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Volumn 1780, Issue 11, 2008, Pages 1362-1367

Redox imbalance in Parkinson's disease

Author keywords

Dopaminergic neuron; Glutathione; Iron; Mitochondrial dysfunction; Oxidative stress; Parkinson's disease

Indexed keywords

5 [4 (2 HYDROXY)PIPERAZIN 1 YLMETHYL]QUINOLIN 8 OL; ALPHA SYNUCLEIN; CANNABIS; CARNITINE; CHELATING AGENT; DOPAMINE; ESTROGEN; GINKGO BILOBA EXTRACT; GLUTATHIONE; IRON; NICOTINAMIDE; QUINOLINE DERIVATIVE; RASAGILINE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIDECARENONE; UNCLASSIFIED DRUG; VK 28;

EID: 49349106093     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.02.005     Document Type: Review
Times cited : (241)

References (92)
  • 2
    • 0015745743 scopus 로고
    • Brain dopamine and the syndromes of Parkinson and Huntington. Clinical, morphological and neurochemical correlations
    • Bernheimer H., Birkmayer W., Hornykiewicz O., Jellinger K., and Seitelberger F. Brain dopamine and the syndromes of Parkinson and Huntington. Clinical, morphological and neurochemical correlations. J. Neurol. Sci. 20 (1973) 415-455
    • (1973) J. Neurol. Sci. , vol.20 , pp. 415-455
    • Bernheimer, H.1    Birkmayer, W.2    Hornykiewicz, O.3    Jellinger, K.4    Seitelberger, F.5
  • 4
    • 24944525045 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson's disease
    • Gandhi S., and Wood N.W. Molecular pathogenesis of Parkinson's disease. Hum. Mol. Genet. 14 Spec No. 2 (2005) 2749-2755
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.Spec 2 , pp. 2749-2755
    • Gandhi, S.1    Wood, N.W.2
  • 5
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin M.T., and Beal M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 7113 (Oct 19 2006) 787-795
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 6
    • 0037379314 scopus 로고    scopus 로고
    • Bioenergetic approaches for neuroprotection in Parkinson's disease
    • discussion S47-38
    • Beal M.F. Bioenergetic approaches for neuroprotection in Parkinson's disease. Ann. Neurol. 53 Suppl 3 (2003) S39-S47 discussion S47-38
    • (2003) Ann. Neurol. , vol.53 , Issue.SUPPL. 3
    • Beal, M.F.1
  • 7
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: cause or consequence?
    • Suppl
    • Andersen J.K. Oxidative stress in neurodegeneration: cause or consequence?. Nat Med 10 (2004) S18-S25 Suppl
    • (2004) Nat Med , vol.10
    • Andersen, J.K.1
  • 10
    • 0033624419 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in aging and neurodegenerative disease
    • Albers D.S., and Beal M.F. Mitochondrial dysfunction and oxidative stress in aging and neurodegenerative disease. J. Neural Transm., Suppl. 59 (2000) 133-154
    • (2000) J. Neural Transm., Suppl. , vol.59 , pp. 133-154
    • Albers, D.S.1    Beal, M.F.2
  • 11
    • 0024848034 scopus 로고
    • Abnormalities of the electron transport chain in idiopathic Parkinson's disease
    • Parker Jr. W.D., Boyson S.J., and Parks J.K. Abnormalities of the electron transport chain in idiopathic Parkinson's disease. Ann. Neurol. 26 (1989) 719-723
    • (1989) Ann. Neurol. , vol.26 , pp. 719-723
    • Parker Jr., W.D.1    Boyson, S.J.2    Parks, J.K.3
  • 13
    • 0026718086 scopus 로고
    • Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease
    • Mann V.M., Cooper J.M., Krige D., Daniel S.E., Schapira A.H., and Marsden C.D. Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease. Brain 115 Pt 2 (1992) 333-342
    • (1992) Brain , vol.115 , Issue.PART 2 , 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
  • 15
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal M.F. Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol. 58 (2005) 495-505
    • (2005) Ann. Neurol. , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 17
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller F.L., Liu Y., and Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279 (2004) 49064-49073
    • (2004) J. Biol. Chem. , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 18
    • 0034680558 scopus 로고    scopus 로고
    • A detailed interpretation of OH radical footprints in a TBP-DNA complex reveals the role of dynamics in the mechanism of sequence-specific binding
    • Pastor N., Weinstein H., Jamison E., and Brenowitz M. A detailed interpretation of OH radical footprints in a TBP-DNA complex reveals the role of dynamics in the mechanism of sequence-specific binding. J. Mol. Biol. 304 (2000) 55-68
    • (2000) J. Mol. Biol. , vol.304 , pp. 55-68
    • Pastor, N.1    Weinstein, H.2    Jamison, E.3    Brenowitz, M.4
  • 19
    • 0036499736 scopus 로고    scopus 로고
    • Involvement of inducible nitric oxide synthase in inflammation-induced dopaminergic neurodegeneration
    • Iravani M.M., Kashefi K., Mander P., Rose S., and Jenner P. Involvement of inducible nitric oxide synthase in inflammation-induced dopaminergic neurodegeneration. Neuroscience 110 (2002) 49-58
    • (2002) Neuroscience , vol.110 , pp. 49-58
    • Iravani, M.M.1    Kashefi, K.2    Mander, P.3    Rose, S.4    Jenner, P.5
  • 20
    • 0033927959 scopus 로고    scopus 로고
    • Oxidation of LDL by myeloperoxidase and reactive nitrogen species: reaction pathways and antioxidant protection
    • Carr A.C., McCall M.R., and Frei B. Oxidation of LDL by myeloperoxidase and reactive nitrogen species: reaction pathways and antioxidant protection. Arterioscler Thromb Vasc Biol 20 (2000) 1716-1723
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 1716-1723
    • Carr, A.C.1    McCall, M.R.2    Frei, B.3
  • 21
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • discussion S36-28
    • Jenner P. Oxidative stress in Parkinson's disease. Ann. Neurol. 53 Suppl 3 (2003) S26-S36 discussion S36-28
    • (2003) Ann. Neurol. , vol.53 , Issue.SUPPL. 3
    • Jenner, P.1
  • 22
    • 0033521095 scopus 로고    scopus 로고
    • Mass spectrometric quantification of 3-nitrotyrosine, orthotyrosine, and o, o-dityrosine in brain tissue of 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine-treated mice, a model of oxidative stress in Parkinson's disease
    • Pennathur S., Jackson-Lewis V., Przedborski S., and Heinecke J.W. Mass spectrometric quantification of 3-nitrotyrosine, orthotyrosine, and o, o-dityrosine in brain tissue of 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine-treated mice, a model of oxidative stress in Parkinson's disease. J. Biol. Chem. 274 (1999) 34621-34628
    • (1999) J. Biol. Chem. , vol.274 , pp. 34621-34628
    • Pennathur, S.1    Jackson-Lewis, V.2    Przedborski, S.3    Heinecke, J.W.4
  • 23
    • 0033608739 scopus 로고    scopus 로고
    • Increased nitrotyrosine immunoreactivity in substantia nigra neurons in MPTP treated baboons is blocked by inhibition of neuronal nitric oxide synthase
    • Ferrante R.J., Hantraye P., Brouillet E., and Beal M.F. Increased nitrotyrosine immunoreactivity in substantia nigra neurons in MPTP treated baboons is blocked by inhibition of neuronal nitric oxide synthase. Brain Res. 823 (1999) 177-182
    • (1999) Brain Res. , vol.823 , pp. 177-182
    • Ferrante, R.J.1    Hantraye, P.2    Brouillet, E.3    Beal, M.F.4
  • 25
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E., Brown G.C., Feelisch M., and Moncada S. Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 7631-7636
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 26
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry
    • Murray J., Taylor S.W., Zhang B., Ghosh S.S., and Capaldi R.A. Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry. J. Biol. Chem. 278 (2003) 37223-37230
    • (2003) J. Biol. Chem. , vol.278 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3    Ghosh, S.S.4    Capaldi, R.A.5
  • 27
    • 22044436635 scopus 로고    scopus 로고
    • Glutathione depletion in a midbrain-derived immortalized dopaminergic cell line results in limited tyrosine nitration of mitochondrial complex I subunits: implications for Parkinson's disease
    • Bharath S., and Andersen J.K. Glutathione depletion in a midbrain-derived immortalized dopaminergic cell line results in limited tyrosine nitration of mitochondrial complex I subunits: implications for Parkinson's disease. Antioxid. Redox Signal. 7 7-8 (Jul-Aug 2005) 900-910
    • (2005) Antioxid. Redox Signal. , vol.7 , Issue.7-8 , pp. 900-910
    • Bharath, S.1    Andersen, J.K.2
  • 28
    • 33749047253 scopus 로고    scopus 로고
    • Reversible inhibition of mitochondrial complex I activity following chronic dopaminergic glutathione depletion in vitro: implications for Parkinson's disease
    • Chinta S.J., and Andersen J.K. Reversible inhibition of mitochondrial complex I activity following chronic dopaminergic glutathione depletion in vitro: implications for Parkinson's disease. Free Radic. Biol. Med. 41 9 (Nov 1 2006) 1442-1448
    • (2006) Free Radic. Biol. Med. , vol.41 , Issue.9 , pp. 1442-1448
    • Chinta, S.J.1    Andersen, J.K.2
  • 29
    • 0029751104 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of Parkinson's disease
    • Jenner P., and Olanow C.W. Oxidative stress and the pathogenesis of Parkinson's disease. Neurology 47 (1996) S161-S170
    • (1996) Neurology , vol.47
    • Jenner, P.1    Olanow, C.W.2
  • 30
    • 0030641754 scopus 로고    scopus 로고
    • Understanding Parkinson's disease
    • Youdim M.B., and Riederer P. Understanding Parkinson's disease. Sci Am 276 (1997) 52-59
    • (1997) Sci Am , vol.276 , pp. 52-59
    • Youdim, M.B.1    Riederer, P.2
  • 32
    • 8644252682 scopus 로고    scopus 로고
    • Inhibition of brain mitochondrial respiration by dopamine and its metabolites: implications for Parkinson's disease and catecholamine-associated diseases
    • Gluck M.R., and Zeevalk G.D. Inhibition of brain mitochondrial respiration by dopamine and its metabolites: implications for Parkinson's disease and catecholamine-associated diseases. J. Neurochem. 91 4 (Nov 2004) 788-795
    • (2004) J. Neurochem. , vol.91 , Issue.4 , pp. 788-795
    • Gluck, M.R.1    Zeevalk, G.D.2
  • 33
    • 0020308323 scopus 로고
    • Parkinson's disease: a disorder due to nigral glutathione deficiency?
    • Perry T.L., Godin D.V., and Hansen S. Parkinson's disease: a disorder due to nigral glutathione deficiency?. Neurosci. Lett. 33 (1982) 305-310
    • (1982) Neurosci. Lett. , vol.33 , pp. 305-310
    • Perry, T.L.1    Godin, D.V.2    Hansen, S.3
  • 34
    • 0022553605 scopus 로고
    • Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients
    • Perry T.L., and Yong V.W. Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients. Neurosci. Lett. 67 (1986) 269-274
    • (1986) Neurosci. Lett. , vol.67 , pp. 269-274
    • Perry, T.L.1    Yong, V.W.2
  • 35
    • 0030724621 scopus 로고    scopus 로고
    • Alterations in the distribution of glutathione in the substantia nigra in Parkinson's disease
    • Pearce R.K., Owen A., Daniel S., Jenner P., and Marsden C.D. Alterations in the distribution of glutathione in the substantia nigra in Parkinson's disease. J. Neural Transm. 104 (1997) 661-677
    • (1997) J. Neural Transm. , vol.104 , pp. 661-677
    • Pearce, R.K.1    Owen, A.2    Daniel, S.3    Jenner, P.4    Marsden, C.D.5
  • 36
    • 0027329923 scopus 로고
    • Presymptomatic detection of Parkinson's disease
    • Jenner P. Presymptomatic detection of Parkinson's disease. J. Neural Transm., Suppl. 40 (1993) 23-36
    • (1993) J. Neural Transm., Suppl. , vol.40 , pp. 23-36
    • Jenner, P.1
  • 37
    • 0029751104 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of Parkinson's disease
    • Jenner P., and Olanow C.W. Oxidative stress and the pathogenesis of Parkinson's disease. Neurology 47 (1996) S161-S170
    • (1996) Neurology , vol.47
    • Jenner, P.1    Olanow, C.W.2
  • 38
    • 0034714346 scopus 로고    scopus 로고
    • Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease
    • Jha N., Jurma O., Lalli G., Liu Y., Pettus E.H., Greenamyre J.T., Liu R.M., Forman H.J., and Andersen J.K. Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease. J. Biol. Chem. 275 (2000) 26096-26101
    • (2000) J. Biol. Chem. , vol.275 , pp. 26096-26101
    • Jha, N.1    Jurma, O.2    Lalli, G.3    Liu, Y.4    Pettus, E.H.5    Greenamyre, J.T.6    Liu, R.M.7    Forman, H.J.8    Andersen, J.K.9
  • 39
    • 38449097902 scopus 로고    scopus 로고
    • Inducible alterations of glutathione levels in adult dopaminergic midbrain neurons results in nigrostriatal degeneration
    • Chinta S.J., kumar M.J., Hsu M., Rajagopalan S., Kaur D., Rane A., Nicholls D.G., Choi J., and Andersen J.K. Inducible alterations of glutathione levels in adult dopaminergic midbrain neurons results in nigrostriatal degeneration. J. Neurosci. 27 51 (Dec 19 2007) 13997-14006
    • (2007) J. Neurosci. , vol.27 , Issue.51 , pp. 13997-14006
    • Chinta, S.J.1    kumar, M.J.2    Hsu, M.3    Rajagopalan, S.4    Kaur, D.5    Rane, A.6    Nicholls, D.G.7    Choi, J.8    Andersen, J.K.9
  • 40
    • 0029970099 scopus 로고    scopus 로고
    • Depletion of brain glutathione results in a decrease of glutathione reductase activity; an enzyme susceptible to oxidative damage
    • Barker J.E., Heales S.J., Cassidy A., Bolanos J.P., Land J.M., and Clark J.B. Depletion of brain glutathione results in a decrease of glutathione reductase activity; an enzyme susceptible to oxidative damage. Brain Res. 716 (1996) 118-122
    • (1996) Brain Res. , vol.716 , pp. 118-122
    • Barker, J.E.1    Heales, S.J.2    Cassidy, A.3    Bolanos, J.P.4    Land, J.M.5    Clark, J.B.6
  • 41
    • 0036813225 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) mediates recovery of motor neurons from excitotoxic mitochondrial injury
    • Kenchappa R.S., Diwakar L., Boyd M.R., and Ravindranath V. Thioltransferase (glutaredoxin) mediates recovery of motor neurons from excitotoxic mitochondrial injury. J. Neurosci. 22 (2002) 8402-8410
    • (2002) J. Neurosci. , vol.22 , pp. 8402-8410
    • Kenchappa, R.S.1    Diwakar, L.2    Boyd, M.R.3    Ravindranath, V.4
  • 42
    • 0032842038 scopus 로고    scopus 로고
    • Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: implications for Parkinson's disease
    • Berman S.B., and Hastings T.G. Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: implications for Parkinson's disease. J. Neurochem. 73 (1999) 1127-1137
    • (1999) J. Neurochem. , vol.73 , pp. 1127-1137
    • Berman, S.B.1    Hastings, T.G.2
  • 43
    • 0028215392 scopus 로고
    • Effects of l-cysteine on the oxidation chemistry of dopamine: new reaction pathways of potential relevance to idiopathic Parkinson's disease
    • Zhang F., and Dryhurst G. Effects of l-cysteine on the oxidation chemistry of dopamine: new reaction pathways of potential relevance to idiopathic Parkinson's disease. J. Med. Chem. 37 (1994) 1084-1098
    • (1994) J. Med. Chem. , vol.37 , pp. 1084-1098
    • Zhang, F.1    Dryhurst, G.2
  • 44
    • 0031722906 scopus 로고    scopus 로고
    • Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species
    • Spencer J.P., Jenner P., Daniel S.E., Lees A.J., Marsden D.C., and Halliwell B. Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species. J. Neurochem. 71 (1998) 2112-2122
    • (1998) J. Neurochem. , vol.71 , pp. 2112-2122
    • Spencer, J.P.1    Jenner, P.2    Daniel, S.E.3    Lees, A.J.4    Marsden, D.C.5    Halliwell, B.6
  • 45
    • 4644285991 scopus 로고    scopus 로고
    • Perspectives on MAO-B in aging and neurological disease: where do we go from here?
    • Kumar M.J., and Andersen J.K. Perspectives on MAO-B in aging and neurological disease: where do we go from here?. Mol. Neurobiol. 30 (2004) 77-89
    • (2004) Mol. Neurobiol. , vol.30 , pp. 77-89
    • Kumar, M.J.1    Andersen, J.K.2
  • 46
    • 0023942459 scopus 로고
    • Localization of distinct monoamine oxidase A and monoamine oxidase B cell populations in human brainstem
    • Westlund K.N., Denney R.M., Rose R.M., and Abell C.W. Localization of distinct monoamine oxidase A and monoamine oxidase B cell populations in human brainstem. Neuroscience 25 (1988) 439-456
    • (1988) Neuroscience , vol.25 , pp. 439-456
    • Westlund, K.N.1    Denney, R.M.2    Rose, R.M.3    Abell, C.W.4
  • 48
    • 0027344414 scopus 로고
    • Recent advances in pharmacological therapy of Parkinson's disease
    • Riederer P., Lange K.W., and Youdim M.B. Recent advances in pharmacological therapy of Parkinson's disease. Adv. Neurol. 60 (1993) 626-635
    • (1993) Adv. Neurol. , vol.60 , pp. 626-635
    • Riederer, P.1    Lange, K.W.2    Youdim, M.B.3
  • 49
    • 3042654997 scopus 로고    scopus 로고
    • Does cellular iron dysregulation play a causative role in Parkinson's disease?
    • Kaur D., and Andersen J. Does cellular iron dysregulation play a causative role in Parkinson's disease?. Ageing Res. Rev. 3 (2004) 327-343
    • (2004) Ageing Res. Rev. , vol.3 , pp. 327-343
    • Kaur, D.1    Andersen, J.2
  • 50
    • 3042654997 scopus 로고    scopus 로고
    • Does cellular iron dysregulation play a causative role in Parkinson's disease?
    • Kaur D., and Andersen J. Does cellular iron dysregulation play a causative role in Parkinson's disease?. Ageing Res. Rev. 3 3 (Jul 2004) 327-343
    • (2004) Ageing Res. Rev. , vol.3 , Issue.3 , pp. 327-343
    • Kaur, D.1    Andersen, J.2
  • 51
    • 0030864433 scopus 로고    scopus 로고
    • Desferrioxamine and vitamin E protect against iron and MPTP-induced neurodegeneration in mice
    • Lan J., and Jiang D.H. Desferrioxamine and vitamin E protect against iron and MPTP-induced neurodegeneration in mice. J. Neural Trans. 104 (1997) 469-481
    • (1997) J. Neural Trans. , vol.104 , pp. 469-481
    • Lan, J.1    Jiang, D.H.2
  • 52
    • 0343550312 scopus 로고    scopus 로고
    • Apomorphine protects against MPTP-induced neurotoxicity in mice
    • Grunblatt E., Mandel S., Berkuzki T., and Youdim M.B. Apomorphine protects against MPTP-induced neurotoxicity in mice. Mov. Disord. 14 (1999) 612-618
    • (1999) Mov. Disord. , vol.14 , pp. 612-618
    • Grunblatt, E.1    Mandel, S.2    Berkuzki, T.3    Youdim, M.B.4
  • 54
    • 0030864433 scopus 로고    scopus 로고
    • Desferrioxamine and vitamin E protect against iron and MPTP-induced neurodegeneration in mice
    • Lan J., and Jiang D.H. Desferrioxamine and vitamin E protect against iron and MPTP-induced neurodegeneration in mice. J. Neural Trans. 104 (1997) 469-481
    • (1997) J. Neural Trans. , vol.104 , pp. 469-481
    • Lan, J.1    Jiang, D.H.2
  • 55
    • 0343550312 scopus 로고    scopus 로고
    • Apomorphine protects against MPTP-induced neurotoxicity in mice
    • Grunblatt E., Mandel S., Berkuzki T., and Youdim M.B. Apomorphine protects against MPTP-induced neurotoxicity in mice. Mov. Disord. 14 (1999) 612-618
    • (1999) Mov. Disord. , vol.14 , pp. 612-618
    • Grunblatt, E.1    Mandel, S.2    Berkuzki, T.3    Youdim, M.B.4
  • 58
    • 0032031011 scopus 로고    scopus 로고
    • Neural heme oxygenase-1 expression in idiopathic Parkinson's disease
    • Schipper H.M., Liberman A., and Stopa E.G. Neural heme oxygenase-1 expression in idiopathic Parkinson's disease. Exp. Neurol. 150 (1998) 60-68
    • (1998) Exp. Neurol. , vol.150 , pp. 60-68
    • Schipper, H.M.1    Liberman, A.2    Stopa, E.G.3
  • 59
    • 0034007822 scopus 로고    scopus 로고
    • Pathoanatomy of Parkinson's disease
    • Braak H., and Braak E. Pathoanatomy of Parkinson's disease. J Neurol 247 Suppl 2 (2000) II3-II10
    • (2000) J Neurol , vol.247 , Issue.SUPPL. 2
    • Braak, H.1    Braak, E.2
  • 63
    • 0037237927 scopus 로고    scopus 로고
    • Oxidative stress and nitration in neurodegeneration: cause, effect, or association?
    • Ischiropoulos H., and Beckman J.S. Oxidative stress and nitration in neurodegeneration: cause, effect, or association?. J. Clin. Invest. 111 (2003) 163-169
    • (2003) J. Clin. Invest. , vol.111 , pp. 163-169
    • Ischiropoulos, H.1    Beckman, J.S.2
  • 64
    • 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 Jr. P.T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294 (2001) 1346-1349
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 65
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein
    • Uversky V.N., Li J., and Fink A.L. Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. J. Biol. Chem. 23 276(47) (2001) 44284-44296
    • (2001) J. Biol. Chem. , vol.23 , Issue.276 47 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 66
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M., Hsu L.J., Xia Y., Takeda A., Sisk A., Sundsmo M., and Masliah E. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport 10 (1999) 717-721
    • (1999) Neuroreport , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6    Masliah, E.7
  • 67
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky V.N., Li J., and Fink A.L. Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 276 (2001) 44284-44296
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 70
    • 0038711511 scopus 로고    scopus 로고
    • Effects of oxidative and nitrative challenges on alpha-synuclein fibrillogenesis involve distinct mechanisms of protein modifications
    • Norris E.H., Giasson B.I., Ischiropoulos H., and Lee V.M. Effects of oxidative and nitrative challenges on alpha-synuclein fibrillogenesis involve distinct mechanisms of protein modifications. J. Biol. Chem. 278 (2003) 27230-27240
    • (2003) J. Biol. Chem. , vol.278 , pp. 27230-27240
    • Norris, E.H.1    Giasson, B.I.2    Ischiropoulos, H.3    Lee, V.M.4
  • 71
    • 33845746706 scopus 로고    scopus 로고
    • Ion channel blockade attenuates aggregated alpha synuclein induction of microglial reactive oxygen species: relevance for the pathogenesis of Parkinson's disease
    • Thomas M.P., Chartrand K., Reynolds A., Vitvitsky V., Banerjee R., and Gendelman H.E. Ion channel blockade attenuates aggregated alpha synuclein induction of microglial reactive oxygen species: relevance for the pathogenesis of Parkinson's disease. J. Neurochem. 100 (2007) 503-519
    • (2007) J. Neurochem. , vol.100 , pp. 503-519
    • Thomas, M.P.1    Chartrand, K.2    Reynolds, A.3    Vitvitsky, V.4    Banerjee, R.5    Gendelman, H.E.6
  • 72
    • 3142523288 scopus 로고    scopus 로고
    • Genetic clues to the pathogenesis of Parkinson's disease
    • Suppl
    • Vila M., and Przedborski S. Genetic clues to the pathogenesis of Parkinson's disease. Nat. Med. 10 (2004) S58-S62 Suppl
    • (2004) Nat. Med. , vol.10
    • Vila, M.1    Przedborski, S.2
  • 73
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M., Hsu L.J., Xia Y., Takeda A., Sisk A., Sundsmo M., and Masliah E. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport 10 (1999) 717-721
    • (1999) Neuroreport , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6    Masliah, E.7
  • 75
    • 0035066885 scopus 로고    scopus 로고
    • Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
    • Lee F.J., Liu F., Pristupa Z.B., and Niznik H.B. Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. Faseb J. 15 (2001) 916-926
    • (2001) Faseb J. , vol.15 , pp. 916-926
    • Lee, F.J.1    Liu, F.2    Pristupa, Z.B.3    Niznik, H.B.4
  • 80
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier T.C. Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. 36 (2001) 1539-1550
    • (2001) Exp. Gerontol. , vol.36 , pp. 1539-1550
    • Squier, T.C.1
  • 81
    • 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 R.J., Lorentz H., and Rinne U.K. Oxygen toxicity protecting enzymes in Parkinson's disease. Increase of superoxide dismutase-like activity in the substantia nigra and basal nucleus. J. Neurol. Sci. 86 (1988) 321-331
    • (1988) J. Neurol. Sci. , vol.86 , pp. 321-331
    • Marttila, R.J.1    Lorentz, H.2    Rinne, U.K.3
  • 82
    • 34249911463 scopus 로고    scopus 로고
    • Monamine oxidase inhibitors: current and emerging agents for Parkinson disease
    • Fernandez H.H., and Chen J.J. Monamine oxidase inhibitors: current and emerging agents for Parkinson disease. Clin. Neuropharmacol. 30 (2007) 150-168
    • (2007) Clin. Neuropharmacol. , vol.30 , pp. 150-168
    • Fernandez, H.H.1    Chen, J.J.2
  • 83
    • 11144316146 scopus 로고    scopus 로고
    • Bifunctional drug derivatives of MAO-B inhibitor rasagiline and iron chelator VK-28 as a more effective approach to treatment of brain ageing and ageing neurodegenerative diseases
    • Youdim M.B., Fridkin M., and Zheng H. Bifunctional drug derivatives of MAO-B inhibitor rasagiline and iron chelator VK-28 as a more effective approach to treatment of brain ageing and ageing neurodegenerative diseases. Mech. Ageing Dev. 126 (2005) 317-326
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 317-326
    • Youdim, M.B.1    Fridkin, M.2    Zheng, H.3
  • 84
    • 10244246626 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in Alzheimer's and Parkinson's diseases and coenzyme Q10 as a potential treatment
    • Beal M.F. Mitochondrial dysfunction and oxidative damage in Alzheimer's and Parkinson's diseases and coenzyme Q10 as a potential treatment. J. Bioenerg. Biomembr. 36 (2004) 381-386
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 381-386
    • Beal, M.F.1
  • 85
    • 33847105184 scopus 로고    scopus 로고
    • Advances in the treatment of Parkinson's disease
    • Singh N., Pillay V., and Choonara Y.E. Advances in the treatment of Parkinson's disease. Prog. Neurobiol. 81 (2007) 29-44
    • (2007) Prog. Neurobiol. , vol.81 , pp. 29-44
    • Singh, N.1    Pillay, V.2    Choonara, Y.E.3
  • 86
    • 1842621154 scopus 로고    scopus 로고
    • Iron and alpha-synuclein in the substantia nigra of MPTP-treated mice: effect of neuroprotective drugs R-apomorphine and green tea polyphenol (-)-epigallocatechin-3-gallate
    • Mandel S., Maor G., and Youdim M.B. Iron and alpha-synuclein in the substantia nigra of MPTP-treated mice: effect of neuroprotective drugs R-apomorphine and green tea polyphenol (-)-epigallocatechin-3-gallate. J. Mol. Neurosci. 24 (2004) 401-416
    • (2004) J. Mol. Neurosci. , vol.24 , pp. 401-416
    • Mandel, S.1    Maor, G.2    Youdim, M.B.3
  • 88
    • 33646796739 scopus 로고    scopus 로고
    • In vitro and in vivo neuroprotection by gamma-glutamylcysteine ethyl ester against MPTP: relevance to the role of glutathione in Parkinson's disease
    • Chinta S.J., Rajagopalan S., Butterfield D.A., and Andersen J.K. In vitro and in vivo neuroprotection by gamma-glutamylcysteine ethyl ester against MPTP: relevance to the role of glutathione in Parkinson's disease. Neurosci. Lett. 402 (2006) 137-141
    • (2006) Neurosci. Lett. , vol.402 , pp. 137-141
    • Chinta, S.J.1    Rajagopalan, S.2    Butterfield, D.A.3    Andersen, J.K.4
  • 89
    • 33846418007 scopus 로고    scopus 로고
    • Characterization of intracellular elevation of glutathione (GSH) with glutathione monoethyl ester and GSH in brain and neuronal cultures: relevance to Parkinson's disease
    • Zeevalk G.D., Manzino L., Sonsalla P.K., and Bernard L.P. Characterization of intracellular elevation of glutathione (GSH) with glutathione monoethyl ester and GSH in brain and neuronal cultures: relevance to Parkinson's disease. Exp. Neurol. 203 (2007) 512-520
    • (2007) Exp. Neurol. , vol.203 , pp. 512-520
    • Zeevalk, G.D.1    Manzino, L.2    Sonsalla, P.K.3    Bernard, L.P.4
  • 90
    • 0036778280 scopus 로고    scopus 로고
    • Pre-treatment with R-lipoic acid alleviates the effects of GSH depletion in PC12 cells: implications for Parkinson's disease therapy
    • Bharat S., Cochran B.C., Hsu M., Liu J., Ames B.N., and Andersen J.K. Pre-treatment with R-lipoic acid alleviates the effects of GSH depletion in PC12 cells: implications for Parkinson's disease therapy. Neurotoxicology 23 (2002) 479-486
    • (2002) Neurotoxicology , vol.23 , pp. 479-486
    • Bharat, S.1    Cochran, B.C.2    Hsu, M.3    Liu, J.4    Ames, B.N.5    Andersen, J.K.6
  • 91
    • 34347369328 scopus 로고    scopus 로고
    • Activation of apoptosis signal regulating kinase 1 (ASK1) and translocation of death-associated protein, Daxx, in substantia nigra pars compacta in a mouse model of Parkinson's disease: protection by alpha-lipoic acid
    • Karunakaran S., Diwakar L., Saeed U., Agarwal V., Ramakrishnan S., Iyengar S., and Ravindranath V. Activation of apoptosis signal regulating kinase 1 (ASK1) and translocation of death-associated protein, Daxx, in substantia nigra pars compacta in a mouse model of Parkinson's disease: protection by alpha-lipoic acid. Faseb J. 21 (2007) 2226-2236
    • (2007) Faseb J. , vol.21 , pp. 2226-2236
    • Karunakaran, S.1    Diwakar, L.2    Saeed, U.3    Agarwal, V.4    Ramakrishnan, S.5    Iyengar, S.6    Ravindranath, V.7


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