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Volumn 11, Issue 4, 2012, Pages 430-438

Mitochondria as an easy target to oxidative stress events in Parkinson's disease

Author keywords

Mitochondria; Oxidative stress; Parkinson's disease; Tyrosine hydroxylase

Indexed keywords

PARKIN; REACTIVE OXYGEN METABOLITE; TYROSINE 3 MONOOXYGENASE;

EID: 84862528681     PISSN: 18715273     EISSN: 19963181     Source Type: Journal    
DOI: 10.2174/187152712800792875     Document Type: Article
Times cited : (41)

References (106)
  • 2
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer, W.; Przedborski, S. Parkinson's disease: mechanisms and models. Neuron, 2003, 39, 889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 3
    • 36248938279 scopus 로고    scopus 로고
    • The pathogenesis of cell death in Parkinson's disease
    • Olanow, C.W. The pathogenesis of cell death in Parkinson's disease. Mov. Disord., 2007, 22, S335-S342.
    • (2007) Mov. Disord , vol.22
    • Olanow, C.W.1
  • 4
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson, M.P. Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol., 2000, 1, 120-129.
    • (2000) Nat. Rev. Mol. Cell Biol , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 5
    • 79959242100 scopus 로고    scopus 로고
    • Mitochondrial contribution to Parkinson's disease pathogenesis
    • Schapira, A.H.; Gegg, M. Mitochondrial contribution to Parkinson's disease pathogenesis. Parkinsons Dis., 2011, 2011, 159160.
    • (2011) Parkinsons Dis , vol.2011 , pp. 159160
    • Schapira, A.H.1    Gegg, M.2
  • 6
    • 67649319285 scopus 로고    scopus 로고
    • Mitochondria in the etiology of Parkinson's disease
    • Schapira, A.H. Mitochondria in the etiology of Parkinson's disease. Handb. Clin. Neurol., 2007, 83, 479-491.
    • (2007) Handb. Clin. Neurol , vol.83 , pp. 479-491
    • Schapira, A.H.1
  • 7
    • 80855139395 scopus 로고    scopus 로고
    • Mitochondrial pathology in Parkinson's disease
    • Schapira, A.H. Mitochondrial pathology in Parkinson's disease. Mt. Sinai J. Med., 2011, 78(6), 872-881.
    • (2011) Mt. Sinai J. Med , vol.78 , Issue.6 , pp. 872-881
    • Schapira, A.H.1
  • 8
    • 34247631275 scopus 로고    scopus 로고
    • Multiple hit hypotheses for dopamine neuron loss in Parkinson's disease
    • Sulzer, D. Multiple hit hypotheses for dopamine neuron loss in Parkinson's disease. Trends Neurosci., 2007, 30, 244-250.
    • (2007) Trends Neurosci , vol.30 , pp. 244-250
    • Sulzer, D.1
  • 9
    • 57649155208 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease: A mechanism of pathogenic and therapeutic significance
    • Zhou, C.; Huang, Y.; Przedborski, S. Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance. Ann. NY Acad. Sci., 2008, 1147, 93-104.
    • (2008) Ann. NY Acad. Sci , vol.1147 , pp. 93-104
    • Zhou, C.1    Huang, Y.2    Przedborski, S.3
  • 10
    • 77956228435 scopus 로고    scopus 로고
    • Novel cell death signaling pathways in neurotoxicity models of dopaminergic degeneration: Relevance to oxidative stress and neuroinflammation in Parkinson's disease
    • Kanthasamy, A.; Jin, H.; Mehrotra, S.; Mishra, R.; Kanthasamy, A.; Rana, A. Novel cell death signaling pathways in neurotoxicity models of dopaminergic degeneration: relevance to oxidative stress and neuroinflammation in Parkinson's disease. Neurotoxicology, 2010, 31(5), 555-561.
    • (2010) Neurotoxicology , vol.31 , Issue.5 , pp. 555-561
    • Kanthasamy, A.1    Jin, H.2    Mehrotra, S.3    Mishra, R.4    Kanthasamy, A.5    Rana, A.6
  • 11
    • 77956216928 scopus 로고    scopus 로고
    • Reactive oxygen species: Stuck in the middle of neurodegeneration
    • Patten, D.A.; Germain, M.; Kelly, M.A.; Slack, R.S. Reactive oxygen species: stuck in the middle of neurodegeneration. J. Alzheimers Dis., 2010, 20(Suppl 2), S357-S367.
    • (2010) J. Alzheimers Dis , vol.20 , Issue.SUPPL. 2
    • Patten, D.A.1    Germain, M.2    Kelly, M.A.3    Slack, R.S.4
  • 12
    • 63849244747 scopus 로고    scopus 로고
    • Increased oxidation of certain glycolysis and energy metabolism enzymes in the frontal cortex in Lewy body diseases
    • Gómez, A.; Ferrer, I. Increased oxidation of certain glycolysis and energy metabolism enzymes in the frontal cortex in Lewy body diseases. J. Neurosci. Res., 2009, 87(4), 1002-1013.
    • (2009) J. Neurosci. Res , vol.87 , Issue.4 , pp. 1002-1013
    • Gómez, A.1    Ferrer, I.2
  • 14
    • 0035144650 scopus 로고    scopus 로고
    • Oxidative post-translational modifications of alpha-synuclein in the 1- methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease
    • Przedborski, S.; Chen, Q.; Vila, M.; Giasson, B.I.; Djaldatti, R.; Vukosavic, S.; Souza, J.M.; Jackson-Lewis, V.; Lee, V.M.; Ischiropoulos, H. Oxidative post-translational modifications of alpha-synuclein in the 1- methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease. J. Neurochem., 2001, 76, 637-640.
    • (2001) J. Neurochem , vol.76 , pp. 637-640
    • Przedborski, S.1    Chen, Q.2    Vila, M.3    Giasson, B.I.4    Djaldatti, R.5    Vukosavic, S.6    Souza, J.M.7    Jackson-Lewis, V.8    Lee, V.M.9    Ischiropoulos, H.10
  • 15
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative Stress in Parkinson's Disease
    • Jenner, P. Oxidative Stress in Parkinson's Disease. Ann. Neurol., 2003, 53(Suppl 3), S26-S38.
    • (2003) Ann. Neurol , vol.53 , Issue.SUPPL. 3
    • Jenner, P.1
  • 16
    • 68149156531 scopus 로고    scopus 로고
    • Oxidative modifications, mitochondrial dysfunction, and impaired protein degradation in Parkinson's disease: How neurons are lost in the Bermuda triangle
    • Tsika, E.; Ischiropoulos, H.; Malkus, K.A. Oxidative modifications, mitochondrial dysfunction, and impaired protein degradation in Parkinson's disease: how neurons are lost in the Bermuda triangle. Mol. Neurodegener., 2009, 4, 24.
    • (2009) Mol. Neurodegener , vol.4 , pp. 24
    • Tsika, E.1    Ischiropoulos, H.2    Malkus, K.A.3
  • 18
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovitch, I. Superoxide radical and superoxide dismutases. Ann. Rev. Biochem., 1995, 64, 97-112.
    • (1995) Ann. Rev. Biochem , vol.64 , pp. 97-112
    • Fridovitch, I.1
  • 19
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher, P.; Beckman, J.S.; Liaudet, S. Nitric oxide and peroxynitrite in health and disease. Physiol Rev., 2007 87, (1), 315-424.
    • (2007) Physiol Rev , vol.87 , Issue.1 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, S.3
  • 21
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Dröge, W. Free radicals in the physiological control of cell function. Physiol. Rev., 2002, 82, 47-95.
    • (2002) Physiol. Rev , vol.82 , pp. 47-95
    • Dröge, W.1
  • 22
    • 0034693038 scopus 로고    scopus 로고
    • Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite
    • Reiter, C. D.; Teng, R. J.; Beckman, J. S. Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite. J. Biol. Chem., 2000, 275(42), 32460-32466.
    • (2000) J. Biol. Chem , vol.275 , Issue.42 , pp. 32460-32466
    • Reiter, C.D.1    Teng, R.J.2    Beckman, J.S.3
  • 23
    • 11244318376 scopus 로고    scopus 로고
    • Resveratrol protects against peroxynitrite-induced thiol oxidation in blood platelets
    • Olas, B.; Nowak, P.; Wachowicz, B. Resveratrol protects against peroxynitrite-induced thiol oxidation in blood platelets. Cell Mol. Biol. Lett., 2004, 9(4A), 577-587.
    • (2004) Cell Mol. Biol. Lett , vol.9 , Issue.4 A , pp. 577-587
    • Olas, B.1    Nowak, P.2    Wachowicz, B.3
  • 24
    • 0026484388 scopus 로고
    • The oxidant stress hypothesis in Parkinson's disease: Evidence supporting it
    • Fahn, S.; Cohen, G. The oxidant stress hypothesis in Parkinson's disease: evidence supporting it. Ann. Neurol., 1992, 32, 804-812.
    • (1992) Ann. Neurol , vol.32 , pp. 804-812
    • Fahn, S.1    Cohen, G.2
  • 25
    • 0022475372 scopus 로고
    • Lipid peroxidation as cause of nigral cell death in Parkinson's disease
    • Dexter, D.; Carter, C.; Agid, F. Lipid peroxidation as cause of nigral cell death in Parkinson's disease. Lancet, 1986, 8507, 639-640.
    • (1986) Lancet , vol.8507 , pp. 639-640
    • Dexter, D.1    Carter, C.2    Agid, F.3
  • 26
    • 34250016055 scopus 로고    scopus 로고
    • Apoptotic neuronal death in Parkinson's disease: Involvement of nitric oxide
    • Singh, S.; Dikshit, M. Apoptotic neuronal death in Parkinson's disease: involvement of nitric oxide. Brain Res. Rev., 2007, 54, 233-250.
    • (2007) Brain Res. Rev , vol.54 , pp. 233-250
    • Singh, S.1    Dikshit, M.2
  • 27
    • 33845932083 scopus 로고    scopus 로고
    • S-nitrosylation of Bcl-2 inhibits its ubiquitin-proteasomal degradation. A novel antiapoptotic mechanism that suppresses apoptosis
    • Azad, N.; Vallyathan, V.; Wang, L.; Tantishaiyakul, V.; Stehlik, C.; Leonard, S.S.; Rojanasakul, Y. S-nitrosylation of Bcl-2 inhibits its ubiquitin-proteasomal degradation. A novel antiapoptotic mechanism that suppresses apoptosis. J. Biol. Chem., 2006, 281, 34124-34134.
    • (2006) J. Biol. Chem , vol.281 , pp. 34124-34134
    • Azad, N.1    Vallyathan, V.2    Wang, L.3    Tantishaiyakul, V.4    Stehlik, C.5    Leonard, S.S.6    Rojanasakul, Y.7
  • 28
    • 79952857040 scopus 로고    scopus 로고
    • Regulation of neuronal oxidative and nitrosative stress by endogenous protective pathways and disease processes
    • Hardingham, G.E.; Lipton, S.A. Regulation of neuronal oxidative and nitrosative stress by endogenous protective pathways and disease processes. Antiox. Redox Signal., 2011, 14(8), 1421-1424.
    • (2011) Antiox. Redox Signal , vol.14 , Issue.8 , pp. 1421-1424
    • Hardingham, G.E.1    Lipton, S.A.2
  • 29
    • 0031577534 scopus 로고    scopus 로고
    • Inhibition of caspase-3 by S-nitrosation and oxidation caused by nitric oxide
    • Mohr, S.; Zech, B.; Lapetina, E.G.; Brune, B. Inhibition of caspase-3 by S-nitrosation and oxidation caused by nitric oxide. Biochem. Biophys. Res. Commun., 1997, 238, 387-391.
    • (1997) Biochem. Biophys. Res. Commun , vol.238 , pp. 387-391
    • Mohr, S.1    Zech, B.2    Lapetina, E.G.3    Brune, B.4
  • 30
    • 0030878073 scopus 로고    scopus 로고
    • Oxidative DNA damage in the parkinsonian brain: An apparent selective increase in 8- hydroxyguanine levels in substantia nigra
    • Alam, Z.I.; Jenner, A.; Daniel, S.E.; Lees, A.J.; Cairns, N., Marsden, C.D.; Jenner, P.; Halliwell, B. Oxidative DNA damage in the parkinsonian brain: an apparent selective increase in 8- hydroxyguanine levels in substantia nigra. J. Neurochem., 1997, 69(3), 1196-1203.
    • (1997) J. Neurochem , vol.69 , Issue.3 , pp. 1196-1203
    • Alam, Z.I.1    Jenner, A.2    Daniel, S.E.3    Lees, A.J.4    Cairns, N.5    Marsden, C.D.6    Jenner, P.7    Halliwell, B.8
  • 31
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • Szabo, C.; Ischiropoulos, H.; Radi, R. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat. Rev. Drug Discov., 2007, 6, 662-680.
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 33
    • 75949120541 scopus 로고    scopus 로고
    • Dysfunctional mitochondria uphold calpain activation: Contribution to Parkinson's disease pathology
    • Esteves, A.R.; Arduino, D.M.; Swerdlow, R.H.; Oliveira, C.R.; Cardoso, S.M. Dysfunctional mitochondria uphold calpain activation: contribution to Parkinson's disease pathology. Neurobiol. Dis., 2010, 3, 723-730.
    • (2010) Neurobiol. Dis , vol.3 , pp. 723-730
    • Esteves, A.R.1    Arduino, D.M.2    Swerdlow, R.H.3    Oliveira, C.R.4    Cardoso, S.M.5
  • 34
    • 68649112842 scopus 로고    scopus 로고
    • Oxidative and nitrosative stress in Parkinson's disease
    • Tsang, A.H.K.; Chung, K.K.K. Oxidative and nitrosative stress in Parkinson's disease. Biochim. Biophys. Acta, 2009, 1792, 643-650.
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 643-650
    • Tsang, A.H.K.1    Chung, K.K.K.2
  • 35
    • 50949117770 scopus 로고    scopus 로고
    • Dopaminergic neuron-specific oxidative stress caused by dopamine itself
    • Miyazaki, I.; Asanuma, M. Dopaminergic neuron-specific oxidative stress caused by dopamine itself. Acta Med. Okayama, 2008, 62(3), 141-150.
    • (2008) Acta Med. Okayama , vol.62 , Issue.3 , pp. 141-150
    • Miyazaki, I.1    Asanuma, M.2
  • 36
    • 0028834228 scopus 로고
    • Peroxynitrite-mediated inhibition of DOPA synthesis in PC12 cells
    • Ischiropoulos, H.; Duran, D.; Horwitz, J. Peroxynitrite-mediated inhibition of DOPA synthesis in PC12 cells. J. Neurochem., 1995, 65, 2366-2372.
    • (1995) J. Neurochem , vol.65 , pp. 2366-2372
    • Ischiropoulos, H.1    Duran, D.2    Horwitz, J.3
  • 37
    • 0030250041 scopus 로고    scopus 로고
    • Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration
    • Gow, A.; Duran, D.; Thom, S.R.; Ischiropoulos, H. Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration. Arch. Biochem. Biophys., 1996, 333(1), 42-48.
    • (1996) Arch. Biochem. Biophys , vol.333 , Issue.1 , pp. 42-48
    • Gow, A.1    Duran, D.2    Thom, S.R.3    Ischiropoulos, H.4
  • 38
    • 0026034279 scopus 로고
    • Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: An X-ray microanalysis
    • Hirsch, E.C.; Brandel, J.P.; Galle, P.; Javoy-Agid, F.; Agid, Y. Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: an X-ray microanalysis. J. Neurochem., 1991, 56, 446-451.
    • (1991) J. Neurochem , vol.56 , pp. 446-451
    • Hirsch, E.C.1    Brandel, J.P.2    Galle, P.3    Javoy-Agid, F.4    Agid, Y.5
  • 40
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M.P. How mitochondria produce reactive oxygen species. Biochem. J., 2009, 417, 1-13.
    • (2009) Biochem. J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 41
    • 55849122639 scopus 로고    scopus 로고
    • Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis
    • Henchcliffe, C.; Flint Beal, M. Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis. Nat. Clin. Prac. Neurol., 2008, 4, 600-609.
    • (2008) Nat. Clin. Prac. Neurol , vol.4 , pp. 600-609
    • Henchcliffe, C.1    Flint Beal, M.2
  • 42
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens, J.F. Mitochondrial formation of reactive oxygen species. J. Physiol., 2003, 552, 335-344.
    • (2003) J. Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 43
    • 57649233079 scopus 로고    scopus 로고
    • The role of mitochondria in reactive oxygen species metabolism and signaling
    • Starkov, A.A. The role of mitochondria in reactive oxygen species metabolism and signaling. Ann. NY Acad. Sci., 2008, 1147, 37-52.
    • (2008) Ann. NY Acad. Sci , vol.1147 , pp. 37-52
    • Starkov, A.A.1
  • 44
    • 0033937733 scopus 로고    scopus 로고
    • The role of mitochondria in the pathogenesis of neurodegenerative diseases
    • Manfredi, G.; Beal, M.F. The role of mitochondria in the pathogenesis of neurodegenerative diseases. Brain Pathol., 2000, 10, 462-472.
    • (2000) Brain Pathol , vol.10 , pp. 462-472
    • Manfredi, G.1    Beal, M.F.2
  • 45
    • 48249156188 scopus 로고    scopus 로고
    • Mitochondrial disorders in the nervous system
    • DiMauro, S.; Schon, E.A. Mitochondrial disorders in the nervous system. Ann. Rev. Neuroscience, 2008, 31, 91-123.
    • (2008) Ann. Rev. Neuroscience , vol.31 , pp. 91-123
    • Dimauro, S.1    Schon, E.A.2
  • 46
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin, M.T.; Flint Beal, M. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature, 2006, 443, 787-795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Flint Beal, M.2
  • 47
    • 37049004489 scopus 로고    scopus 로고
    • Mitochondria in the aetiology and pathogenesis of Parkinson's disease
    • Schapira, A.H. Mitochondria in the aetiology and pathogenesis of Parkinson's disease. Lancet Neurol., 2008, 7, 97-109.
    • (2008) Lancet Neurol , vol.7 , pp. 97-109
    • Schapira, A.H.1
  • 48
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney, P.M.; Xie, J.; Capaldi, R.A.; Bennett, J.P. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci., 2006, 26, 5256-5264.
    • (2006) J. Neurosci , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett, J.P.4
  • 49
  • 50
    • 56349113200 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by mitochondrial complex I: Implications in neurodegeneration
    • Fato, R.; Bergamini, C.; Leoni, S.; Strocchi, P.; Lenaz, G. Generation of reactive oxygen species by mitochondrial complex I: implications in neurodegeneration. Neurochem. Res., 2008, 33, 2487-2501.
    • (2008) Neurochem. Res , vol.33 , pp. 2487-2501
    • Fato, R.1    Bergamini, C.2    Leoni, S.3    Strocchi, P.4    Lenaz, G.5
  • 51
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of Snitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi, E.; Brown, G.C.; Feelisch, M.; Moncada, S. Persistent inhibition of cell respiration by nitric oxide: crucial role of Snitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl. Acad. Sci. USA, 1998, 95, 7631-7636.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 53
    • 0027435899 scopus 로고
    • Iron induced oxidative stress and mitochondrial dysfunction: Relevance to Parkinson's disease
    • Hartley, A.; Cooper, J.M.; Schapira, A.H. Iron induced oxidative stress and mitochondrial dysfunction: relevance to Parkinson's disease. Brain Res., 1993, 627, 349-353.
    • (1993) Brain Res , vol.627 , pp. 349-353
    • Hartley, A.1    Cooper, J.M.2    Schapira, A.H.3
  • 54
    • 0027185713 scopus 로고
    • Altered mitochondrial function, iron metabolism and glutathione levels in Parkinson's disease
    • Jenner, P. Altered mitochondrial function, iron metabolism and glutathione levels in Parkinson's disease. Acta Neurol. Scand., 1993, 87, 6-13.
    • (1993) Acta Neurol. Scand , vol.87 , pp. 6-13
    • Jenner, P.1
  • 55
    • 77951939586 scopus 로고    scopus 로고
    • Iron-mediated oxidative stress plays an essential role in ferritin-induced cell death
    • Bresgen, N.; Jaksch, H.; Lacher, H.; Ohlenschläger, I.; Uchida, K.; Eckl, P.M. Iron-mediated oxidative stress plays an essential role in ferritin-induced cell death. Free Radic. Biol. Med., 2010, 48(10), 1347-1357.
    • (2010) Free Radic. Biol. Med , vol.48 , Issue.10 , pp. 1347-1357
    • Bresgen, N.1    Jaksch, H.2    Lacher, H.3    Ohlenschläger, I.4    Uchida, K.5    Eckl, P.M.6
  • 57
    • 0038799736 scopus 로고    scopus 로고
    • Oxidative DNA damage: Mechanisms, mutation, and disease
    • Cooke, M.S.; Evans, M.D.; Dizdaroglu, M.; Lunec, J. Oxidative DNA damage: mechanisms, mutation, and disease. FASEB, 2003, 17, 1195-1214.
    • (2003) FASEB , vol.17 , pp. 1195-1214
    • Cooke, M.S.1    Evans, M.D.2    Dizdaroglu, M.3    Lunec, J.4
  • 58
    • 0032911488 scopus 로고    scopus 로고
    • Parkinson's disease is associated with oxidative damage to cytoplasmic DNA and RNA in substantia nigra neurons
    • Zhang, J.; Perry, G.; Smith, M.A.; Robertson, D.; Olson, S.G.; Doyle G.; Graham, D.G.; Montine, T.J. Parkinson's disease is associated with oxidative damage to cytoplasmic DNA and RNA in substantia nigra neurons. Am. J. Pathol., 1999, 154, 1423-1429.
    • (1999) Am. J. Pathol , vol.154 , pp. 1423-1429
    • Zhang, J.1    Perry, G.2    Smith, M.A.3    Robertson, D.4    Olson, S.G.5    Doyle, G.6    Graham, D.G.7    Montine, T.J.8
  • 59
    • 10744231633 scopus 로고    scopus 로고
    • Somatic mitochondrial DNA mutations in cortex and substantia nigra in aging and Parkinson's disease
    • Simon, D.K.; Lin, M. T.; Zheng, L.; Liu, G-J.; Ahn, C.H.; Kim, L.M.; Beal, M.F.; Johns, D. Somatic mitochondrial DNA mutations in cortex and substantia nigra in aging and Parkinson's disease. Neurobiol. Aging, 2004, 25(1), 71-81.
    • (2004) Neurobiol. Aging , vol.25 , Issue.1 , pp. 71-81
    • Simon, D.K.1    Lin, M.T.2    Zheng, L.3    Liu, G.-J.4    Ahn, C.H.5    Kim, L.M.6    Beal, M.F.7    Johns, D.8
  • 60
    • 0024541837 scopus 로고
    • Mitochondrial DNA, mutations as an important contributor to ageing and degenerative diseases
    • Linnane, A.W.; Marzuki, S.; Ozawa, T.; Tanaka, M. Mitochondrial DNA, mutations as an important contributor to ageing and degenerative diseases. Lancet, 1989, 1, 642-645.
    • (1989) Lancet , vol.1 , pp. 642-645
    • Linnane, A.W.1    Marzuki, S.2    Ozawa, T.3    Tanaka, M.4
  • 61
    • 59349086549 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations and aging: Devils in the details?
    • Khrapko, K.; Vijg, J. Mitochondrial DNA mutations and aging: devils in the details? Trends Genet., 2009, 25, 91-98.
    • (2009) Trends Genet , vol.25 , pp. 91-98
    • Khrapko, K.1    Vijg, J.2
  • 62
    • 33644859083 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system. From a vague idea, through basic mechanisms, and onto human diseases and drug targeting
    • Ciechanover, A. The ubiquitin proteolytic system. From a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology, 2006, 66(1) S7-S19.
    • (2006) Neurology , vol.66 , Issue.1
    • Ciechanover, A.1
  • 63
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies, K.J. Degradation of oxidized proteins by the 20S proteasome. Biochimie, 2001, 83(3-4), 301-310.
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 301-310
    • Davies, K.J.1
  • 64
    • 33745315287 scopus 로고    scopus 로고
    • S-nitrosylated proteindisulphide isomerase links protein misfolding to neurodegeneration
    • Uehara, T.; Nakamura, T.; Yao, D.; Shi, Z.Q.; Gu, Z.; Ma, Y.; Masliah, E.; Nomura, Y.; Lipton, S.A. S-nitrosylated proteindisulphide isomerase links protein misfolding to neurodegeneration, Nature, 2006, 441, 513-517.
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4    Gu, Z.5    Ma, Y.6    Masliah, E.7    Nomura, Y.8    Lipton, S.A.9
  • 67
    • 0344875488 scopus 로고    scopus 로고
    • Inactivation of parkin by oxidative stress and C-terminal truncations: A protective role of molecular chaperones
    • Winklhofer, K.F.; Henn, I.H.; Kay-Jackson, P.C.; Heller, U.; Tatzelt, J. Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones, J. Biol. Chem., 2003, 278, 47199-47208.
    • (2003) J. Biol. Chem , vol.278 , pp. 47199-47208
    • Winklhofer, K.F.1    Henn, I.H.2    Kay-Jackson, P.C.3    Heller, U.4    Tatzelt, J.5
  • 68
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung, K.K.; Thomas, B.; Li, X.; Pletnikova, O.; Troncoso, J.C.; Marsh, L.; Dawson, V.L.; Dawson, T.M. S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science, 2004, 304, 1328-1331.
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6    Dawson, V.L.7    Dawson, T.M.8
  • 72
    • 49649097747 scopus 로고    scopus 로고
    • Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
    • Gautier, C.A.; Kitada, T.; Shen, J. Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc. Natl. Acad. Sci. USA, 2008, 105(32), 11364-11369.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.32 , pp. 11364-11369
    • Gautier, C.A.1    Kitada, T.2    Shen, J.3
  • 74
    • 79954616687 scopus 로고    scopus 로고
    • Lu CSPARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons
    • Wang, H.L.; Chou, A.H.; Wu, A.S.; Chen, S.Y.; Weng, Y.H.; Kao, Y.C.; Yeh, T.H.; Chu, P.J.; Lu CSPARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons. Biochim. Biophys. Acta, 2011, 1812(6), 674-684.
    • (2011) Biochim. Biophys. Acta , vol.1812 , Issue.6 , pp. 674-684
    • Wang, H.L.1    Chou, A.H.2    Wu, A.S.3    Chen, S.Y.4    Weng, Y.H.5    Kao, Y.C.6    Yeh, T.H.7    Chu, P.J.8
  • 75
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of alpha- synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • Devi, L.; Raghavendran, V.; Prabhu, B.M.; Avadhani, N.G.; Anandatheertha-varada, H.K. Mitochondrial import and accumulation of alpha- synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J. Biol. Chem., 2008, 283, 9089-9100.
    • (2008) J. Biol. Chem , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheertha-Varada, H.K.5
  • 76
    • 0031017290 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by tyrosine hydroxylase: A possible contribution to the degeneration of Dopaminergic neurons
    • Haavik, J.; Almas, B.; Flatmark, T. Generation of reactive oxygen species by tyrosine hydroxylase: A possible contribution to the degeneration of Dopaminergic neurons? J. Neurochem., 1997, 68, 328-332.
    • (1997) J. Neurochem , vol.68 , pp. 328-332
    • Haavik, J.1    Almas, B.2    Flatmark, T.3
  • 77
    • 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.; 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., 2007, 100, 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
  • 79
    • 13944279784 scopus 로고    scopus 로고
    • Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: An ES- derived cell model of primary Parkinsonism
    • Martinat, C.; Shendelman, S.; Jonason, A.; Leete, T.; Beal, M.F.; Yang, L.; Floss, T.; Abeliovich, A. Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: an ES- derived cell model of primary Parkinsonism. PLoS Biol., 2004, 2, e327.
    • (2004) PLoS Biol , vol.2
    • Martinat, C.1    Shendelman, S.2    Jonason, A.3    Leete, T.4    Beal, M.F.5    Yang, L.6    Floss, T.7    Abeliovich, A.8
  • 81
    • 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.; Hastings, T.G. Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: implications for Parkinson's disease. J. Neurochem., 1999, 73(3), 1127-1137.
    • (1999) J. Neurochem , vol.73 , Issue.3 , pp. 1127-1137
    • Berman, S.B.1    Hastings, T.G.2
  • 82
    • 0345328791 scopus 로고    scopus 로고
    • Mitochondrial impairment is accompanied by impaired oxidative DNA repair in the nucleus
    • Delsite, R.L.; Rasmussen, L.J.; Rasmussen, A.K.; Kalen, A.; Goswami, P.C.; Singh, K.K. Mitochondrial impairment is accompanied by impaired oxidative DNA repair in the nucleus. Mutagenesis, 2003, 18(6), 497-503.
    • (2003) Mutagenesis , vol.18 , Issue.6 , pp. 497-503
    • Delsite, R.L.1    Rasmussen, L.J.2    Rasmussen, A.K.3    Kalen, A.4    Goswami, P.C.5    Singh, K.K.6
  • 84
    • 25644439977 scopus 로고    scopus 로고
    • Immobilization stress causes increases in tetrahydrobiopterin, dopamine, and neuro- melanin and oxidative damage in the nigrostriatal system
    • Kim, S.T.; Chang, J.W.; Choi, J.H.; Kim, S.W.; Hwang, O. Immobilization stress causes increases in tetrahydrobiopterin, dopamine, and neuro- melanin and oxidative damage in the nigrostriatal system. J. Neurochem., 2005, 95, 89-98.
    • (2005) J. Neurochem , vol.95 , pp. 89-98
    • Kim, S.T.1    Chang, J.W.2    Choi, J.H.3    Kim, S.W.4    Hwang, O.5
  • 85
    • 0037879052 scopus 로고    scopus 로고
    • The mitochondrial membrane potential (deltapsi(m)) in apoptosis: An update
    • Ly, J.D.; Grubb, D.R.; Lawen, A. The mitochondrial membrane potential (deltapsi(m)) in apoptosis: an update. Apoptosis, 2003, 8, 115-128.
    • (2003) Apoptosis , vol.8 , pp. 115-128
    • Ly, J.D.1    Grubb, D.R.2    Lawen, A.3
  • 86
    • 0033032999 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson's disease, Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia
    • Schapira, A.H. Mitochondrial involvement in Parkinson's disease, Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia. Biochim. Biophys. Acta, 1999, 1410, 159-170.
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 159-170
    • Schapira, A.H.1
  • 87
    • 0038201683 scopus 로고    scopus 로고
    • Effects of amphetamines on mitochondrial function: Role of free radicals and oxidative stress
    • Brown, J.M.; Yamamoto, B.K. Effects of amphetamines on mitochondrial function: role of free radicals and oxidative stress. Pharmacol. Ther., 2003, 99, 45-53.
    • (2003) Pharmacol. Ther , vol.99 , pp. 45-53
    • Brown, J.M.1    Yamamoto, B.K.2
  • 88
    • 0037632905 scopus 로고    scopus 로고
    • Dopamine-dependent cytotoxicity of tetrahydrobiopterin: A possible mechanism for selective neurodegeneration in Parkinson's disease
    • Choi, H.J.; Kim, S.W.; Lee, S.Y.; Hwang, O. Dopamine-dependent cytotoxicity of tetrahydrobiopterin: a possible mechanism for selective neurodegeneration in Parkinson's disease. J. Neurochem., 2003, 86, 143-152.
    • (2003) J. Neurochem , vol.86 , pp. 143-152
    • Choi, H.J.1    Kim, S.W.2    Lee, S.Y.3    Hwang, O.4
  • 89
    • 0029433534 scopus 로고
    • Tyrosine hydroxylase: Human isoforms, structure and regulation in physiology and pathology
    • Nagatsu, T. Tyrosine hydroxylase: human isoforms, structure and regulation in physiology and pathology. Essays Biochem., 1995, 30, 15-35.
    • (1995) Essays Biochem , vol.30 , pp. 15-35
    • Nagatsu, T.1
  • 90
    • 0029586876 scopus 로고
    • Immunocytochemical localization of GTP cyclohydrolase I in the brain, adrenal gland, and liver of mice
    • Nagatsu, I.; Ichinose, H.; Sakai, M.; Titani, K.; Suzuki, M.; Nagatsu, T. Immunocytochemical localization of GTP cyclohydrolase I in the brain, adrenal gland, and liver of mice. J. Neural Transm. Gen. Sect., 1995, 102, 175-188.
    • (1995) J. Neural Transm. Gen. Sect , vol.102 , pp. 175-188
    • Nagatsu, I.1    Ichinose, H.2    Sakai, M.3    Titani, K.4    Suzuki, M.5    Nagatsu, T.6
  • 91
    • 0030017489 scopus 로고    scopus 로고
    • Intricate regulation of tyrosine hydroxylase activity and gene expression
    • Kumer, S.C.; Vrana, K.E. Intricate regulation of tyrosine hydroxylase activity and gene expression. J. Neurochem., 1996, 67, 443-462.
    • (1996) J. Neurochem , vol.67 , pp. 443-462
    • Kumer, S.C.1    Vrana, K.E.2
  • 92
    • 44249120317 scopus 로고    scopus 로고
    • Activation of tyrosine hydroxylase mRNA translation by cAMP in midbrain dopaminergic neurons
    • Chen, X.; Xu, L.; Radcliffe, P.; Sun, B.; Tank, A.W. Activation of tyrosine hydroxylase mRNA translation by cAMP in midbrain dopaminergic neurons. Mol. Pharmacol., 2008, 3(6), 1816-1828.
    • (2008) Mol. Pharmacol , vol.3 , Issue.6 , pp. 1816-1828
    • Chen, X.1    Xu, L.2    Radcliffe, P.3    Sun, B.4    Tank, A.W.5
  • 94
    • 0025353854 scopus 로고
    • Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40
    • Haycock, J.W. Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40. J. Biol. Chem., 1990, 265(20), 11662-11691.
    • (1990) J. Biol. Chem , vol.265 , Issue.20 , pp. 11662-11691
    • Haycock, J.W.1
  • 95
    • 0027053393 scopus 로고
    • Regulation of tyrosine hydroxylase gene transcription rate and tyrosine hydroxylase mRNA stability by cyclic AMP and glucocorticoid
    • Fossom, L.H.; Sterling, C.R.; Tank, A.W. Regulation of tyrosine hydroxylase gene transcription rate and tyrosine hydroxylase mRNA stability by cyclic AMP and glucocorticoid. Mol. Pharmacol., 1992, 42(5), 898-908.
    • (1992) Mol. Pharmacol , vol.42 , Issue.5 , pp. 898-908
    • Fossom, L.H.1    Sterling, C.R.2    Tank, A.W.3
  • 96
    • 80054834577 scopus 로고    scopus 로고
    • Protein Kinase c-dependent dephosphorylation of tyrosine hydroxylase requires the B56d heterotrimeric form of protein phosphatase 2A
    • Ahn, J.-H.; Kim, Y.; Kim, H-S.; Greengard, P.; Nairn, A.C. Protein Kinase c-dependent dephosphorylation of tyrosine hydroxylase requires the B56d heterotrimeric form of protein phosphatase 2A. PLoS ONE, 2011, 6(1), e26292.
    • (2011) PLoS ONE , vol.6 , Issue.1
    • Ahn, J.-H.1    Kim, Y.2    Kim, H.-S.3    Greengard, P.4    Nairn, A.C.5
  • 97
    • 0041589260 scopus 로고    scopus 로고
    • The autoxidation of tetrahydrobiopterin revisited. Proof of superoxide formation from reaction of tetrahydrobiopterin with molecular oxygen
    • Kirsch, M.; Korth, H.G.; Stenert, V.; Sustmann, R.; de Groot, H. The autoxidation of tetrahydrobiopterin revisited. Proof of superoxide formation from reaction of tetrahydrobiopterin with molecular oxygen. J. Biol. Chem., 2003, 278(27), 24481-24490.
    • (2003) J. Biol. Chem , vol.278 , Issue.27 , pp. 24481-24490
    • Kirsch, M.1    Korth, H.G.2    Stenert, V.3    Sustmann, R.4    de Groot, H.5
  • 98
    • 0029833673 scopus 로고    scopus 로고
    • Restoration of endothelium-dependent vasodilation after reperfusion injury by tetrahydrobiopterin
    • Tiefenbacher, C.P.; Chilian, W.M.; Mitchell, M.; DeFily, D.V. Restoration of endothelium-dependent vasodilation after reperfusion injury by tetrahydrobiopterin. Circulation, 1996, 94, 1423-1429.
    • (1996) Circulation , vol.94 , pp. 1423-1429
    • Tiefenbacher, C.P.1    Chilian, W.M.2    Mitchell, M.3    Defily, D.V.4
  • 100
    • 0036724608 scopus 로고    scopus 로고
    • Tetrahydrobiopterin deficiency increases neuronal vulnerability to hypoxia
    • Delgado-Esteban, M.; Almeida, A.; Medina, J.M. Tetrahydrobiopterin deficiency increases neuronal vulnerability to hypoxia. J. Neurochem., 2002, 82(5), 1148-1159.
    • (2002) J. Neurochem , vol.82 , Issue.5 , pp. 1148-1159
    • Delgado-Esteban, M.1    Almeida, A.2    Medina, J.M.3
  • 102
    • 0034141542 scopus 로고    scopus 로고
    • Effects of phosphorylation on binding of catecholamines to tyrosine hydroxylase: Specificity and thermodynamics
    • Ramsey, A.J.; Fitzpatrick, P.F. Effects of phosphorylation on binding of catecholamines to tyrosine hydroxylase: Specificity and thermodynamics. Biochemistry, 2000, 39, 773-778.
    • (2000) Biochemistry , vol.39 , pp. 773-778
    • Ramsey, A.J.1    Fitzpatrick, P.F.2
  • 103
    • 0032560609 scopus 로고    scopus 로고
    • Effects of phosphorylation of serine-40 of tyrosine hydroxylase in binding of catecholamines-Evidence for a novel regulatory mechnanism
    • Ramsey, A.J.; Fitzpatrick, P.F. Effects of phosphorylation of serine-40 of tyrosine hydroxylase in binding of catecholamines-Evidence for a novel regulatory mechnanism. Biochemistry, 1998, 37, 8980-8986.
    • (1998) Biochemistry , vol.37 , pp. 8980-8986
    • Ramsey, A.J.1    Fitzpatrick, P.F.2
  • 104
    • 1842612454 scopus 로고    scopus 로고
    • Dopamine neurons release transmitter via a flickering fusion pore
    • Staal, R.G.; Mosharov, E.V.; Sulzer, D. Dopamine neurons release transmitter via a flickering fusion pore. Nat. Neurosci., 2004, 7(4), 341-346.
    • (2004) Nat. Neurosci , vol.7 , Issue.4 , pp. 341-346
    • Staal, R.G.1    Mosharov, E.V.2    Sulzer, D.3
  • 106
    • 41149108952 scopus 로고    scopus 로고
    • α-Synuclein aggregation alters tyrosine hydroxylase phosphorilation and immunoreactivity: Lessons from viral trasduction of knockout mice
    • Alerte, T.N.M.; Akinfolarin, A.A.; Friedrich, E.E.; Mader, S.A.; Hong, C-S.; Ruth G., Perez, R.G. α-Synuclein aggregation alters tyrosine hydroxylase phosphorilation and immunoreactivity: lessons from viral trasduction of knockout mice. Neurosci. Lett., 2008, 435(1), 24-29.
    • (2008) Neurosci. Lett , vol.435 , Issue.1 , pp. 24-29
    • Alerte, T.N.M.1    Akinfolarin, A.A.2    Friedrich, E.E.3    Mader, S.A.4    Hong, C.-S.5    Ruth, G.6    Perez, R.G.7


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