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Volumn 44, Issue 3 SUPPL. 1, 1998, Pages

Mitochondrial dysfunction in Parkinson's disease

Author keywords

[No Author keywords available]

Indexed keywords

AUTOSOMAL RECESSIVE DISORDER; BRAIN MITOCHONDRION; CHROMOSOME 6Q; CONFERENCE PAPER; ENZYME DEFICIENCY; GENE LOCUS; HUMAN; MITOCHONDRIAL RESPIRATION; NERVE CELL NECROSIS; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL;

EID: 0031711713     PISSN: 03645134     EISSN: None     Source Type: Journal    
DOI: 10.1002/ana.410440715     Document Type: Conference Paper
Times cited : (152)

References (107)
  • 1
    • 0011205743 scopus 로고
    • Mitochondrial production of superoxide radical and hydrogen peroxide
    • Boveris A. Mitochondrial production of superoxide radical and hydrogen peroxide. Adv Exp Biol Med 1977;10:161-169
    • (1977) Adv Exp Biol Med , vol.10 , pp. 161-169
    • Boveris, A.1
  • 2
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase of respiratory chains
    • Walker JE. The NADH:ubiquinone oxidoreductase of respiratory chains. Q Rev Biophys 1992;25:253-324
    • (1992) Q Rev Biophys , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 3
    • 0026487290 scopus 로고
    • Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria: Application of a novel strategy for sequencing proteins using the polymerase chain reaction
    • Walker JE, Arimendi JM, Dupuis A, et al. Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria: application of a novel strategy for sequencing proteins using the polymerase chain reaction. J Mol Biol 1992;226:1051-1072
    • (1992) J Mol Biol , vol.226 , pp. 1051-1072
    • Walker, J.E.1    Arimendi, J.M.2    Dupuis, A.3
  • 4
    • 0021810979 scopus 로고
    • Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
    • Nicklas WJ, Vyas I, Heikkila RE. Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. Life Sci 1985;36:2503-2508
    • (1985) Life Sci , vol.36 , pp. 2503-2508
    • Nicklas, W.J.1    Vyas, I.2    Heikkila, R.E.3
  • 5
    • 0022516015 scopus 로고
    • Inhibition of mitochondrial NADH dehydrogenase by pyridine derivatives and its possible relation to experimental and idiopathic parkinsonism
    • Ramsay RR, Salach JI, Dadgar J, Singer TP. Inhibition of mitochondrial NADH dehydrogenase by pyridine derivatives and its possible relation to experimental and idiopathic parkinsonism. Biochem Biophys Res Commun 1986;135:269-275
    • (1986) Biochem Biophys Res Commun , vol.135 , pp. 269-275
    • Ramsay, R.R.1    Salach, J.I.2    Dadgar, J.3    Singer, T.P.4
  • 6
    • 0023114219 scopus 로고
    • Inhibition of mitochondrial NADH-ubiquinone oxidoreductase activity by 1-methyl-4-phenylpyridinium ion
    • Mizuno Y, Saitoh T, Sone N. Inhibition of mitochondrial NADH-ubiquinone oxidoreductase activity by 1-methyl-4-phenylpyridinium ion. Biochem Biophys Res Commun 1987; 143:294-299
    • (1987) Biochem Biophys Res Commun , vol.143 , pp. 294-299
    • Mizuno, Y.1    Saitoh, T.2    Sone, N.3
  • 9
    • 0024330311 scopus 로고
    • Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease
    • Mizuno Y, Ohta S, Tanaka M, et al. Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease. Biochem Biophys Res Commun 1989;163:1450-1455
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 1450-1455
    • Mizuno, Y.1    Ohta, S.2    Tanaka, M.3
  • 10
    • 0025942723 scopus 로고
    • Immunohistochemical studies on complex I, II, III, and IV of mitochondria in Parkinson's disease
    • Hattori N, Tanaka M, Ozawa T, Mizuno Y. Immunohistochemical studies on complex I, II, III, and IV of mitochondria in Parkinson's disease. Ann Neurol 1991;30:563-571
    • (1991) Ann Neurol , vol.30 , pp. 563-571
    • Hattori, N.1    Tanaka, M.2    Ozawa, T.3    Mizuno, Y.4
  • 11
    • 0028316759 scopus 로고
    • Unaltered aconitase activity, but decreased complex I activity in substantia nigra pars compacta of patients with Parkinson's disease
    • Janetzky B, Hauck S, Youdim MBH, et al. Unaltered aconitase activity, but decreased complex I activity in substantia nigra pars compacta of patients with Parkinson's disease. Neurosci Lett 1994;169:126-128
    • (1994) Neurosci Lett , vol.169 , pp. 126-128
    • Janetzky, B.1    Hauck, S.2    Youdim, M.B.H.3
  • 15
    • 0027515694 scopus 로고
    • Mitochondrial respiratory chain activity in skeletal muscle from patients with Parkinson's disease
    • Cardellach F, Martí MJ, Fernández-Solá J, et al. Mitochondrial respiratory chain activity in skeletal muscle from patients with Parkinson's disease. Neurology 1993;43:2258-2262
    • (1993) Neurology , vol.43 , pp. 2258-2262
    • Cardellach, F.1    Martí, M.J.2    Fernández-Solá, J.3
  • 16
    • 0027971104 scopus 로고
    • Mitochondrial respiratory failure in skeletal muscle from patients with Parkinson's disease and multiple system atrophy
    • Blin O, Desnuelle C, Rascol O, et al. Mitochondrial respiratory failure in skeletal muscle from patients with Parkinson's disease and multiple system atrophy. J Neurol Sci 1994;125: 95-101
    • (1994) J Neurol Sci , vol.125 , pp. 95-101
    • Blin, O.1    Desnuelle, C.2    Rascol, O.3
  • 17
    • 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 1992; 115:333-342
    • (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
  • 19
    • 0027431450 scopus 로고
    • Respiratory chain and mitochondrial DNA in muscle and brain in Parkinson's disease patients
    • Didonato S, Zeviani M, Giovannini P, et al. Respiratory chain and mitochondrial DNA in muscle and brain in Parkinson's disease patients. Neurology 1993;43:2262-2268
    • (1993) Neurology , vol.43 , pp. 2262-2268
    • Didonato, S.1    Zeviani, M.2    Giovannini, P.3
  • 20
    • 0028106607 scopus 로고
    • Unaltered respiratory chain enzyme activity and mitochondrial DNA in skeletal muscle from patients with idiopathic Parkinson's syndrome
    • Reichmann H, Janetzky B, Bischof F, et al. Unaltered respiratory chain enzyme activity and mitochondrial DNA in skeletal muscle from patients with idiopathic Parkinson's syndrome. Eur Neurol 1994;34:263-267
    • (1994) Eur Neurol , vol.34 , pp. 263-267
    • Reichmann, H.1    Janetzky, B.2    Bischof, F.3
  • 21
    • 0029396976 scopus 로고
    • Generalized mitochondrial dysfunction in Parkinson's disease detected by magnetic resonance spectroscopy of muscle
    • Penn AMW, Roberts T, Hodder J, Allen PS, Shu G, Martin WRW. Generalized mitochondrial dysfunction in Parkinson's disease detected by magnetic resonance spectroscopy of muscle. Neurology 1995;45:2097-2099
    • (1995) Neurology , vol.45 , pp. 2097-2099
    • Penn, A.M.W.1    Roberts, T.2    Hodder, J.3    Allen, P.S.4    Shu, G.5    Martin, W.R.W.6
  • 22
    • 0024848034 scopus 로고
    • Abnormalities of the electron transport chain in idiopathic Parkinson's disease
    • Parker WD Jr, Boyson SJ, Parks JK. Abnormalities of the electron transport chain in idiopathic Parkinson's disease. Ann Neurol 1989;26:719-723
    • (1989) Ann Neurol , vol.26 , pp. 719-723
    • Parker Jr., W.D.1    Boyson, S.J.2    Parks, J.K.3
  • 23
    • 0026544129 scopus 로고
    • Mitochondrial complex I and II activities of lymphocytes and platelets in Parkinson's disease
    • Yoshino H, Nakagawa-Hattori Y, Kondo T, Mizuno Y. Mitochondrial complex I and II activities of lymphocytes and platelets in Parkinson's disease. J Neural Transm 1992;4: 27-34
    • (1992) J Neural Transm , vol.4 , pp. 27-34
    • Yoshino, H.1    Nakagawa-Hattori, Y.2    Kondo, T.3    Mizuno, Y.4
  • 24
    • 0027750939 scopus 로고
    • Electron transfer complexes I and IV of platelets are abnormal in Parkinson's disease but normal in Parkinson-plus syndromes
    • Benecke R, Strümper P, Weiss H. Electron transfer complexes I and IV of platelets are abnormal in Parkinson's disease but normal in Parkinson-plus syndromes. Brain 1993;116:1451-1463
    • (1993) Brain , vol.116 , pp. 1451-1463
    • Benecke, R.1    Strümper, P.2    Weiss, H.3
  • 25
    • 0029050583 scopus 로고
    • Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinson's disease
    • Haas RH, Nasirian F, Nakano K, et al. Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinson's disease. Ann Neurol 1995;37:714-722
    • (1995) Ann Neurol , vol.37 , pp. 714-722
    • Haas, R.H.1    Nasirian, F.2    Nakano, K.3
  • 27
    • 0031031845 scopus 로고    scopus 로고
    • Platelet mitochondrial respiratory chain function in Parkinson's disease
    • Blake CT, Spitz E, Leehey M, Hoffer BJ, Boyson SJ. Platelet mitochondrial respiratory chain function in Parkinson's disease. Mov Disord 1997;12:3-8
    • (1997) Mov Disord , vol.12 , pp. 3-8
    • Blake, C.T.1    Spitz, E.2    Leehey, M.3    Hoffer, B.J.4    Boyson, S.J.5
  • 28
    • 0027401575 scopus 로고
    • Respiratory chain enzyme activities in lymphocytes from untreated patients with Parkinson's disease
    • Barroso N, Campos Y, Huertas R, et al. Respiratory chain enzyme activities in lymphocytes from untreated patients with Parkinson's disease. Clin Chim Acta 1993;39:667-669
    • (1993) Clin Chim Acta , vol.39 , pp. 667-669
    • Barroso, N.1    Campos, Y.2    Huertas, R.3
  • 29
    • 0029932989 scopus 로고    scopus 로고
    • Respiratory-chain enzyme activities in isolated mitochondria of lymphocytes from untreated Parkinson's disease patients
    • Martin MA, Molina JA, Jimenez-Jimenez FJ, et al. Respiratory-chain enzyme activities in isolated mitochondria of lymphocytes from untreated Parkinson's disease patients. Neurology 1996;46:1343-1346
    • (1996) Neurology , vol.46 , pp. 1343-1346
    • Martin, M.A.1    Molina, J.A.2    Jimenez-Jimenez, F.J.3
  • 30
    • 0029065393 scopus 로고
    • Deficiencies of NADH and succinate dehydrogenases in degenerative disease and myopathies
    • Singer TP, Ramsay RR, Ackrell BA. Deficiencies of NADH and succinate dehydrogenases in degenerative disease and myopathies. Biochim Biophys Acta 1995;1271:211-219
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 211-219
    • Singer, T.P.1    Ramsay, R.R.2    Ackrell, B.A.3
  • 32
    • 0031017696 scopus 로고    scopus 로고
    • Altered calcium homeostasis in cells transformed by mitochondrial from individuals with Parkinson's disease
    • Sheehan JP, Sweardlow RH, Parkier WD, Miller SW, Davis RE, Tuttle JB. Altered calcium homeostasis in cells transformed by mitochondrial from individuals with Parkinson's disease. J Neurochem 1997;68:1221-1233
    • (1997) J Neurochem , vol.68 , pp. 1221-1233
    • Sheehan, J.P.1    Sweardlow, R.H.2    Parkier, W.D.3    Miller, S.W.4    Davis, R.E.5    Tuttle, J.B.6
  • 33
    • 0028176592 scopus 로고
    • An immunohistochemical study on α-ketoglutarate dehydrogenase complex in Parkinson's disease
    • Mizuno Y, Matuda S, Yoshino H, Mori H, Hattori N, Ikebe S. An immunohistochemical study on α-ketoglutarate dehydrogenase complex in Parkinson's disease. Ann Neurol 1994; 35:204-210
    • (1994) Ann Neurol , vol.35 , pp. 204-210
    • Mizuno, Y.1    Matuda, S.2    Yoshino, H.3    Mori, H.4    Hattori, N.5    Ikebe, S.6
  • 34
    • 0019423856 scopus 로고
    • Sequence and organization of the human mitochondrial genome
    • Anderson S, Bankier AT, Barrell BG, et al. Sequence and organization of the human mitochondrial genome. Nature 1981; 90:457-465
    • (1981) Nature , vol.90 , pp. 457-465
    • Anderson, S.1    Bankier, A.T.2    Barrell, B.G.3
  • 35
    • 0025113789 scopus 로고
    • Increase of deleted mitochondrial DNA in the striatum in Parkinson's disease and senescence
    • Ikebe S, Tanaka M, Ohno K, et al. Increase of deleted mitochondrial DNA in the striatum in Parkinson's disease and senescence. Biochem Biophys Res Commun 1990;170:1044-1048
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 1044-1048
    • Ikebe, S.1    Tanaka, M.2    Ohno, K.3
  • 37
    • 0027021442 scopus 로고
    • Mosaicism for a specific somatic mitochondrial DNA mutation in adult human brain
    • Soong K, Hinton DR, Cortopassi G, Arnheim N. Mosaicism for a specific somatic mitochondrial DNA mutation in adult human brain. Nature Genet 1992;2:318-323
    • (1992) Nature Genet , vol.2 , pp. 318-323
    • Soong, K.1    Hinton, D.R.2    Cortopassi, G.3    Arnheim, N.4
  • 38
    • 0026471872 scopus 로고
    • Accumulation of deletions in human mitochondrial DNA during normal aging: Analysis by quantitative PCR
    • Simonetti S, Chen X, DiMauro S, Schon EA. Accumulation of deletions in human mitochondrial DNA during normal aging: analysis by quantitative PCR. Biochim Biophys Acta 1992;1180:113-122
    • (1992) Biochim Biophys Acta , vol.1180 , pp. 113-122
    • Simonetti, S.1    Chen, X.2    DiMauro, S.3    Schon, E.A.4
  • 39
    • 0030449566 scopus 로고    scopus 로고
    • Mitochondrial DNA polymorphism in substantia nigra
    • Kapsa RM, Jean-Francois MJ, Lertrit P, et al. Mitochondrial DNA polymorphism in substantia nigra. J Neurol Sci 1996; 144:204-211
    • (1996) J Neurol Sci , vol.144 , pp. 204-211
    • Kapsa, R.M.1    Jean-Francois, M.J.2    Lertrit, P.3
  • 41
    • 0027055332 scopus 로고
    • Age-associated oxygen damage and mutations in mitochondrial DNA in human hearts
    • Hayakawa M, Hattori K, Sugiyama S, Ozawa T. Age-associated oxygen damage and mutations in mitochondrial DNA in human hearts. Biochem Biophys Res Commun 1992; 189:979-985
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 979-985
    • Hayakawa, M.1    Hattori, K.2    Sugiyama, S.3    Ozawa, T.4
  • 42
    • 0026740057 scopus 로고
    • New insights into the cause of Parkinson's disease
    • Jenner P, Schapira AH, Marsden CD. New insights into the cause of Parkinson's disease. Neurology 1992;42:2241-2250
    • (1992) Neurology , vol.42 , pp. 2241-2250
    • Jenner, P.1    Schapira, A.H.2    Marsden, C.D.3
  • 43
    • 0028854722 scopus 로고
    • Point mutations of mitochondrial genome in Parkinson's disease
    • Ikebe S, Tanaka M, Ozawa T. Point mutations of mitochondrial genome in Parkinson's disease. Mol Brain Res 1995;28: 281-295
    • (1995) Mol Brain Res , vol.28 , pp. 281-295
    • Ikebe, S.1    Tanaka, M.2    Ozawa, T.3
  • 44
    • 0023811053 scopus 로고
    • Normal oxidative damage to mitochondrial and nuclear DNA is extensive
    • Richter C, Park J-W, Ames BN. Normal oxidative damage to mitochondrial and nuclear DNA is extensive. Proc Natl Acad Sci USA 1988;85:6465-6467
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6465-6467
    • Richter, C.1    Park, J.-W.2    Ames, B.N.3
  • 45
    • 0018307726 scopus 로고
    • Characterization of a hasten-like protein extracted from mitochondria
    • Caron F, Jacq C, Rouviere-Yaniv J. Characterization of a hasten-like protein extracted from mitochondria. Proc Natl Acad Sci USA 1979;76:4265-4269
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4265-4269
    • Caron, F.1    Jacq, C.2    Rouviere-Yaniv, J.3
  • 46
    • 0019978703 scopus 로고
    • Replication of animal mitochondrial DNA
    • Clayton DA. Replication of animal mitochondrial DNA. Cell 1982;28:693-705
    • (1982) Cell , vol.28 , pp. 693-705
    • Clayton, D.A.1
  • 47
    • 0014690248 scopus 로고
    • Apparent turnover of mitochondrial deoxyribonucleic acid and mitochondrial phospholipids in the tissue of rat
    • Gross NJ, Getz GS, Rubinowitz M. Apparent turnover of mitochondrial deoxyribonucleic acid and mitochondrial phospholipids in the tissue of rat. J Biol Chem 1969;244:1552-1562
    • (1969) J Biol Chem , vol.244 , pp. 1552-1562
    • Gross, N.J.1    Getz, G.S.2    Rubinowitz, M.3
  • 48
    • 0019861198 scopus 로고
    • Fidelity of mammalian DNA polymerase
    • Kunkel TA, Loeb LA. Fidelity of mammalian DNA polymerase. Science 1981;213:765-767
    • (1981) Science , vol.213 , pp. 765-767
    • Kunkel, T.A.1    Loeb, L.A.2
  • 50
    • 0031584966 scopus 로고    scopus 로고
    • Mitochondrial tRNA(Gln) and tRNA(Thr) gene variants in Parkinson's disease
    • Mayr-Wohlfart U, Rodel G, Hennesberg A. Mitochondrial tRNA(Gln) and tRNA(Thr) gene variants in Parkinson's disease. Eur J Med Res 1997;2:111-113
    • (1997) Eur J Med Res , vol.2 , pp. 111-113
    • Mayr-Wohlfart, U.1    Rodel, G.2    Hennesberg, A.3
  • 53
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Annu Rev Biochem 1985;54:1015-1069
    • (1985) Annu Rev Biochem , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 54
    • 0021866528 scopus 로고
    • Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase
    • Chomyn A, Mariottini P, Cleeter MWJ, et al. Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature 1985;314:592-597
    • (1985) Nature , vol.314 , pp. 592-597
    • Chomyn, A.1    Mariottini, P.2    Cleeter, M.W.J.3
  • 55
    • 0023032242 scopus 로고
    • URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit
    • Chomyn A, Cleeter MWJ, Ragan CI, Riley M, Dolittle RF, Attardi G. URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit. Science 1986;234:614-618
    • (1986) Science , vol.234 , pp. 614-618
    • Chomyn, A.1    Cleeter, M.W.J.2    Ragan, C.I.3    Riley, M.4    Dolittle, R.F.5    Attardi, G.6
  • 56
    • 0021958744 scopus 로고
    • EPR studies of iron-sulfur clusters in isolated subunits and subtractions of NADH-ubiquinone oxidoreductase
    • Ohnishi T, Ragan CI, Hatefi Y. EPR studies of iron-sulfur clusters in isolated subunits and subtractions of NADH-ubiquinone oxidoreductase. J Biol Chem 1985;260:2782-2788
    • (1985) J Biol Chem , vol.260 , pp. 2782-2788
    • Ohnishi, T.1    Ragan, C.I.2    Hatefi, Y.3
  • 57
    • 0029024362 scopus 로고
    • Molecular cloning and characterization of the active human mitochondrial NADH:ubiquinone oxidoreductase 24-kDa gene (NDUFV2) and its pseudogene
    • de Coo R, Buddiger P, Smeets H, et al. Molecular cloning and characterization of the active human mitochondrial NADH:ubiquinone oxidoreductase 24-kDa gene (NDUFV2) and its pseudogene. Genomics 1995;26:461-466
    • (1995) Genomics , vol.26 , pp. 461-466
    • De Coo, R.1    Buddiger, P.2    Smeets, H.3
  • 58
    • 0028853902 scopus 로고
    • Structural organization and chromosomal localization of the human nuclear gene (NDUFV2) for the 24-kDa iron-sulfur subunit of complex I in mitochondrial respiratory chain
    • Hattori N, Suzuki H, Wang Y, et al. Structural organization and chromosomal localization of the human nuclear gene (NDUFV2) for the 24-kDa iron-sulfur subunit of complex I in mitochondrial respiratory chain. Biochem Biophys Res Commun 1995;216:771-777
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 771-777
    • Hattori, N.1    Suzuki, H.2    Wang, Y.3
  • 59
    • 0032054295 scopus 로고    scopus 로고
    • Allele in the 24-kDa subunit gene (NDUFV2) ot mitochondrial complex I and susceptibility to Parkinson's disease
    • Hattori N, Yoshino H, Tanaka M, Suzuki H, Mizuno Y. Allele in the 24-kDa subunit gene (NDUFV2) ot mitochondrial complex I and susceptibility to Parkinson's disease. Genomics 1998;49:52-58
    • (1998) Genomics , vol.49 , pp. 52-58
    • Hattori, N.1    Yoshino, H.2    Tanaka, M.3    Suzuki, H.4    Mizuno, Y.5
  • 60
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G, Steppuhn J, Herrmann RG. Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 1989;180:535-545
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 61
    • 0028600070 scopus 로고
    • A helical element in the C-terminal domain of the N. plumbaginifolia F1 beta presequence is important for recognition by the mitochondrial processing peptidase
    • Sjoling S, Eriksson AC, Glaser E. A helical element in the C-terminal domain of the N. plumbaginifolia F1 beta presequence is important for recognition by the mitochondrial processing peptidase. J Biol Chem 1994;269:32059-32062
    • (1994) J Biol Chem , vol.269 , pp. 32059-32062
    • Sjoling, S.1    Eriksson, A.C.2    Glaser, E.3
  • 62
    • 0023111239 scopus 로고
    • Inhibition of mitochondrial alpha-ketoglutarate dehydrogenase by 1-methyl-4-phenyl-pyridinium ion
    • Mizuno Y, Saitoh T, Sone N. Inhibition of mitochondrial alpha-ketoglutarate dehydrogenase by 1-methyl-4-phenyl-pyridinium ion. Biochem Biophys Res Commun 1987;143: 971-976
    • (1987) Biochem Biophys Res Commun , vol.143 , pp. 971-976
    • Mizuno, Y.1    Saitoh, T.2    Sone, N.3
  • 63
    • 0022972426 scopus 로고
    • Brain α-ketoglutarate dehydrogenase complex: Kinetic properties, regional distribution, and effects of inhibitors
    • Lai JCK, Cooper AJL. Brain α-ketoglutarate dehydrogenase complex: kinetic properties, regional distribution, and effects of inhibitors. J Neurochem 1986;47:1376-1386
    • (1986) J Neurochem , vol.47 , pp. 1376-1386
    • Lai, J.C.K.1    Cooper, A.J.L.2
  • 64
    • 0027935643 scopus 로고
    • Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex
    • Nakano K, Takase C, Sakamoto T, et al. Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. Eur J Biochem 1994;224:179-189
    • (1994) Eur J Biochem , vol.224 , pp. 179-189
    • Nakano, K.1    Takase, C.2    Sakamoto, T.3
  • 65
    • 0027515844 scopus 로고
    • An unspliced cDNA for human dihydrolipoamide succinyltransferase: Characterization and mapping of the gene to chromosome 14q24.2-q24.3
    • Nakano K, Takase C, Sakamoto T, et al. An unspliced cDNA for human dihydrolipoamide succinyltransferase: characterization and mapping of the gene to chromosome 14q24.2-q24.3. Biochem Biophys Res Commun 1993;196:527-533
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 527-533
    • Nakano, K.1    Takase, C.2    Sakamoto, T.3
  • 66
    • 0027759516 scopus 로고
    • Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3
    • Nakano K, Matuda S, Sakamoto T, et al. Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3. Biochim Biophys Acta 1993; 1216:360-368
    • (1993) Biochim Biophys Acta , vol.1216 , pp. 360-368
    • Nakano, K.1    Matuda, S.2    Sakamoto, T.3
  • 67
    • 0031891886 scopus 로고    scopus 로고
    • Polymorphism of the gene encoding dihydrolipoamide succinyltransferase, a subunit of α-ketoglutarate dehydrogenase complex, is associated with the susceptibility to Parkinson disease: A population based study
    • Kobayashi T, Matsumine H, Matsubayashi S, Matuda S, Mizuno Y. Polymorphism of the gene encoding dihydrolipoamide succinyltransferase, a subunit of α-ketoglutarate dehydrogenase complex, is associated with the susceptibility to Parkinson disease: a population based study. Ann Neurol 1998;43:120-123
    • (1998) Ann Neurol , vol.43 , pp. 120-123
    • Kobayashi, T.1    Matsumine, H.2    Matsubayashi, S.3    Matuda, S.4    Mizuno, Y.5
  • 68
    • 0024321178 scopus 로고
    • A selective increase in particulate superoxide dismutase activity in parkinsonian substantia nigra
    • Saggu H, Cooksey J, Dexter D, et al. A selective increase in particulate superoxide dismutase activity in parkinsonian substantia nigra. J Neurochem 1989;53:692-697
    • (1989) J Neurochem , vol.53 , pp. 692-697
    • Saggu, H.1    Cooksey, J.2    Dexter, D.3
  • 69
    • 0026688441 scopus 로고
    • The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles
    • Borgstahl GEO, Parge HE, Hickey MJ, Beyer WF Jr, Halliwell RA, Tainer JA. The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell 1992;71:107-118
    • (1992) Cell , vol.71 , pp. 107-118
    • Borgstahl, G.E.O.1    Parge, H.E.2    Hickey, M.J.3    Beyer Jr., W.F.4    Halliwell, R.A.5    Tainer, J.A.6
  • 71
    • 0023918054 scopus 로고
    • Isolation of cDNAs encoding human manganese superoxide dismutase
    • Heckl K. Isolation of cDNAs encoding human manganese superoxide dismutase. Nucleic Acids Res 1988;16:6224
    • (1988) Nucleic Acids Res , vol.16 , pp. 6224
    • Heckl, K.1
  • 72
    • 0023902809 scopus 로고
    • Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase
    • Ho YS, Crapo JD. Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase. FEB Lett 1988;229:256-260
    • (1988) FEB Lett , vol.229 , pp. 256-260
    • Ho, Y.S.1    Crapo, J.D.2
  • 73
    • 0030582372 scopus 로고    scopus 로고
    • Structural dimorphism in the mitochondrial targeting sequence in the human Mn SOD 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. Structural dimorphism in the mitochondrial targeting sequence in the human Mn SOD 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 1996;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
  • 74
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou PY, Fasman GD. Prediction of protein conformation. Biochemistry 1974;13:222-245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 75
    • 0022725788 scopus 로고
    • A chemically synthesized presequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers
    • Roise D, Horvath SJ, Tomich JM, Richards J, Schatz G. A chemically synthesized presequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. EMBO J 1986;5: 1327-1334
    • (1986) EMBO J , vol.5 , pp. 1327-1334
    • Roise, D.1    Horvath, S.J.2    Tomich, J.M.3    Richards, J.4    Schatz, G.5
  • 76
    • 16944362288 scopus 로고    scopus 로고
    • Localization of a gene for autosomal recessive form of juvenile parkinsonism (AR-JP) to chromosome 6q25.2-27
    • Matsumine H, Saito M, Shimoda-Matsubayashi S, et al. Localization of a gene for autosomal recessive form of juvenile parkinsonism (AR-JP) to chromosome 6q25.2-27. Am J Hum Genet 1997;60:588-596
    • (1997) Am J Hum Genet , vol.60 , pp. 588-596
    • Matsumine, H.1    Saito, M.2    Shimoda-Matsubayashi, S.3
  • 77
    • 0015590978 scopus 로고
    • Paralysis agitans of early onset with marked diurnal fluctuation of symptoms
    • Yamamura Y, Sobue I, Ando K, Iida M, Yanagi T, Kono C. Paralysis agitans of early onset with marked diurnal fluctuation of symptoms. Neurology 1973;23:239-244
    • (1973) Neurology , vol.23 , pp. 239-244
    • Yamamura, Y.1    Sobue, I.2    Ando, K.3    Iida, M.4    Yanagi, T.5    Kono, C.6
  • 78
    • 0030015934 scopus 로고    scopus 로고
    • Clinical analysis of 17 patients in 12 Japanese families with autosomal-recessive type juvenile parkinsonism
    • Ishikawa A, Tsuji S. Clinical analysis of 17 patients in 12 Japanese families with autosomal-recessive type juvenile parkinsonism. Neurology 1996;47:160-169
    • (1996) Neurology , vol.47 , pp. 160-169
    • Ishikawa, A.1    Tsuji, S.2
  • 79
    • 0028198309 scopus 로고
    • Familial juvenile parkinsonism: Clinical and pathologic study in a family
    • Takahashi H, Ohama E, Suzuki S, et al. Familial juvenile parkinsonism: clinical and pathologic study in a family. Neurology 1994;44:437-441
    • (1994) Neurology , vol.44 , pp. 437-441
    • Takahashi, H.1    Ohama, E.2    Suzuki, S.3
  • 80
    • 0026499456 scopus 로고
    • Sublocalization of the gene encoding manganese superoxide dismutase (Mn SOD/sod 2) to 6q25 by fluorescence in situ hybridization and somatic cell hybrid mapping
    • Church SL, Grant JW, Meese EU, Trent JM. Sublocalization of the gene encoding manganese superoxide dismutase (Mn SOD/sod 2) to 6q25 by fluorescence in situ hybridization and somatic cell hybrid mapping. Genomics 1992;14:823-825
    • (1992) Genomics , vol.14 , pp. 823-825
    • Church, S.L.1    Grant, J.W.2    Meese, E.U.3    Trent, J.M.4
  • 81
    • 0030716843 scopus 로고    scopus 로고
    • Mn SOD activity and protein in a patient with chromosome 6-linked autosomal recessive parkinsonism in comparison with Parkinson's disease and control
    • Shimoda-Matsubayashi S, Hattori T, Matsumine H, et al. Mn SOD activity and protein in a patient with chromosome 6-linked autosomal recessive parkinsonism in comparison with Parkinson's disease and control. Neurology 1997;49:1257-1262
    • (1997) Neurology , vol.49 , pp. 1257-1262
    • Shimoda-Matsubayashi, S.1    Hattori, T.2    Matsumine, H.3
  • 82
    • 0030593511 scopus 로고    scopus 로고
    • A novel enzyme enantio-selectively synthesizes (R)salsolinol, a precursor of a dopaminergic neurotoxin, N-methyl(R)-salsolinol
    • Naoi M, Maruyama W, Dostert P, Kohda K, Kaiya T. A novel enzyme enantio-selectively synthesizes (R)salsolinol, a precursor of a dopaminergic neurotoxin, N-methyl(R)-salsolinol. Neurosci Lett 1996;212:183-186
    • (1996) Neurosci Lett , vol.212 , pp. 183-186
    • Naoi, M.1    Maruyama, W.2    Dostert, P.3    Kohda, K.4    Kaiya, T.5
  • 83
    • 0023854275 scopus 로고
    • Inhibition of mitochondrial NADH-ubiquinone oxidoreductase activity and ATP synthesis by tetrahydroisoquinoline
    • Suzuki K, Mizuno Y, Yoshida M. Inhibition of mitochondrial NADH-ubiquinone oxidoreductase activity and ATP synthesis by tetrahydroisoquinoline. Neurosci Lett 1988;86:105-108
    • (1988) Neurosci Lett , vol.86 , pp. 105-108
    • Suzuki, K.1    Mizuno, Y.2    Yoshida, M.3
  • 84
    • 0029564605 scopus 로고
    • Inhibition of complex I by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)
    • McNaught KSP, Thull U, Carrupt PA, et al. Inhibition of complex I by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Biochem Pharmacol 1995;50:1903-1911
    • (1995) Biochem Pharmacol , vol.50 , pp. 1903-1911
    • McNaught, K.S.P.1    Thull, U.2    Carrupt, P.A.3
  • 85
    • 0030070870 scopus 로고    scopus 로고
    • Effects of isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) on mitochondrial respiration
    • McNaught KSP, Thull U, Carrupt PA, et al. Effects of isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) on mitochondrial respiration. Biochem Pharmacol 1996;51:1503-1511
    • (1996) Biochem Pharmacol , vol.51 , pp. 1503-1511
    • McNaught, K.S.P.1    Thull, U.2    Carrupt, P.A.3
  • 86
    • 0030051311 scopus 로고    scopus 로고
    • Effect of dopamine, dimethoxyphenylethylamine, papaverine, and related compounds on mitochondrial respiration and complex I activity
    • Morikawa N, Nakagawa-Hattori Y, Mizuno Y. Effect of dopamine, dimethoxyphenylethylamine, papaverine, and related compounds on mitochondrial respiration and complex I activity. J Neurochem 1996;66:1174-1181
    • (1996) J Neurochem , vol.66 , pp. 1174-1181
    • Morikawa, N.1    Nakagawa-Hattori, Y.2    Mizuno, Y.3
  • 87
    • 0031706179 scopus 로고    scopus 로고
    • Effects of various tetrahydroisoquinoline derivatives on mitochondrial respiration and the electron transfer complexes
    • in press
    • Morikawa N, Naio M, Maruyama W, et al. Effects of various tetrahydroisoquinoline derivatives on mitochondrial respiration and the electron transfer complexes. J Neural Trans 1998 [in press].
    • (1998) J Neural Trans
    • Morikawa, N.1    Naio, M.2    Maruyama, W.3
  • 88
    • 0025688141 scopus 로고
    • Mitochondrial respiratory inhibition by N-methylated betacarboline derivatives structurally resembling N-methyl-4-phenylpyridine
    • Albores R, Heafsey EJ, Drucker G, Fields JZ, Collins MA. Mitochondrial respiratory inhibition by N-methylated betacarboline derivatives structurally resembling N-methyl-4-phenylpyridine. Proc Natl Acad Sci USA 1990;87:9368-9372
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9368-9372
    • Albores, R.1    Heafsey, E.J.2    Drucker, G.3    Fields, J.Z.4    Collins, M.A.5
  • 89
    • 0023894885 scopus 로고
    • Presence of tetrahydroisoquinoline and 1-methyl-tetrahydro-isoquinoline in foods: Compounds related to Parkinson's disease
    • Makino Y, Ohta S, Tachikawa O, Hirobe M. Presence of tetrahydroisoquinoline and 1-methyl-tetrahydro-isoquinoline in foods: compounds related to Parkinson's disease. Life Sci 1988;43:373-378
    • (1988) Life Sci , vol.43 , pp. 373-378
    • Makino, Y.1    Ohta, S.2    Tachikawa, O.3    Hirobe, M.4
  • 90
    • 0023698218 scopus 로고
    • Migration of tetrahydroisoquinoline, a possible parkinsonian neurotoxin, into monkey brain from blood as proved by gas chromatography-mass spectrometry
    • Niwa T, Takeda N, Tatematsu A, Matsuura S, Yoshida M, Nagatsu T. Migration of tetrahydroisoquinoline, a possible parkinsonian neurotoxin, into monkey brain from blood as proved by gas chromatography-mass spectrometry. J Chrornatogt 1988;452:85-91
    • (1988) J Chrornatogt , vol.452 , pp. 85-91
    • Niwa, T.1    Takeda, N.2    Tatematsu, A.3    Matsuura, S.4    Yoshida, M.5    Nagatsu, T.6
  • 91
    • 0024359987 scopus 로고
    • A N-methyltransferase in human brain catalyzes N-methylation of 1,2,3,4-tetrahydroisoquinoline into N-methyl-1,2,3,4-tetrahydroisoquinoline, a precursor of a dopaminergic neurotoxin N-methylisoquinolinium ion
    • Naoi M, Matsuura S, Takahashi T, Nagatsu T. A N-methyltransferase in human brain catalyzes N-methylation of 1,2,3,4-tetrahydroisoquinoline into N-methyl-1,2,3,4-tetrahydroisoquinoline, a precursor of a dopaminergic neurotoxin N-methylisoquinolinium ion. Biochem Biophys Res Commun 1989;161:1213-1219
    • (1989) Biochem Biophys Res Commun , vol.161 , pp. 1213-1219
    • Naoi, M.1    Matsuura, S.2    Takahashi, T.3    Nagatsu, T.4
  • 92
    • 0030060483 scopus 로고    scopus 로고
    • Dopamine-derived endogenous 1(R),2(N)-dimethyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline, N-methyl-(R)-salsolinol, induced parkinsonism in rat: Biochemical, pathological and behavioral studies
    • Naoi M, Maruyama W, Dostert P, et al. Dopamine-derived endogenous 1(R),2(N)-dimethyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline, N-methyl-(R)-salsolinol, induced parkinsonism in rat: biochemical, pathological and behavioral studies. Brain Res 1996;709:285-295
    • (1996) Brain Res , vol.709 , pp. 285-295
    • Naoi, M.1    Maruyama, W.2    Dostert, P.3
  • 93
    • 0031043805 scopus 로고    scopus 로고
    • A dopaminergic neurotoxin, 1(R),2(N)-dimethyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline, N-methyl(R) salsolinol, and its oxidation product, 1,2 (N)-dimethyl-6,7-dihydroxyisoquinolinium ion, accumulate in the nigrostriatal system of the human brain
    • Maruyama W, Sobue G, Matsubara K, Hashizume Y, Dostert P, Naoi M. A dopaminergic neurotoxin, 1(R),2(N)-dimethyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline, N-methyl(R) salsolinol, and its oxidation product, 1,2 (N)-dimethyl-6,7-dihydroxyisoquinolinium ion, accumulate in the nigrostriatal system of the human brain. Neurosci Lett 1997;223:61-64
    • (1997) Neurosci Lett , vol.223 , pp. 61-64
    • Maruyama, W.1    Sobue, G.2    Matsubara, K.3    Hashizume, Y.4    Dostert, P.5    Naoi, M.6
  • 94
    • 0029891783 scopus 로고    scopus 로고
    • A dopaminergic neurotoxin, (R)-N-methylsalsolinol, increases in Parkinsonian cerebrospinal fluid
    • Maruyama W, Abe T, Tohgi H, Dostert P, Naoi M. A dopaminergic neurotoxin, (R)-N-methylsalsolinol, increases in Parkinsonian cerebrospinal fluid. Ann Neurol 1996;40:119-122
    • (1996) Ann Neurol , vol.40 , pp. 119-122
    • Maruyama, W.1    Abe, T.2    Tohgi, H.3    Dostert, P.4    Naoi, M.5
  • 95
    • 0029440852 scopus 로고
    • + analogs, in the lumbar cerebrospinal fluid of patients with Parkinson's disease
    • + analogs, in the lumbar cerebrospinal fluid of patients with Parkinson's disease. Neurology 1995; 45:2240-2245
    • (1995) Neurology , vol.45 , pp. 2240-2245
    • Matsubara, K.1    Kobayashi, S.2    Kobayashi, Y.3
  • 96
    • 0030462474 scopus 로고    scopus 로고
    • Elevated levels of harman and norharman in cerebrospinal fluid of Parkinsonian patients
    • Kuhn W, Muller T, Grosse H, Dierks T, Rommelspacher H. Elevated levels of harman and norharman in cerebrospinal fluid of Parkinsonian patients. J Neurol Sci 1996;103:1435-1440
    • (1996) J Neurol Sci , vol.103 , pp. 1435-1440
    • Kuhn, W.1    Muller, T.2    Grosse, H.3    Dierks, T.4    Rommelspacher, H.5
  • 97
    • 0024585155 scopus 로고
    • Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease
    • Dexter DT, Carter CJ, Wells FR, et al. Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease. J Neurochem 1989;52:381-389
    • (1989) J Neurochem , vol.52 , pp. 381-389
    • Dexter, D.T.1    Carter, C.J.2    Wells, F.R.3
  • 98
    • 0026635461 scopus 로고
    • Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease
    • Jenner P, Dexter DT, Sian J, Schapira AHV, Marsden CG. Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease. Ann Neurol 1992; 32:S82-S87
    • (1992) Ann Neurol , vol.32
    • Jenner, P.1    Dexter, D.T.2    Sian, J.3    Schapira, A.H.V.4    Marsden, C.G.5
  • 99
    • 0027497409 scopus 로고
    • Review: The possible role of iron in the etiopathogenesis of Parkinson's disease
    • Youdim MBH, Ben-Shachar, Riederer P. Review: the possible role of iron in the etiopathogenesis of Parkinson's disease. Mov Disord 1993;8:1-12
    • (1993) Mov Disord , vol.8 , pp. 1-12
    • Youdim, M.B.H.1    Ben-Shachar2    Riederer, P.3
  • 101
    • 0026606054 scopus 로고
    • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal
    • Uchida K, Stadtman ER. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Proc Natl Acad Sci USA 1992;89:4544-4548
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4544-4548
    • Uchida, K.1    Stadtman, E.R.2
  • 102
    • 0024996681 scopus 로고
    • The oxidative inactivation of mitochondrial electron transport chain components and ATPase
    • Zhang Y, Marcillat O, Giulvi C, Ernster L, Davis KJA. The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J Biol Chem 1990;165:16330-16336
    • (1990) J Biol Chem , vol.165 , pp. 16330-16336
    • Zhang, Y.1    Marcillat, O.2    Giulvi, C.3    Ernster, L.4    Davis, K.J.A.5
  • 103
    • 0028266425 scopus 로고
    • Iron accumulation in the substantia nigra of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced hemiparkinsonian monkeys
    • Mochizuki H, Imai H, Endo K, et al. Iron accumulation in the substantia nigra of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced hemiparkinsonian monkeys. Neurosci Lett 1994;168:251-253
    • (1994) Neurosci Lett , vol.168 , pp. 251-253
    • Mochizuki, H.1    Imai, H.2    Endo, K.3
  • 104
    • 0023766185 scopus 로고
    • Oxygen toxicity protecting enzymes in Parkinson's disease: Increase of superoxide dismutase-like activity in the substantia nigra and basal nucleus
    • Marttila RJ, Lorentz H, Rinne UK. Oxygen toxicity protecting enzymes in Parkinson's disease: increase of superoxide dismutase-like activity in the substantia nigra and basal nucleus. J Neurol Sci 1988;86:321-331
    • (1988) J Neurol Sci , vol.86 , pp. 321-331
    • Marttila, R.J.1    Lorentz, H.2    Rinne, U.K.3
  • 105
    • 0031589982 scopus 로고    scopus 로고
    • An immunohistochemical study on manganese superoxide dismutase in Parkinson's disease
    • Yoritaka A, Hattori N, Mori H, Kato K, Mizuno Y. An immunohistochemical study on manganese superoxide dismutase in Parkinson's disease. J Neurol Sci 1997;148:181-186
    • (1997) J Neurol Sci , vol.148 , pp. 181-186
    • Yoritaka, A.1    Hattori, N.2    Mori, H.3    Kato, K.4    Mizuno, Y.5
  • 106
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian J, Dexter DT, Lees AJ, et al. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann Neurol 1994;36: 348-355
    • (1994) Ann Neurol , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3
  • 107
    • 0030582838 scopus 로고    scopus 로고
    • Mitochondrial respiratory enzyme function and superoxide dismutase activity following brain glutathione depletion in the rat
    • Seaton TA, Jenner P, Marsden CD. Mitochondrial respiratory enzyme function and superoxide dismutase activity following brain glutathione depletion in the rat. Biochem Pharmacol 1996;52:1657-1663
    • (1996) Biochem Pharmacol , vol.52 , pp. 1657-1663
    • Seaton, T.A.1    Jenner, P.2    Marsden, C.D.3


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