메뉴 건너뛰기




Volumn 552, Issue 2, 2003, Pages 335-344

Mitochondrial formation of reactive oxygen species

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CYTOCHROME C; CYTOCHROME C OXIDASE; MITOCHONDRIAL ENZYME; OXYGEN; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; XENOBIOTIC AGENT; NITRIC OXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE (UBIQUINONE); UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 0142150051     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.2003.049478     Document Type: Review
Times cited : (3895)

References (108)
  • 1
    • 0028024601 scopus 로고
    • Evidence for superoxide radical production by a simple flavoprotein: Glucose oxidase
    • Al Bekairi AM, Nagi MN, Shoeb HA & Al Sawaf HA (1994). Evidence for superoxide radical production by a simple flavoprotein: glucose oxidase. Biochem Mol Biol Int 34, 233-238.
    • (1994) Biochem. Mol. Biol. Int. , vol.34 , pp. 233-238
    • Al Bekairi, A.M.1    Nagi, M.N.2    Shoeb, H.A.3    Al Sawaf, H.A.4
  • 5
    • 0034458228 scopus 로고    scopus 로고
    • The NADPH oxicase of endothelial cells
    • Babior BM (2000). The NADPH oxicase of endothelial cells. IUBMB Life 50, 267-269.
    • (2000) IUBMB Life , vol.50 , pp. 267-269
    • Babior, B.M.1
  • 7
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity and relation to aging and longevity
    • Barja G (1999). Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity and relation to aging and longevity. J Bioenerg Biomembr 31, 347-366.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 347-366
    • Barja, G.1
  • 8
    • 0031721246 scopus 로고    scopus 로고
    • Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon
    • Barja G & Herrero A J (1998). Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon. J Bioenerg Biomembr 30, 235-243.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 235-243
    • Barja, G.1    Herrero, A.J.2
  • 9
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide superoxide and peroxynitrite: The good the bad and the ugly
    • Beckman JS & Koppenol WH (1996). Nitric oxide superoxide and peroxynitrite: the good the bad and the ugly. Am J Physiol 271, C1424-1437.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 11
    • 0025286523 scopus 로고
    • The participation of coenzyme Q in free radical production and antioxidation
    • Beyer RE (1990). The participation of coenzyme Q in free radical production and antioxidation. Free Radic Biol Med 8, 545-565.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 545-565
    • Beyer, R.E.1
  • 12
    • 0020376270 scopus 로고
    • Mitochondrial lipid peroxidation by cumene hydroperoxide and its prevention by succinate
    • Bindoli A, Cavallini L & Jocelyn P (1982). Mitochondrial lipid peroxidation by cumene hydroperoxide and its prevention by succinate. Biochim Biophys Acta 681, 496-503.
    • (1982) Biochim. Biophys. Acta , vol.681 , pp. 496-503
    • Bindoli, A.1    Cavallini, L.2    Jocelyn, P.3
  • 13
    • 0032435447 scopus 로고    scopus 로고
    • Oxidative DNA damage processing and changes with aging
    • Bohr V, Anson RM, Mazur S & Dianov G (1998). Oxidative DNA damage processing and changes with aging. Toxicol Lett 102-103, 47-52.
    • (1998) Toxicol. Lett. , vol.102-103 , pp. 47-52
    • Bohr, V.1    Anson, R.M.2    Mazur, S.3    Dianov, G.4
  • 14
    • 0037373449 scopus 로고    scopus 로고
    • Mitochondria from females exhibit higher antioxidant gene expression and lower oxidative damage than males
    • Borras C, Sastre J, Garcia-Sala D, Lloret A, Pallardo FV & Vina J (2003). Mitochondria from females exhibit higher antioxidant gene expression and lower oxidative damage than males. Free Radic Biol Med 34, 546-552.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 546-552
    • Borras, C.1    Sastre, J.2    Garcia-Sala, D.3    Lloret, A.4    Pallardo, F.V.5    Vina, J.6
  • 15
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris A, Cadenas E & Stoppani AOM (1976). Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem J 156, 435-444.
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.M.3
  • 16
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A, Oshino N & Chance B (1972). The cellular production of hydrogen peroxide. Biochem J 128, 617-630.
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 17
    • 0016719078 scopus 로고
    • The reaction between the superoxide anion radical and cytochrome c
    • Butler J, Jayson GG & Swallow AJ (1975). The reaction between the superoxide anion radical and cytochrome c. Biochim Biophys Acta 408, 215-222.
    • (1975) Biochim. Biophys. Acta , vol.408 , pp. 215-222
    • Butler, J.1    Jayson, G.G.2    Swallow, A.J.3
  • 18
    • 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 AOM (1977). 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) Arch. Biochem. Biophys. , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.M.4
  • 19
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation oxidative stress and aging
    • Cadenas E & Davies KJ (2000). Mitochondrial free radical generation oxidative stress and aging. Free Radic Biol Med 29, 222-230.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 20
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai JY & Jones DP (1998). Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J Biol Chem 273, 11401-11404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, J.Y.1    Jones, D.P.2
  • 21
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • Cassina A& Radi R (1996). Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch Biochem Biophys 328, 309-316.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 22
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H & Boveris A (1979). Hydroperoxide metabolism in mammalian organs. Physiol Rev 59, 527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 24
    • 0030694267 scopus 로고    scopus 로고
    • Redox regulation of the mitochondrial permeability transition pore
    • Chernyak BV (1997). Redox regulation of the mitochondrial permeability transition pore. Biosci Rep 17, 293-302.
    • (1997) Biosci. Rep. , vol.17 , pp. 293-302
    • Chernyak, B.V.1
  • 26
    • 0034663539 scopus 로고    scopus 로고
    • Effects of nitric oxide and peroxynitrite on the cytochrome oxidase K(m) for oxygen: Implications for mitochondrial pathology
    • 1459
    • Cooper CE & Davies NA (2000). Effects of nitric oxide and peroxynitrite on the cytochrome oxidase K(m) for oxygen: implications for mitochondrial pathology. Biochim Biophys Acta 1459, 390-396.
    • (2000) Biochim. Biophys. Acta , pp. 390-396
    • Cooper, C.E.1    Davies, N.A.2
  • 30
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W (2002). Free radicals in the physiological control of cell function. Physiol Rev 82, 47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 31
    • 0026718790 scopus 로고
    • Succinate-dependent lipid peroxidation and its prevention by reduced ubiquinone in beef heart submitochondrial particles
    • Eto Y, Kang D, Hasegawa E, Takeshige K & Minakami S (1992). Succinate-dependent lipid peroxidation and its prevention by reduced ubiquinone in beef heart submitochondrial particles. Arch Biochem Biophys 295, 101-106.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 101-106
    • Eto, Y.1    Kang, D.2    Hasegawa, E.3    Takeshige, K.4    Minakami, S.5
  • 32
    • 0037441390 scopus 로고    scopus 로고
    • External alternative NADH dehydrogenase of Saccharomyces cerevisiae: A potential source of superoxide
    • Fang J & Beattie DS (2003). External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide. Free Radic Biol Med 34, 478-488.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 478-488
    • Fang, J.1    Beattie, D.S.2
  • 34
    • 0033593230 scopus 로고    scopus 로고
    • Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL
    • Finucane DM, Bossy-Wetzel E, Waterhouse NJ, Cotter TG & Green DR (1999). Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL. J Biol Chem 274, 2225-2233.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2225-2233
    • Finucane, D.M.1    Bossy-Wetzel, E.2    Waterhouse, N.J.3    Cotter, T.G.4    Green, D.R.5
  • 35
    • 0017293045 scopus 로고
    • Dihydroorotate-dependent superoxide production in rat brain and liver. A function of the primary dehydrogenase
    • Forman HJ & Kennedy J (1976). Dihydroorotate-dependent superoxide production in rat brain and liver. A function of the primary dehydrogenase. Arch Biochem Biophys 173, 219-224.
    • (1976) Arch. Biochem. Biophys. , vol.173 , pp. 219-224
    • Forman, H.J.1    Kennedy, J.2
  • 36
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I (1995). Superoxide radical and superoxide dismutases. Annu Rev Biochem 64, 97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 37
    • 0035929367 scopus 로고    scopus 로고
    • The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2
    • Genova ME, Ventura B, Giuliano G, Bovina C, Formiggini G, Parenti CG & Lenaz G (2001). The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2. FEBS Lett 505, 364-368.
    • (2001) FEBS Lett. , vol.505 , pp. 364-368
    • Genova, M.E.1    Ventura, B.2    Giuliano, G.3    Bovina, C.4    Formiggini, G.5    Parenti, C.G.6    Lenaz, G.7
  • 38
    • 33645999557 scopus 로고
    • Oxygen poisioning and X-irradiation: A mechanism in common
    • Gerschman R, Gilbert DL, Nye SW, Dwyer P & Fenn WO (1954). Oxygen poisioning and X-irradiation: a mechanism in common. Science 119, 623-626.
    • (1954) Science , vol.119 , pp. 623-626
    • Gerschman, R.1    Gilbert, D.L.2    Nye, S.W.3    Dwyer, P.4    Fenn, W.O.5
  • 39
    • 0030697859 scopus 로고    scopus 로고
    • Nitric oxide synthase activity in mitochondria
    • Ghafourifar P & Richter C (1997). Nitric oxide synthase activity in mitochondria. FEBS Lett 418, 291-296.
    • (1997) FEBS Lett. , vol.418 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 40
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi C, Poderoso JJ & Boveris A (1998). Production of nitric oxide by mitochondria. J Biol Chem 273, 11038-11043.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 41
    • 0344673472 scopus 로고    scopus 로고
    • Analysis of mitochondrial targeting sequence and coding region polymorphisms of the manganese superoxide dismutase gene in German Parkinson disease patients
    • Grasbon-Frodl EM, Kosel S, Riess O, Muller U, Mehraein P & Graeber MB (1999). Analysis of mitochondrial targeting sequence and coding region polymorphisms of the manganese superoxide dismutase gene in German Parkinson disease patients. Biochem Biophys Res Commun 255, 749-752.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 749-752
    • Grasbon-Frodl, E.M.1    Kosel, S.2    Riess, O.3    Muller, U.4    Mehraein, P.5    Graeber, M.B.6
  • 43
    • 0029054761 scopus 로고
    • Vitamin E oxidation in rat liver mitochondria
    • Ham AJ & Liebler DC (1995). Vitamin E oxidation in rat liver mitochondria. Biochemistry 34, 5754-5761.
    • (1995) Biochemistry , vol.34 , pp. 5754-5761
    • Ham, A.J.1    Liebler, D.C.2
  • 44
    • 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 (2003). Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol. J Biol Chem 278, 5557-5563.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5
  • 45
    • 0035863011 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
    • Han D, Williams E & Cadenas E (2001). Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem J 353, 411-416.
    • (2001) Biochem. J. , vol.353 , pp. 411-416
    • Han, D.1    Williams, E.2    Cadenas, E.3
  • 46
    • 0030589009 scopus 로고    scopus 로고
    • The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA
    • Hauptmann N, Grimsby J, Shih JC & Cadenas E (1996). The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA. Arch Biochem Biophys 335, 295-304.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 295-304
    • Hauptmann, N.1    Grimsby, J.2    Shih, J.C.3    Cadenas, E.4
  • 47
    • 0037235145 scopus 로고    scopus 로고
    • Multiple mediators of plant programmed cell death: Interplay of conserved cell death mechanisms and plant-specific regulators
    • Hoeberichts FA & Woltering EJ (2003). Multiple mediators of plant programmed cell death: interplay of conserved cell death mechanisms and plant-specific regulators. Bioessays 25, 47-57.
    • (2003) Bioessays , vol.25 , pp. 47-57
    • Hoeberichts, F.A.1    Woltering, E.J.2
  • 48
    • 0035797151 scopus 로고    scopus 로고
    • Mitochondria as subcellular targets for clinically useful anthracyclines
    • Jung K & Reszka R (2001). Mitochondria as subcellular targets for clinically useful anthracyclines. Adv Drug Deliv Rev 49, 87-105.
    • (2001) Adv. Drug Deliv. Rev. , vol.49 , pp. 87-105
    • Jung, K.1    Reszka, R.2
  • 49
    • 0027930057 scopus 로고
    • Evidence for nitric oxide-mediated oxidative damage in chronic inflammation: Nitrotyrosine in serum and synovial fluid from rheumatoid patients
    • Kaur H & Halliwell B (1994). Evidence for nitric oxide-mediated oxidative damage in chronic inflammation: nitrotyrosine in serum and synovial fluid from rheumatoid patients. FEBS Lett 350, 9-12.
    • (1994) FEBS Lett. , vol.350 , pp. 9-12
    • Kaur, H.1    Halliwell, B.2
  • 50
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G, Dallaporta B & Resche-Rigon M (1998). The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol 60, 619-642.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 51
    • 0027365312 scopus 로고
    • Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian
    • Ku H-H, Brunk UT & Sohal RS (1993). Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian. Free Radic Biol Med 15, 621-627.
    • (1993) Free Radic. Biol. Med. , vol.15 , pp. 621-627
    • Ku, H.-H.1    Brunk, U.T.2    Sohal, R.S.3
  • 52
    • 0036903625 scopus 로고    scopus 로고
    • Complex I-mediated reactive oxygen species generation: Modulation by cytochrome c and NAD(P)+ oxidation-reduction state
    • Kushnareva Y, Murphy AN & Andreyev A (2002). Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem J 368, 545-553.
    • (2002) Biochem. J. , vol.368 , pp. 545-553
    • Kushnareva, Y.1    Murphy, A.N.2    Andreyev, A.3
  • 54
    • 0036139856 scopus 로고    scopus 로고
    • The mitochondrial production of reactive oxygen species: Mechanisms and implications in human pathology
    • Lenaz G (2001). The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology. IUBMB Life 52, 159-164.
    • (2001) IUBMB Life , vol.52 , pp. 159-164
    • Lenaz, G.1
  • 55
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES & Wang X (1997). Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 56
    • 0028965665 scopus 로고
    • Superoxide from glucose oxidase or from nitroblue tetrazolium
    • Liochev SI & Fridovich I (1995). Superoxide from glucose oxidase or from nitroblue tetrazolium. Arch Biochem Biophys 318, 408-410.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 408-410
    • Liochev, S.I.1    Fridovich, I.2
  • 57
    • 0032533982 scopus 로고    scopus 로고
    • Lucigenin as mediator of superoxide production: Revisited
    • Liochev SI & Fridovich I (1998). Lucigenin as mediator of superoxide production: revisited. Free Radic Biol Med 25, 926-928.
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 926-928
    • Liochev, S.I.1    Fridovich, I.2
  • 58
    • 0032732998 scopus 로고    scopus 로고
    • Superoxide and iron: Partners in crime
    • Liochev SI & Fridovich I (1999). Superoxide and iron: partners in crime. IUBMB Life 48, 157-161.
    • (1999) IUBMB Life , vol.48 , pp. 157-161
    • Liochev, S.I.1    Fridovich, I.2
  • 59
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R & Wang X (1996). Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86, 147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 61
    • 0024212517 scopus 로고
    • Superoxide dismutase: The first twenty years (1968-1988)
    • McCord JM & Fridovich I (1988). Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med 5, 363-369.
    • (1988) Free Radic. Biol. Med. , vol.5 , pp. 363-369
    • McCord, J.M.1    Fridovich, I.2
  • 62
    • 0017339395 scopus 로고
    • Vectorial chemiosmotic processes
    • Mitchell P (1977). Vectorial chemiosmotic processes. Annu Rev Biochem 46, 996-1005.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 996-1005
    • Mitchell, P.1
  • 63
    • 0035874637 scopus 로고    scopus 로고
    • Activation of NFkappaB and MnSOD gene expression by free radical scavengers in human microvascular endothelial cells
    • Murley JS, Kataoka Y, Hallahan DE, Roberts JC & Grdina DJ (2001). Activation of NFkappaB and MnSOD gene expression by free radical scavengers in human microvascular endothelial cells. Free Radic Biol Med 30, 1426-1439.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1426-1439
    • Murley, J.S.1    Kataoka, Y.2    Hallahan, D.E.3    Roberts, J.C.4    Grdina, D.J.5
  • 64
    • 0036830474 scopus 로고    scopus 로고
    • Mitochondrial function and dysfunction in the cell: Its relevance to aging and aging-related disease
    • Nicholls DG (2002). Mitochondrial function and dysfunction in the cell: its relevance to aging and aging-related disease. Int J Biochem Cell Biol 34, 1372-1381.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 1372-1381
    • Nicholls, D.G.1
  • 65
    • 0035910414 scopus 로고    scopus 로고
    • The rotary machine in the cell ATP synthase
    • Noji H & Yoshida M (2001). The rotary machine in the cell ATP synthase. J Biol Chem 276, 1665-1668.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1665-1668
    • Noji, H.1    Yoshida, M.2
  • 66
    • 0034306791 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis
    • Nomura K, Imai H, Koumura T, Kobayashi T & Nakagawa Y (2000). Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis. Biochem J 351, 183-193.
    • (2000) Biochem. J. , vol.351 , pp. 183-193
    • Nomura, K.1    Imai, H.2    Koumura, T.3    Kobayashi, T.4    Nakagawa, Y.5
  • 67
    • 0023190840 scopus 로고
    • Increase in manganese superoxide dismutase activity in the mouse heart after X-irradiation
    • Oberley LW, St Clair DK, Autor AP & Oberley TD (1987). Increase in manganese superoxide dismutase activity in the mouse heart after X-irradiation. Arch Biochem Biophys 254, 69-80.
    • (1987) Arch. Biochem. Biophys. , vol.254 , pp. 69-80
    • Oberley, L.W.1    St Clair, D.K.2    Autor, A.P.3    Oberley, T.D.4
  • 68
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria
    • Okado-Matsumoto A & Fridovich I (2001). Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria. J Biol Chem 276, 38388-38393.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 70
    • 0020491044 scopus 로고
    • The cytochrome c peroxidase activity of cytochrome oxidase
    • Orii Y (1982). The cytochrome c peroxidase activity of cytochrome oxidase. J Biol Chem. 257, 9246-9248.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9246-9248
    • Orii, Y.1
  • 71
    • 0028220114 scopus 로고
    • Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • Orr WC & Sohal RS (1994). Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 263, 1128-1130.
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 72
    • 0027948525 scopus 로고
    • Hydrogen peroxide metabolism in skeletal muscle mitochondria
    • Phung CD, Ezieme JA & Turrens JF (1994). Hydrogen peroxide metabolism in skeletal muscle mitochondria. Arch Biochem Biophys 315, 479-482.
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 479-482
    • Phung, C.D.1    Ezieme, J.A.2    Turrens, J.F.3
  • 73
    • 0021337432 scopus 로고
    • On the mechanism of production of superoxide radical by reaction mixtures containing NADH, phenazine methosulfate and nitroblue tetrazolium
    • Picker SD & Fridovich I (1984). On the mechanism of production of superoxide radical by reaction mixtures containing NADH, phenazine methosulfate and nitroblue tetrazolium. Arch Biochem Biophys 228, 155-158.
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 155-158
    • Picker, S.D.1    Fridovich, I.2
  • 74
    • 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, Riobó N, Schöpfer F & Boveris A (1996). Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch Biochem Biophys 328, 85-92.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobó, N.4    Schöpfer, F.5    Boveris, A.6
  • 75
    • 0024510080 scopus 로고
    • Problems associated with spin trapping oxygen-centered free radicals in biological systems
    • Pou S, Hassett DJ, Britigan BE, Cohen MS & Rosen GM (1989). Problems associated with spin trapping oxygen-centered free radicals in biological systems. Anal Biochem 177, 1-6.
    • (1989) Anal. Biochem. , vol.177 , pp. 1-6
    • Pou, S.1    Hassett, D.J.2    Britigan, B.E.3    Cohen, M.S.4    Rosen, G.M.5
  • 76
    • 0037337634 scopus 로고    scopus 로고
    • Optic neuropathy induced by reductions in mitochondrial superoxide dismutase
    • Qi X, Lewin AS, Hauswirth WW & Guy J (2003). Optic neuropathy induced by reductions in mitochondrial superoxide dismutase. Invest Ophthalmol Vis Sci 44, 1088-1096.
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 1088-1096
    • Qi, X.1    Lewin, A.S.2    Hauswirth, W.W.3    Guy, J.4
  • 77
    • 0036244508 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite interactions with mitochondria
    • Radi R, Cassina A & Hodara R (2002a). Nitric oxide and peroxynitrite interactions with mitochondria. Biol Chem 383, 401-409.
    • (2002) Biol. Chem. , vol.383 , pp. 401-409
    • Radi, R.1    Cassina, A.2    Hodara, R.3
  • 80
    • 0023811053 scopus 로고
    • Normal oxidative damage to mitochondrial and nuclear DNA is extensive
    • Richter C, Park JW & Ames BN (1988). Normal oxidative damage to mitochondrial and nuclear DNA is extensive. Proc Natl Acad Sci U S A 85, 6465-6467.
    • (1988) Proc. Natl. Acad. Sci. U S A , vol.85 , pp. 6465-6467
    • Richter, C.1    Park, J.W.2    Ames, B.N.3
  • 81
    • 0028151406 scopus 로고
    • Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives
    • Rubbo H, Radi R, Trujillo M, Telleri R, Kalyanaraman B, Barnes S, Kirk M & Freeman BA (1994). Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives. J Biol Chem 269, 26066-26075.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26066-26075
    • Rubbo, H.1    Radi, R.2    Trujillo, M.3    Telleri, R.4    Kalyanaraman, B.5    Barnes, S.6    Kirk, M.7    Freeman, B.A.8
  • 84
    • 0036710591 scopus 로고    scopus 로고
    • Signal transduction to hypoxia-inducible factor 1
    • Semenza G (2002). Signal transduction to hypoxia-inducible factor 1. Biochem Pharmacol 64, 993-998.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 993-998
    • Semenza, G.1
  • 85
    • 0037402801 scopus 로고    scopus 로고
    • Selective microglial activation in the rat rotenone model of Parkinson's disease
    • Sherer TB, Betarbet R, Kim JH & Greenamyre JT (2003a). Selective microglial activation in the rat rotenone model of Parkinson's disease. Neurosci Lett 341, 87-90.
    • (2003) Neurosci. Lett. , vol.341 , pp. 87-90
    • Sherer, T.B.1    Betarbet, R.2    Kim, J.H.3    Greenamyre, J.T.4
  • 86
    • 0037229425 scopus 로고    scopus 로고
    • Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation
    • Sherer TB, Kim JH, Betarbet R & Greenamyre JT (2003b). Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation. Exp Neurol 179, 9-16.
    • (2003) Exp. Neurol. , vol.179 , pp. 9-16
    • Sherer, T.B.1    Kim, J.H.2    Betarbet, R.3    Greenamyre, J.T.4
  • 87
    • 0030582372 scopus 로고    scopus 로고
    • Structural dimorphism in the mitochondrial targeting sequence in the human manganese superoxide dismutase gene. A predictive evidence for conformational change to influence mitochondrial transport and a study of allelic association in Parkinson's disease
    • Shimoda-Matsubayashi S, Matsumine H, Kobayashi T, Nakagawa-Hattori Y, Shimizu Y & Mizuno Y (1996). Structural dimorphism in the mitochondrial targeting sequence in the human manganese superoxide dismutase gene. A predictive evidence for conformational change to influence mitochondrial transport and a study of allelic association in Parkinson's disease. Biochem Biophys Res Commun 226, 561-565.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 561-565
    • Shimoda-Matsubayashi, S.1    Matsumine, H.2    Kobayashi, T.3    Nakagawa-Hattori, Y.4    Shimizu, Y.5    Mizuno, Y.6
  • 88
    • 0027328852 scopus 로고
    • Protein oxidative damage is associated with life expectancy of houseflies
    • Sohal RS, Agarwal S, Dubey A & Orr WC (1993). Protein oxidative damage is associated with life expectancy of houseflies. Proc Natl Acad Sci U S A 90, 7255-7259.
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 7255-7259
    • Sohal, R.S.1    Agarwal, S.2    Dubey, A.3    Orr, W.C.4
  • 91
    • 0037339203 scopus 로고    scopus 로고
    • The Ala16Val genetic dimorphism modulates the import of human manganese superoxide dismutase into rat liver mitochondria
    • Sutton A, Khoury H, Prip-Buus C, Cepanec C, Pessayre D & Degoul F (2003). The Ala16Val genetic dimorphism modulates the import of human manganese superoxide dismutase into rat liver mitochondria. Pharmacogenetics 13, 145-157.
    • (2003) Pharmacogenetics , vol.13 , pp. 145-157
    • Sutton, A.1    Khoury, H.2    Prip-Buus, C.3    Cepanec, C.4    Pessayre, D.5    Degoul, F.6
  • 92
    • 0035800889 scopus 로고    scopus 로고
    • Methods of detection of vascular reactive species. Nitric oxide superoxde hydrogen peroxide and peroxynitrite
    • Tarpey MM & Fridovich I (2001). Methods of detection of vascular reactive species. Nitric oxide superoxde hydrogen peroxide and peroxynitrite. Circ Res 89, 224-236.
    • (2001) Circ. Res. , vol.89 , pp. 224-236
    • Tarpey, M.M.1    Fridovich, I.2
  • 93
    • 0037228511 scopus 로고    scopus 로고
    • Rotenone neurotoxicity: A new window on environmental causes of Parkinson's disease and related brain amyloidoses
    • Trojanowski JQ (2003). Rotenone neurotoxicity: a new window on environmental causes of Parkinson's disease and related brain amyloidoses. Exp Neurol 179, 6-8.
    • (2003) Exp. Neurol. , vol.179 , pp. 6-8
    • Trojanowski, J.Q.1
  • 94
    • 0025358947 scopus 로고
    • The protonmotive Q cycle
    • Trumpower BL (1990). The protonmotive Q cycle. J Biol Chem 265, 11409-11412.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11409-11412
    • Trumpower, B.L.1
  • 95
    • 0034979160 scopus 로고    scopus 로고
    • Induction of TNF-a and MnSOD by endotoxin: Role of membrane CD14 and Toll-like receptor-4
    • Tsan MF, Clark RN, Goyert SM & White JE (2001). Induction of TNF-a and MnSOD by endotoxin: role of membrane CD14 and Toll-like receptor-4. Am J Physiol Cell Physiol 280, C1422-1430.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280
    • Tsan, M.F.1    Clark, R.N.2    Goyert, S.M.3    White, J.E.4
  • 96
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens JF, Alexandre A & Lehninger AL (1985). Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch Biochem Biophys 237, 408-414.
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 97
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens JF & Boveris A (1980). Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J 191, 421-427.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 98
    • 0020397137 scopus 로고
    • The effect of hyperoxia on superoxide production by lung submitochondrial particles
    • Turrens JF, Freeman BA, Levitt JG & Crapo JD (1982). The effect of hyperoxia on superoxide production by lung submitochondrial particles. Arch Biochem Biophys 217, 401-410.
    • (1982) Arch. Biochem. Biophys. , vol.217 , pp. 401-410
    • Turrens, J.F.1    Freeman, B.A.2    Levitt, J.G.3    Crapo, J.D.4
  • 100
    • 0037388067 scopus 로고    scopus 로고
    • Misfolded CuZnSOD and amyotrophic lateral sclerosis
    • Valentine JS & Hart PJ (2003). Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 100, 3617-3622.
    • (2003) Proc. Natl. Acad. Sci. U S A , vol.100 , pp. 3617-3622
    • Valentine, J.S.1    Hart, P.J.2
  • 101
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • Vignais PV (2002). The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol Life Sci 59, 1428-1459.
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 103
    • 0037158626 scopus 로고    scopus 로고
    • 2 sensing in hypoxic pulmonary vasoconstriction: The mitochondrial door re-opens
    • 2 sensing in hypoxic pulmonary vasoconstriction: the mitochondrial door re-opens. Respir Physiol Neurobiol 132, 81-91.
    • (2002) Respir. Physiol. Neurobiol. , vol.132 , pp. 81-91
    • Waypa, G.B.1    Schumacker, P.T.2
  • 105
    • 0001694692 scopus 로고
    • The two redox potentials for oxygen reduction to superoxide
    • Wood PM (1987). The two redox potentials for oxygen reduction to superoxide. Trends Biochem Sci 12, 250-251.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 250-251
    • Wood, P.M.1
  • 107
    • 0036718504 scopus 로고    scopus 로고
    • Reactive oxygen species production by the mitochondrial respiratory chain in isolated rat hepatocytes and liver mitochondria: Studies using myxothiazol
    • Young TA, Cunningham CC & Bailey SM (2002). Reactive oxygen species production by the mitochondrial respiratory chain in isolated rat hepatocytes and liver mitochondria: studies using myxothiazol. Arch Biochem Biophys 405, 65-72.
    • (2002) Arch. Biochem. Biophys. , vol.405 , pp. 65-72
    • Young, T.A.1    Cunningham, C.C.2    Bailey, S.M.3
  • 108
    • 0032545269 scopus 로고    scopus 로고
    • Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria
    • Zhang L, Yu L & Yu CA (1998). Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria. J Biol Chem 273, 33972-33976.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.