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Volumn 111, Issue 2, 2003, Pages 163-169

Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; COPPER; DOPAMINE; FERRITIN; FLAVOPROTEIN; IRON; OXIDIZING AGENT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE DISMUTASE; ZINC;

EID: 0037237927     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI200317638     Document Type: Review
Times cited : (683)

References (76)
  • 1
    • 0031842223 scopus 로고    scopus 로고
    • Oxidative damage to proteins, lipids, and DNA in cortical brain regions from patients with dementia with Lewy bodies
    • Lyras, L., et al. 1998. Oxidative damage to proteins, lipids, and DNA in cortical brain regions from patients with dementia with Lewy bodies. J. Neurochem. 71:302-312.
    • (1998) J. Neurochem. , vol.71 , pp. 302-312
    • Lyras, L.1
  • 2
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley, K., et al. 1998. Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J. Neurosci. 18:8126-8132.
    • (1998) J. Neurosci. , vol.18 , pp. 8126-8132
    • Hensley, K.1
  • 3
    • 0033762711 scopus 로고    scopus 로고
    • Increased 8,12-iso-iPF2alpha-VI in Alzheimer's disease: Correlation of a noninvasive index of lipid peroxidation with disease severity
    • Pratico, D., et al. 2000. Increased 8,12-iso-iPF2alpha-VI in Alzheimer's disease: correlation of a noninvasive index of lipid peroxidation with disease severity. Ann. Neurol. 48:809-812.
    • (2000) Ann. Neurol. , vol.48 , pp. 809-812
    • Pratico, D.1
  • 4
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
    • Giasson, B.I., et al. 2000. Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science. 290:985-989.
    • (2000) Science , vol.290 , pp. 985-989
    • Giasson, B.I.1
  • 5
    • 0030851761 scopus 로고    scopus 로고
    • Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis
    • Beal, M.F., et al. 1997. Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann. Neurol. 42:644-654.
    • (1997) Ann. Neurol. , vol.42 , pp. 644-654
    • Beal, M.F.1
  • 6
    • 0029592005 scopus 로고
    • Activation of the inducible form of nitric oxide synthase in the brains of patients with multiple sclerosis
    • Bagasra, O., et al. 1995. Activation of the inducible form of nitric oxide synthase in the brains of patients with multiple sclerosis. Proc. Natl. Acad. Sci. USA. 92:12041-12045.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12041-12045
    • Bagasra, O.1
  • 7
    • 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
  • 8
    • 0035818520 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals
    • Moskovitz, J., et al. 2001. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc. Natl. Acad. Sci. USA. 98:12920-12925.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12920-12925
    • Moskovitz, J.1
  • 9
    • 0032823578 scopus 로고    scopus 로고
    • Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain
    • Gabbita, S.P., Aksenov, M.Y., Lovell, M.A., and Markesbery, W.R. 1999. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J. Neurochem. 73:1660-1666.
    • (1999) J. Neurochem. , vol.73 , pp. 1660-1666
    • Gabbita, S.P.1    Aksenov, M.Y.2    Lovell, M.A.3    Markesbery, W.R.4
  • 10
    • 0037123638 scopus 로고    scopus 로고
    • Premature aging in mice deficient in DNA repair and transcription
    • De Boer, J., et al. 2002. Premature aging in mice deficient in DNA repair and transcription. Science. 296:1276-1279.
    • (2002) Science , vol.296 , pp. 1276-1279
    • De Boer, J.1
  • 11
    • 0030071721 scopus 로고    scopus 로고
    • Downregulation of Cu/Zn superoxide dismutase leads to cell death via the nitric oxide-peroxynitrite pathway
    • Troy, C.M., Derossi, D., Prochiantz, A., Greene, L.A., and Shelanski, M.L. 1996. Downregulation of Cu/Zn superoxide dismutase leads to cell death via the nitric oxide-peroxynitrite pathway. J. Neurosci. 16:253-261.
    • (1996) J. Neurosci. , vol.16 , pp. 253-261
    • Troy, C.M.1    Derossi, D.2    Prochiantz, A.3    Greene, L.A.4    Shelanski, M.L.5
  • 12
    • 16944366242 scopus 로고    scopus 로고
    • Reduction of Cu, Zn-superoxide dismutase activity exacerbates neuronal cell injury and edema formation after transient focal cerebral ischemia
    • Kondo, T., et al. 1997. Reduction of Cu, Zn-superoxide dismutase activity exacerbates neuronal cell injury and edema formation after transient focal cerebral ischemia. J. Neurosci. 17:4180-4189.
    • (1997) J. Neurosci. , vol.17 , pp. 4180-4189
    • Kondo, T.1
  • 13
    • 0029838063 scopus 로고    scopus 로고
    • Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice
    • Lebovitz, R.M., et al. 1996. Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc. Natl. Acad. Sci. USA. 93:9782-9787.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9782-9787
    • Lebovitz, R.M.1
  • 14
    • 0033969953 scopus 로고    scopus 로고
    • Enhanced N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine toxicity in mice deficient in Cu, Zn-superoxide dismutase or glutathione peroxidase
    • Zhang, J., Graham, D.G., Montine, T.J., and Ho, Y.S. 2000. Enhanced N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine toxicity in mice deficient in Cu, Zn-superoxide dismutase or glutathione peroxidase. J. Neuropathol. Exp. Neurol. 59:53-61.
    • (2000) J. Neuropathol. Exp. Neurol. , vol.59 , pp. 53-61
    • Zhang, J.1    Graham, D.G.2    Montine, T.J.3    Ho, Y.S.4
  • 15
    • 0035910076 scopus 로고    scopus 로고
    • Delayed-onset ataxia in mice lacking alpha-tocopherol transfer protein: Model for neuronal degeneration caused by chronic oxidative stress
    • Yokota, T., et al. 2001. Delayed-onset ataxia in mice lacking alpha-tocopherol transfer protein: model for neuronal degeneration caused by chronic oxidative stress. Proc. Natl. Acad. Sci. USA. 98:15185-15190.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15185-15190
    • Yokota, T.1
  • 16
    • 0030967165 scopus 로고    scopus 로고
    • A controlled trial of selegiline, alpha-tocopherol, or both as treatment for Alzheimer's disease. The Alzheimer's Disease Cooperative Study
    • Sano, M., et al. 1997. A controlled trial of selegiline, alpha-tocopherol, or both as treatment for Alzheimer's disease. The Alzheimer's Disease Cooperative Study. N. Engl. J. Med. 336:1216-1222.
    • (1997) N. Engl. J. Med. , vol.336 , pp. 1216-1222
    • Sano, M.1
  • 17
    • 0035007860 scopus 로고    scopus 로고
    • A double-blind, placebo-controlled randomized clinical trial of alpha-tocopherol (vitamin E) in the treatment of amyotrophic lateral sclerosis
    • ALS riluzole-tocopherol Study Group
    • Desnuelle, C., Dib, M., Garrel, C., and Favier, A. 2001. A double-blind, placebo-controlled randomized clinical trial of alpha-tocopherol (vitamin E) in the treatment of amyotrophic lateral sclerosis. ALS riluzole-tocopherol Study Group. Amyotroph. Lateral Scler. Other Motor Neuron Disord. 2:9-18.
    • (2001) Amyotroph. Lateral Scler. Other Motor Neuron Disord. , vol.2 , pp. 9-18
    • Desnuelle, C.1    Dib, M.2    Garrel, C.3    Favier, A.4
  • 18
    • 0035949516 scopus 로고    scopus 로고
    • Dehydroascorbic acid, a blood-brain barrier transportable form of vitamin C, mediates potent cerebroprotection in experimental stroke
    • Huang, J., et al. 2001. Dehydroascorbic acid, a blood-brain barrier transportable form of vitamin C, mediates potent cerebroprotection in experimental stroke. Proc. Natl. Acad. Sci. USA. 98:11720-11724.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11720-11724
    • Huang, J.1
  • 19
    • 85047699109 scopus 로고    scopus 로고
    • Ascorbic-acid transporter Slc23a1 is essential for vitamin C transport into brain and for perinatal survival
    • Sotiriou, S., et al. 2002. Ascorbic-acid transporter Slc23a1 is essential for vitamin C transport into brain and for perinatal survival. Nat. Med. 8:514-517.
    • (2002) Nat. Med. , vol.8 , pp. 514-517
    • Sotiriou, S.1
  • 20
    • 0033601338 scopus 로고    scopus 로고
    • Cu(II) potentiation of Alzheimer Abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction
    • Huang, X., et al. 1999. Cu(II) potentiation of Alzheimer Abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction. J. Biol. Chem. 274:37111-37116.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37111-37116
    • Huang, X.1
  • 21
    • 0033638815 scopus 로고    scopus 로고
    • Amyloid precursor proteins inhibit heme oxygenase activity and augment neurotoxicity in Alzheimer's disease
    • Takahashi, M., et al. 2000. Amyloid precursor proteins inhibit heme oxygenase activity and augment neurotoxicity in Alzheimer's disease. Neuron. 28:461-473.
    • (2000) Neuron. , vol.28 , pp. 461-473
    • Takahashi, M.1
  • 22
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny, R.A., et al. 2001. Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron. 30:665-676.
    • (2001) Neuron. , vol.30 , pp. 665-676
    • Cherny, R.A.1
  • 23
    • 0025911148 scopus 로고
    • Cold-induced brain edema and infarction are reduced in transgenic mice overexpressing Cu, Zn-superoxide dismutase
    • Chan, P.H., Yang, G.Y., Chen, S.F., Carlson, E., and Epstein, C.J. 1991. Cold-induced brain edema and infarction are reduced in transgenic mice overexpressing Cu, Zn-superoxide dismutase. Ann. Neurol. 29:482-486.
    • (1991) Ann. Neurol. , vol.29 , pp. 482-486
    • Chan, P.H.1    Yang, G.Y.2    Chen, S.F.3    Carlson, E.4    Epstein, C.J.5
  • 24
    • 0026583465 scopus 로고
    • Transgenic mice with increased Cu/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity
    • Przedborski, S., et al. 1992. Transgenic mice with increased Cu/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity. J. Neurosci. 12:1658-1667.
    • (1992) J. Neurosci. , vol.12 , pp. 1658-1667
    • Przedborski, S.1
  • 25
    • 0028899401 scopus 로고
    • Overexpressing Cu/Zn superoxide dismutase enhances survival of transplanted neurons in a rat model of Parkinson's disease
    • Nakao, N., et al. 1995. Overexpressing Cu/Zn superoxide dismutase enhances survival of transplanted neurons in a rat model of Parkinson's disease. Nat. Med. 1:226-231.
    • (1995) Nat. Med. , vol.1 , pp. 226-231
    • Nakao, N.1
  • 26
    • 17344371804 scopus 로고    scopus 로고
    • Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: Suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction
    • Keller, J.N., et al. 1998. Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction. J. Neurosci. 18:687-697.
    • (1998) J. Neurosci. , vol.18 , pp. 687-697
    • Keller, J.N.1
  • 27
    • 0029927787 scopus 로고    scopus 로고
    • Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthase-deficient mice
    • Dawson, V.L., Kizushi, V.M., Huang, P.L., Snyder, S.H., and Dawson, T.M. 1996. Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthase-deficient mice. J. Neurosci. 16:2479-2487.
    • (1996) J. Neurosci. , vol.16 , pp. 2479-2487
    • Dawson, V.L.1    Kizushi, V.M.2    Huang, P.L.3    Snyder, S.H.4    Dawson, T.M.5
  • 28
    • 0034977020 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase overexpression improves behavioral outcome from closed head injury in the mouse
    • Pineda, J.A., et al. 2001. Extracellular superoxide dismutase overexpression improves behavioral outcome from closed head injury in the mouse. J. Neurotrauma. 18:625-634.
    • (2001) J. Neurotrauma. , vol.18 , pp. 625-634
    • Pineda, J.A.1
  • 29
    • 0034722098 scopus 로고    scopus 로고
    • Prevention of 1-methyl-4-phenylpyridinium- and 6-hydroxydopamine-induced nitration of tyrosine hydroxylase and neurotoxicity by EUK-134, a superoxide dismutase and catalase mimetic, in cultured dopaminergic neurons
    • Pong, K., Doctrow, S.R., and Baudry, M. 2000. Prevention of 1-methyl-4-phenylpyridinium- and 6-hydroxydopamine-induced nitration of tyrosine hydroxylase and neurotoxicity by EUK-134, a superoxide dismutase and catalase mimetic, in cultured dopaminergic neurons. Brain Res. 881:182-189.
    • (2000) Brain Res. , vol.881 , pp. 182-189
    • Pong, K.1    Doctrow, S.R.2    Baudry, M.3
  • 30
    • 0028220114 scopus 로고
    • Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • Orr, W.C., and Sohal, R.S. 1994. Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science. 263:1128-1130.
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 31
    • 0034284973 scopus 로고    scopus 로고
    • Extension of life-span with superoxide dismutase/catalase mimetics
    • Melov, S., et al. 2000. Extension of life-span with superoxide dismutase/catalase mimetics. Science. 289:1567-1569.
    • (2000) Science , vol.289 , pp. 1567-1569
    • Melov, S.1
  • 32
    • 0031864164 scopus 로고    scopus 로고
    • Extension of Drosophila lifespan by overexpression of human SOD1 in motor neurons
    • Parkes, T.L., et al. 1998. Extension of Drosophila lifespan by overexpression of human SOD1 in motor neurons. Nat. Genet. 19:171-174.
    • (1998) Nat. Genet. , vol.19 , pp. 171-174
    • Parkes, T.L.1
  • 33
    • 0029908226 scopus 로고    scopus 로고
    • Origin and functional consequences of the complex I defect in Parkinson's disease
    • Swerdlow, R.H., et al. 1996. Origin and functional consequences of the complex I defect in Parkinson's disease. Ann. Neurol. 40:663-671.
    • (1996) Ann. Neurol. , vol.40 , pp. 663-671
    • Swerdlow, R.H.1
  • 34
    • 12644257598 scopus 로고    scopus 로고
    • Mutations in mitochondrial cytochrome c oxidase genes segregate with late-onset Alzheimer disease
    • Davis, R.E., et al. 1997. Mutations in mitochondrial cytochrome c oxidase genes segregate with late-onset Alzheimer disease. Proc. Natl. Acad. Sci. USA. 94:4526-4531.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4526-4531
    • Davis, R.E.1
  • 35
    • 17744417909 scopus 로고    scopus 로고
    • NADPH oxidase contributes directly to oxidative stress and apoptosis in nerve growth factor-deprived sympathetic neurons
    • Tammariello, S.P., Quinn, M.T., and Estus, S. 2000. NADPH oxidase contributes directly to oxidative stress and apoptosis in nerve growth factor-deprived sympathetic neurons. J. Neurosci. 20:RC53.
    • (2000) J. Neurosci. , vol.20
    • Tammariello, S.P.1    Quinn, M.T.2    Estus, S.3
  • 36
    • 0028641246 scopus 로고
    • Peroxynitrite versus hydroxyl radical: The role of nitric oxide in superoxide-dependent cerebral injury
    • C.C. Chiueh, D.L. Gilbert, and C.A. Colton, editors. New York Academy of Sciences. New York, New York, USA
    • Beckman, J.S. 1994. Peroxynitrite versus hydroxyl radical: the role of nitric oxide in superoxide-dependent cerebral injury. In The neurobiology of NO_and_OH. C.C. Chiueh, D.L. Gilbert, and C.A. Colton, editors. New York Academy of Sciences. New York, New York, USA. 69-75.
    • (1994) The Neurobiology of NO_and_OH , pp. 69-75
    • Beckman, J.S.1
  • 37
    • 0017240322 scopus 로고
    • Studies on the chlorinating activity of myeloperoxidase
    • Harrison, J.E., and Schultz, J. 1976. Studies on the chlorinating activity of myeloperoxidase. J. Biol. Chem. 251:1371-1374.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1371-1374
    • Harrison, J.E.1    Schultz, J.2
  • 38
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: Defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and meyloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan, M.L., et al. 2002. A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and meyloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J. Biol. Chem. 277:17415-17427.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17415-17427
    • Brennan, M.L.1
  • 39
    • 0029844003 scopus 로고    scopus 로고
    • Inhibition of neuronal nitric oxide synthase prevents MPTP-induced parkinsonism in baboons
    • Hantraye, P., et al. 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
  • 40
    • 0033565586 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase activation and peroxynitrite formation in ischemic stroke linked to neural damage
    • Eliasson, M.J., et al. 1999. Neuronal nitric oxide synthase activation and peroxynitrite formation in ischemic stroke linked to neural damage. J. Neurosci. 19:5910-5918.
    • (1999) J. Neurosci. , vol.19 , pp. 5910-5918
    • Eliasson, M.J.1
  • 41
    • 16944366580 scopus 로고    scopus 로고
    • Mechanisms of reduced striatal NMDA excitotoxicity in type I nitric oxide synthase knock-out mice
    • Ayata, C., et al. 1997. Mechanisms of reduced striatal NMDA excitotoxicity in type I nitric oxide synthase knock-out mice. J. Neurosci. 17:6908-6917.
    • (1997) J. Neurosci. , vol.17 , pp. 6908-6917
    • Ayata, C.1
  • 42
    • 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., et al. 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
  • 43
    • 0032710609 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase stimulates dopaminergic neurodegeneration in the MPTP model of Parkinson disease
    • Liberatore, G.T., et al. 1999. Inducible nitric oxide synthase stimulates dopaminergic neurodegeneration in the MPTP model of Parkinson disease. Nat. Med. 5:1403-1409.
    • (1999) Nat. Med. , vol.5 , pp. 1403-1409
    • Liberatore, G.T.1
  • 44
    • 10244235267 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase in tangle-beating neurons of patients with Alzheimer's disease
    • Vodovotz, Y., et al. 1996. Inducible nitric oxide synthase in tangle-beating neurons of patients with Alzheimer's disease. J. Exp. Med. 184:1425-1433.
    • (1996) J. Exp. Med. , vol.184 , pp. 1425-1433
    • Vodovotz, Y.1
  • 45
    • 0034548047 scopus 로고    scopus 로고
    • The peroxynitrite scavenger uric acid prevents inflammatory cell invasion into central nervous system in experimental allergic encephalomyelitis through maintenance of blood-central nervous system barrier integrity
    • Kean, R.B., Spitsin, S.V., Mikheeva, T., Scott, G.S., and Hooper, D.C. 2000. The peroxynitrite scavenger uric acid prevents inflammatory cell invasion into central nervous system in experimental allergic encephalomyelitis through maintenance of blood-central nervous system barrier integrity. J. Immunol. 165:6511-6518.
    • (2000) J. Immunol. , vol.165 , pp. 6511-6518
    • Kean, R.B.1    Spitsin, S.V.2    Mikheeva, T.3    Scott, G.S.4    Hooper, D.C.5
  • 46
    • 0346232735 scopus 로고    scopus 로고
    • Uric acid protects neurons against excitotoxic and metabolic insults in cell culture, and against focal ischemic brain injury in vivo
    • Yu, Z.F., Bruce-Keller, A.J., Goodman, Y., and Mattson, M.P. 1998. Uric acid protects neurons against excitotoxic and metabolic insults in cell culture, and against focal ischemic brain injury in vivo. J. Neurosci. Res. 53:613-625.
    • (1998) J. Neurosci. Res. , vol.53 , pp. 613-625
    • Yu, Z.F.1    Bruce-Keller, A.J.2    Goodman, Y.3    Mattson, M.P.4
  • 47
    • 0036522967 scopus 로고    scopus 로고
    • Blockade of microglial activation is neuroprotective in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model of Parkinson disease
    • Wu, D.C., et al. 2002. Blockade of microglial activation is neuroprotective in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model of Parkinson disease. J. Neurosci. 22:1763-1771.
    • (2002) J. Neurosci. , vol.22 , pp. 1763-1771
    • Wu, D.C.1
  • 48
    • 0037007645 scopus 로고    scopus 로고
    • Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice
    • Zhu, S., et al. 2002. Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice. Nature. 417:74-78.
    • (2002) Nature , vol.417 , pp. 74-78
    • Zhu, S.1
  • 49
    • 0036584232 scopus 로고    scopus 로고
    • Peroxynitrite mediates neurotoxicity of amyloid beta-peptide1-42- and lipopolysaccharide-activated microglia
    • Xie, Z., et al. 2002. Peroxynitrite mediates neurotoxicity of amyloid beta-peptide1-42- and lipopolysaccharide-activated microglia. J. Neurosci. 22:3484-3492.
    • (2002) J. Neurosci. , vol.22 , pp. 3484-3492
    • Xie, Z.1
  • 50
    • 0033681149 scopus 로고    scopus 로고
    • Chronic systemic pesticide exposure reproduces features of Parkinson's disease
    • Betarbet, R., et al. 2000. Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nat. Neurosci. 3:1301-1306.
    • (2000) Nat. Neurosci. , vol.3 , pp. 1301-1306
    • Betarbet, R.1
  • 51
    • 0037127197 scopus 로고    scopus 로고
    • The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: Paraquat and alpha-synuclein
    • Manning-Bog, A.B., et al. 2002. The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein. J. Biol. Chem. 277:1641-1644.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1641-1644
    • Manning-Bog, A.B.1
  • 52
    • 0037085288 scopus 로고    scopus 로고
    • Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors
    • Lee, H.J., Shin, S.Y., Choi, C., Lee, Y.H., and Lee, S.J. 2002. Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors. J. Biol. Chem. 277:5411-5417.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5411-5417
    • Lee, H.J.1    Shin, S.Y.2    Choi, C.3    Lee, Y.H.4    Lee, S.J.5
  • 53
    • 0035887860 scopus 로고    scopus 로고
    • Induction of alpha-synuclein aggregation by intracellular nitrative insult
    • Paxinou, E., et al. 2001. Induction of alpha-synuclein aggregation by intracellular nitrative insult. J. Neurosci. 21:8053-8061.
    • (2001) J. Neurosci. , vol.21 , pp. 8053-8061
    • Paxinou, E.1
  • 54
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos, M.H., et al. 1997. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science. 276:2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1
  • 55
    • 0030882856 scopus 로고    scopus 로고
    • Alpha-synuclein in Lewy bodies
    • Spillantini, M.G., et al. 1997. Alpha-synuclein in Lewy bodies. Nature. 388:839-840.
    • (1997) Nature , vol.388 , pp. 839-840
    • Spillantini, M.G.1
  • 56
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto, M., et al. 1999. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport. 10:717-721.
    • (1999) Neuroreport , vol.10 , pp. 717-721
    • Hashimoto, M.1
  • 57
    • 0034663039 scopus 로고    scopus 로고
    • The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity
    • Ostrerova-Golts, N., et al. 2000. The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity. J. Neurosci. 20:6048-6054.
    • (2000) J. Neurosci. , vol.20 , pp. 6048-6054
    • Ostrerova-Golts, N.1
  • 58
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • Souza, J.M., Giasson, B.I., Chen, Q., Lee, V.M., and Ischiropoulos, H. 2000. Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 275:18344-18349.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 60
    • 0034326816 scopus 로고    scopus 로고
    • Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity
    • Tabrizi, S.J., et al. 2000. Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity. Hum. Mol. Genet. 9:2683-2689.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2683-2689
    • Tabrizi, S.J.1
  • 61
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of alpha-synuclein: A mechanism for selective neurodegeneration in Parkinson disease
    • Xu, J., et al. 2002. Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat. Med. 8:600-606.
    • (2002) Nat. Med. , vol.8 , pp. 600-606
    • Xu, J.1
  • 62
    • 0029933450 scopus 로고    scopus 로고
    • Role of oxidation in the neurotoxic effects of intrastriatal dopamine injections
    • Hastings, T.G., Lewis, D.A., and Zigmond, M.J. 1996. Role of oxidation in the neurotoxic effects of intrastriatal dopamine injections. Proc. Natl. Acad. Sci. USA. 93:1956-1961.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1956-1961
    • Hastings, T.G.1    Lewis, D.A.2    Zigmond, M.J.3
  • 63
    • 0035066885 scopus 로고    scopus 로고
    • Direct binding and functional coupling of a-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
    • Lee, F.J.S., Liu, F., Pristupa, Z.B., and Niznik, H.B. 2001. Direct binding and functional coupling of a-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB J. 15:916-926.
    • (2001) FASEB J. , vol.15 , pp. 916-926
    • Lee, F.J.S.1    Liu, F.2    Pristupa, Z.B.3    Niznik, H.B.4
  • 64
    • 0037092442 scopus 로고    scopus 로고
    • A role for a-synuclein in the regulation of dopamine biosynthesis
    • Perez, R.G., et al. 2002. A role for a-synuclein in the regulation of dopamine biosynthesis. J. Neurosci. 22:3090-3099.
    • (2002) J. Neurosci. , vol.22 , pp. 3090-3099
    • Perez, R.G.1
  • 65
    • 0034624017 scopus 로고    scopus 로고
    • The parkinsonism-inducing drug 1-methyl-4-phenylpyridinium triggers intracellular dopamine oxidation. A novel mechanism of toxicity
    • Lotharius, J., and O'Malley, K.L. 2000. The parkinsonism-inducing drug 1-methyl-4-phenylpyridinium triggers intracellular dopamine oxidation. A novel mechanism of toxicity. J. Biol. Chem. 275:38581-38588.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38581-38588
    • Lotharius, J.1    O'Malley, K.L.2
  • 66
    • 0034077041 scopus 로고    scopus 로고
    • Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system
    • Abeliovich, A., et al. 2000. Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron. 25:239-252.
    • (2000) Neuron. , vol.25 , pp. 239-252
    • Abeliovich, A.1
  • 67
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway, K.A., Rochet, J.C., Bieganski, R.M., and Lansbury, P.T., Jr. 2001. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science. 294:1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury P.T., Jr.4
  • 68
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation
    • Gurney, M.E., et al. 1994. Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science. 264:1772-1775.
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1
  • 69
    • 0034696741 scopus 로고    scopus 로고
    • Toxicity of ALS-linked SOD1 mutants
    • Williamson, T.L., et al. 2000. Toxicity of ALS-linked SOD1 mutants. Science. 288:399.
    • (2000) Science , vol.288 , pp. 399
    • Williamson, T.L.1
  • 70
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow, J.P., et al. 1997. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69:1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1
  • 71
    • 0039251419 scopus 로고    scopus 로고
    • Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase
    • Estévez, A.G., et al. 1999. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science. 286:2498-2500.
    • (1999) Science , vol.286 , pp. 2498-2500
    • Estévez, A.G.1
  • 72
    • 0031890108 scopus 로고    scopus 로고
    • Nitric oxide and superoxide contribute to motor neuron apoptosis induced by trophic factor deprivation
    • Estévez, A.G., et al. 1998. Nitric oxide and superoxide contribute to motor neuron apoptosis induced by trophic factor deprivation. J. Neurosci. 18:923-931.
    • (1998) J. Neurosci. , vol.18 , pp. 923-931
    • Estévez, A.G.1
  • 73
    • 0036212119 scopus 로고    scopus 로고
    • Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading
    • Subramaniam, J.R., et al. 2002. Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading. Nat. Neurosci. 5:301-307.
    • (2002) Nat. Neurosci. , vol.5 , pp. 301-307
    • Subramaniam, J.R.1
  • 74
    • 0036144231 scopus 로고    scopus 로고
    • Peroxynitrite triggers a phenotypic transformation in spinal cord astrocytes that induces motor neuron apoptosis
    • Cassina, P., et al. 2002. Peroxynitrite triggers a phenotypic transformation in spinal cord astrocytes that induces motor neuron apoptosis. J. Neurosci. Res. 67:21-29.
    • (2002) J. Neurosci. Res. , vol.67 , pp. 21-29
    • Cassina, P.1
  • 75
    • 0034941118 scopus 로고    scopus 로고
    • Mutation in the gene encoding ferritin light polypeptide causes dominant adult-onset basal ganglia disease
    • Curtis, A.R., et al. 2001. Mutation in the gene encoding ferritin light polypeptide causes dominant adult-onset basal ganglia disease. Nat. Genet. 28:350-354.
    • (2001) Nat. Genet. , vol.28 , pp. 350-354
    • Curtis, A.R.1
  • 76
    • 0034935036 scopus 로고    scopus 로고
    • A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome
    • Zhou, B., et al. 2001. A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat. Genet. 28:345-349.
    • (2001) Nat. Genet. , vol.28 , pp. 345-349
    • Zhou, B.1


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