메뉴 건너뛰기




Volumn 174, Issue 1-2, 1997, Pages 305-319

Reactive oxygen species, mitochondria, apoptosis and aging

Author keywords

Mitochondrial DNA; Mitochondrial metabolism; Superoxide radicals

Indexed keywords

ANTIOXIDANT; MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE; SUPEROXIDE;

EID: 0030809576     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006873518427     Document Type: Article
Times cited : (461)

References (156)
  • 1
    • 0002137104 scopus 로고
    • Reactive oxygen species and the central nervous system
    • L Packer, L Prilipko, Y Christen (eds). Springer-Verlag, Berlin
    • Halliwell B: Reactive oxygen species and the central nervous system. In: L Packer, L Prilipko, Y Christen (eds). Free Radicals in the Brain, Springer-Verlag, Berlin, 1992, pp21-40
    • (1992) Free Radicals in the Brain , pp. 21-40
    • Halliwell, B.1
  • 3
    • 0028558576 scopus 로고
    • The development of mitochondrial medicine
    • Luft R: The development of mitochondrial medicine. Proc Nat Acad Sci USA 91: 8731-8738, 1994
    • (1994) Proc Nat Acad Sci USA , vol.91 , pp. 8731-8738
    • Luft, R.1
  • 4
    • 0028018477 scopus 로고
    • Oxidative stress and mitochondria dysfunction in neurodegeneration
    • Trischler H-J, Packer L, Medori R: Oxidative stress and mitochondria dysfunction in neurodegeneration. Biochem Mol Biol Intern 34: 169-180, 1994
    • (1994) Biochem Mol Biol Intern , vol.34 , pp. 169-180
    • Trischler, H.-J.1    Packer, L.2    Medori, R.3
  • 6
    • 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
  • 7
    • 0025845335 scopus 로고
    • Evidence for superoxide radical-dependent coronary vasospasm after angioplasty in intact dogs
    • Laurindo FRM, da Luz PL, Uint L, Rocha TF, Jaeger RG, Lopes EA: Evidence for superoxide radical-dependent coronary vasospasm after angioplasty in intact dogs. Circulation 83: 1705-1715, 1991
    • (1991) Circulation , vol.83 , pp. 1705-1715
    • Laurindo, F.R.M.1    Da Luz, P.L.2    Uint, L.3    Rocha, T.F.4    Jaeger, R.G.5    Lopes, E.A.6
  • 8
    • 0014519946 scopus 로고
    • Growth and physiology of Azotobacter ehroococcum in continuous cultures
    • Dalton H, Postgate JP: Growth and physiology of Azotobacter ehroococcum in continuous cultures. J Gen Microbiol 56: 307-319, 1969a
    • (1969) J Gen Microbiol , vol.56 , pp. 307-319
    • Dalton, H.1    Postgate, J.P.2
  • 9
    • 0014386264 scopus 로고
    • Effect of oxygen on growth of Azotobacter ehroococcum in batch and continuous cultures
    • Dalton H, Postgate JP: Effect of oxygen on growth of Azotobacter ehroococcum in batch and continuous cultures. J Gen Microbiol 54: 463-473, 1969b
    • (1969) J Gen Microbiol , vol.54 , pp. 463-473
    • Dalton, H.1    Postgate, J.P.2
  • 10
    • 0018722245 scopus 로고
    • Respiratory-chain characteristics of mutants of Azatobacter vinelandii negative to tetramethyl-p-phenylenediamine oxidase
    • Huffman P, Morgan TV, Der Vartanian DV: Respiratory-chain characteristics of mutants of Azatobacter vinelandii negative to tetramethyl-p-phenylenediamine oxidase. Eur J Biochem 100: 19-27, 1979
    • (1979) Eur J Biochem , vol.100 , pp. 19-27
    • Huffman, P.1    Morgan, T.V.2    Der Vartanian, D.V.3
  • 11
    • 0019122194 scopus 로고
    • Respiratory properties of cytochrome-c-deficient mutants of Azotobacter vinelandii
    • Huffman P, Morgan TV, Der Vartanian DV: Respiratory properties of cytochrome-c-deficient mutants of Azotobacter vinelandii. Eur J Biochem 110: 349-354, 1980
    • (1980) Eur J Biochem , vol.110 , pp. 349-354
    • Huffman, P.1    Morgan, T.V.2    Der Vartanian, D.V.3
  • 12
    • 0025030204 scopus 로고
    • Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: Mutants deficient in the cytochrome d complex are unable to fix nitrogen in air
    • Kelly MJS, Poole RK, Yates MG, Kenney C: Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air. J Bacteriol 172: 6010-6019, 1990
    • (1990) J Bacteriol , vol.172 , pp. 6010-6019
    • Kelly, M.J.S.1    Poole, R.K.2    Yates, M.G.3    Kenney, C.4
  • 13
    • 0028048861 scopus 로고
    • Oxygen reactions with bacterial oxidases and globins: Binding, reduction and regulation
    • Poole RK: Oxygen reactions with bacterial oxidases and globins: binding, reduction and regulation. Antonie van Leeuwenhoek 65: 289-310, 1994
    • (1994) Antonie Van Leeuwenhoek , vol.65 , pp. 289-310
    • Poole, R.K.1
  • 14
    • 0024962043 scopus 로고
    • Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli
    • Puustinen A, Finel M, Virkki M, Wikström M: Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli. FEBS Lett 249: 163-167, 1989
    • (1989) FEBS Lett , vol.249 , pp. 163-167
    • Puustinen, A.1    Finel, M.2    Virkki, M.3    Wikström, M.4
  • 16
    • 0026755167 scopus 로고
    • PH Dependence of proton translocation by Escherichia coll
    • Verkhovskaya M, Verkhovsky M, Wikström M: pH Dependence of proton translocation by Escherichia coll. J Biol Chem 267: 14559-14562, 1992
    • (1992) J Biol Chem , vol.267 , pp. 14559-14562
    • Verkhovskaya, M.1    Verkhovsky, M.2    Wikström, M.3
  • 17
    • 0026006133 scopus 로고
    • A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA)
    • Dassa J, Fsihi H, Marck C, Dion M, Kieffer-Bontemps M, Boquet PL: A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA). Mol Gen Genet 229: 341-352, 1991
    • (1991) Mol Gen Genet , vol.229 , pp. 341-352
    • Dassa, J.1    Fsihi, H.2    Marck, C.3    Dion, M.4    Kieffer-Bontemps, M.5    Boquet, P.L.6
  • 20
    • 0028606480 scopus 로고
    • The relationship between electron flux and the redox poise of the quinone pool in plant mitochondria
    • Van den Bergen CWM, Wagner AM, Krab K, Moore AL: The relationship between electron flux and the redox poise of the quinone pool in plant mitochondria. Fur J Biochem 226: 1071-1078, 1994
    • (1994) Fur J Biochem , vol.226 , pp. 1071-1078
    • Van Den Bergen, C.W.M.1    Wagner, A.M.2    Krab, K.3    Moore, A.L.4
  • 21
    • 0028598697 scopus 로고
    • The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen
    • Ribas-Carbo M, Berry JA, Azcon-Bieto J, Siedow JN: The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen. Biochim Biophys Acta 1188: 205-212, 1994
    • (1994) Biochim Biophys Acta , vol.1188 , pp. 205-212
    • Ribas-Carbo, M.1    Berry, J.A.2    Azcon-Bieto, J.3    Siedow, J.N.4
  • 23
    • 0022802381 scopus 로고
    • Redox linked proton translocation in cytochrome oxidase: The importance of gating electron flow
    • Blair DF, Gelles J, Chan SI: Redox linked proton translocation in cytochrome oxidase: the importance of gating electron flow. Biophys J 50: 713-733, 1986
    • (1986) Biophys J , vol.50 , pp. 713-733
    • Blair, D.F.1    Gelles, J.2    Chan, S.I.3
  • 24
    • 0028589402 scopus 로고
    • Mechanistic and phenomenological features of proton pumps in the respiratory chain of mitochondria
    • Papa S, Lorusso M, Capitanio N: Mechanistic and phenomenological features of proton pumps in the respiratory chain of mitochondria. J Bioenerg Biomemb 26: 609-618, 1994
    • (1994) J Bioenerg Biomemb , vol.26 , pp. 609-618
    • Papa, S.1    Lorusso, M.2    Capitanio, N.3
  • 25
    • 0026079023 scopus 로고
    • Flux ratios and pump stoichiometries at site-II and site-III in liver mitochondria - Effect of slips and leaks
    • Luvisetto S, Conti E, Buss M, Az zone GF: Flux ratios and pump stoichiometries at site-II and site-III in liver mitochondria - Effect of slips and leaks. J Biol Chem 266: 1034-1042, 1991
    • (1991) J Biol Chem , vol.266 , pp. 1034-1042
    • Luvisetto, S.1    Conti, E.2    Buss, M.3    Az Zone, G.F.4
  • 26
    • 0024417971 scopus 로고
    • The relative proton stoicheiometries of the mitochondrial proton pumps are independent on the proton motive force
    • Brown GC: The relative proton stoicheiometries of the mitochondrial proton pumps are independent on the proton motive force. J Biol Chem 264: 14704-14709, 1989
    • (1989) J Biol Chem , vol.264 , pp. 14704-14709
    • Brown, G.C.1
  • 28
    • 0025799527 scopus 로고
    • - stoichiometry of mitochondrial cytochrome complexes reconstituted in liposomes. Rate dependent changes of the stoichiometry in the cytochrome c oxidase vesicles
    • - stoichiometry of mitochondrial cytochrome complexes reconstituted in liposomes. Rate dependent changes of the stoichiometry in the cytochrome c oxidase vesicles. FEBS Lett 288: 179-182, 1991
    • (1991) FEBS Lett , vol.288 , pp. 179-182
    • Capitanio, N.1    Capitanio, G.2    De Nitto, E.3    Villani, G.4    Papa, S.5
  • 29
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock GT, Wikström MKF: Oxygen activation and the conservation of energy in cell respiration. Nature 356: 301-309, 1992
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.K.F.2
  • 31
    • 0020397137 scopus 로고
    • The effect of hyperoxia on superoxide production by lung submitochondrial particles
    • Turrens JF, Zeman BA, Levitt JG, Crapo JD: The effect of hyperoxia on superoxide production by lung submitochondrial particles. Arch Biochem Biophys 217: 401-110, 1982
    • (1982) Arch Biochem Biophys , vol.217 , pp. 401-1110
    • Turrens, J.F.1    Zeman, B.A.2    Levitt, J.G.3    Crapo, J.D.4
  • 33
    • 9444252661 scopus 로고
    • Studies of superoxide radical generation in the NADH:ubiquinone-reductase segment of the respiratory chain with the aid of a spin probe 2,2,6,6-tetramethyl-4-oxopiperidine-N-oxyl
    • Russ.
    • Ksenzenko MYu, Konstantinov AA, Khomutov GB, Ruuge EK: Studies of superoxide radical generation in the NADH:ubiquinone-reductase segment of the respiratory chain with the aid of a spin probe 2,2,6,6-tetramethyl-4-oxopiperidine-N-oxyl. Biol Membrany 6: 840-849 (Russ.), 1989
    • (1989) Biol Membrany , vol.6 , pp. 840-849
    • Ksenzenko, M.Yu.1    Konstantinov, A.A.2    Khomutov, G.B.3    Ruuge, E.K.4
  • 35
    • 0025756918 scopus 로고
    • Enzymatic mechanisms of superoxide production
    • Cross AR, Jones OTG: Enzymatic mechanisms of superoxide production. Biochim Biophys Acta 1057: 281-298, 1991
    • (1991) Biochim Biophys Acta , vol.1057 , pp. 281-298
    • Cross, A.R.1    Jones, O.T.G.2
  • 36
    • 0028453111 scopus 로고
    • Superoxide radical generation by the mitochondrial respiratory chain of isolated cardiomyocytes
    • Russ
    • Kashkarov KP, Vasilyeva EV, Ruuge EK: Superoxide radical generation by the mitochondrial respiratory chain of isolated cardiomyocytes. Biochemistry (Moscow) 59: 813-818 (Russ), 1994
    • (1994) Biochemistry (Moscow) , vol.59 , pp. 813-818
    • Kashkarov, Kp.1    Vasilyeva, E.V.2    Ruuge, E.K.3
  • 37
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey V: Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem 269: 22459-22462, 1994
    • (1994) J Biol Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 38
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH debydrogenase of bovine heart mitochondria
    • Turrens JS, Boveris A: Generation of superoxide anion by the NADH debydrogenase of bovine heart mitochondria. Biochem J 191: 421-427, 1980
    • (1980) Biochem J , vol.191 , pp. 421-427
    • Turrens, J.S.1    Boveris, A.2
  • 39
    • 0026689868 scopus 로고
    • Comparison of the effect of a mitochondrial uncoupler, 2,4-dinitrophenol and adrenaline on oxygen radical production in the isolated perfused rat liver
    • Okuda M, Lee H-C, Kumar C, Chance B: Comparison of the effect of a mitochondrial uncoupler, 2,4-dinitrophenol and adrenaline on oxygen radical production in the isolated perfused rat liver. Acta Physiol Scand 145: 159-168, 1992
    • (1992) Acta Physiol Scand , vol.145 , pp. 159-168
    • Okuda, M.1    Lee, H.-C.2    Kumar, C.3    Chance, B.4
  • 40
    • 0025349462 scopus 로고
    • Coupling site and rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles
    • Kotlyar AB, Sled VD, Burbaev DS, Moroz JA, Vinogradov AD: Coupling site and rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles. FEBS Lett 264: 17-20, 1990
    • (1990) FEBS Lett , vol.264 , pp. 17-20
    • Kotlyar, A.B.1    Sled, V.D.2    Burbaev, D.S.3    Moroz, J.A.4    Vinogradov, A.D.5
  • 43
    • 0028705369 scopus 로고
    • - concentration as a special function of respiratory systems of the cells
    • Russ
    • - concentration as a special function of respiratory systems of the cells. Biochemistry (Moscow) 59: 1910-1912 (Russ), 1994
    • (1994) Biochemistry (Moscow) , vol.59 , pp. 1910-1912
    • Skulachev, V.P.1
  • 44
    • 21844507143 scopus 로고
    • Non-phosphorylating respiration as a mechanism to minimize formation of reactive oxygen species in the cell
    • Russ
    • Skulachev VP: Non-phosphorylating respiration as a mechanism to minimize formation of reactive oxygen species in the cell. Mol Biologiya 29: 709-715 (Russ), 1995
    • (1995) Mol Biologiya , vol.29 , pp. 709-715
    • Skulachev, V.P.1
  • 45
    • 9444280512 scopus 로고
    • The role of nonphosphorylating respiration in minimizing formation of reactive oxygen species
    • Skulachev VP: The role of nonphosphorylating respiration in minimizing formation of reactive oxygen species. J Mol Med 73: B55, 1995
    • (1995) J Mol Med , vol.73
    • Skulachev, V.P.1
  • 46
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev VP: Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Quart Rev Biophys 29: 169-202, 1996
    • (1996) Quart Rev Biophys , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 47
    • 9444221181 scopus 로고
    • The contribution of mitochondrial proton leak to basal metabolic rate in the rat
    • Rolfe DES, Brand MD: The contribution of mitochondrial proton leak to basal metabolic rate in the rat. 8th Europ Bioenerg Conf Abstr (Valencia), 1994, p 101
    • (1994) 8th Europ Bioenerg Conf Abstr (Valencia) , pp. 101
    • Rolfe, D.E.S.1    Brand, M.D.2
  • 48
    • 0016294206 scopus 로고
    • The influence of respiration and ATP hydrolysis on the proton-electrochemical gradient across the inner membrane of rat-liver mitochondria as determined by ion distribution
    • Nicholls DG: The influence of respiration and ATP hydrolysis on the proton-electrochemical gradient across the inner membrane of rat-liver mitochondria as determined by ion distribution. Eur J Biochem 50: 305-315, 1974
    • (1974) Eur J Biochem , vol.50 , pp. 305-315
    • Nicholls, D.G.1
  • 49
    • 0024422115 scopus 로고
    • Slip and leak in mitochondrial oxidative phosphorylation
    • Murphy MP: Slip and leak in mitochondrial oxidative phosphorylation. Biochim Biophys Acta 977: 123-141, 1989
    • (1989) Biochim Biophys Acta , vol.977 , pp. 123-141
    • Murphy, M.P.1
  • 50
    • 0027260708 scopus 로고
    • Thyroid hormone action on mitochondrial energy transfer
    • Soboll S: Thyroid hormone action on mitochondrial energy transfer. Biochim Biophys Acta 1144: 1-16, 1993
    • (1993) Biochim Biophys Acta , vol.1144 , pp. 1-16
    • Soboll, S.1
  • 51
    • 0027227273 scopus 로고
    • The quantitative contributions of mitochondrial proton leak and ATP turnover reactions to the changed respiration rates of hepatocytes from rats of different thyroid status
    • Harper M-E, Brand MD: The quantitative contributions of mitochondrial proton leak and ATP turnover reactions to the changed respiration rates of hepatocytes from rats of different thyroid status. J Biol Chem 268: 14850-14860, 1993
    • (1993) J Biol Chem , vol.268 , pp. 14850-14860
    • Harper, M.-E.1    Brand, M.D.2
  • 53
    • 0024334620 scopus 로고
    • Rapid stimulation of hepatic oxygen consumption by 3,5-iodo-L-thyronine
    • Horst C, Rokos H, Seitz HJ: Rapid stimulation of hepatic oxygen consumption by 3,5-iodo-L-thyronine. Biochem J 261: 945-950, 1989
    • (1989) Biochem J , vol.261 , pp. 945-950
    • Horst, C.1    Rokos, H.2    Seitz, H.J.3
  • 54
    • 0025369214 scopus 로고
    • The proton leak across the mitochondrial inner membrane
    • Brand MD: The proton leak across the mitochondrial inner membrane. Biochim Biophys Acta 1018: 128-133, 1990
    • (1990) Biochim Biophys Acta , vol.1018 , pp. 128-133
    • Brand, M.D.1
  • 56
    • 0027395439 scopus 로고
    • Effect of 3,3′-di-iodothyronine and 3,5-di-iodothyronine on rat liver mitochondria
    • Lanni A, Moreno M, Cioffi M, Goglia F: Effect of 3,3′-di-iodothyronine and 3,5-di-iodothyronine on rat liver mitochondria. J Endocrynol 136: 59-64, 1993
    • (1993) J Endocrynol , vol.136 , pp. 59-64
    • Lanni, A.1    Moreno, M.2    Cioffi, M.3    Goglia, F.4
  • 58
    • 0022597123 scopus 로고
    • Direct thyroid hormone activation of mitochondria: The role of adenine nucleotide translocase
    • Sterling K: Direct thyroid hormone activation of mitochondria: the role of adenine nucleotide translocase. Endocrinology 119: 292-295, 1986
    • (1986) Endocrinology , vol.119 , pp. 292-295
    • Sterling, K.1
  • 59
    • 0023481760 scopus 로고
    • Direct thyroid hormone activation of mitochondria: Identification of adenine nucleotide translocase (AdNT) as the hormone receptor
    • Sterling K: Direct thyroid hormone activation of mitochondria: identification of adenine nucleotide translocase (AdNT) as the hormone receptor. Transact Ass Am Physicians 100: 284-293, 1987
    • (1987) Transact Ass Am Physicians , vol.100 , pp. 284-293
    • Sterling, K.1
  • 60
    • 0026291509 scopus 로고
    • Thyroid hormone action: Identification of the mitochondrial thyroid hormone receptor as adenine nucleotide translocase
    • Sterling K: Thyroid hormone action: identification of the mitochondrial thyroid hormone receptor as adenine nucleotide translocase. Thyroid 1: 167-171, 1991
    • (1991) Thyroid , vol.1 , pp. 167-171
    • Sterling, K.1
  • 61
    • 0024357458 scopus 로고
    • Thyroid hormone effect on rat heart mitochondrial proteins and affinity labelling with N-bromoacetyl-3,3′,5-triiodo-L-thyronine. Lack of direct effect on the adenine nucleotide translocase
    • Rasmussen UB, Kohrle J, Rokos H, Hesch R-D: Thyroid hormone effect on rat heart mitochondrial proteins and affinity labelling with N-bromoacetyl-3,3′,5-triiodo-L-thyronine. Lack of direct effect on the adenine nucleotide translocase. FEBS Lett 255: 385-390, 1989
    • (1989) FEBS Lett , vol.255 , pp. 385-390
    • Rasmussen, U.B.1    Kohrle, J.2    Rokos, H.3    Hesch, R.-D.4
  • 62
    • 0026693011 scopus 로고
    • The mechanism of the increase in mitochondrial proton permeability induced by thyroid hormones
    • Brand MD, Steverding D, Kadenbach B, Stevenson PM, Hafner RP: The mechanism of the increase in mitochondrial proton permeability induced by thyroid hormones. Eur J Biochem 296: 775-781, 1992
    • (1992) Eur J Biochem , vol.296 , pp. 775-781
    • Brand, M.D.1    Steverding, D.2    Kadenbach, B.3    Stevenson, P.M.4    Hafner, R.P.5
  • 63
    • 0016592885 scopus 로고
    • Some biochemical and physicochemical properties of the potent uncoupler SF 6847 (3,5-ditert-butyl-4-hydroxy-benzylidene-malononitrile)
    • Terada H: Some biochemical and physicochemical properties of the potent uncoupler SF 6847 (3,5-ditert-butyl-4-hydroxy-benzylidene-malononitrile). Biochim Biophys Acta 387: 519-532, 1975
    • (1975) Biochim Biophys Acta , vol.387 , pp. 519-532
    • Terada, H.1
  • 64
    • 0020033137 scopus 로고
    • The interaction of highly active uncouplers with mitochondria
    • Terada H: The interaction of highly active uncouplers with mitochondria. Biochim Biophys Acta 639: 225-242, 1981
    • (1981) Biochim Biophys Acta , vol.639 , pp. 225-242
    • Terada, H.1
  • 65
    • 0024299837 scopus 로고
    • Unique action of a modified weakly acidic uncoupler without an acidic group, methylated SF 6847, as an inhibitor of oxidative phosphorylation with no uncoupling activity: Possible identity of uncoupler binding protein
    • Terada H, Fukui Y, Shinohara Y, Ju-chi M: Unique action of a modified weakly acidic uncoupler without an acidic group, methylated SF 6847, as an inhibitor of oxidative phosphorylation with no uncoupling activity: possible identity of uncoupler binding protein. Biochim Biophys Acta 933: 193-199, 1988
    • (1988) Biochim Biophys Acta , vol.933 , pp. 193-199
    • Terada, H.1    Fukui, Y.2    Shinohara, Y.3    Ju-chi, M.4
  • 66
    • 0026755197 scopus 로고
    • Mechanism of loss of thermodynamic control in mitochondria due to hyperthyroidism and temperature
    • Luvisetto S, Schmehl I, Intravaia E, Conti E, Azzone GF: Mechanism of loss of thermodynamic control in mitochondria due to hyperthyroidism and temperature. J Biol Chem 267: 15348-15355, 1992
    • (1992) J Biol Chem , vol.267 , pp. 15348-15355
    • Luvisetto, S.1    Schmehl, I.2    Intravaia, E.3    Conti, E.4    Azzone, G.F.5
  • 68
    • 0010634594 scopus 로고
    • Quantitative analyses of uncoupling activity of SF6846 (2,6-di-t-butyl-4-(2,2-dicyanovinyl)phenol) and its analogs with spinach chloroplasts
    • Miyoshi H, Fujita T: Quantitative analyses of uncoupling activity of SF6846 (2,6-di-t-butyl-4-(2,2-dicyanovinyl)phenol) and its analogs with spinach chloroplasts. Biochim Biophys Acta 894: 339-345, 1987
    • (1987) Biochim Biophys Acta , vol.894 , pp. 339-345
    • Miyoshi, H.1    Fujita, T.2
  • 69
    • 0028099867 scopus 로고
    • 6-Ketocholestanol abolishes the effect of the most potent uncouplers of oxidative phosphorylation in mitochondria
    • Starkov AA, Dedukhova VI, Skulachev VP: 6-Ketocholestanol abolishes the effect of the most potent uncouplers of oxidative phosphorylation in mitochondria. FEBS Lett 355: 305-308, 1994
    • (1994) FEBS Lett , vol.355 , pp. 305-308
    • Starkov, A.A.1    Dedukhova, V.I.2    Skulachev, V.P.3
  • 70
    • 0027333450 scopus 로고
    • A 3D model of the peripheral benzodiazepine receptor and its implication in intramitochondrial cholesterol transport
    • Bernassau JM, Reversat JL, Ferrara P, Caput D, Lefur G: A 3D model of the peripheral benzodiazepine receptor and its implication in intramitochondrial cholesterol transport. J Mol Graphics 11: 236-244, 1993
    • (1993) J Mol Graphics , vol.11 , pp. 236-244
    • Bernassau, J.M.1    Reversat, J.L.2    Ferrara, P.3    Caput, D.4    Lefur, G.5
  • 71
    • 0021299462 scopus 로고
    • Cellular organization for steroidogenesis
    • Hall PF: Cellular organization for steroidogenesis. Int Rev Cytology 86: 53-95, 1984
    • (1984) Int Rev Cytology , vol.86 , pp. 53-95
    • Hall, P.F.1
  • 72
    • 0023746681 scopus 로고
    • The regulation of intracellular transport of cholesterol in bovine adrenal cells: Purification of a novel protein
    • Yanagibashi K, Ohno Y, Kazwamura M, Hall PF: The regulation of intracellular transport of cholesterol in bovine adrenal cells: purification of a novel protein. Endocrinology 123: 2075-2082, 1988
    • (1988) Endocrinology , vol.123 , pp. 2075-2082
    • Yanagibashi, K.1    Ohno, Y.2    Kazwamura, M.3    Hall, P.F.4
  • 73
    • 0029569091 scopus 로고
    • Molecular and functional properties of mitochondrial benzodiazepine receptors
    • Krueger KE: Molecular and functional properties of mitochondrial benzodiazepine receptors. Biochim. Biophys. Acta 1241:453-470, 1995
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 453-470
    • Krueger, K.E.1
  • 74
    • 0027973404 scopus 로고
    • Altered peripheral benzodiazepine receptor binding in cardiac and liver tissues from thyroidectomized rats
    • Kragie L, Smiehorowski R: Altered peripheral benzodiazepine receptor binding in cardiac and liver tissues from thyroidectomized rats. Life Sci 55: 1911-1918, 1994
    • (1994) Life Sci , vol.55 , pp. 1911-1918
    • Kragie, L.1    Smiehorowski, R.2
  • 75
    • 0028095807 scopus 로고
    • Mitochondrial calcium transport: Physiological and pathological relevance
    • Gunter TE, Gunter KK, Sheu S-S, Gavin CE: Mitochondrial calcium transport: physiological and pathological relevance. Am J Physiol 267: C313-C339, 1994
    • (1994) Am J Physiol , vol.267
    • Gunter, T.E.1    Gunter, K.K.2    Sheu, S.-S.3    Gavin, C.E.4
  • 76
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
    • Bernardi P, Broekemeier KM, Pfeiffer DR: Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane. J Bioenerg Biomembr 26: 509-517, 1994
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekemeier, K.M.2    Pfeiffer, D.R.3
  • 77
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M, Szabo I: The mitochondrial permeability transition. Biochim Biophys Acta 1241: 139-176, 1995
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 78
    • 0018306632 scopus 로고
    • Hydroperoxides can modulate the redox state of pyridine nucleotides and the calcium balance in rat liver mitochondria
    • Lotscher HR, Winterhalter KH, Carafoli E, Richter C: Hydroperoxides can modulate the redox state of pyridine nucleotides and the calcium balance in rat liver mitochondria. Proc Nat Acad Sci USA 76: 4340-4344, 1979
    • (1979) Proc Nat Acad Sci USA , vol.76 , pp. 4340-4344
    • Lotscher, H.R.1    Winterhalter, K.H.2    Carafoli, E.3    Richter, C.4
  • 79
    • 0023726162 scopus 로고
    • Permeability of inner mitochondrial membrane and oxidative stress
    • Carbonera D, Azzone GF: Permeability of inner mitochondrial membrane and oxidative stress. Biochim Biophys Acta 943: 245-255, 1988
    • (1988) Biochim Biophys Acta , vol.943 , pp. 245-255
    • Carbonera, D.1    Azzone, G.F.2
  • 81
    • 0025964021 scopus 로고
    • 2+-induced permeabilization of rat liver mitochondria
    • 2+-induced permeabilization of rat liver mitochondria. FEBS Lett 279: 45-48, 1991
    • (1991) FEBS Lett , vol.279 , pp. 45-48
    • Eriksson, O.1
  • 82
    • 0025959239 scopus 로고
    • 2+: An alternative mechanism for the cardiotoxicity of doxorubicin
    • 2+: an alternative mechanism for the cardiotoxicity of doxorubicin. Toxicol Appl Pharmacol 107: 117-128, 1991
    • (1991) Toxicol Appl Pharmacol , vol.107 , pp. 117-128
    • Chacon, E.1    Acosta, D.2
  • 83
    • 0026644609 scopus 로고
    • Production of reactive oxygen by mitochondria from normoxic and hypoxic rat heart tissue
    • Paraidathathu T, DeGroot H, Kehrer JP: Production of reactive oxygen by mitochondria from normoxic and hypoxic rat heart tissue. Free Rad Biol Med 13: 289-297, 1992
    • (1992) Free Rad Biol Med , vol.13 , pp. 289-297
    • Paraidathathu, T.1    Degroot, H.2    Kehrer, J.P.3
  • 84
    • 0026801183 scopus 로고
    • Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient
    • Bernardi P: Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. J Biol Chem 267: 8834-8839, 1992
    • (1992) J Biol Chem , vol.267 , pp. 8834-8839
    • Bernardi, P.1
  • 85
    • 0028239794 scopus 로고
    • The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents
    • Petronilli V, Costantini P, Scorrano E, Colonna R, Passamonti S, Bernardi P: The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents. J Biol Chem 269: 16638-16642, 1994
    • (1994) J Biol Chem , vol.269 , pp. 16638-16642
    • Petronilli, V.1    Costantini, P.2    Scorrano, E.3    Colonna, R.4    Passamonti, S.5    Bernardi, P.6
  • 87
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner PR , Raineri I, Epstein LB, White CW: Superoxide radical and iron modulate aconitase activity in mammalian cells. J Biol Chem 270: 13399-13405, 1995
    • (1995) J Biol Chem , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 88
    • 0027141376 scopus 로고
    • Aconitase, a two-faced protein: Enzyme and iron regulatory factor
    • Beinert H, Kennedy MC: Aconitase, a two-faced protein: enzyme and iron regulatory factor. FASEB J 7: 1442-1449, 1993
    • (1993) FASEB J , vol.7 , pp. 1442-1449
    • Beinert, H.1    Kennedy, M.C.2
  • 92
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery DM, Nunez G, Milliman CT, Schreiber RD, Korsmeyer SJ: Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348: 334-336, 1990
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.M.1    Nunez, G.2    Milliman, C.T.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 96
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the Bcl-2 oncoprotein residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC: Investigation of the subcellular distribution of the Bcl-2 oncoprotein residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res 53: 4701-4714, 1993
    • (1993) Cancer Res , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 98
    • 0028019746 scopus 로고
    • Cell-free apoptosis in Xenopus egg extracts: Inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria
    • Newmeyer DD, Forschon DM, Reed JC: Cell-free apoptosis in Xenopus egg extracts: inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria. Cell 79: 353-364, 1994
    • (1994) Cell , vol.79 , pp. 353-364
    • Newmeyer, D.D.1    Forschon, D.M.2    Reed, J.C.3
  • 99
    • 0346931602 scopus 로고
    • Oxidative stress and apoptosis
    • RG Cutler, L Packer, J Bertram, A Mori (eds). Birkhauser Verlag, Basel
    • Slater AFG, Orrenius S: Oxidative stress and apoptosis. In: RG Cutler, L Packer, J Bertram, A Mori (eds). Oxidative Stress and Aging. Birkhauser Verlag, Basel, 1995, pp 21-25
    • (1995) Oxidative Stress and Aging , pp. 21-25
    • Slater, A.F.G.1    Orrenius, S.2
  • 100
    • 0029036412 scopus 로고
    • Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis
    • Petit PX, Lecoeur H, Zorn E, Dauguet C, Mignotte B, Gougeon ML: Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis. J Cell Biol 130: 157-167, 1995
    • (1995) J Cell Biol , vol.130 , pp. 157-167
    • Petit, P.X.1    Lecoeur, H.2    Zorn, E.3    Dauguet, C.4    Mignotte, B.5    Gougeon, M.L.6
  • 103
    • 0028933889 scopus 로고
    • Oxygen stress induces an apoptotic cell death associated with fragmentation of mitochondrial genome
    • Yoneda M, Katsumata K, Hayakawa M, Tanaka M, Ozawa T: Oxygen stress induces an apoptotic cell death associated with fragmentation of mitochondrial genome. Biochim Biophys Res Commun 209: 723-729, 1995
    • (1995) Biochim Biophys Res Commun , vol.209 , pp. 723-729
    • Yoneda, M.1    Katsumata, K.2    Hayakawa, M.3    Tanaka, M.4    Ozawa, T.5
  • 104
    • 0029983059 scopus 로고    scopus 로고
    • Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis
    • Zamzami N, Marchetti P, Castedo M, Hirsch T, Susin S, Masse B, Kroemer G: Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis. FEBS Lett 384: 53-57, 1996
    • (1996) FEBS Lett , vol.384 , pp. 53-57
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Hirsch, T.4    Susin, S.5    Masse, B.6    Kroemer, G.7
  • 108
    • 0027292241 scopus 로고
    • Rapid accumulation of deleted mitochondrial deoxyribonucleic acid in postmenopausal ovaries
    • Kitagawa T, Suganuma N, Nawa A, Kikkava F, Tanaka M, Ozawa T, Tomoda Y: Rapid accumulation of deleted mitochondrial deoxyribonucleic acid in postmenopausal ovaries. Biol Reprod 49: 730-736, 1993
    • (1993) Biol Reprod , vol.49 , pp. 730-736
    • Kitagawa, T.1    Suganuma, N.2    Nawa, A.3    Kikkava, F.4    Tanaka, M.5    Ozawa, T.6    Tomoda, Y.7
  • 109
    • 0029002367 scopus 로고
    • The development of mitochondrial medicine
    • Luft R: The development of mitochondrial medicine. Biochim Biophys Acta 1271: 1-6, 1995
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 1-6
    • Luft, R.1
  • 111
    • 0026795635 scopus 로고
    • Protein oxidation and Aging
    • Stadtman ER: Protein oxidation and Aging. Science, 1220-1224, 1992
    • (1992) Science , pp. 1220-1224
    • Stadtman, E.R.1
  • 114
    • 0028109380 scopus 로고
    • Correlation between mitochondrial DNA 4977-bp deletion and respiratory chain enzyme activities in aging human skeletal muscles
    • Lezza AMS, Boffoli D, Scacco S, Cantatore P, Gadaleta MN: Correlation between mitochondrial DNA 4977-bp deletion and respiratory chain enzyme activities in aging human skeletal muscles. Biochem Biophys Res Commun 205: 772-779, 1994
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 772-779
    • Lezza, A.M.S.1    Boffoli, D.2    Scacco, S.3    Cantatore, P.4    Gadaleta, M.N.5
  • 115
    • 9444257330 scopus 로고
    • The mitochondrial DNA injury theory of aging: Concepts and supporting facts
    • Glasgow
    • Miquel J: The mitochondrial DNA injury theory of aging: concepts and supporting facts. Abstr of Intern Symp Genetics of Death, Glasgow, 1995
    • (1995) Abstr of Intern Symp Genetics of Death
    • Miquel, J.1
  • 116
    • 0007007923 scopus 로고
    • Mitochondria, free radicals, neurodegeneration and aging
    • RG Cutler, L Packer, J Bertram, A Mori (eds). Birkhauser Verlag, Basel
    • Schapira AHV: Mitochondria, free radicals, neurodegeneration and aging. In: RG Cutler, L Packer, J Bertram, A Mori (eds). Oxidative Stress and Aging. Birkhauser Verlag, Basel, 1995, pp 159-169
    • (1995) Oxidative Stress and Aging , pp. 159-169
    • Schapira, A.H.V.1
  • 117
    • 0029071519 scopus 로고
    • Protective roles of cytokines against radiation: Induction of mitochondrial MnSOD
    • Wong GHW: Protective roles of cytokines against radiation: induction of mitochondrial MnSOD. Biochim Biophys Acta 1271: 205-209, 1995
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 205-209
    • Wong, G.H.W.1
  • 118
    • 0029029471 scopus 로고
    • Modelling the effects of age-related mtDNA mutation accumulation; complex I deficiency, superoxide and cell death
    • Cortopassi G, Wang E: Modelling the effects of age-related mtDNA mutation accumulation; complex I deficiency, superoxide and cell death. Biochim Biophys Acta 1271: 171-176, 1995
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 171-176
    • Cortopassi, G.1    Wang, E.2
  • 119
    • 0027426263 scopus 로고
    • Absence of electron transport (Rho° State) restores growth of a manganese - Superoxide dismutase - deficient Saccharomyces cerevisiae in hyperoxia
    • Guidot DM, McCord JM, Wright RM, Repine JE: Absence of electron transport (Rho° State) restores growth of a manganese - superoxide dismutase - deficient Saccharomyces cerevisiae in hyperoxia. J Biol Chem 268: 26699-26703, 1993
    • (1993) J Biol Chem , vol.268 , pp. 26699-26703
    • Guidot, D.M.1    McCord, J.M.2    Wright, R.M.3    Repine, J.E.4
  • 121
    • 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
  • 123
    • 0029039854 scopus 로고
    • Simultaneous overexpression of copper- And zinc-containing superoxide dismutase and catalase retards age-related oxidative damage and increases metabolic potential in Drosophila melanogaster
    • Sohal RS, Agarwal A, Agarwal S, Orr WC: Simultaneous overexpression of copper- and zinc-containing superoxide dismutase and catalase retards age-related oxidative damage and increases metabolic potential in Drosophila melanogaster. J Biol Chem 270: 15671-15674, 1995
    • (1995) J Biol Chem , vol.270 , pp. 15671-15674
    • Sohal, R.S.1    Agarwal, A.2    Agarwal, S.3    Orr, W.C.4
  • 124
    • 0027534583 scopus 로고
    • Modulation of membrane phospholipid fatty acid composition by age and food restriction
    • Laganiere S, Yu BP: Modulation of membrane phospholipid fatty acid composition by age and food restriction. Gerontology 39: 7-18, 1993
    • (1993) Gerontology , vol.39 , pp. 7-18
    • Laganiere, S.1    Yu, B.P.2
  • 125
    • 0019317502 scopus 로고
    • Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation
    • Robinson NC, Strey F, Talbert L: Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation. Biochemistry 19: 3656-3661, 1980
    • (1980) Biochemistry , vol.19 , pp. 3656-3661
    • Robinson, N.C.1    Strey, F.2    Talbert, L.3
  • 126
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • Hoch FL: Cardiolipins and biomembrane function. Biochim Biophys Acta 1113, 71-133, 1992
    • (1992) Biochim Biophys Acta , vol.1113 , pp. 71-133
    • Hoch, F.L.1
  • 127
    • 0024558293 scopus 로고
    • Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria
    • Krämer R, Palmieri F: Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria. Biochim Biophys Acta 974: 1-23, 1989
    • (1989) Biochim Biophys Acta , vol.974 , pp. 1-23
    • Krämer, R.1    Palmieri, F.2
  • 128
    • 0027302325 scopus 로고
    • Conformational changes in oxidized phospholipids and their preferential hydrolysis by phospholipase A2: A monolayer study
    • van den Bergh JJm, Op den Kamp JA, Lubin BH, Kuypers FA: Conformational changes in oxidized phospholipids and their preferential hydrolysis by phospholipase A2: a monolayer study. Biochemistry 32: 4962-4967, 1993
    • (1993) Biochemistry , vol.32 , pp. 4962-4967
    • Van Den Bergh, J.Jm.1    Op Den Kamp, J.A.2    Lubin, B.H.3    Kuypers, F.A.4
  • 129
    • 0027214754 scopus 로고
    • Rat liver mitochondrial phospholipase A2 is an endotoxin-stimulated membrane-associated enzyme of Kupifer cells which is released during liver perfusion
    • Hatch GM, Vance DE, Wilton DC: Rat liver mitochondrial phospholipase A2 is an endotoxin-stimulated membrane-associated enzyme of Kupifer cells which is released during liver perfusion. Biochem J 293: 143-150, 1993
    • (1993) Biochem J , vol.293 , pp. 143-150
    • Hatch, G.M.1    Vance, D.E.2    Wilton, D.C.3
  • 134
    • 0030581498 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications
    • Papa S: Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications. Biochim Biophys Acta 1276: 87-105, 1996
    • (1996) Biochim Biophys Acta , vol.1276 , pp. 87-105
    • Papa, S.1
  • 135
    • 0016413018 scopus 로고
    • The effect of age on mitochondrial ultrastructure and enzymes
    • Wilson PD, Franks LM: The effect of age on mitochondrial ultrastructure and enzymes. Adv Exp Med Biol 53: 171-183, 1975
    • (1975) Adv Exp Med Biol , vol.53 , pp. 171-183
    • Wilson, P.D.1    Franks, L.M.2
  • 136
    • 0018083874 scopus 로고
    • Evidence for increased degeneration of mito-chondria in old rats. A brief note
    • Murfitt RR, Sanadi DR: Evidence for increased degeneration of mito-chondria in old rats. A brief note. Mech Ageing Dev 8: 197-291, 1978
    • (1978) Mech Ageing Dev , vol.8 , pp. 197-291
    • Murfitt, R.R.1    Sanadi, D.R.2
  • 137
  • 141
    • 0026624980 scopus 로고
    • Mitochondrial DNA diseases
    • Wallace DC: Mitochondrial DNA diseases. Ann Rev Biochem 61: 1175-1212, 1992
    • (1992) Ann Rev Biochem , vol.61 , pp. 1175-1212
    • Wallace, D.C.1
  • 142
    • 0022555846 scopus 로고
    • Genetics of mitochondrial biogenesis
    • Tzagoloff A, Myers AM: Genetics of mitochondrial biogenesis. Annul Rev Biochem 55: 249-285, 1986
    • (1986) Annul Rev Biochem , vol.55 , pp. 249-285
    • Tzagoloff, A.1    Myers, A.M.2
  • 146
    • 0025674177 scopus 로고
    • Detection of a specific mitochondrial DNA deletion in tissues of older humans
    • Cortopassi GA, Arnheim N: Detection of a specific mitochondrial DNA deletion in tissues of older humans. Nucl Acids Res 18: 6927-6933, 1990
    • (1990) Nucl Acids Res , vol.18 , pp. 6927-6933
    • Cortopassi, G.A.1    Arnheim, N.2
  • 147
    • 0002951288 scopus 로고
    • S Papa, JM Tager (eds). Birkhauser, Basel
    • Ozawa T: In Biochemistry of Cell Membranes. S Papa, JM Tager (eds). Birkhauser, Basel, 1995, pp 339-361
    • (1995) Biochemistry of Cell Membranes , pp. 339-361
    • Ozawa, T.1
  • 149
    • 0026732706 scopus 로고
    • A pattern of accumulation of a somatic deletion of mitochondrial DNA in aging human tissues
    • Cortopassi GA, Shibata D, Soong NW, Arnheim N: A pattern of accumulation of a somatic deletion of mitochondrial DNA in aging human tissues. Proc Natl Acad Sci USA 89: 7370-7374, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7370-7374
    • Cortopassi, G.A.1    Shibata, D.2    Soong, N.W.3    Arnheim, N.4
  • 150
    • 0025836655 scopus 로고
    • Introduction of disease-related mitochondrial DNA deletions into HeLa cells lacking mitochondrial DNA results in mitochondrial dysfunction
    • Hayashi JI, Ohta S, Kikuchi A, Takemitsu M, Goto YI, Nonaka I: Introduction of disease-related mitochondrial DNA deletions into HeLa cells lacking mitochondrial DNA results in mitochondrial dysfunction. Proc Natl Acad Sci USA 88: 10614-10618, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10614-10618
    • Hayashi, J.I.1    Ohta, S.2    Kikuchi, A.3    Takemitsu, M.4    Goto, Y.I.5    Nonaka, I.6
  • 151
    • 0026608057 scopus 로고
    • MELAS mutation in mtDNA binding site for transcription termination factor causes defects in protein synthesis and in respiration but no change in levels of upstream and downstream mature transcripts
    • Chomyn AA, Martinuzzi A, Yoneda M, Gada A, Hurko O, Johns D, Lai ST, Nonaka I, Angelini C, Attardi G: MELAS mutation in mtDNA binding site for transcription termination factor causes defects in protein synthesis and in respiration but no change in levels of upstream and downstream mature transcripts. Proc Natl Acad Sci USA 89: 4221-4225, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4221-4225
    • Chomyn, A.A.1    Martinuzzi, A.2    Yoneda, M.3    Gada, A.4    Hurko, O.5    Johns, D.6    Lai, S.T.7    Nonaka, I.8    Angelini, C.9    Attardi, G.10
  • 153
    • 0028176651 scopus 로고
    • Oxidative stress as a mediator of apoptosis
    • Butthe TM, Sandstrom PA: Oxidative stress as a mediator of apoptosis. Immunol Today 15: 7-10, 1994
    • (1994) Immunol Today , vol.15 , pp. 7-10
    • Butthe, T.M.1    Sandstrom, P.A.2
  • 154
    • 0025732732 scopus 로고
    • Dose-dependent induction of apoptosis in human tumour cell lines by widely diverging stimuli
    • Lennon SV, Martin SJ, Cotter TG: Dose-dependent induction of apoptosis in human tumour cell lines by widely diverging stimuli. Cell Prolif 24: 203-204, 1991
    • (1991) Cell Prolif , vol.24 , pp. 203-204
    • Lennon, S.V.1    Martin, S.J.2    Cotter, T.G.3
  • 155
    • 0027525966 scopus 로고
    • Different in situ hybridization patterns of mitochondrial DNA in cytocrome c oxidase-deficient extraocular muscle fibers in the elderly
    • Müller-Hocker J, Seibel P, Schneiderbanger K, Kadenbach B: Different in situ hybridization patterns of mitochondrial DNA in cytocrome c oxidase-deficient extraocular muscle fibers in the elderly. Virchows Archiv A Pathol Anat 422: 7-15, 1993
    • (1993) Virchows Archiv A Pathol Anat , vol.422 , pp. 7-15
    • Müller-Hocker, J.1    Seibel, P.2    Schneiderbanger, K.3    Kadenbach, B.4
  • 156
    • 0028216544 scopus 로고
    • Nuclear but not mitochondrial genome involvement in human age-related mitochondrial dysfunction. Functional integrity of mitochondrial DNA from aged subjects
    • Hayashi JI, Ohta S, Kagawa Kondi H, Kaneda H, Yonekawa H, Takai D, Miyabayashi S: Nuclear but not mitochondrial genome involvement in human age-related mitochondrial dysfunction. Functional integrity of mitochondrial DNA from aged subjects. J Biol Chem 269: 6878-6883, 1994
    • (1994) J Biol Chem , vol.269 , pp. 6878-6883
    • Hayashi, J.I.1    Ohta, S.2    Kagawa Kondi, H.3    Kaneda, H.4    Yonekawa, H.5    Takai, D.6    Miyabayashi, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.