem cell senescence and protects from radiation-induced mucositis
    • Iglesias-Bartolome R, et al: mTOR inhibition prevents epithelial stem cell senescence and protects from radiation-induced mucositis. Cell Stem Cell 2012; 11: 401-414.
    • (2012) Cell Stem Cell , vol.11 , pp. 401-414
    • Iglesias-Bartolome, R.1
  • 139
    • 84883395307 scopus 로고    scopus 로고
    • Lamin A deregulation in human mesenchymal stem cells promotes an impairment in their chondrogenic potential and imbalance in their response to oxidative stress
    • Mateos J, et al: Lamin A deregulation in human mesenchymal stem cells promotes an impairment in their chondrogenic potential and imbalance in their response to oxidative stress. Stem Cell Res 2013; 11: 1137-1148.
    • (2013) Stem Cell Res , vol.11 , pp. 1137-1148
    • Mateos, J.1
  • 140
    • 84878516294 scopus 로고    scopus 로고
    • PGC-1alpha prevents apoptosis in adipose-derived stem cells by reducing reactive oxygen species production in a diabetic microenvironment
    • Jiang XY, et al: PGC-1alpha prevents apoptosis in adipose-derived stem cells by reducing reactive oxygen species production in a diabetic microenvironment. Diabetes Res Clin Pract 2013; 100: 368-375.
    • (2013) Diabetes Res Clin Pract , vol.100 , pp. 368-375
    • Jiang, X.Y.1
  • 141
    • 84860539151 scopus 로고    scopus 로고
    • NADPH oxidase2 regulates bone marrow microenvironment following hindlimb ischemia: Role in reparative mobilization of progenitor cells
    • Urao N, et al: NADPH oxidase2 regulates bone marrow microenvironment following hindlimb ischemia: role in reparative mobilization of progenitor cells. Stem Cells 2012; 30: 923-934.
    • (2012) Stem Cells , vol.30 , pp. 923-934
    • Urao, N.1
  • 142
    • 77956217067 scopus 로고    scopus 로고
    • Regulation of the HIF-1alpha level is essential for hematopoietic stem cells
    • Takubo K, et al: Regulation of the HIF-1alpha level is essential for hematopoietic stem cells. Cell Stem Cell 2010; 7: 391-402.
    • (2010) Cell Stem Cell , vol.7 , pp. 391-402
    • Takubo, K.1
  • 143
    • 35848943667 scopus 로고    scopus 로고
    • Hematopoietic stem cell quiescence attenuates DNA damage response and permits DNA damage accumulation during aging
    • Rossi DJ, et al: Hematopoietic stem cell quiescence attenuates DNA damage response and permits DNA damage accumulation during aging. Cell Cycle 2007; 6: 2371-2376.
    • (2007) Cell Cycle , vol.6 , pp. 2371-2376
    • Rossi, D.J.1
  • 144
    • 34250007142 scopus 로고    scopus 로고
    • Deficiencies in DNA damage repair limit the function of haematopoietic stem cells with age
    • Rossi DJ, et al: Deficiencies in DNA damage repair limit the function of haematopoietic stem cells with age. Nature 2007; 447: 725-729.
    • (2007) Nature , vol.447 , pp. 725-729
    • Rossi, D.J.1
  • 145
    • 84855417557 scopus 로고    scopus 로고
    • Somatic progenitor cell vulnerability to mitochondrial DNA mutagenesis underlies progeroid phenotypes in Polg mutator mice
    • Ahlqvist KJ, et al: Somatic progenitor cell vulnerability to mitochondrial DNA mutagenesis underlies progeroid phenotypes in Polg mutator mice. Cell Metab 2012; 15: 100-109.
    • (2012) Cell Metab , vol.15 , pp. 100-109
    • Ahlqvist, K.J.1
  • 146
    • 0344622606 scopus 로고
    • The serial cultivation of human diploid cell strains
    • Hayflick L, Moorhead PS: The serial cultivation of human diploid cell strains. Exp Cell Res 1961; 25: 585-621.
    • (1961) Exp Cell Res , vol.25 , pp. 585-621
    • Hayflick, L.1    Moorhead, P.S.2
  • 147
    • 13944270339 scopus 로고    scopus 로고
    • Senescent cells, tumor suppression, and organismal aging: Good citizens, bad neighbors
    • Campisi J: Senescent cells, tumor suppression, and organismal aging: good citizens, bad neighbors. Cell 2005; 120: 513-522.
    • (2005) Cell , vol.120 , pp. 513-522
    • Campisi, J.1
  • 148
    • 0017054251 scopus 로고
    • The cell biology of human aging
    • Hayflick L: The cell biology of human aging. N Engl J Med 1976; 295: 1302-1308.
    • (1976) N Engl J Med , vol.295 , pp. 1302-1308
    • Hayflick, L.1
  • 149
    • 85047689866 scopus 로고    scopus 로고
    • Telomeres, stem cells, senescence, and cancer
    • Sharpless NE, DePinho RA: Telomeres, stem cells, senescence, and cancer. J Clin Invest 2004; 113: 160-168.
    • (2004) J Clin Invest , vol.113 , pp. 160-168
    • Sharpless, N.E.1    Depinho, R.A.2
  • 150
    • 38049057905 scopus 로고    scopus 로고
    • DNA damage in telomeres and mitochondria during cellular senescence: Is there a connection?
    • Passos JF, Saretzki G, von Zglinicki T: DNA damage in telomeres and mitochondria during cellular senescence: is there a connection? Nucleic Acids Res 2007; 35: 7505-7513.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7505-7513
    • Passos, J.F.1    Saretzki, G.2    Von Zglinicki, T.3
  • 151
    • 84878771657 scopus 로고    scopus 로고
    • Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging
    • Ngo JK, Pomatto LC, Davies KJ: Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging. Redox Biol 2013; 1: 258-264.
    • (2013) Redox Biol , vol.1 , pp. 258-264
    • Ngo, J.K.1    Pomatto, L.C.2    Davies, K.J.3
  • 152
    • 14944345009 scopus 로고    scopus 로고
    • Ectopic mTERT expression in mouse embryonic stem cells does not affect differentiation but confers resistance to differentiation- and stress-induced p53-dependent apoptosis
    • Lee MK, Hande MP, Sabapathy K: Ectopic mTERT expression in mouse embryonic stem cells does not affect differentiation but confers resistance to differentiation- and stress-induced p53-dependent apoptosis. J Cell Sci 2005; 118: 819-829.
    • (2005) J Cell Sci , vol.118 , pp. 819-829
    • Lee, M.K.1    Hande, M.P.2    Sabapathy, K.3
  • 153
    • 11244347171 scopus 로고    scopus 로고
    • Glycolytic enzymes can modulate cellular life span
    • Kondoh H, et al: Glycolytic enzymes can modulate cellular life span. Cancer Res 2005; 65: 177-185.
    • (2005) Cancer Res , vol.65 , pp. 177-185
    • Kondoh, H.1
  • 154
    • 0029051426 scopus 로고
    • Oxidative DNA damage and senescence of human diploid fibroblast cells
    • Chen Q, et al: Oxidative DNA damage and senescence of human diploid fibroblast cells. Proc Natl Acad Sci USA 1995; 92: 4337-4341.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4337-4341
    • Chen, Q.1
  • 155
    • 0037470062 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase is a major antioxidant in human fibroblasts and slows telomere shortening
    • Serra V, et al: Extracellular superoxide dismutase is a major antioxidant in human fibroblasts and slows telomere shortening. J Biol Chem 2003; 278: 6824-6830.
    • (2003) J Biol Chem , vol.278 , pp. 6824-6830
    • Serra, V.1
  • 156
    • 43049163718 scopus 로고    scopus 로고
    • Free radicals and senescence
    • Lu T, Finkel T: Free radicals and senescence. Exp Cell Res 2008; 314: 1918-1922.
    • (2008) Exp Cell Res , vol.314 , pp. 1918-1922
    • Lu, T.1    Finkel, T.2
  • 157
    • 0042195820 scopus 로고    scopus 로고
    • Oxygen sensitivity severely limits the replicative lifespan of murine fibroblasts
    • Parrinello S, et al: Oxygen sensitivity severely limits the replicative lifespan of murine fibroblasts. Nat Cell Biol 2003; 5: 741-747.
    • (2003) Nat Cell Biol , vol.5 , pp. 741-747
    • Parrinello, S.1
  • 158
    • 0029127226 scopus 로고
    • Mild hyperoxia shortens telomeres and inhibits proliferation of fibroblasts: A model for senescence?
    • von Zglinicki T, et al: Mild hyperoxia shortens telomeres and inhibits proliferation of fibroblasts: a model for senescence? Exp Cell Res 1995; 220: 186-193.
    • (1995) Exp Cell Res , vol.220 , pp. 186-193
    • Von Zglinicki, T.1
  • 159
    • 0010045614 scopus 로고    scopus 로고
    • Extension of life-span by introduction of telomerase into normal human cells
    • Bodnar AG, et al: Extension of life-span by introduction of telomerase into normal human cells. Science 1998; 279: 349-352.
    • (1998) Science , vol.279 , pp. 349-352
    • Bodnar, A.G.1
  • 160
    • 35448962513 scopus 로고    scopus 로고
    • A continuous correlation between oxidative stress and telomere shortening in fibroblasts
    • Richter T, von Zglinicki T: A continuous correlation between oxidative stress and telomere shortening in fibroblasts. Exp Gerontol 2007; 42: 1039-1042.
    • (2007) Exp Gerontol , vol.42 , pp. 1039-1042
    • Richter, T.1    Von Zglinicki, T.2
  • 161
    • 0038331337 scopus 로고    scopus 로고
    • Mitochondrial dysfunction leads to telomere attrition and genomic instability
    • Liu L, et al: Mitochondrial dysfunction leads to telomere attrition and genomic instability. Aging Cell 2002; 1: 40-46.
    • (2002) Aging Cell , vol.1 , pp. 40-46
    • Liu, L.1
  • 162
    • 0041419866 scopus 로고    scopus 로고
    • MitoQ counteracts telomere shortening and elongates lifespan of fibroblasts under mild oxidative stress
    • Saretzki G, Murphy MP, von Zglinicki T: MitoQ counteracts telomere shortening and elongates lifespan of fibroblasts under mild oxidative stress. Aging Cell 2003; 2: 141-143.
    • (2003) Aging Cell , vol.2 , pp. 141-143
    • Saretzki, G.1    Murphy, M.P.2    Von Zglinicki, T.3
  • 163
    • 0037181064 scopus 로고    scopus 로고
    • Site-specific probing of oxidative reactivity and telomerase function using 7,8-dihydro-8-oxoguanine in telomeric DNA
    • Szalai VA, Singer MJ, Thorp HH: Site-specific probing of oxidative reactivity and telomerase function using 7,8-dihydro-8-oxoguanine in telomeric DNA. J Am Chem Soc 2002; 124: 1625-1631.
    • (2002) J Am Chem Soc , vol.124 , pp. 1625-1631
    • Szalai, V.A.1    Singer, M.J.2    Thorp, H.H.3
  • 164
    • 14844354067 scopus 로고    scopus 로고
    • Oxidative damage in telomeric DNA disrupts recognition by TRF1 and TRF2
    • Opresko PL, et al: Oxidative damage in telomeric DNA disrupts recognition by TRF1 and TRF2. Nucleic Acids Res 2005; 33: 1230-1239.
    • (2005) Nucleic Acids Res , vol.33 , pp. 1230-1239
    • Opresko, P.L.1
  • 165
    • 46249125488 scopus 로고    scopus 로고
    • How shelterin protects mammalian telomeres
    • Palm W, de Lange: How shelterin protects mammalian telomeres. Annu Rev Genet 2008; 42: 301-334.
    • (2008) Annu Rev Genet , vol.42 , pp. 301-334
    • Palm, W.1    De Lange2
  • 166
    • 1842611977 scopus 로고    scopus 로고
    • Antioxidants inhibit nuclear export of telomerase reverse transcriptase and delay replicative senescence of endothelial cells
    • Haendeler J, et al: Antioxidants inhibit nuclear export of telomerase reverse transcriptase and delay replicative senescence of endothelial cells. Circ Res 2004; 94: 768-775.
    • (2004) Circ Res , vol.94 , pp. 768-775
    • Haendeler, J.1
  • 167
    • 4344577088 scopus 로고    scopus 로고
    • Role of p53 in sensing oxidative DNA damage in response to reactive oxygen species-generating agents
    • Achanta G, Huang P: Role of p53 in sensing oxidative DNA damage in response to reactive oxygen species-generating agents. Cancer Res 2004; 64: 6233-6239.
    • (2004) Cancer Res , vol.64 , pp. 6233-6239
    • Achanta, G.1    Huang, P.2
  • 168
    • 78649819167 scopus 로고    scopus 로고
    • Positive feedback between p53 and TRF2 during telomere-damage signalling and cellular senescence
    • Fujita K, et al: Positive feedback between p53 and TRF2 during telomere-damage signalling and cellular senescence. Nat Cell Biol 2010; 12: 1205-1212.
    • (2010) Nat Cell Biol , vol.12 , pp. 1205-1212
    • Fujita, K.1
  • 169
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano M, et al: Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 1997; 88: 593-601412.
    • (1997) Cell , vol.88 , pp. 593-601412
    • Serrano, M.1
  • 170
    • 68949096538 scopus 로고    scopus 로고
    • Mitochondrial dysfunction contributes to oncogene-induced senescence
    • Moiseeva O, et al: Mitochondrial dysfunction contributes to oncogene-induced senescence. Mol Cell Biol 2009; 29: 4495-4507.
    • (2009) Mol Cell Biol , vol.29 , pp. 4495-4507
    • Moiseeva, O.1
  • 171
    • 0036137046 scopus 로고    scopus 로고
    • Ageing and apoptosis
    • Zhang Y, Herman B: Ageing and apoptosis. Mech Ageing Dev 2002; 123: 245-260.
    • (2002) Mech Ageing Dev , vol.123 , pp. 245-260
    • Zhang, Y.1    Herman, B.2
  • 172
    • 84862818143 scopus 로고    scopus 로고
    • Mitochondria-ROS crosstalk in the control of cell death and aging
    • Marchi S, et al: Mitochondria-ROS crosstalk in the control of cell death and aging. J Signal Transduct 2012; 2012: 329635.
    • (2012) J Signal Transduct , vol.2012 , pp. 329635
    • Marchi, S.1
  • 173
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky DJ, Emr SD: Autophagy as a regulated pathway of cellular degradation. Science 2000; 290: 1717-1721.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 174
    • 84862779963 scopus 로고    scopus 로고
    • IP Receptors, mitochondria, and Ca signaling: Implications for aging
    • Decuypere JP, et al: IP Receptors, mitochondria, and Ca signaling: implications for aging. J Aging Res 2011; 2011: 920178.
    • (2011) J Aging Res , vol.2011 , pp. 920178
    • Decuypere, J.P.1
  • 175
    • 72649091698 scopus 로고    scopus 로고
    • Mechanisms of life span extension by rapamycin in the fruit fly Drosophila melanogaster
    • Bjedov I, et al: Mechanisms of life span extension by rapamycin in the fruit fly Drosophila melanogaster . Cell Metab 2010; 11: 35-46.
    • (2010) Cell Metab , vol.11 , pp. 35-46
    • Bjedov, I.1
  • 176
    • 84055190702 scopus 로고    scopus 로고
    • Rapamycin-induced glucose intolerance: Hunger or starvation diabetes
    • Blagosklonny MV: Rapamycin-induced glucose intolerance: hunger or starvation diabetes. Cell Cycle 2011; 10: 4217-4224.
    • (2011) Cell Cycle , vol.10 , pp. 4217-4224
    • Blagosklonny, M.V.1
  • 177
    • 67650944993 scopus 로고    scopus 로고
    • Rapamycin fed late in life extends lifespan in genetically heterogeneous mice
    • Harrison DE, et al: Rapamycin fed late in life extends lifespan in genetically heterogeneous mice. Nature 2009; 460: 392-395.
    • (2009) Nature , vol.460 , pp. 392-395
    • Harrison, D.E.1
  • 179
    • 51349095898 scopus 로고    scopus 로고
    • Restoration of chaperonemediated autophagy in aging liver improves cellular maintenance and hepatic function
    • Zhang C, Cuervo AM: Restoration of chaperonemediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat Med 2008; 14: 959-965.
    • (2008) Nat Med , vol.14 , pp. 959-965
    • Zhang, C.1    Cuervo, A.M.2
  • 180
    • 0042508791 scopus 로고    scopus 로고
    • Neuropathologic changes in Alzheimer's disease
    • Wenk GL: Neuropathologic changes in Alzheimer's disease. J Clin Psychiatry 2003; 64(suppl 9):7-10.
    • (2003) J Clin Psychiatry , vol.64 , Issue.SUPPL. 9 , pp. 7-10
    • Wenk, G.L.1
  • 181
    • 0025734299 scopus 로고
    • The role of oxidative abnormalities in the pathophysiology of Alzheimer's disease
    • Blass JP, Gibson GE: The role of oxidative abnormalities in the pathophysiology of Alzheimer's disease. Rev Neurol (Paris) 1991; 147: 513-525.
    • (1991) Rev Neurol (Paris) , vol.147 , pp. 513-525
    • Blass, J.P.1    Gibson, G.E.2
  • 182
    • 0025183062 scopus 로고
    • Induction of Alzheimer antigens by an uncoupler of oxidative phosphorylation
    • Blass JP, et al: Induction of Alzheimer antigens by an uncoupler of oxidative phosphorylation. Arch Neurol 1990; 47: 864-869.
    • (1990) Arch Neurol , vol.47 , pp. 864-869
    • Blass, J.P.1
  • 183
    • 0035341254 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer's disease
    • Hirai K, et al: Mitochondrial abnormalities in Alzheimer's disease. J Neurosci 2001; 21: 3017-3023.
    • (2001) J Neurosci , vol.21 , pp. 3017-3023
    • Hirai, K.1
  • 184
    • 0026718966 scopus 로고
    • Brain cytochrome oxidase in Alzheimer's disease
    • Kish SJ, et al: Brain cytochrome oxidase in Alzheimer's disease. J Neurochem 1992; 59: 776-779.
    • (1992) J Neurochem , vol.59 , pp. 776-779
    • Kish, S.J.1
  • 185
    • 34648859471 scopus 로고    scopus 로고
    • Oxidative damage in mild cognitive impairment and early Alzheimer's disease
    • Lovell MA, Markesbery WR: Oxidative damage in mild cognitive impairment and early Alzheimer's disease. J Neurosci Res 2007; 85: 3036-3040.
    • (2007) J Neurosci Res , vol.85 , pp. 3036-3040
    • Lovell, M.A.1    Markesbery, W.R.2
  • 186
    • 1842504323 scopus 로고    scopus 로고
    • Redox-active metals, oxidative stress, and Alzheimer's disease pathology
    • Huang X, et al: Redox-active metals, oxidative stress, and Alzheimer's disease pathology. Ann NY Acad Sci 2004; 1012: 153-163.
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 153-163
    • Huang, X.1
  • 187
    • 84860198618 scopus 로고    scopus 로고
    • Mitochondrion-derived reactive oxygen species lead to enhanced amyloid beta formation
    • Leuner K, et al: Mitochondrion-derived reactive oxygen species lead to enhanced amyloid beta formation. Antioxid Redox Signal 2012; 16: 1421-1433.
    • (2012) Antioxid Redox Signal , vol.16 , pp. 1421-1433
    • Leuner, K.1
  • 188
    • 77955283395 scopus 로고    scopus 로고
    • Animal and human studies with the mitochondria-targeted antioxidant MitoQ
    • Smith RA, Murphy MP: Animal and human studies with the mitochondria-targeted antioxidant MitoQ. Ann NY Acad Sci 2010; 1201: 96-103.
    • (2010) Ann NY Acad Sci , vol.1201 , pp. 96-103
    • Smith, R.A.1    Murphy, M.P.2
  • 189
    • 47849101646 scopus 로고    scopus 로고
    • Evaluation of coenzyme Q as an antioxidant strategy for Alzheimer's disease
    • Wadsworth TL, et al: Evaluation of coenzyme Q as an antioxidant strategy for Alzheimer's disease. J Alzheimers Dis 2008; 14: 225-234.
    • (2008) J Alzheimers Dis , vol.14 , pp. 225-234
    • Wadsworth, T.L.1
  • 190
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada HK, et al: Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J Cell Biol 2003; 161: 41-54.
    • (2003) J Cell Biol , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1
  • 191
    • 43849096294 scopus 로고    scopus 로고
    • Brain oxidative stress in a tripletransgenic mouse model of Alzheimer disease
    • Resende R, et al: Brain oxidative stress in a tripletransgenic mouse model of Alzheimer disease. Free Radic Biol Med 2008; 44: 2051-2057.
    • (2008) Free Radic Biol Med , vol.44 , pp. 2051-2057
    • Resende, R.1
  • 192
    • 46449119069 scopus 로고    scopus 로고
    • Free radical-mediated damage to brain in Alzheimer's disease and its transgenic mouse models
    • Sonnen JA, et al: Free radical-mediated damage to brain in Alzheimer's disease and its transgenic mouse models. Free Radic Biol Med 2008; 45: 219-230.
    • (2008) Free Radic Biol Med , vol.45 , pp. 219-230
    • Sonnen, J.A.1
  • 193
    • 80051665640 scopus 로고    scopus 로고
    • Neuroprotective strategies involving ROS in Alzheimer disease
    • Dumont M, Beal MF: Neuroprotective strategies involving ROS in Alzheimer disease. Free Radic Biol Med 2011; 51: 1014-1026.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1014-1026
    • Dumont, M.1    Beal, M.F.2
  • 194
    • 0348111546 scopus 로고    scopus 로고
    • Cytochrome c oxidase is decreased in Alzheimer's disease platelets
    • Cardoso SM, et al: Cytochrome c oxidase is decreased in Alzheimer's disease platelets. Neurobiol Aging 2004; 25: 105-110.
    • (2004) Neurobiol Aging , vol.25 , pp. 105-110
    • Cardoso, S.M.1
  • 195
    • 0036272650 scopus 로고    scopus 로고
    • Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley CS, et al: Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J Neurochem 2002; 80: 91-100.
    • (2002) J Neurochem , vol.80 , pp. 91-100
    • Casley, C.S.1
  • 196
    • 35348923542 scopus 로고    scopus 로고
    • Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a mouse model of Alzheimer's disease
    • Fukui, H, et al: Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 2007; 104: 14163- 14168.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14163-14168
    • Fukui, H.1
  • 197
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya EM, Bowling AC, Beal MF: Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J Neurochem 1994; 63: 2179-2184.
    • (1994) J Neurochem , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 198
    • 38849150935 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress causes hyperphosphorylation of tau
    • Melov S, et al: Mitochondrial oxidative stress causes hyperphosphorylation of tau. PLoS One 2007; 2:e536.
    • (2007) PLoS One , vol.2 , pp. 536
    • Melov, S.1
  • 199
    • 79958721260 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: Implications for neuronal damage
    • Manczak M, Calkins MJ, Reddy PH: Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage. Human molecular genetics 2011; 20: 2495-2509.
    • (2011) Human Molecular Genetics , vol.20 , pp. 2495-2509
    • Manczak, M.1    Calkins, M.J.2    Reddy, P.H.3
  • 200
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • Wang X, et al: Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc Natl Acad Sci USA 2008; 105: 19318- 19323.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19318-19323
    • Wang, X.1
  • 201
    • 34249881080 scopus 로고    scopus 로고
    • Autophagocytosis of mitochondria is prominent in Alzheimer disease
    • Moreira PI, et al: Autophagocytosis of mitochondria is prominent in Alzheimer disease. J Neuropathol Exp Neurol 2007; 66: 525-532.
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 525-532
    • Moreira, P.I.1
  • 202
    • 33750370804 scopus 로고    scopus 로고
    • Understanding the molecular causes of Parkinson's disease
    • Wood-Kaczmar A, Gandhi S, Wood NW: Understanding the molecular causes of Parkinson's disease. Trends Mol Med 2006; 12: 521-528.
    • (2006) Trends Mol Med , vol.12 , pp. 521-528
    • Wood-Kaczmar, A.1    Gandhi, S.2    Wood, N.W.3
  • 203
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston J, et al: Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 1983; 219: 979-980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.1
  • 204
    • 0027995435 scopus 로고
    • Complex I, iron, and ferritin in Parkinson's disease substantia nigra
    • Mann VM, et al: Complex I, iron, and ferritin in Parkinson's disease substantia nigra. Ann Neurol 1994; 36: 876-881.
    • (1994) Ann Neurol , vol.36 , pp. 876-881
    • Mann, V.M.1
  • 205
    • 0032829070 scopus 로고    scopus 로고
    • Evidence of active nerve cell degeneration in the substantia nigra of humans years after 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine exposure
    • Langston JW, et al: Evidence of active nerve cell degeneration in the substantia nigra of humans years after 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine exposure. Ann Neurol 1999; 46: 598-605.
    • (1999) Ann Neurol , vol.46 , pp. 598-605
    • Langston, J.W.1
  • 206
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W, Przedborski S: Parkinson's disease: mechanisms and models. Neuron 2003; 39: 889- 909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 207
    • 37049004489 scopus 로고    scopus 로고
    • Mitochondria in the aetiology and pathogenesis of Parkinson's disease
    • Schapira AH: Mitochondria in the aetiology and pathogenesis of Parkinson's disease. Lancet Neurol 2008; 7: 97-109.
    • (2008) Lancet Neurol , vol.7 , pp. 97-109
    • Schapira, A.H.1
  • 208
    • 1542617769 scopus 로고    scopus 로고
    • Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP
    • Song DD, et al: Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP. Exp Neurol 2004; 186: 158-172.
    • (2004) Exp Neurol , vol.186 , pp. 158-172
    • Song, D.D.1
  • 209
    • 30644471051 scopus 로고    scopus 로고
    • Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death
    • Martin LJ, et al: Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death. J Neurosci 2006; 26: 41-50.
    • (2006) J Neurosci , vol.26 , pp. 41-50
    • Martin, L.J.1
  • 210
    • 78049383132 scopus 로고    scopus 로고
    • Mitochondrial alpha-synuclein accumulation impairs complex i function in dopaminergic neurons and results in increased mitophagy in vivo
    • Chinta SJ, et al: Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo. Neurosci Lett 2010; 486: 235-239.
    • (2010) Neurosci Lett , vol.486 , pp. 235-239
    • Chinta, S.J.1
  • 211
    • 23644442282 scopus 로고    scopus 로고
    • Heat shock prevents alpha-synuclein- induced apoptosis in a yeast model of Parkinson's disease
    • Flower TR, et al: Heat shock prevents alpha-synuclein- induced apoptosis in a yeast model of Parkinson's disease. J Mol Biol 2005; 351: 1081-1100.
    • (2005) J Mol Biol , vol.351 , pp. 1081-1100
    • Flower, T.R.1
  • 212
    • 39049097607 scopus 로고    scopus 로고
    • Oxidative-stress-induced apoptosis in PBLs of two patients with Parkinson disease secondary to alpha-synuclein mutation
    • Battisti C, et al: Oxidative-stress-induced apoptosis in PBLs of two patients with Parkinson disease secondary to alpha-synuclein mutation. J Neurol Sci 2008; 267: 120-124.
    • (2008) J Neurol Sci , vol.267 , pp. 120-124
    • Battisti, C.1
  • 213
    • 77958450202 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fusion by alpha-synuclein is rescued by PINK1, Parkin and DJ-1
    • Kamp F, et al: Inhibition of mitochondrial fusion by alpha-synuclein is rescued by PINK1, Parkin and DJ-1. EMBO J 2010; 29: 3571-3589.
    • (2010) EMBO J , vol.29 , pp. 3571-3589
    • Kamp, F.1
  • 214
    • 84863325404 scopus 로고    scopus 로고
    • Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease
    • Xie W, Chung KK: Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease. J Neurochem 2012; 122: 404-414.
    • (2012) J Neurochem , vol.122 , pp. 404-414
    • Xie, W.1    Chung, K.K.2
  • 215
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, et al: Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 1998; 392: 605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1
  • 216
    • 10044275502 scopus 로고    scopus 로고
    • Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease
    • Rogaeva E, et al: Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease. Arch Neurol 2004; 61: 1898-1904.
    • (2004) Arch Neurol , vol.61 , pp. 1898-1904
    • Rogaeva, E.1
  • 217
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente EM, et al: Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 2004; 304: 1158-1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1
  • 218
    • 33746080412 scopus 로고    scopus 로고
    • Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin
    • Yang Y, et al: Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc Natl Acad Sci USA 2006; 103: 10793-10798.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10793-10798
    • Yang, Y.1
  • 219
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park J, et al: Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 2006; 441: 1157-1161.
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1
  • 220
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark IE, et al: Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 2006; 441: 1162-1166.
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1
  • 221
    • 36049038504 scopus 로고    scopus 로고
    • Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin
    • Exner N, et al: Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. J Neurosci 2007; 27: 12413-12418.
    • (2007) J Neurosci , vol.27 , pp. 12413-12418
    • Exner, N.1
  • 222
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng H, et al: The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila . Proc Natl Acad Sci USA 2008; 105: 14503-14508.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14503-14508
    • Deng, H.1
  • 223
    • 79960826207 scopus 로고    scopus 로고
    • The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons
    • Yu W, et al: The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons. Hum Mol Genet 2011; 20: 3227-3240.
    • (2011) Hum Mol Genet , vol.20 , pp. 3227-3240
    • Yu, W.1
  • 224
    • 84863888014 scopus 로고    scopus 로고
    • Mao-B elevation decreases parkin's ability to efficiently clear damaged mitochondria: Protective effects of rapamycin
    • Siddiqui A, Hanson I, Andersen JK: Mao-B elevation decreases parkin's ability to efficiently clear damaged mitochondria: protective effects of rapamycin. Free Radic Res 2012; 46: 1011-1018.
    • (2012) Free Radic Res , vol.46 , pp. 1011-1018
    • Siddiqui, A.1    Hanson, I.2    Andersen, J.K.3
  • 225
    • 33644778845 scopus 로고    scopus 로고
    • Parkin enhances mitochondrial biogenesis in proliferating cells
    • Kuroda Y, et al: Parkin enhances mitochondrial biogenesis in proliferating cells. Hum Mol Genet 2006; 15: 883-895.
    • (2006) Hum Mol Genet , vol.15 , pp. 883-895
    • Kuroda, Y.1
  • 226
    • 0142217556 scopus 로고    scopus 로고
    • DJ-1( PARK7), a novel gene for autosomal recessive, early onset parkinsonism
    • Bonifati V, et al: DJ-1( PARK7), a novel gene for autosomal recessive, early onset parkinsonism. Neurol Sci 2003; 24: 159-160.
    • (2003) Neurol Sci , vol.24 , pp. 159-160
    • Bonifati, V.1
  • 227
    • 1642527499 scopus 로고    scopus 로고
    • DJ-1 has a role in antioxidative stress to prevent cell death
    • Taira T, et al: DJ-1 has a role in antioxidative stress to prevent cell death. EMBO Rep 2004; 5: 213-218.
    • (2004) EMBO Rep , vol.5 , pp. 213-218
    • Taira, T.1
  • 228
    • 33750052885 scopus 로고    scopus 로고
    • DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2
    • Clements CM, et al: DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc Natl Acad Sci USA 2006; 103: 15091-15096.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15091-15096
    • Clements, C.M.1
  • 229
    • 77956522541 scopus 로고    scopus 로고
    • Loss of the Parkinson's diseaselinked gene DJ-1 perturbs mitochondrial dynamics
    • Irrcher I, et al: Loss of the Parkinson's diseaselinked gene DJ-1 perturbs mitochondrial dynamics. Hum Mol Genet 2010; 19: 3734-3746.
    • (2010) Hum Mol Genet , vol.19 , pp. 3734-3746
    • Irrcher, I.1
  • 230
    • 13844253723 scopus 로고    scopus 로고
    • Nigrostriatal dopaminergic deficits and hypokinesia caused by inactivation of the familial Parkinsonism-linked gene DJ-1
    • Goldberg MS, et al: Nigrostriatal dopaminergic deficits and hypokinesia caused by inactivation of the familial Parkinsonism-linked gene DJ-1. Neuron 2005; 45: 489-496.
    • (2005) Neuron , vol.45 , pp. 489-496
    • Goldberg, M.S.1
  • 231
    • 20144389422 scopus 로고    scopus 로고
    • Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6- tetrahydropyrindine (MPTP) and oxidative stress
    • Kim RH, et al: Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress. Proc Natl Acad Sci USA 2005; 102: 5215-5220.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5215-5220
    • Kim, R.H.1
  • 232
    • 33947282153 scopus 로고    scopus 로고
    • DJ-1 and Parkin modulate dopamine- dependent behavior and inhibit MPTP-induced nigral dopamine neuron loss in mice
    • Paterna JC, et al: DJ-1 and Parkin modulate dopamine- dependent behavior and inhibit MPTP-induced nigral dopamine neuron loss in mice. Mol Ther 2007; 15: 698-704.
    • (2007) Mol Ther , vol.15 , pp. 698-704
    • Paterna, J.C.1
  • 233
    • 77949623516 scopus 로고    scopus 로고
    • Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1
    • Krebiehl G, et al: Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1. PLoS One 2010; 5:e9367.
    • (2010) PLoS One , vol.5 , pp. 9367
    • Krebiehl, G.1
  • 234
    • 84860539187 scopus 로고    scopus 로고
    • Parkinson's disease-associated DJ-1 mutations impair mitochondrial dynamics and cause mitochondrial dysfunction
    • Wang X, et al: Parkinson's disease-associated DJ-1 mutations impair mitochondrial dynamics and cause mitochondrial dysfunction. J Neurochem 2012; 121: 830-839.
    • (2012) J Neurochem , vol.121 , pp. 830-839
    • Wang, X.1
  • 235
    • 33646538477 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2: Relevance to Parkinson's disease
    • Guo L, Wang W, Chen SG: Leucine-rich repeat kinase 2: relevance to Parkinson's disease. Int J Biochem Cell Biol 2006; 38: 1469-1475.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 1469-1475
    • Guo, L.1    Wang, W.2    Chen, S.G.3
  • 236
    • 84863728713 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase2 disturbs mitochondrial dynamics via Dynamin-like protein
    • Niu J, et al: Leucine-rich repeat kinase2 disturbs mitochondrial dynamics via Dynamin-like protein. J Neurochem 2012; 122: 650-658.
    • (2012) J Neurochem , vol.122 , pp. 650-658
    • Niu, J.1
  • 237
    • 84859259002 scopus 로고    scopus 로고
    • LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1
    • Wang X, et al: LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1. Hum Mol Genet 2012; 21: 1931-1944.
    • (2012) Hum Mol Genet , vol.21 , pp. 1931-1944
    • Wang, X.1
  • 238
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • MacDonald ME, et al: A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993; 72: 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
    • Macdonald, M.E.1
  • 240
    • 40849147435 scopus 로고    scopus 로고
    • N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking
    • Orr AL, et al: N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking. J Neurosci 2008; 28: 2783-2792.
    • (2008) J Neurosci , vol.28 , pp. 2783-2792
    • Orr, A.L.1
  • 241
    • 31544446034 scopus 로고    scopus 로고
    • Severe ultrastructural mitochondrial changes in lymphoblasts homozygous for Huntington disease mutation
    • Squitieri F, et al: Severe ultrastructural mitochondrial changes in lymphoblasts homozygous for Huntington disease mutation. Mech Ageing Dev 2006; 127: 217-220.
    • (2006) Mech Ageing Dev , vol.127 , pp. 217-220
    • Squitieri, F.1
  • 242
    • 0036327065 scopus 로고    scopus 로고
    • Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
    • Panov AV, et al: Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat Neurosci 2002; 5: 731-736.
    • (2002) Nat Neurosci , vol.5 , pp. 731-736
    • Panov, A.V.1
  • 243
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calciuminduced permeability transition and cytochrome c release
    • Choo YS, et al: Mutant huntingtin directly increases susceptibility of mitochondria to the calciuminduced permeability transition and cytochrome c release. Human molecular genetics 2004; 13: 1407- 1420.
    • (2004) Human Molecular Genetics , vol.13 , pp. 1407-1420
    • Choo, Y.S.1
  • 244
    • 32044473546 scopus 로고    scopus 로고
    • Low stability of Huntington muscle mitochondria against Ca 2+ in R6/2 mice
    • Gizatullina ZZ, et al: Low stability of Huntington muscle mitochondria against Ca 2+ in R6/2 mice. Ann Neurol 2006; 59: 407-411.
    • (2006) Ann Neurol , vol.59 , pp. 407-411
    • Gizatullina, Z.Z.1
  • 245
    • 12944263711 scopus 로고    scopus 로고
    • The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription
    • Steffan JS, et al: The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sci USA 2000; 97: 6763-6768.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6763-6768
    • Steffan, J.S.1
  • 246
    • 5344252327 scopus 로고    scopus 로고
    • Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1alpha null mice
    • Lin J, et al: Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1alpha null mice. Cell 2004; 119: 121-135.
    • (2004) Cell , vol.119 , pp. 121-135
    • Lin, J.1
  • 247
    • 84860650335 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in ALS
    • Cozzolino M, Carri MT: Mitochondrial dysfunction in ALS. Prog Neurobiol 2012; 97: 54-66.
    • (2012) Prog Neurobiol , vol.97 , pp. 54-66
    • Cozzolino, M.1    Carri, M.T.2
  • 248
    • 20444497908 scopus 로고    scopus 로고
    • Oxidative stress, mitochondrial dysfunction and cellular stress response in Friedreich's ataxia
    • Calabrese V, et al: Oxidative stress, mitochondrial dysfunction and cellular stress response in Friedreich's ataxia. J Neurol Sci 2005; 233: 145-162.
    • (2005) J Neurol Sci , vol.233 , pp. 145-162
    • Calabrese, V.1
  • 249
    • 0344736798 scopus 로고    scopus 로고
    • Loss of m-AAA protease in mitochondria causes complex i deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia
    • Atorino L, et al: Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J Cell Biol 2003; 163: 777-787.
    • (2003) J Cell Biol , vol.163 , pp. 777-787
    • Atorino, L.1
  • 250
    • 33746454624 scopus 로고    scopus 로고
    • Mitochondria and cancer: Warburg addressed
    • Wallace DC: Mitochondria and cancer: Warburg addressed. Cold Spring Harb Symp Quant Biol 2005; 70: 363-374.
    • (2005) Cold Spring Harb Symp Quant Biol , vol.70 , pp. 363-374
    • Wallace, D.C.1
  • 251
    • 18044383110 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in cardiovascular disease
    • Ballinger SW: Mitochondrial dysfunction in cardiovascular disease. Free Radic Biol Med 2005; 38: 1278-1295.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1278-1295
    • Ballinger, S.W.1
  • 252
    • 84865418540 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in pancreatic beta cells
    • Supale S, et al: Mitochondrial dysfunction in pancreatic beta cells. Trends Endocrinol Metab 2012; 23: 477-487.
    • (2012) Trends Endocrinol Metab , vol.23 , pp. 477-487
    • Supale, S.1
  • 254
    • 37049016418 scopus 로고    scopus 로고
    • The role of mitochondrial DNA mutations in aging and sarcopenia: Implications for the mitochondrial vicious cycle theory of aging
    • Hiona A, Leeuwenburgh C: The role of mitochondrial DNA mutations in aging and sarcopenia: implications for the mitochondrial vicious cycle theory of aging. Exp Gerontol 2008; 43: 24-33.
    • (2008) Exp Gerontol , vol.43 , pp. 24-33
    • Hiona, A.1    Leeuwenburgh, C.2
  • 255
    • 33751242066 scopus 로고    scopus 로고
    • High oxidative damage levels in the longest-living rodent, the naked mole-rat
    • Andziak B, et al: High oxidative damage levels in the longest-living rodent, the naked mole-rat. Aging Cell 2006; 5: 463-471.
    • (2006) Aging Cell , vol.5 , pp. 463-471
    • Andziak, B.1
  • 256
    • 34748850786 scopus 로고    scopus 로고
    • Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress
    • Schulz TJ, et al: Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress. Cell Metab 2007; 6: 280-293.
    • (2007) Cell Metab , vol.6 , pp. 280-293
    • Schulz, T.J.1
  • 257
    • 79959547070 scopus 로고    scopus 로고
    • Mitochondria-mediated hormetic response in life span extension of calorie-restricted Saccharomyces cerevisiae
    • Sharma PK, Agrawal V, Roy N: Mitochondria-mediated hormetic response in life span extension of calorie-restricted Saccharomyces cerevisiae . Age (Dordr) 2010; 33: 143-154.
    • (2010) Age (Dordr) , vol.33 , pp. 143-154
    • Sharma, P.K.1    Agrawal, V.2    Roy, N.3
  • 258
    • 77649341027 scopus 로고    scopus 로고
    • Lifespan extension by calorie restriction relies on the Sty1 MAP kinase stress pathway
    • Zuin A, et al: Lifespan extension by calorie restriction relies on the Sty1 MAP kinase stress pathway. EMBO J 2010; 29: 981-991.
    • (2010) EMBO J , vol.29 , pp. 981-991
    • Zuin, A.1
  • 259
    • 0037130175 scopus 로고    scopus 로고
    • Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
    • Lin SJ, et al: Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration. Nature 2002; 418: 344-348.
    • (2002) Nature , vol.418 , pp. 344-348
    • Lin, S.J.1
  • 260
    • 59049086591 scopus 로고    scopus 로고
    • The overexpression of major antioxidant enzymes does not extend the lifespan of mice
    • Perez VI, et al: The overexpression of major antioxidant enzymes does not extend the lifespan of mice. Aging Cell 2009; 8: 73-75.
    • (2009) Aging Cell , vol.8 , pp. 73-75
    • Perez, V.I.1
  • 261
    • 29144486726 scopus 로고    scopus 로고
    • Mutant mitochondrial helicase Twinkle causes multiple mtDNA deletions and a late-onset mitochondrial disease in mice
    • Tyynismaa H, et al: Mutant mitochondrial helicase Twinkle causes multiple mtDNA deletions and a late-onset mitochondrial disease in mice. Proc Natl Acad Sci USA 2005; 102: 17687-17692.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17687-17692
    • Tyynismaa, H.1
  • 262
    • 84868007565 scopus 로고    scopus 로고
    • Physiological roles of mitochondrial reactive oxygen species
    • Sena LA, Chandel NS: Physiological roles of mitochondrial reactive oxygen species. Mol Cell 2012; 48: 158-167.
    • (2012) Mol Cell , vol.48 , pp. 158-167
    • Sena, L.A.1    Chandel, N.S.2
  • 263
    • 80053124673 scopus 로고    scopus 로고
    • Taking a 'good' look at free radicals in the aging process
    • Hekimi S, Lapointe J, Wen Y: Taking a 'good' look at free radicals in the aging process. Trends Cell Biol 2011; 21: 569-576.
    • (2011) Trends Cell Biol , vol.21 , pp. 569-576
    • Hekimi, S.1    Lapointe, J.2    Wen, Y.3
  • 264
    • 0031030678 scopus 로고    scopus 로고
    • Structural and functional conservation of the Caenorhabditis elegans timing gene clk-1
    • Ewbank JJ, et al: Structural and functional conservation of the Caenorhabditis elegans timing gene clk-1. Science 1997; 275: 980-983.
    • (1997) Science , vol.275 , pp. 980-983
    • Ewbank, J.J.1
  • 265
    • 66149135335 scopus 로고    scopus 로고
    • Reversal of the mitochondrial phenotype and slow development of oxidative biomarkers of aging in long-lived Mclk1+/- mice
    • Lapointe J, et al: Reversal of the mitochondrial phenotype and slow development of oxidative biomarkers of aging in long-lived Mclk1+/- mice. J Biol Chem 2009; 284: 20364-20374.
    • (2009) J Biol Chem , vol.284 , pp. 20364-20374
    • Lapointe, J.1
  • 266
    • 78650455712 scopus 로고    scopus 로고
    • A mitochondrial superoxide signal triggers increased longevity in Caenorhabditis elegans
    • Yang W, Hekimi S: A mitochondrial superoxide signal triggers increased longevity in Caenorhabditis elegans . PLoS Biol 2010; 8:e1000556.
    • (2010) PLoS Biol , vol.8
    • Yang, W.1    Hekimi, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.