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Volumn 88, Issue 6, 2004, Pages 1352-1360

Mice deficient in dihydrolipoamide dehydrogenase show increased vulnerability to MPTP, malonate and 3-nitropropionic acid neurotoxicity

Author keywords

Alzheimer; Huntington; Mitochondria; Neurodegenerative diseases; Oxidative damage; Parkinson

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; 3 NITROPROPIONIC ACID; DIHYDROLIPOAMIDE DEHYDROGENASE; MALONIC ACID; MITOCHONDRIAL ENZYME; OXOGLUTARATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE; TYROSINE 3 MONOOXYGENASE;

EID: 12144290495     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.02263.x     Document Type: Article
Times cited : (89)

References (54)
  • 1
    • 0343983913 scopus 로고
    • 3-Nitropropionate, the toxic substance of Indigo/era, is a suicide inactivator of succinate dehydrogenase
    • Alston T. A., Mela L. and Bright H. J. (1977) 3-Nitropropionate, the toxic substance of Indigo/era, is a suicide inactivator of succinate dehydrogenase. Proc. Natl Acad. Sci. USA 74, 3767-3771.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 3767-3771
    • Alston, T.A.1    Mela, L.2    Bright, H.J.3
  • 2
    • 0000522311 scopus 로고
    • Limitations of the phenazine methosulfate assay for succinic and related dehydrogenases
    • Arrigon O. and Singer T. (1962) Limitations of the phenazine methosulfate assay for succinic and related dehydrogenases. Nature 193, 1256-1258.
    • (1962) Nature , vol.193 , pp. 1256-1258
    • Arrigon, O.1    Singer, T.2
  • 3
    • 0035344211 scopus 로고    scopus 로고
    • Experimental models of Parkinson's disease
    • Beal M. F. (2001) Experimental models of Parkinson's disease. Nat. Rev. Neurosci. 2, 325-334.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 325-334
    • Beal, M.F.1
  • 5
    • 0027204154 scopus 로고
    • Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate
    • Beal M. F., Brouillet E., Jenkins B., Henshaw R., Rosen B. and Hyman B. T. (1993b) Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate. J. Neurochem. 61, 1147-1150.
    • (1993) J. Neurochem. , vol.61 , pp. 1147-1150
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.3    Henshaw, R.4    Rosen, B.5    Hyman, B.T.6
  • 7
    • 0035668684 scopus 로고    scopus 로고
    • Increased oxidatve damage to DNA in transgenic mouse model of Huntington's disease
    • Bodganov M. B., Andreassen O. A., Dedeoglu A., Ferrante R. J. and Beal M. F. (2001) Increased oxidatve damage to DNA in transgenic mouse model of Huntington's disease. J. Neurochem. 79, 1246-1249.
    • (2001) J. Neurochem. , vol.79 , pp. 1246-1249
    • Bodganov, M.B.1    Andreassen, O.A.2    Dedeoglu, A.3    Ferrante, R.J.4    Beal, M.F.5
  • 8
    • 0029118136 scopus 로고
    • Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates
    • Brouillet E., Hantraye P., Ferrante R. J., Dolan R., Leroy-Willig A., Kowall N. W. and Beal M. F. (1995) Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates. Proc. Natl Acad. Sci. USA 92, 7105-7109.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7105-7109
    • Brouillet, E.1    Hantraye, P.2    Ferrante, R.J.3    Dolan, R.4    Leroy-Willig, A.5    Kowall, N.W.6    Beal, M.F.7
  • 9
    • 0032903802 scopus 로고    scopus 로고
    • Oxidative stress in Huntington's disease
    • Browne S. E., Ferrante R. J. and Beal M. F. (1999) Oxidative stress in Huntington's disease. Brain Pathol. 9, 147-163.
    • (1999) Brain Pathol. , vol.9 , pp. 147-163
    • Browne, S.E.1    Ferrante, R.J.2    Beal, M.F.3
  • 10
    • 0021917344 scopus 로고
    • Distribution of phosphate-activated glutaminase, succinic dehydrogenase, pyruvate dehydrogenase and gamma-glutamyl transpeptidase in post-mortem brain from Huntington's disease and agonal cases
    • Butterworth J., Yates C. M. and Reynolds G. P. (1985) Distribution of phosphate-activated glutaminase, succinic dehydrogenase, pyruvate dehydrogenase and gamma-glutamyl transpeptidase in post-mortem brain from Huntington's disease and agonal cases. J. Neurol. Sci. 67, 161-171.
    • (1985) J. Neurol. Sci. , vol.67 , pp. 161-171
    • Butterworth, J.1    Yates, C.M.2    Reynolds, G.P.3
  • 11
    • 0025650037 scopus 로고
    • Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease
    • Butterworth R. F. and Besnard A. M. (1990) Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease. Metab. Brain Dis. 5, 179-184.
    • (1990) Metab. Brain Dis. , vol.5 , pp. 179-184
    • Butterworth, R.F.1    Besnard, A.M.2
  • 12
    • 0033000269 scopus 로고    scopus 로고
    • Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: Inhibition of alpha-ketoglutarate dehydrogenase
    • Chinopoulos C., Tretter L. and. Adam-Vizi V. (1999) Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: inhibition of alpha-ketoglutarate dehydrogenase. J. Neurochem. 73, 220-228.
    • (1999) J. Neurochem. , vol.73 , pp. 220-228
    • Chinopoulos, C.1    Tretter, L.2    Adam-Vizi, V.3
  • 13
    • 0018801043 scopus 로고
    • Inactivation of succinate dehydrogenase by 3-nitropropionate
    • Coles C. J., Edmondson D. E. and Singer T. P. (1979) Inactivation of succinate dehydrogenase by 3-nitropropionate. J. Biol. Chem. 254, 5161-5167.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5161-5167
    • Coles, C.J.1    Edmondson, D.E.2    Singer, T.P.3
  • 16
    • 0023732664 scopus 로고
    • Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease
    • Gibson G. E., Sheu R. K. F., Blass J. P., Baker A., Carlson K. C. and Harding B. and. Perrino P. (1988) Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease. Arch. Neurol. 45, 836-840.
    • (1988) Arch. Neurol. , vol.45 , pp. 836-840
    • Gibson, G.E.1    Sheu, R.K.F.2    Blass, J.P.3    Baker, A.4    Carlson, K.C.5    Harding, B.6    Perrino, P.7
  • 19
    • 0037117306 scopus 로고    scopus 로고
    • Oxidative stress increases internal calcium stores and reduces a key mitochondrial enzyme
    • Gibson G. E., Zhang H., Xu H., Park L. C. and Jeitner T. M. (2002) Oxidative stress increases internal calcium stores and reduces a key mitochondrial enzyme. Biochim. Biophys. Acta 1586, 177-189.
    • (2002) Biochim. Biophys. Acta , vol.1586 , pp. 177-189
    • Gibson, G.E.1    Zhang, H.2    Xu, H.3    Park, L.C.4    Jeitner, T.M.5
  • 22
    • 0020465435 scopus 로고
    • Basal ganglia degeneration, myelin alterations, and enzyme inhibition in mice induced by the plant toxin 3-nitropropionic acid
    • Gould D. H. and Gustine D. L. (1982) Basal ganglia degeneration, myelin alterations, and enzyme inhibition in mice induced by the plant toxin 3-nitropropionic acid. Neuropathol. Appl. Neurobiol. 8, 377-393.
    • (1982) Neuropathol. Appl. Neurobiol. , vol.8 , pp. 377-393
    • Gould, D.H.1    Gustine, D.L.2
  • 23
    • 0022345539 scopus 로고
    • Brain enzyme and clinical alterations induced in rats and mice by nitroaliphatic toxicants
    • Gould D. H., Wilson M. P. and Hamar D. W. (1985) Brain enzyme and clinical alterations induced in rats and mice by nitroaliphatic toxicants. Toxicol. Lett. 27, 83-89.
    • (1985) Toxicol. Lett. , vol.27 , pp. 83-89
    • Gould, D.H.1    Wilson, M.P.2    Hamar, D.W.3
  • 24
    • 0027198567 scopus 로고
    • Inhibition of succinate dehydrogenase by malonic acid produces an 'excitotoxic' lesion in rat striatum
    • Greene J. G., Porter R. H., Eller R. V. and Greenamyre J. T. (1993) Inhibition of succinate dehydrogenase by malonic acid produces an 'excitotoxic' lesion in rat striatum. J. Neurochem. 61, 1151-1154.
    • (1993) J. Neurochem. , vol.61 , pp. 1151-1154
    • Greene, J.G.1    Porter, R.H.2    Eller, R.V.3    Greenamyre, J.T.4
  • 25
    • 0029844003 scopus 로고    scopus 로고
    • Inhibition of neuronal nitric oxide synthase prevents MPTP-induced parkinsonism in baboons
    • Hantraye P., Brouillet E., Ferrante R., Palfi S., Dolan R., Matthews R. T. and Beal M. F. (1996) Inhibition of neuronal nitric oxide synthase prevents MPTP-induced parkinsonism in baboons. Nat. Med. 2, 1017-1021.
    • (1996) Nat. Med. , vol.2 , pp. 1017-1021
    • Hantraye, P.1    Brouillet, E.2    Ferrante, R.3    Palfi, S.4    Dolan, R.5    Matthews, R.T.6    Beal, M.F.7
  • 26
    • 0029098594 scopus 로고
    • Selective inhibition of the tricarboxylic acid cycle of GABAergic neurons with 3-nitropropionic acid in vivo
    • Hassel B. and Sonnewald U. (1995) Selective inhibition of the tricarboxylic acid cycle of GABAergic neurons with 3-nitropropionic acid In vivo. J Neurochem. 65, 1184-1191.
    • (1995) J. Neurochem. , vol.65 , pp. 1184-1191
    • Hassel, B.1    Sonnewald, U.2
  • 27
    • 0028158077 scopus 로고
    • The role of calcium in the regulation of pyruvate dehydrogenase in synaotosomes
    • Huang H. M., Toral-Barza L., Sheu K. F. R. and Gibson G. E. (1994) The role of calcium in the regulation of pyruvate dehydrogenase in synaotosomes. Neurochem. Res. 19, 89-95.
    • (1994) Neurochem. Res. , vol.19 , pp. 89-95
    • Huang, H.M.1    Toral-Barza, L.2    Sheu, K.F.R.3    Gibson, G.E.4
  • 28
    • 0032563567 scopus 로고    scopus 로고
    • Secondary inhibition of 2-ketoglutarate dehydrogenase complex by MPTP
    • Joffe G. T. P., Parks J. K. and Parker W. D. Jr (1998) Secondary inhibition of 2-ketoglutarate dehydrogenase complex by MPTP. Neuroreport 9, 2781-2783.
    • (1998) Neuroreport , vol.9 , pp. 2781-2783
    • Joffe, G.T.P.1    Parks, J.K.2    Parker Jr., W.D.3
  • 29
    • 0031445917 scopus 로고    scopus 로고
    • Targeted disruption of the murine dihydrolipoamide dehydrogenase gene (Dld) results in perigastrulation lethality
    • Johnson M. T., Yang H.-S., Magnuson T. and Patel M. S. (1997) Targeted disruption of the murine dihydrolipoamide dehydrogenase gene (Dld) results in perigastrulation lethality. Proc. Natl Acad. Sci. USA 94, 14512-14517.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 14512-14517
    • Johnson, M.T.1    Yang, H.-S.2    Magnuson, T.3    Patel, M.S.4
  • 30
    • 0038714406 scopus 로고    scopus 로고
    • Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain
    • Kanamori T., Nishimaki K., Asoh S. et al. (2003) Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain. EMBO J. 22, 2913-2923.
    • (2003) EMBO J. , vol.22 , pp. 2913-2923
    • Kanamori, T.1    Nishimaki, K.2    Asoh, S.3
  • 31
    • 0032944035 scopus 로고    scopus 로고
    • Decreased brain protein levels of cytochrome oxidase subunits in Alzheimer's disease an in hereditary spinocerebellar ataxia disorders: A nonspecific change?
    • Kish S. J., Mastrogiacomo F., Guttman M., Furukawa Y., Taanman J. W., Dozic S., Pandolfo M., Lamarche J., DiStefano L. and Chang L. J. (1999) Decreased brain protein levels of cytochrome oxidase subunits in Alzheimer's disease an in hereditary spinocerebellar ataxia disorders: a nonspecific change? J. Neurochem. 72, 700-707.
    • (1999) J. Neurochem. , vol.72 , pp. 700-707
    • Kish, S.J.1    Mastrogiacomo, F.2    Guttman, M.3    Furukawa, Y.4    Taanman, J.W.5    Dozic, S.6    Pandolfo, M.7    Lamarche, J.8    DiStefano, L.9    Chang, L.J.10
  • 32
    • 0031891886 scopus 로고    scopus 로고
    • Association between the gene encoding the E2 subunit α -ketoglutarate dehydrogenase complex and Parkinson's disease
    • Kobayashi T., Matsumine H., Matuda S. and Mizuno Y. (1998) Association between the gene encoding the E2 subunit α-ketoglutarate dehydrogenase complex and Parkinson's disease. Ann. Neurol. 43, 120-123.
    • (1998) Ann. Neurol. , vol.43 , pp. 120-123
    • Kobayashi, T.1    Matsumine, H.2    Matuda, S.3    Mizuno, Y.4
  • 33
    • 0019945166 scopus 로고
    • Studies on the pyruvate dehydrogenase complex in brain with the arylamine acetyl-transferase-coupled assay
    • Ksiezak-Reding H., Blass J. P. and Gibson G. E. (1982) Studies on the pyruvate dehydrogenase complex in brain with the arylamine acetyl-transferase-coupled assay. J. Neurochem. 38, 1627-1636.
    • (1982) J. Neurochem. , vol.38 , pp. 1627-1636
    • Ksiezak-Reding, H.1    Blass, J.P.2    Gibson, G.E.3
  • 34
    • 0028989810 scopus 로고
    • Inhibition of alpha-ketoglutarate dehydrogenase by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine (MPTP)
    • McNaught K. S., Altomare C., Cellamare S., Carotti A., Thull U., Carrupt P. A., Testa B., Jenner P. and Marsden C. D. (1995) Inhibition of alpha-ketoglutarate dehydrogenase by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Neuroreport 6, 1105-1108.
    • (1995) Neuroreport , vol.6 , pp. 1105-1108
    • McNaught, K.S.1    Altomare, C.2    Cellamare, S.3    Carotti, A.4    Thull, U.5    Carrupt, P.A.6    Testa, B.7    Jenner, P.8    Marsden, C.D.9
  • 35
    • 0023720115 scopus 로고
    • Studies on the toxicity of 1-methyl-4-phenylpyridinium ion (MPP+) against mitochondria of mouse brain
    • Mizuno Y., Sone N., Suzuki K. and Saitoh T. (1988) Studies on the toxicity of 1-methyl-4-phenylpyridinium ion (MPP+) against mitochondria of mouse brain. J. Neurol. Sci. 86, 97-110.
    • (1988) J. Neurol. Sci. , vol.86 , pp. 97-110
    • Mizuno, Y.1    Sone, N.2    Suzuki, K.3    Saitoh, T.4
  • 36
    • 0025230826 scopus 로고
    • Postmortem changes in mitochondrial respiratory enzymes in brain and a preliminary observation in Parkinson's disease
    • Mizuno Y., Suzuki K. and Ohta S. (1990) Postmortem changes in mitochondrial respiratory enzymes in brain and a preliminary observation in Parkinson's disease. J. Neurol. Sci. 96, 49-57.
    • (1990) J. Neurol. Sci. , vol.96 , pp. 49-57
    • Mizuno, Y.1    Suzuki, K.2    Ohta, S.3
  • 37
    • 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. and Ikebe S.-I. (1994) An immunohistochemical study on α-ketoglutarate dehydrogenase complex in Parkinson's disease. Ann. Neurol. 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.-I.6
  • 39
    • 0030001887 scopus 로고    scopus 로고
    • Chronic 3-nitropropionic acid treatment in baboons replicates the cognitive and motor deficits of Huntington's Disease
    • Palfi S., Ferrante R. J., Brouillet E., Beal M. F., Dolan R., Guyot M. C., Peschanski M. and Hantraye P. (1996) Chronic 3-nitropropionic acid treatment in baboons replicates the cognitive and motor deficits of Huntington's Disease. J. Neurosci. 16, 3019-3025.
    • (1996) J. Neurosci. , vol.16 , pp. 3019-3025
    • Palfi, S.1    Ferrante, R.J.2    Brouillet, E.3    Beal, M.F.4    Dolan, R.5    Guyot, M.C.6    Peschanski, M.7    Hantraye, P.8
  • 40
    • 0033048258 scopus 로고    scopus 로고
    • Metabolic impairment induces oxidative stress, compromises inflammatory responses, and inactivates a key mitochondrial enzyme in microglia
    • Park L. C., Zhang H., Sheu K. F., Calingasan N. Y., Kristal B. S., Lindsay J. G. and Gibson G. E. (1999) Metabolic impairment induces oxidative stress, compromises inflammatory responses, and inactivates a key mitochondrial enzyme in microglia. J. Neurochem. 72, 1948-1958.
    • (1999) J. Neurochem. , vol.72 , pp. 1948-1958
    • Park, L.C.1    Zhang, H.2    Sheu, K.F.3    Calingasan, N.Y.4    Kristal, B.S.5    Lindsay, J.G.6    Gibson, G.E.7
  • 41
    • 0342635463 scopus 로고    scopus 로고
    • Striatal oxidative damage parallels the expression of a neurological phenotype in mice transgenic for the mutation of Huntington's disease
    • Perez-Severiano F., Rios C. and Segovia J. (2000) Striatal oxidative damage parallels the expression of a neurological phenotype in mice transgenic for the mutation of Huntington's disease. Brain Res. 862, 234-237.
    • (2000) Brain Res. , vol.862 , pp. 234-237
    • Perez-Severiano, F.1    Rios, C.2    Segovia, J.3
  • 42
    • 0019332560 scopus 로고
    • 3-Carbanionic substrate analogues bind very tightly to fumarase and aspartase
    • Porter D. J. T. and Bright H. J. (1980) 3-Carbanionic substrate analogues bind very tightly to fumarase and aspartase. J. Biol. Chem. 255, 4772-4780.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4772-4780
    • Porter, D.J.T.1    Bright, H.J.2
  • 43
    • 0029984860 scopus 로고    scopus 로고
    • Role of neuronal nitric oxide in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity
    • Przedborski S., Jackon-Lewis V., Yokoyama R., Shibata T., Dawson V. L. and Dawson T. M. (1996) Role of neuronal nitric oxide in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity. Proc. Natl Acad. Sci. USA 93, 4565-4571.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4565-4571
    • Przedborski, S.1    Jackon-Lewis, V.2    Yokoyama, R.3    Shibata, T.4    Dawson, V.L.5    Dawson, T.M.6
  • 44
  • 45
    • 0025700680 scopus 로고
    • Respiratory failure and stimulation of glycolysis in Chinese hamster ovary cells exposed to normobaric hyperoxia
    • Schooner W. G., Wanamarta A. H., van der Kleivan Moorsel J. M., Jakobs C. and Joenje H. (1990) Respiratory failure and stimulation of glycolysis in Chinese hamster ovary cells exposed to normobaric hyperoxia. J. Biol. Chem. 265, 1118-1124.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1118-1124
    • Schooner, W.G.1    Wanamarta, A.H.2    Van Der Kleivan Moorsel, J.M.3    Jakobs, C.4    Joenje, H.5
  • 46
    • 0026073545 scopus 로고
    • Characterization of oxygen-resistant Chinese hamster ovary cells. III. Relative resistance of succinate and alpha-ketoglutarate dehydrogenase to hyperoxic inactivation
    • Schooner W. G., Wanamarta A. H., van der Kleivan Moorsel J. M., Jakobs C. and Joenje H. (1991) Characterization of oxygen-resistant Chinese hamster ovary cells. III. Relative resistance of succinate and alpha-ketoglutarate dehydrogenase to hyperoxic inactivation. Free Radic. Biol. Med. 10, 111-118.
    • (1991) Free Radic. Biol. Med. , vol.10 , pp. 111-118
    • Schooner, W.G.1    Wanamarta, A.H.2    Van Der Kleivan Moorsel, J.M.3    Jakobs, C.4    Joenje, H.5
  • 49
    • 0033787328 scopus 로고    scopus 로고
    • Oxidative metabolites of 5-S-cysteinyldopamine inhibit the alpha-ketoglutarate dehydrogenase complex: Possible relevance to the pathogenesis of Parkinson's disease
    • Shen X. M., Li H. and Dryhurst G. (2000) Oxidative metabolites of 5-S-cysteinyldopamine inhibit the alpha-ketoglutarate dehydrogenase complex: possible relevance to the pathogenesis of Parkinson's disease. J. Neural Transm. 107, 959-978.
    • (2000) J. Neural Transm. , vol.107 , pp. 959-978
    • Shen, X.M.1    Li, H.2    Dryhurst, G.3
  • 51
    • 0028387219 scopus 로고
    • Abnormality of the alpha-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer's disease
    • Sheu R.-K. F., Cooper A. J., Koike K., Koike M., Lindsay J. G. and Blass J. P. (1994) Abnormality of the alpha-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer's disease. Ann. Neurol. 35, 312-318.
    • (1994) Ann. Neurol. , vol.35 , pp. 312-318
    • Sheu, R.-K.F.1    Cooper, A.J.2    Koike, K.3    Koike, M.4    Lindsay, J.G.5    Blass, J.P.6
  • 52
    • 0020685951 scopus 로고
    • Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain
    • Sorbi S., Bird E. D. and Blass J. P. (1983) Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain. Ann. Neurol. 13, 72-78.
    • (1983) Ann. Neurol. , vol.13 , pp. 72-78
    • Sorbi, S.1    Bird, E.D.2    Blass, J.P.3
  • 53
    • 0042433242 scopus 로고    scopus 로고
    • 2 production by membrane potential and NAD(P)H redox state
    • 2 production by membrane potential and NAD(P)H redox state. J. Neurochem. 86, 1101-1107.
    • (2003) J. Neurochem. , vol.86 , pp. 1101-1107
    • Starkov, A.A.1    Fiskum, G.2


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