메뉴 건너뛰기




Volumn 292, Issue 2, 2007, Pages

The mitochondrial energy transduction system and the aging process

Author keywords

Complexes I and IV; Nitric oxide synthase; Oxidative damage; Survival

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA TOCOPHEROL; ANTIOXIDANT; BIOLOGICAL MARKER; CALCIUM; CYTOCHROME C OXIDASE; DNA; FREE RADICAL; HYDROGEN PEROXIDE; NITRIC OXIDE SYNTHASE; OXYGEN; PHOSPHOLIPID; PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 33847059997     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00213.2006     Document Type: Review
Times cited : (582)

References (161)
  • 1
    • 24044536651 scopus 로고    scopus 로고
    • Mineral and vitamin deficiencies can accelerate the mitochondrial decay of aging
    • Ames BN, Atamna H, Killilea DW. Mineral and vitamin deficiencies can accelerate the mitochondrial decay of aging. Mol Aspects Med 26: 363-378, 2005.
    • (2005) Mol Aspects Med , vol.26 , pp. 363-378
    • Ames, B.N.1    Atamna, H.2    Killilea, D.W.3
  • 2
    • 10044230387 scopus 로고    scopus 로고
    • On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide
    • Antunes F, Boveris A, Cadenas E. On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide. Proc Natl Acad Sci USA 101: 16774-16779, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16774-16779
    • Antunes, F.1    Boveris, A.2    Cadenas, E.3
  • 3
    • 0038340930 scopus 로고    scopus 로고
    • Mitochondrial dysfunctions during aging: Vitamin E deficiency or caloric restriction-two different ways of modulating stress
    • Armeni T, Principato G, Quiles JL, Pieri C, Bompadre S, Battino M. Mitochondrial dysfunctions during aging: vitamin E deficiency or caloric restriction-two different ways of modulating stress. J Bioenerg Biomembr 35: 181-191, 2003.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 181-191
    • Armeni, T.1    Principato, G.2    Quiles, J.L.3    Pieri, C.4    Bompadre, S.5    Battino, M.6
  • 4
    • 0025363999 scopus 로고
    • Ischaemic injury mediator
    • Beckman JS. Ischaemic injury mediator. Nature 345: 27-28, 1990.
    • (1990) Nature , vol.345 , pp. 27-28
    • Beckman, J.S.1
  • 5
    • 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 78: 547-581, 1998.
    • (1998) Physiol Rev , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 6
    • 0032788956 scopus 로고    scopus 로고
    • Aging and acute exercise enhance free radical generation in rat skeletal muscle
    • Bejma J, Ji LL. Aging and acute exercise enhance free radical generation in rat skeletal muscle. J Appl Physiol 87: 465-470, 1999.
    • (1999) J Appl Physiol , vol.87 , pp. 465-470
    • Bejma, J.1    Ji, L.L.2
  • 7
    • 0026600596 scopus 로고
    • The mitochondrial electron transfer alteration as a factor involved in the brain aging
    • Benzi G, Pastoris O, Marzatico F, Villa RF, Dagani F, Curti D. The mitochondrial electron transfer alteration as a factor involved in the brain aging. Neurobiol Aging 13: 361-368, 1992.
    • (1992) Neurobiol Aging , vol.13 , pp. 361-368
    • Benzi, G.1    Pastoris, O.2    Marzatico, F.3    Villa, R.F.4    Dagani, F.5    Curti, D.6
  • 8
    • 3242728502 scopus 로고    scopus 로고
    • Cytochrome oxidase activity in hippocampal synaptic mitochondria during aging: A quantitative cytochemical investigation
    • Bertoni-Freddari C, Fattoretti P, Giorgetti B, Solazzi M, Balietti M, Casoli T, Di SG. Cytochrome oxidase activity in hippocampal synaptic mitochondria during aging: a quantitative cytochemical investigation. Ann NY Acad Sci 1019: 33-36, 2004.
    • (2004) Ann NY Acad Sci , vol.1019 , pp. 33-36
    • Bertoni-Freddari, C.1    Fattoretti, P.2    Giorgetti, B.3    Solazzi, M.4    Balietti, M.5    Casoli, T.6    Di, S.G.7
  • 9
    • 0032726599 scopus 로고    scopus 로고
    • Effects of aging on cerebellar noradrenergic function and motor learning: Nutritional interventions
    • Bickford PC, Shukitt-Hale B, Joseph J. Effects of aging on cerebellar noradrenergic function and motor learning: nutritional interventions. Mech Ageing Dev 111: 141-154, 1999.
    • (1999) Mech Ageing Dev , vol.111 , pp. 141-154
    • Bickford, P.C.1    Shukitt-Hale, B.2    Joseph, J.3
  • 11
    • 0033574624 scopus 로고    scopus 로고
    • Direct EPR detection of the carbonate radical anion produced from peroxynitrite and carbon dioxide
    • Bonini MG, Radi R, Ferrer-Sueta G, Ferreira AM, Augusto O. Direct EPR detection of the carbonate radical anion produced from peroxynitrite and carbon dioxide. J Biol Chem 274: 10802-10806, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 10802-10806
    • Bonini, M.G.1    Radi, R.2    Ferrer-Sueta, G.3    Ferreira, A.M.4    Augusto, O.5
  • 12
    • 0034456720 scopus 로고    scopus 로고
    • Mitochondrial production of hydrogen peroxide regulation by nitric oxide and the role of ubisemiquinone
    • Boveris A, Cadenas E. Mitochondrial production of hydrogen peroxide regulation by nitric oxide and the role of ubisemiquinone. IUBMB Life 50: 245-250, 2000.
    • (2000) IUBMB Life , vol.50 , pp. 245-250
    • Boveris, A.1    Cadenas, E.2
  • 13
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris A, Cadenas E, Stoppani AO. Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem J 156: 435-444, 1976.
    • (1976) Biochem J , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.3
  • 14
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A, Chance B. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem J 134: 707-716, 1973.
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 17
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A, Oshino N, Chance B. The cellular production of hydrogen peroxide. Biochem J 128: 617-630, 1972.
    • (1972) Biochem J , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 18
    • 0032311441 scopus 로고    scopus 로고
    • ATP synthase-past and future
    • Boyer PD. ATP synthase-past and future. Biochim Biophys Acta 1365: 3-9, 1998.
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 3-9
    • Boyer, P.D.1
  • 19
    • 0030034875 scopus 로고    scopus 로고
    • Exercise training for coronary artery disease in the elderly
    • Brechue WF, Pollock ML. Exercise training for coronary artery disease in the elderly. Clin Geriatr Med 12: 207-229, 1996.
    • (1996) Clin Geriatr Med , vol.12 , pp. 207-229
    • Brechue, W.F.1    Pollock, M.L.2
  • 20
    • 1342282382 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase
    • Brookes PS. Mitochondrial nitric oxide synthase. Mitochondrion 3: 187-204, 2004.
    • (2004) Mitochondrion , vol.3 , pp. 187-204
    • Brookes, P.S.1
  • 21
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown GC, Cooper CE. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett 356: 295-298, 1994.
    • (1994) FEBS Lett , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 22
    • 0037300717 scopus 로고    scopus 로고
    • Modifications of glyceraldehyde-3-phosphate dehydrogenase induced by increasing concentrations of peroxynitrite: Early recognition by 20S proteasome
    • Buchczyk DP, Grune T, Sies H, Klotz LO. Modifications of glyceraldehyde-3-phosphate dehydrogenase induced by increasing concentrations of peroxynitrite: early recognition by 20S proteasome. Biol Chem 384: 237-241, 2003.
    • (2003) Biol Chem , vol.384 , pp. 237-241
    • Buchczyk, D.P.1    Grune, T.2    Sies, H.3    Klotz, L.O.4
  • 24
    • 0018837597 scopus 로고
    • Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria
    • Cadenas E, Boveris A. Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria. Biochem J 188: 31-37, 1980.
    • (1980) Biochem J , vol.188 , pp. 31-37
    • Cadenas, E.1    Boveris, A.2
  • 25
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • Cadenas E, Boveris A, Ragan CI, Stoppani AO. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch Biochem Biophys 180: 248-257, 1977.
    • (1977) Arch Biochem Biophys , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 26
    • 0037395951 scopus 로고    scopus 로고
    • Historical review: Mitochondria and calcium: ups and downs of an unusual relationship
    • Carafoli E. Historical review: mitochondria and calcium: ups and downs of an unusual relationship. Trends Biochem Sci 28: 175-181, 2003.
    • (2003) Trends Biochem Sci , vol.28 , pp. 175-181
    • Carafoli, E.1
  • 27
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • Cassina A, Radi R. Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch Biochem Biophys 328: 309-316, 1996.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 28
    • 0043269302 scopus 로고    scopus 로고
    • Function and structure of complex II of the respiratory chain
    • Cecchini G. Function and structure of complex II of the respiratory chain. Annu Rev Biochem 72: 77-109, 2003.
    • (2003) Annu Rev Biochem , vol.72 , pp. 77-109
    • Cecchini, G.1
  • 29
    • 0028948660 scopus 로고
    • Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases
    • Chagnon P, Betard C, Robitaille Y, Cholette A, Gauvreau D. Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases. Neuroreport 6: 711-715, 1995.
    • (1995) Neuroreport , vol.6 , pp. 711-715
    • Chagnon, P.1    Betard, C.2    Robitaille, Y.3    Cholette, A.4    Gauvreau, D.5
  • 30
    • 0017324767 scopus 로고
    • Electron transfer: Pathways mechanisms and controls
    • Chance B. Electron transfer: pathways mechanisms and controls. Annu Rev Biochem 46: 967-980, 1977.
    • (1977) Annu Rev Biochem , vol.46 , pp. 967-980
    • Chance, B.1
  • 31
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 59: 527-605, 1979.
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 32
  • 33
    • 0001717675 scopus 로고
    • Inhibition of electron and energy transfer in mitochondria. I. Effects of Amytal, thiopental, rotenone, progesterone, and methylene glycol
    • Chance B, Williams GR, Hollunger G. Inhibition of electron and energy transfer in mitochondria. I. Effects of Amytal, thiopental, rotenone, progesterone, and methylene glycol. J Biol Chem 238: 418-431, 1963.
    • (1963) J Biol Chem , vol.238 , pp. 418-431
    • Chance, B.1    Williams, G.R.2    Hollunger, G.3
  • 34
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham DE. Calcium signaling. Cell 80: 259-268, 1995.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 35
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases
    • Cleeter MW, Cooper JM, Darley-Usmar VM, Moncada S, Schapira AH. Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Lett 345: 50-54, 1994.
    • (1994) FEBS Lett , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 36
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E, Brown GC, Feelisch M, Moncada S. Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc Natl Acad Sci USA 95: 7631-7636, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 37
    • 0033573981 scopus 로고    scopus 로고
    • On the mechanism by which vascular endothelial cells regulate their oxygen consumption
    • Clementi E, Brown GC, Foxwell N, Moncada S. On the mechanism by which vascular endothelial cells regulate their oxygen consumption. Proc Natl Acad Sci USA 96: 1559-1562, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1559-1562
    • Clementi, E.1    Brown, G.C.2    Foxwell, N.3    Moncada, S.4
  • 40
    • 0015228860 scopus 로고
    • Likelihood of human pheromones
    • Comfort A. Likelihood of human pheromones. Nature 230: 432-433, 1971.
    • (1971) Nature , vol.230 , pp. 432-433
    • Comfort, A.1
  • 42
    • 1942447877 scopus 로고    scopus 로고
    • The cytochrome bc1 complex: Function in the context of structure
    • Crofts AR. The cytochrome bc1 complex: function in the context of structure. Annu Rev Physiol 66: 689-733, 2004.
    • (2004) Annu Rev Physiol , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 43
    • 24944542226 scopus 로고    scopus 로고
    • Oxidative stress and aging: Catalase is a longevity determinant enzyme
    • Cutler RG. Oxidative stress and aging: catalase is a longevity determinant enzyme. Rejuvenation Res 8: 138-140, 2005.
    • (2005) Rejuvenation Res , vol.8 , pp. 138-140
    • Cutler, R.G.1
  • 44
    • 4043129527 scopus 로고    scopus 로고
    • The powerhouse takes control of the cell; the role of mitochondria in signal transduction
    • Darley-Usmar V. The powerhouse takes control of the cell; the role of mitochondria in signal transduction. Free Radic Biol Med 37: 753-754, 2004.
    • (2004) Free Radic Biol Med , vol.37 , pp. 753-754
    • Darley-Usmar, V.1
  • 45
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W, Przedborski S. Parkinson's disease: mechanisms and models. Neuron 39: 889-909, 2003.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 46
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson TM, Dawson VL. Molecular pathways of neurodegeneration in Parkinson's disease. Science 302: 819-822, 2003.
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 47
    • 0016701593 scopus 로고
    • Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues
    • Dionisi O, Galeotti T, Terranova T, Azzi A. Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues. Biochim Biophys Acta 403: 292-300, 1975.
    • (1975) Biochim Biophys Acta , vol.403 , pp. 292-300
    • Dionisi, O.1    Galeotti, T.2    Terranova, T.3    Azzi, A.4
  • 48
    • 0142063539 scopus 로고    scopus 로고
    • Method for measuring ATP production in isolated mitochondria: ATP production in brain and liver mitochondria of Fischer-344 rats with age and caloric restriction
    • Drew B, Leeuwenburgh C. Method for measuring ATP production in isolated mitochondria: ATP production in brain and liver mitochondria of Fischer-344 rats with age and caloric restriction. Am J Physiol Regul Integr Comp Physiol 285: R1259-R1267, 2003.
    • (2003) Am J Physiol Regul Integr Comp Physiol , vol.285
    • Drew, B.1    Leeuwenburgh, C.2
  • 49
    • 0037064058 scopus 로고    scopus 로고
    • Biochemistry of mitochondrial nitric-oxide synthase
    • Elfering SL, Sarkela TM, Giulivi C. Biochemistry of mitochondrial nitric-oxide synthase. J Biol Chem 277: 38079-38086, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 38079-38086
    • Elfering, S.L.1    Sarkela, T.M.2    Giulivi, C.3
  • 50
    • 0017158231 scopus 로고
    • Free radicals and the action of inhibitors of radical processes under pathological states and ageing in living organisms and in man
    • Emanuel NM. Free radicals and the action of inhibitors of radical processes under pathological states and ageing in living organisms and in man. Q Rev Biophys 9: 283-308, 1976.
    • (1976) Q Rev Biophys , vol.9 , pp. 283-308
    • Emanuel, N.M.1
  • 51
    • 25144463436 scopus 로고    scopus 로고
    • Age-associated decline in mitochondrial respiration and electron transport in Drosophila melanogaster
    • Ferguson M, Mockett RJ, Shen Y, Orr WC, Sohal RS. Age-associated decline in mitochondrial respiration and electron transport in Drosophila melanogaster. Biochem J 390: 501-511, 2005.
    • (2005) Biochem J , vol.390 , pp. 501-511
    • Ferguson, M.1    Mockett, R.J.2    Shen, Y.3    Orr, W.C.4    Sohal, R.S.5
  • 52
    • 84873778494 scopus 로고
    • A macromolecular repeating unit of mitochondrial structure and function correlated electron microscopic and biochemical studies of isolated mitochondria and submitochondrial particles of beef heart muscle
    • Fernandez-Moran H, Oda T, Blair PV, Green DE. A macromolecular repeating unit of mitochondrial structure and function correlated electron microscopic and biochemical studies of isolated mitochondria and submitochondrial particles of beef heart muscle. J Cell Biol 22: 63-100, 1964.
    • (1964) J Cell Biol , vol.22 , pp. 63-100
    • Fernandez-Moran, H.1    Oda, T.2    Blair, P.V.3    Green, D.E.4
  • 54
    • 0029978498 scopus 로고    scopus 로고
    • Age-related losses of cognitive function and motor skills in mice are associated with oxidative protein damage in the brain
    • Forster MJ, Dubey A, Dawson KM, Stutts WA, Lal H, Sohal RS. Age-related losses of cognitive function and motor skills in mice are associated with oxidative protein damage in the brain. Proc Natl Acad Sci USA 93: 4765-4769, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4765-4769
    • Forster, M.J.1    Dubey, A.2    Dawson, K.M.3    Stutts, W.A.4    Lal, H.5    Sohal, R.S.6
  • 56
    • 1642451816 scopus 로고    scopus 로고
    • The gross structure of the respiratory complex I: A Lego System
    • Friedrich T, Bottcher B. The gross structure of the respiratory complex I: a Lego System. Biochim Biophys Acta 1608: 1-9, 2004.
    • (2004) Biochim Biophys Acta , vol.1608 , pp. 1-9
    • Friedrich, T.1    Bottcher, B.2
  • 57
  • 58
    • 0030697859 scopus 로고    scopus 로고
    • Nitric oxide synthase activity in mitochondria
    • Ghafourifar P, Richter C. Nitric oxide synthase activity in mitochondria. FEBS Lett 418: 291-296, 1997.
    • (1997) FEBS Lett , vol.418 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 59
    • 0033615544 scopus 로고    scopus 로고
    • Mitochondrial nitricoxide synthase stimulation causes cytochrome c release from isolated mitochondria. Evidence for intramitochondrial peroxynitrite formation
    • Ghafourifar P, Schenk U, Klein SD, Richter C. Mitochondrial nitricoxide synthase stimulation causes cytochrome c release from isolated mitochondria. Evidence for intramitochondrial peroxynitrite formation. J Biol Chem 274: 31185-31188, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 31185-31188
    • Ghafourifar, P.1    Schenk, U.2    Klein, S.D.3    Richter, C.4
  • 60
    • 0038784529 scopus 로고    scopus 로고
    • Are ubiquitination pathways central to Parkinson's disease?
    • Giasson BI, Lee VM. Are ubiquitination pathways central to Parkinson's disease? Cell 114: 1-8, 2003.
    • (2003) Cell , vol.114 , pp. 1-8
    • Giasson, B.I.1    Lee, V.M.2
  • 61
    • 0028903557 scopus 로고
    • Strain, stress, neurodegeneration and longevity
    • Gilad GM, Gilad VH. Strain, stress, neurodegeneration and longevity. Mech Ageing Dev 78: 75-83, 1995.
    • (1995) Mech Ageing Dev , vol.78 , pp. 75-83
    • Gilad, G.M.1    Gilad, V.H.2
  • 62
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi C, Poderoso JJ, Boveris A. Production of nitric oxide by mitochondria. J Biol Chem 273: 11038-11043, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 63
    • 0027473685 scopus 로고
    • Time course and mechanism of oxidative stress and tissue damage in rat liver subjected to in vivo ischemia-reperfusion
    • Gonzalez-Flecha B, Cutrin JC, Boveris A. Time course and mechanism of oxidative stress and tissue damage in rat liver subjected to in vivo ischemia-reperfusion. J Clin Invest 91: 456-464, 1993.
    • (1993) J Clin Invest , vol.91 , pp. 456-464
    • Gonzalez-Flecha, B.1    Cutrin, J.C.2    Boveris, A.3
  • 65
    • 0020068653 scopus 로고
    • On the enzymic mechanism of oxidative phosphorylation
    • Green DE, Vande ZH. On the enzymic mechanism of oxidative phosphorylation. Proc Natl Acad Sci USA 79: 1064-1068, 1982.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1064-1068
    • Green, D.E.1    Vande, Z.H.2
  • 66
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T, Merker K, Sandig G, Davies KJ. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 305: 709-718, 2003.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 67
    • 0027159339 scopus 로고
    • A mitochondrial porin cDNA predicts the existence of multiple human porins
    • Ha H, Hajek P, Bedwell DM, Burrows PD. A mitochondrial porin cDNA predicts the existence of multiple human porins. J Biol Chem 268: 12143-12149, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 12143-12149
    • Ha, H.1    Hajek, P.2    Bedwell, D.M.3    Burrows, P.D.4
  • 69
    • 0037458619 scopus 로고    scopus 로고
    • Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
    • Han D, Antunes F, Canali R, Rettori D, Cadenas E. Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol. J Biol Chem 278: 5557-5563, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5
  • 70
    • 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 A Biol Sci Med Sci 11: 298-300, 1956.
    • (1956) J Gerontol A Biol Sci Med Sci , vol.11 , pp. 298-300
    • Harman, D.1
  • 71
    • 33744478401 scopus 로고    scopus 로고
    • Free radical theory of aging: An update: increasing the functional life span
    • Harman D. Free radical theory of aging: an update: increasing the functional life span. Ann NY Acad Sci 1067: 10-21, 2006.
    • (2006) Ann NY Acad Sci , vol.1067 , pp. 10-21
    • Harman, D.1
  • 72
    • 84975751684 scopus 로고
    • Complex I inhibitors induce dose-dependent apoptosis in PC12 cells: Relevance to Parkinson's disease
    • Hartley A, Stone JM, Heron C, Cooper JM, Schapira AH. Complex I inhibitors induce dose-dependent apoptosis in PC12 cells: relevance to Parkinson's disease. J Neurochem 63: 1987-1990, 1994.
    • (1994) J Neurochem , vol.63 , pp. 1987-1990
    • Hartley, A.1    Stone, J.M.2    Heron, C.3    Cooper, J.M.4    Schapira, A.H.5
  • 73
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Annu Rev Biochem 54: 1015-1069, 1985.
    • (1985) Annu Rev Biochem , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 74
    • 23044477952 scopus 로고    scopus 로고
    • Organization of iron-sulfur clusters in respiratory complex I
    • Hinchliffe P, Sazanov LA. Organization of iron-sulfur clusters in respiratory complex I. Science 309: 771-774, 2005.
    • (2005) Science , vol.309 , pp. 771-774
    • Hinchliffe, P.1    Sazanov, L.A.2
  • 75
    • 0026077298 scopus 로고
    • Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I)
    • Hofhaus G, Weiss H, Leonard K. Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I). J Mol Biol 221: 1027-1043, 1991.
    • (1991) J Mol Biol , vol.221 , pp. 1027-1043
    • Hofhaus, G.1    Weiss, H.2    Leonard, K.3
  • 76
    • 0030294728 scopus 로고    scopus 로고
    • Cytochrome c oxidase defects of the human substantia nigra in normal aging
    • Itoh K, Weis S, Mehraein P, and Muller-Hocker J. Cytochrome c oxidase defects of the human substantia nigra in normal aging. Neurobiol Aging 17: 843-848, 1996.
    • (1996) Neurobiol Aging , vol.17 , pp. 843-848
    • Itoh, K.1    Weis, S.2    Mehraein, P.3    Muller-Hocker, J.4
  • 77
    • 0035028427 scopus 로고    scopus 로고
    • Exercise at old age: Does it increase or alleviate oxidative stress?
    • Ji LL. Exercise at old age: does it increase or alleviate oxidative stress? Ann NY Acad Sci 928: 236-247, 2001.
    • (2001) Ann NY Acad Sci , vol.928 , pp. 236-247
    • Ji, L.L.1
  • 81
    • 11144318614 scopus 로고    scopus 로고
    • Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: Effects of biological aging
    • Kanski J, Behring A, Pelling J, Schoneich C. Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging. Am J Physiol Heart Circ Physiol 288: H371-H381, 2005.
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Kanski, J.1    Behring, A.2    Pelling, J.3    Schoneich, C.4
  • 82
    • 0000402167 scopus 로고
    • Oxidation of fatty acids and tricarboxilic acid cycle intermediates by isolated rat liver mitochondria
    • Kennedy EP, Lehninger AL. Oxidation of fatty acids and tricarboxilic acid cycle intermediates by isolated rat liver mitochondria. J Biol Chem 179: 957-969, 1949.
    • (1949) J Biol Chem , vol.179 , pp. 957-969
    • Kennedy, E.P.1    Lehninger, A.L.2
  • 83
    • 0030781227 scopus 로고    scopus 로고
    • Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis
    • Kissner R, Nauser T, Bugnon P, Lye PG, Koppenol WH. Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis. Chem Res Toxicol 10: 1285-1292, 1997.
    • (1997) Chem Res Toxicol , vol.10 , pp. 1285-1292
    • Kissner, R.1    Nauser, T.2    Bugnon, P.3    Lye, P.G.4    Koppenol, W.H.5
  • 84
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov SS, Skulachev VP, Starkov AA. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett 416: 15-18, 1997.
    • (1997) FEBS Lett , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 86
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G, Dallaporta B, and Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol 60: 619-642, 1998.
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 87
    • 11244351578 scopus 로고    scopus 로고
    • Supplementation of L-carnitine improves mitochondrial enzymes in heart and skeletal muscle of aged rats
    • Kumaran S, Subathra M, Balu M, Panneerselvam C. Supplementation of L-carnitine improves mitochondrial enzymes in heart and skeletal muscle of aged rats. Exp Aging Res 31: 55-67, 2005.
    • (2005) Exp Aging Res , vol.31 , pp. 55-67
    • Kumaran, S.1    Subathra, M.2    Balu, M.3    Panneerselvam, C.4
  • 89
    • 1342307974 scopus 로고    scopus 로고
    • The effect of aging and caloric restriction on mitochondrial protein density and oxygen consumption
    • Lambert AJ, Wang B, Yardley J, Edwards J, Merry BJ. The effect of aging and caloric restriction on mitochondrial protein density and oxygen consumption. Exp Gerontol 39: 289-295, 2004.
    • (2004) Exp Gerontol , vol.39 , pp. 289-295
    • Lambert, A.J.1    Wang, B.2    Yardley, J.3    Edwards, J.4    Merry, B.J.5
  • 90
    • 0033025991 scopus 로고    scopus 로고
    • Mitochondrial coenzyme Q content and aging
    • Lass A, Kwong L, Sohal RS. Mitochondrial coenzyme Q content and aging. Biofactors 9: 199-205, 1999.
    • (1999) Biofactors , vol.9 , pp. 199-205
    • Lass, A.1    Kwong, L.2    Sohal, R.S.3
  • 91
    • 0000955838 scopus 로고
    • Water uptake and extrusion by mitochondria in relation to oxidative phosphorylation
    • Lehninger AL. Water uptake and extrusion by mitochondria in relation to oxidative phosphorylation. Physiol Rev 42: 467-517, 1962.
    • (1962) Physiol Rev , vol.42 , pp. 467-517
    • Lehninger, A.L.1
  • 92
    • 33847074765 scopus 로고
    • Fatty acid oxidation in the liver
    • Leloir LF, Munoz JM. Fatty acid oxidation in the liver. Biochem J 33: 734-746, 1939.
    • (1939) Biochem J , vol.33 , pp. 734-746
    • Leloir, L.F.1    Munoz, J.M.2
  • 94
    • 0035145954 scopus 로고    scopus 로고
    • Aging decreases electron transport complex III activity in heart interfibrillar mitochondria by alteration of the cytochrome c binding site
    • Lesnefsky EJ, Gudz TI, Moghaddas S, Migita CT, Ikeda-Saito M, Turkaly PJ, Hoppel CL. Aging decreases electron transport complex III activity in heart interfibrillar mitochondria by alteration of the cytochrome c binding site. J Mol Cell Cardiol 33: 37-47, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 37-47
    • Lesnefsky, E.J.1    Gudz, T.I.2    Moghaddas, S.3    Migita, C.T.4    Ikeda-Saito, M.5    Turkaly, P.J.6    Hoppel, C.L.7
  • 96
    • 0037133319 scopus 로고    scopus 로고
    • Age-associated mitochondrial oxidative decay: Improvement of carnitine acetyltransferase substrate-binding af-finity and activity in brain by feeding old rats acetyl-L-carnitine and/or R-α-lipoic acid
    • Liu J, Killilea DW, Ames BN. Age-associated mitochondrial oxidative decay: improvement of carnitine acetyltransferase substrate-binding af-finity and activity in brain by feeding old rats acetyl-L-carnitine and/or R-α-lipoic acid. Proc Natl Acad Sci USA 99: 1876-1881, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1876-1881
    • Liu, J.1    Killilea, D.W.2    Ames, B.N.3
  • 98
    • 13244292394 scopus 로고    scopus 로고
    • Time-course of mitochondrial gene expressions in mice brains: Implications for mitochondrial dysfunction, oxidative damage, and cytochrome c in aging
    • Manczak M, Jung Y, Park BS, Partovi D, Reddy PH. Time-course of mitochondrial gene expressions in mice brains: implications for mitochondrial dysfunction, oxidative damage, and cytochrome c in aging. J Neurochem 92: 494-504, 2005.
    • (2005) J Neurochem , vol.92 , pp. 494-504
    • Manczak, M.1    Jung, Y.2    Park, B.S.3    Partovi, D.4    Reddy, P.H.5
  • 99
    • 12244257527 scopus 로고    scopus 로고
    • Nitric oxide from inflammatory-activated glia synergizes with hypoxia to induce neuronal death
    • Mander P, Borutaite V, Moncada S, Brown GC. Nitric oxide from inflammatory-activated glia synergizes with hypoxia to induce neuronal death. J Neurosci Res 79: 208-215, 2005.
    • (2005) J Neurosci Res , vol.79 , pp. 208-215
    • Mander, P.1    Borutaite, V.2    Moncada, S.3    Brown, G.C.4
  • 100
    • 0026718086 scopus 로고
    • Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease
    • Mann VM, Cooper JM, Krige D, Daniel SE, Schapira AH, Marsden CD. Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease. Brain 115: 333-342, 1992.
    • (1992) Brain , vol.115 , pp. 333-342
    • Mann, V.M.1    Cooper, J.M.2    Krige, D.3    Daniel, S.E.4    Schapira, A.H.5    Marsden, C.D.6
  • 101
    • 0028278620 scopus 로고
    • Age-related changes in glutathione and lipid peroxide content in mouse synaptic mitochondria: Relationship to cytochrome c oxidase decline
    • Martinez M, Ferrandiz ML, De Juan E, Miquel J. Age-related changes in glutathione and lipid peroxide content in mouse synaptic mitochondria: relationship to cytochrome c oxidase decline. Neurosci Lett 170: 121-124, 1994.
    • (1994) Neurosci Lett , vol.170 , pp. 121-124
    • Martinez, M.1    Ferrandiz, M.L.2    De Juan, E.3    Miquel, J.4
  • 102
    • 0036483748 scopus 로고    scopus 로고
    • Exercise and skeletal muscle ageing: Cellular and molecular mechanisms
    • McArdle A, Vasilaki A, Jackson M. Exercise and skeletal muscle ageing: cellular and molecular mechanisms. Aging Res Rev 1: 79-93, 2002.
    • (2002) Aging Res Rev , vol.1 , pp. 79-93
    • McArdle, A.1    Vasilaki, A.2    Jackson, M.3
  • 103
    • 33847048372 scopus 로고
    • Aging
    • Oxford, UK: Oxford University Press, chapt. 11
    • McCarter RJM. Aging. In: Handbook of Physiology. Oxford, UK: Oxford University Press, 1995, chapt. 11.
    • (1995) Handbook of Physiology
    • McCarter, R.J.M.1
  • 104
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack JG, Halestrap AP, Denton RM. Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol Rev 70: 391-425, 1990.
    • (1990) Physiol Rev , vol.70 , pp. 391-425
    • McCormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 105
    • 0029033862 scopus 로고
    • Mitochondrial changes associated with glutathione defi-ciency
    • Meister A. Mitochondrial changes associated with glutathione defi-ciency. Biochim Biophys Acta 1271: 35-42, 1995.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 35-42
    • Meister, A.1
  • 106
    • 0013844789 scopus 로고
    • Stoichiometry of proton translocation through the respiratory chain and adenosine triphosphatase systems of rat liver mitochondria
    • Mitchell P, Moyle J. Stoichiometry of proton translocation through the respiratory chain and adenosine triphosphatase systems of rat liver mitochondria. Nature 208: 147-151, 1965.
    • (1965) Nature , vol.208 , pp. 147-151
    • Mitchell, P.1    Moyle, J.2
  • 107
    • 0014470420 scopus 로고
    • Estimation of membrane potential and pH difference across the cristae membrane of rat liver mitochondria
    • Mitchell P, Moyle J. Estimation of membrane potential and pH difference across the cristae membrane of rat liver mitochondria. Eur J Biochem 7: 471-484, 1969.
    • (1969) Eur J Biochem , vol.7 , pp. 471-484
    • Mitchell, P.1    Moyle, J.2
  • 109
    • 2542509453 scopus 로고    scopus 로고
    • Defects of the respiratory chain in various tissues of old monkeys: A cytochemical-immunocytochemical study
    • Muller-Hocker J, Schafer S, Link TA, Possekel S, Hammer C. Defects of the respiratory chain in various tissues of old monkeys: a cytochemical-immunocytochemical study. Mech Ageing Dev 86: 197-213, 1996.
    • (1996) Mech Ageing Dev , vol.86 , pp. 197-213
    • Muller-Hocker, J.1    Schafer, S.2    Link, T.A.3    Possekel, S.4    Hammer, C.5
  • 112
    • 6344289360 scopus 로고    scopus 로고
    • Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging
    • Navarro A, Boveris A. Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging. Am J Physiol Regul Integr Comp Physiol 287: R1244-R1249, 2004.
    • (2004) Am J Physiol Regul Integr Comp Physiol , vol.287
    • Navarro, A.1    Boveris, A.2
  • 113
    • 1342309919 scopus 로고    scopus 로고
    • Beneficial effects of moderate exercise on mice aging: Survival, behavior, oxidative stress, and mitochondrial electron transfer
    • Navarro A, Gomez C, Lopez-Cepero JM, Boveris A. Beneficial effects of moderate exercise on mice aging: survival, behavior, oxidative stress, and mitochondrial electron transfer. Am J Physiol Regul Integr Comp Physiol 286: R505-R511, 2004.
    • (2004) Am J Physiol Regul Integr Comp Physiol , vol.286
    • Navarro, A.1    Gomez, C.2    Lopez-Cepero, J.M.3    Boveris, A.4
  • 116
    • 33845463230 scopus 로고    scopus 로고
    • Dietary thioproline decreases spontaneous food intake and increases survival and neurological function in mice
    • Navarro A, Sanchez-Pino MJ, Gomez C, Bandez MJ, Cadenas E, Boveris A. Dietary thioproline decreases spontaneous food intake and increases survival and neurological function in mice. Antioxid Redox Signal 9: 131-191, 2007.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 131-191
    • Navarro, A.1    Sanchez-Pino, M.J.2    Gomez, C.3    Bandez, M.J.4    Cadenas, E.5    Boveris, A.6
  • 118
    • 0345279953 scopus 로고    scopus 로고
    • Myocardial and skeletal muscle aging and changes in oxidative stress in relationship to rigorous exercise training
    • Navarro-Arevalo A, Canavate C, Sanchez-Pino MJ. Myocardial and skeletal muscle aging and changes in oxidative stress in relationship to rigorous exercise training. Mech Ageing Dev 108: 207-217, 1999.
    • (1999) Mech Ageing Dev , vol.108 , pp. 207-217
    • Navarro-Arevalo, A.1    Canavate, C.2    Sanchez-Pino, M.J.3
  • 121
    • 13844262622 scopus 로고    scopus 로고
    • Intracellular generation of reactive oxygen species by mitochondria
    • Nohl H, Gille L, Staniek K. Intracellular generation of reactive oxygen species by mitochondria. Biochem Pharmacol 69: 719-723, 2005.
    • (2005) Biochem Pharmacol , vol.69 , pp. 719-723
    • Nohl, H.1    Gille, L.2    Staniek, K.3
  • 122
    • 24144489726 scopus 로고    scopus 로고
    • Coenzyme Q10 protects from aging-related oxidative stress and improves mitochondrial function in heart of rats fed a polyunsaturated fatty acid (PUFA)-rich diet
    • Ochoa JJ, Quiles JL, Huertas JR, Mataix J. Coenzyme Q10 protects from aging-related oxidative stress and improves mitochondrial function in heart of rats fed a polyunsaturated fatty acid (PUFA)-rich diet. J Gerontol A Biol Sci Med Sci 60: 970-975, 2005.
    • (2005) J Gerontol A Biol Sci Med Sci , vol.60 , pp. 970-975
    • Ochoa, J.J.1    Quiles, J.L.2    Huertas, J.R.3    Mataix, J.4
  • 123
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto A, Fridovich I. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J Biol Chem 276: 38388-38393, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 124
    • 0036227594 scopus 로고    scopus 로고
    • Melatonin protects hepatic mitochondrial respiratory chain activity in senescence-accelerated mice
    • Okatani Y, Wakatsuki A, Reiter RJ. Melatonin protects hepatic mitochondrial respiratory chain activity in senescence-accelerated mice. J Pineal Res 32: 143-148, 2002.
    • (2002) J Pineal Res , vol.32 , pp. 143-148
    • Okatani, Y.1    Wakatsuki, A.2    Reiter, R.J.3
  • 125
    • 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 263: 1128-1130, 1994.
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 126
    • 29344469822 scopus 로고
    • Electron microscopy of mitochondria and other cytoplasmic structures
    • edited by Gaebler OH. New York: Academic
    • Palade GE. Electron microscopy of mitochondria and other cytoplasmic structures. In: Enzymes: Units of Biological Structure and Function, edited by Gaebler OH. New York: Academic, 1956, p. 185.
    • (1956) Enzymes: Units of Biological Structure and Function , pp. 185
    • Palade, G.E.1
  • 127
    • 0025087726 scopus 로고
    • Evidence for a defect in NADH: Ubiquinone oxidoreductase (complex I) in Huntington's disease
    • Parker WD Jr, Boyson SJ, Luder AS and Parks JK. Evidence for a defect in NADH: ubiquinone oxidoreductase (complex I) in Huntington's disease. Neurology 40: 1231-1234, 1990.
    • (1990) Neurology , vol.40 , pp. 1231-1234
    • Parker Jr, W.D.1    Boyson, S.J.2    Luder, A.S.3    Parks, J.K.4
  • 128
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Poderoso JJ, Carreras MC, Lisdero C, Riobo N, Schopfer F, Boveris A. Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch Biochem Biophys 328: 85-92, 1996.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobo, N.4    Schopfer, F.5    Boveris, A.6
  • 129
    • 0033621429 scopus 로고    scopus 로고
    • The regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol
    • Poderoso JJ, Lisdero C, Schopfer F, Riobo N, Carreras MC, Cadenas E, Boveris A. The regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol. J Biol Chem 274: 37709-37716, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 37709-37716
    • Poderoso, J.J.1    Lisdero, C.2    Schopfer, F.3    Riobo, N.4    Carreras, M.C.5    Cadenas, E.6    Boveris, A.7
  • 130
    • 33646539981 scopus 로고
    • A soluble protein fraction required for coupling phosphorylation to oxidation in submitochondrial fragments of beef heart mitochondria
    • Pullman ME, Penefsky H, Racker E. A soluble protein fraction required for coupling phosphorylation to oxidation in submitochondrial fragments of beef heart mitochondria. Arch Biochem Biophys 76: 227-230, 1958.
    • (1958) Arch Biochem Biophys , vol.76 , pp. 227-230
    • Pullman, M.E.1    Penefsky, H.2    Racker, E.3
  • 131
    • 0036452555 scopus 로고    scopus 로고
    • Exercise training decreases DNA damage and increases DNA repair and resistance against oxidative stress of proteins in aged rat skeletal muscle
    • Radak Z, Naito H, Kaneko T, Tahara S, Nakamoto H, Takahashi R, Cardozo-Pelaez F, Goto S. Exercise training decreases DNA damage and increases DNA repair and resistance against oxidative stress of proteins in aged rat skeletal muscle. Pflügers Arch 445: 273-278, 2002.
    • (2002) Pflügers Arch , vol.445 , pp. 273-278
    • Radak, Z.1    Naito, H.2    Kaneko, T.3    Tahara, S.4    Nakamoto, H.5    Takahashi, R.6    Cardozo-Pelaez, F.7    Goto, S.8
  • 134
    • 0025328406 scopus 로고
    • Effect of dietary restriction on the age-dependent changes in the expression of antioxidant enzymes in rat liver
    • Rao G, Xia E, Nadakavukaren MJ, Richardson A. Effect of dietary restriction on the age-dependent changes in the expression of antioxidant enzymes in rat liver. J Nutr 120: 602-609, 1990.
    • (1990) J Nutr , vol.120 , pp. 602-609
    • Rao, G.1    Xia, E.2    Nadakavukaren, M.J.3    Richardson, A.4
  • 135
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation
    • Riobo NA, Clementi E, Melani M, Boveris A, Cadenas E, Moncada S, Poderoso JJ. Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation. Biochem J 359: 139-145, 2001.
    • (2001) Biochem J , vol.359 , pp. 139-145
    • Riobo, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6    Poderoso, J.J.7
  • 137
    • 0034646624 scopus 로고    scopus 로고
    • Nitric oxide reaction with lipid peroxyl radicals spares alpha-tocopherol during lipid peroxidation. Greater oxidant protection from the pair nitric oxide/alpha-tocopherol than alpha-tocopherol/ascorbate
    • Rubbo H, Radi R, Anselmi D, Kirk M, Barnes S, Butler J, Eiserich JP, Freeman BA. Nitric oxide reaction with lipid peroxyl radicals spares alpha-tocopherol during lipid peroxidation. Greater oxidant protection from the pair nitric oxide/alpha-tocopherol than alpha-tocopherol/ascorbate. J Biol Chem 275: 10812-10818, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 10812-10818
    • Rubbo, H.1    Radi, R.2    Anselmi, D.3    Kirk, M.4    Barnes, S.5    Butler, J.6    Eiserich, J.P.7    Freeman, B.A.8
  • 138
    • 20044384556 scopus 로고    scopus 로고
    • Dietary restriction at old age lowers mitochondrial oxygen radical production and leak at complex I and oxidative DNA damage in rat brain
    • Sanz A, Caro P, Ibanez J, Gomez J, Gredilla R, Barja G. Dietary restriction at old age lowers mitochondrial oxygen radical production and leak at complex I and oxidative DNA damage in rat brain. J Bioenerg Biomembr 37: 83-90, 2005.
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 83-90
    • Sanz, A.1    Caro, P.2    Ibanez, J.3    Gomez, J.4    Gredilla, R.5    Barja, G.6
  • 142
    • 0037362863 scopus 로고    scopus 로고
    • Lifelong caloric restriction increases expression of apoptosis repressor with a caspase recruitment domain (ARC) in the brain
    • Shelke RR, Leeuwenburgh C. Lifelong caloric restriction increases expression of apoptosis repressor with a caspase recruitment domain (ARC) in the brain. FASEB J 17: 494-496, 2003.
    • (2003) FASEB J , vol.17 , pp. 494-496
    • Shelke, R.R.1    Leeuwenburgh, C.2
  • 143
  • 144
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi T, Wang F, Stieren E, Tong Q. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J Biol Chem 280: 13560-13567, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 146
    • 33847072403 scopus 로고
    • The ultrastructure of mitochondria; the ultrastructure of the ground substance of the cytoplasm
    • New York: Interscience
    • Sjostrand FS. The ultrastructure of mitochondria; the ultrastructure of the ground substance of the cytoplasm. In: Fine Structure of Cells. New York: Interscience, 1955, p. 16-222.
    • (1955) Fine Structure of Cells , pp. 16-222
    • Sjostrand, F.S.1
  • 147
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress caloric restriction, aging
    • Sohal RS, Weindruch R. Oxidative stress caloric restriction, aging. Science 273: 59-63, 1996.
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 148
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre J, Buckingham JA, Roebuck SJ, Brand MD. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem 277: 44784-44790, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 149
    • 0036710399 scopus 로고    scopus 로고
    • Importance of individuality in oxidative stress and aging
    • Stadtman ER. Importance of individuality in oxidative stress and aging. Free Radic Biol Med 33: 597-604, 2002.
    • (2002) Free Radic Biol Med , vol.33 , pp. 597-604
    • Stadtman, E.R.1
  • 150
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens JF, Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J 191: 421-427, 1980.
    • (1980) Biochem J , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 152
    • 33646118481 scopus 로고    scopus 로고
    • Mitochondrial metabolic states and membrane potential modulate mtNOS activity
    • Valdez LB, Zaobornyj T, Boveris A. Mitochondrial metabolic states and membrane potential modulate mtNOS activity. Biochim Biophys Acta 1757: 166-172, 2006.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 166-172
    • Valdez, L.B.1    Zaobornyj, T.2    Boveris, A.3
  • 153
    • 18244393163 scopus 로고    scopus 로고
    • Why females live longer than males? Importance of the upregulation of longevity-associated genes by oestrogenic compounds
    • Vina J, Borras C, Gambini J, Sastre J, Pallardo FV. Why females live longer than males? Importance of the upregulation of longevity-associated genes by oestrogenic compounds. FEBS Lett 579: 2541-2545, 2005.
    • (2005) FEBS Lett , vol.579 , pp. 2541-2545
    • Vina, J.1    Borras, C.2    Gambini, J.3    Sastre, J.4    Pallardo, F.V.5
  • 154
    • 0142151379 scopus 로고    scopus 로고
    • Mitochondrial theory of aging: Importance to explain why females live longer than males
    • Vina J, Sastre J, Pallardo F, Borras C. Mitochondrial theory of aging: importance to explain why females live longer than males. Antioxid Redox Signal 5: 549-556, 2003.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 549-556
    • Vina, J.1    Sastre, J.2    Pallardo, F.3    Borras, C.4
  • 155
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker JE. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q Rev Biophys 25: 253-324, 1992.
    • (1992) Q Rev Biophys , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 157
    • 0030466371 scopus 로고    scopus 로고
    • The retardation of aging by caloric restriction: Studies in rodents and primates
    • Weindruch R. The retardation of aging by caloric restriction: studies in rodents and primates. Toxicol Pathol 24: 742-745, 1996.
    • (1996) Toxicol Pathol , vol.24 , pp. 742-745
    • Weindruch, R.1
  • 159
    • 0032573066 scopus 로고    scopus 로고
    • Mitochondrial adenine nucleotide translocase is modified oxidatively during aging
    • Yan LJ, Sohal RS. Mitochondrial adenine nucleotide translocase is modified oxidatively during aging. Proc Natl Acad Sci USA 95: 12896-12901, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12896-12901
    • Yan, L.J.1    Sohal, R.S.2
  • 160
    • 28244454785 scopus 로고    scopus 로고
    • Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice
    • Yarian CS, Toroser D, Sohal RS. Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice. Mech Ageing Dev 127: 79-84, 2006.
    • (2006) Mech Ageing Dev , vol.127 , pp. 79-84
    • Yarian, C.S.1    Toroser, D.2    Sohal, R.S.3
  • 161
    • 19344371066 scopus 로고    scopus 로고
    • Effect of sustained hypobaric hypoxia during maturation and aging on rat myocardium. II. mtNOS activity
    • Zaobornyj T, Valdez LB, La PP, Costa LE, Boveris A. Effect of sustained hypobaric hypoxia during maturation and aging on rat myocardium. II. mtNOS activity. J Appl Physiol 98: 2370 -2375, 2005.
    • (2005) J Appl Physiol , vol.98 , pp. 2370-2375
    • Zaobornyj, T.1    Valdez, L.B.2    La, P.P.3    Costa, L.E.4    Boveris, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.