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Volumn 2015, Issue , 2015, Pages

Mitochondrial dysfunction and α -synuclein synaptic pathology in Parkinson's disease: Who's on first?

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN;

EID: 84928485187     PISSN: None     EISSN: 20420080     Source Type: Journal    
DOI: 10.1155/2015/108029     Document Type: Review
Times cited : (86)

References (136)
  • 1
    • 84887934289 scopus 로고    scopus 로고
    • Genetics of Parkinsons disease: The yield
    • M. Spatola and C. Wider, "Genetics of Parkinsons disease: the yield," Parkinsonism and Related Disorders, vol. 20, supplement 1, pp. S35-S38, 2014.
    • (2014) Parkinsonism and Related Disorders , vol.20 , pp. S35-S38
    • Spatola, M.1    Wider, C.2
  • 2
    • 80855131515 scopus 로고    scopus 로고
    • Clinical aspects of familial forms of frontotemporal dementia associated with parkinsonism
    • S. Fujioka and Z. K. Wszolek, "Clinical aspects of familial forms of frontotemporal dementia associated with parkinsonism," Journal of Molecular Neuroscience, vol. 45, no. 3, pp. 359-365, 2011.
    • (2011) Journal of Molecular Neuroscience , vol.45 , Issue.3 , pp. 359-365
    • Fujioka, S.1    Wszolek, Z.K.2
  • 3
    • 84857968555 scopus 로고    scopus 로고
    • Mitochondria and programmed cell death in Parkinsons disease: Apoptosis and beyond
    • C. Perier, J. Bove, and M. Vila, "Mitochondria and programmed cell death in Parkinsons disease: apoptosis and beyond," Antioxidants and Redox Signaling, vol. 16, no. 9, pp. 883-895, 2012.
    • (2012) Antioxidants and Redox Signaling , vol.16 , Issue.9 , pp. 883-895
    • Perier, C.1    Bove, J.2    Vila, M.3
  • 5
    • 84875259777 scopus 로고    scopus 로고
    • An ERcentric view of Parkinsons disease
    • G. Mercado, P. Valdes, and C. Hetz, "An ERcentric view of Parkinsons disease," Trends in Molecular Medicine, vol. 19, no. 3, pp. 165-175, 2013.
    • (2013) Trends in Molecular Medicine , vol.19 , Issue.3 , pp. 165-175
    • Mercado, G.1    Valdes, P.2    Hetz, C.3
  • 6
    • 34347359673 scopus 로고    scopus 로고
    • Rejuvenation protects neurons in mouse models of Parkinsons disease
    • C. S. Chan, J. N. Guzman, E. Ilijic et al. , "Rejuvenation protects neurons in mouse models of Parkinsons disease," Nature, vol. 447, no. 7148, pp. 1081-1086, 2007.
    • (2007) Nature , vol.447 , Issue.7148 , pp. 1081-1086
    • Chan, C.S.1    Guzman, J.N.2    Ilijic, E.3
  • 7
    • 84902535538 scopus 로고    scopus 로고
    • The centrality of mitochondria in the pathogenesis and treatment of Parkinsons disease
    • A. Camilleri and N. Vassallo, "The centrality of mitochondria in the pathogenesis and treatment of Parkinsons disease," CNS Neuroscience andTherapeutics, vol. 20, no. 7, pp. 591-602, 2014.
    • (2014) CNS Neuroscience AndTherapeutics , vol.20 , Issue.7 , pp. 591-602
    • Camilleri, A.1    Vassallo, N.2
  • 8
    • 65549102934 scopus 로고    scopus 로고
    • Inducible over-expression of wild type α-synuclein in human neuronal cells leads to caspase-dependent non-apoptotic death
    • K. Vekrellis, M. Xilouri, E. Emmanouilidou, and L. Stefanis, "Inducible over-expression of wild type α-synuclein in human neuronal cells leads to caspase-dependent non-apoptotic death," Journal of Neurochemistry, vol. 109, no. 5, pp. 1348-1362, 2009.
    • (2009) Journal of Neurochemistry , vol.109 , Issue.5 , pp. 1348-1362
    • Vekrellis, K.1    Xilouri, M.2    Emmanouilidou, E.3    Stefanis, L.4
  • 9
    • 79551647443 scopus 로고    scopus 로고
    • Induction of the unfolded protein response by α-synuclein in experimental models of Parkinsons disease
    • A. Bellucci, L. Navarria, M. Zaltieri et al. , "Induction of the unfolded protein response by α-synuclein in experimental models of Parkinsons disease," Journal of Neurochemistry, vol. 116, no. 4, pp. 588-605, 2011.
    • (2011) Journal of Neurochemistry , vol.116 , Issue.4 , pp. 588-605
    • Bellucci, A.1    Navarria, L.2    Zaltieri, M.3
  • 10
    • 84878892468 scopus 로고    scopus 로고
    • Calciumentry and α-synuclein inclusions elevate dendritic mitochondrial oxidant stress in dopaminergic neurons
    • D. I. Dryanovski, J. N. Guzman, Z. Xie et al. , "Calciumentry and α-synuclein inclusions elevate dendritic mitochondrial oxidant stress in dopaminergic neurons,"The Journal of Neuroscience, vol. 33, no. 24, pp. 10154-10164, 2013.
    • (2013) The Journal of Neuroscience , vol.33 , Issue.24 , pp. 10154-10164
    • Dryanovski, D.I.1    Guzman, J.N.2    Xie, Z.3
  • 14
    • 84888394934 scopus 로고    scopus 로고
    • Inflammation and α-synucleins prion-like behavior in Parkinsons disease-is there a link?
    • C. M. Lema Tome, T. Tyson, N. L. Rey, S. Grathwohl, M. Britschgi, and P. Brundin, "Inflammation and α-synucleins prion-like behavior in Parkinsons disease-is there a link?" Molecular neurobiology, vol. 47, no. 2, pp. 561-574, 2013.
    • (2013) Molecular Neurobiology , vol.47 , Issue.2 , pp. 561-574
    • Lema Tome, C.M.1    Tyson, T.2    Rey, N.L.3    Grathwohl, S.4    Britschgi, M.5    Brundin, P.6
  • 16
    • 39749123263 scopus 로고    scopus 로고
    • Axonal alphasynuclein aggregates herald centripetal degeneration of cardiac sympathetic nerve in Parkinsons disease
    • S. Orimo, T. Uchihara, A. Nakamura et al. , "Axonal alphasynuclein aggregates herald centripetal degeneration of cardiac sympathetic nerve in Parkinsons disease," Brain, vol. 131, no. 3, pp. 642-650, 2008.
    • (2008) Brain , vol.131 , Issue.3 , pp. 642-650
    • Orimo, S.1    Uchihara, T.2    Nakamura, A.3
  • 17
    • 84897567836 scopus 로고    scopus 로고
    • Mitochondrial trafficking and anchoring in neurons: New insight and implications
    • Z. H. Sheng, "Mitochondrial trafficking and anchoring in neurons: new insight and implications," Journal of Cell Biology, vol. 204, no. 7, pp. 1087-1098, 2014.
    • (2014) Journal of Cell Biology , vol.204 , Issue.7 , pp. 1087-1098
    • Sheng, Z.H.1
  • 18
    • 81255149611 scopus 로고    scopus 로고
    • The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in Parkinsons disease
    • D. J. Surmeier, J. N. Guzman, J. Sanchez-Padilla, and P. T. Schumacker, "The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in Parkinsons disease," Neuroscience, vol. 198, pp. 221-231, 2011.
    • (2011) Neuroscience , vol.198 , pp. 221-231
    • Surmeier, D.J.1    Guzman, J.N.2    Sanchez-Padilla, J.3    Schumacker, P.T.4
  • 20
    • 0034118103 scopus 로고    scopus 로고
    • Coupled oscillator model of the dopaminergic neuron of the substantia nigra
    • C. J. Wilson and J. C. Callaway, "Coupled oscillator model of the dopaminergic neuron of the substantia nigra," Journal of Neurophysiology, vol. 83, no. 5, pp. 3084-3100, 2000.
    • (2000) Journal of Neurophysiology , vol.83 , Issue.5 , pp. 3084-3100
    • Wilson, C.J.1    Callaway, J.C.2
  • 21
    • 33745013111 scopus 로고    scopus 로고
    • Oxidative stress and neurodegeneration: Where are we now?
    • B. Halliwell, "Oxidative stress and neurodegeneration: where are we now?" Journal of Neurochemistry, vol. 97, no. 6, pp. 1634-1658, 2006.
    • (2006) Journal of Neurochemistry , vol.97 , Issue.6 , pp. 1634-1658
    • Halliwell, B.1
  • 24
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • J. J. Palacino, D. Sagi, M. S. Goldberg et al. , "Mitochondrial dysfunction and oxidative damage in parkin-deficient mice," The Journal of Biological Chemistry, vol. 279, no. 18, pp. 18614-18622, 2004.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18614-18622
    • Palacino, J.J.1    Sagi, D.2    Goldberg, M.S.3
  • 25
    • 70449377127 scopus 로고    scopus 로고
    • Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis
    • L. Parisiadou, C. Xie, J. C. Hyun et al. , "Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis," The Journal of Neuroscience, vol. 29, no. 44, pp. 13971-13980, 2009.
    • (2009) The Journal of Neuroscience , vol.29 , Issue.44 , pp. 13971-13980
    • Parisiadou, L.1    Xie, C.2    Hyun, J.C.3
  • 26
    • 79952020818 scopus 로고    scopus 로고
    • Genetic mouse models for Parkinsons disease display severe pathology in glial cell mitochondria
    • S. Schmidt, B. Linnartz, S. Mendritzki et al. , "Genetic mouse models for Parkinsons disease display severe pathology in glial cell mitochondria," Human Molecular Genetics, vol. 20, no. 6, pp. 1197-1211, 2011.
    • (2011) Human Molecular Genetics , vol.20 , Issue.6 , pp. 1197-1211
    • Schmidt, S.1    Linnartz, B.2    Mendritzki, S.3
  • 27
    • 84857953098 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in genetic animal models of Parkinsons disease
    • A. Trancikova, E. Tsika, and D. J. Moore, "Mitochondrial dysfunction in genetic animal models of Parkinsons disease," Antioxidants and Redox Signaling, vol. 16, no. 9, pp. 896-919, 2012.
    • (2012) Antioxidants and Redox Signaling , vol.16 , Issue.9 , pp. 896-919
    • Trancikova, A.1    Tsika, E.2    Moore, D.J.3
  • 29
    • 0038711511 scopus 로고    scopus 로고
    • Effects of oxidative and nitrative challenges on α-synuclein fibrillogenesis involve distinctmechanisms of protein modifications
    • E. H. Norris, B. I. Giasson, H. Ischiropoulos, and V. M.-Y. Lee, "Effects of oxidative and nitrative challenges on α-synuclein fibrillogenesis involve distinctmechanisms of protein modifications," Journal of Biological Chemistry, vol. 278, no. 29, pp. 27230-27240, 2003.
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 27230-27240
    • Norris, E.H.1    Giasson, B.I.2    Ischiropoulos, H.3    Lee, V.M.-Y.4
  • 31
    • 77957264418 scopus 로고    scopus 로고
    • The synaptic pathology of α-synuclein aggregation in dementia with Lewy bodies, Parkinsons disease and Parkinsons disease dementia
    • W. J. Schulz-Schaeffer, "The synaptic pathology of α-synuclein aggregation in dementia with Lewy bodies, Parkinsons disease and Parkinsons disease dementia," Acta Neuropathologica, vol. 120, no. 2, pp. 131-143, 2010.
    • (2010) Acta Neuropathologica , vol.120 , Issue.2 , pp. 131-143
    • Schulz-Schaeffer, W.J.1
  • 32
    • 14844300111 scopus 로고    scopus 로고
    • Nonlinear progression of Parkinson disease as determined by serial positron emission tomographic imaging of striatal fluorodopa F 18 activity
    • R. Hilker, K. Schweitzer, S. Coburger et al. , "Nonlinear progression of Parkinson disease as determined by serial positron emission tomographic imaging of striatal fluorodopa F 18 activity," Archives of Neurology, vol. 62, no. 3, pp. 378-382, 2005.
    • (2005) Archives of Neurology , vol.62 , Issue.3 , pp. 378-382
    • Hilker, R.1    Schweitzer, K.2    Coburger, S.3
  • 33
    • 13144258735 scopus 로고    scopus 로고
    • Microglial activation and dopamine terminal loss in early Parkinsons disease
    • Y. Ouchi, E. Yoshikawa, Y. Sekine et al. , "Microglial activation and dopamine terminal loss in early Parkinsons disease," Annals of Neurology, vol. 57, no. 2, pp. 168-175, 2005.
    • (2005) Annals of Neurology , vol.57 , Issue.2 , pp. 168-175
    • Ouchi, Y.1    Yoshikawa, E.2    Sekine, Y.3
  • 34
    • 33846668043 scopus 로고    scopus 로고
    • In-vivo quantification of dose-dependent dopamine transporter blockade in the rat striatum with small animal SPECT
    • S. Nikolaus, C. Antke, M. Beu et al. , "In-vivo quantification of dose-dependent dopamine transporter blockade in the rat striatum with small animal SPECT," Nuclear Medicine Communications, vol. 28, no. 3, pp. 207-213, 2007.
    • (2007) Nuclear Medicine Communications , vol.28 , Issue.3 , pp. 207-213
    • Nikolaus, S.1    Antke, C.2    Beu, M.3
  • 35
    • 84902170828 scopus 로고    scopus 로고
    • Is Parkinsons disease a vesicular dopamine storage disorder? Evidence from a study in isolated synaptic vesicles of human and nonhuman primate striatum
    • C. Pifl, A. Rajput, H. Reither et al. , "Is Parkinsons disease a vesicular dopamine storage disorder? Evidence from a study in isolated synaptic vesicles of human and nonhuman primate striatum," The Journal of Neuroscience, vol. 34, no. 24, pp. 8210-8218, 2014.
    • (2014) The Journal of Neuroscience , vol.34 , Issue.24 , pp. 8210-8218
    • Pifl, C.1    Rajput, A.2    Reither, H.3
  • 36
    • 0034077041 scopus 로고    scopus 로고
    • Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system
    • A. Abeliovich, Y. Schmitz, I. Farinas et al. , "Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system," Neuron, vol. 25, no. 1, pp. 239-252, 2000.
    • (2000) Neuron , vol.25 , Issue.1 , pp. 239-252
    • Abeliovich, A.1    Schmitz, Y.2    Farinas, I.3
  • 38
    • 84899889312 scopus 로고    scopus 로고
    • Accumulation of oligomer-prone alpha-synuclein exacerbates synaptic and neuronal degeneration in vivo
    • E. Rockenstein, S. Nuber, C. R. Overk et al. , "Accumulation of oligomer-prone alpha-synuclein exacerbates synaptic and neuronal degeneration in vivo," Brain, vol. 137, no. 5, pp. 1496-1513, 2014.
    • (2014) Brain , vol.137 , Issue.5 , pp. 1496-1513
    • Rockenstein, E.1    Nuber, S.2    Overk, C.R.3
  • 39
    • 84893488562 scopus 로고    scopus 로고
    • Presynaptic alpha-synuclein aggregation in a mouse model of Parkinsons disease
    • K. J. Spinelli, J. K. Taylor, V. R. Osterberg et al. , "Presynaptic alpha-synuclein aggregation in a mouse model of Parkinsons disease," Journal of Neuroscience, vol. 34, no. 6, pp. 2037-2050, 2014.
    • (2014) Journal of Neuroscience , vol.34 , Issue.6 , pp. 2037-2050
    • Spinelli, K.J.1    Taylor, J.K.2    Osterberg, V.R.3
  • 40
    • 84908221942 scopus 로고    scopus 로고
    • α-synuclein multimers cluster synaptic vesicles and attenuate recycling
    • L. Wang, U. Das, D. A. Scott, Y. Tang, P. McLean, and S. Roy, "α-synuclein multimers cluster synaptic vesicles and attenuate recycling," Current Biology, vol. 24, no. 19, pp. 2319-2326, 2014.
    • (2014) Current Biology , vol.24 , Issue.19 , pp. 2319-2326
    • Wang, L.1    Das, U.2    Scott, D.A.3    Tang, Y.4    McLean, P.5    Roy, S.6
  • 41
    • 51649089030 scopus 로고    scopus 로고
    • Alpha-synuclein aggregation and cell death triggered by energy deprivation and dopamine overload are counteracted by D2/D3 receptor activation
    • A. Bellucci, G. Collo, I. Sarnico, L. Battistin, C. Missale, and P. Spano, "Alpha-synuclein aggregation and cell death triggered by energy deprivation and dopamine overload are counteracted by D2/D3 receptor activation," Journal of Neurochemistry, vol. 106, no. 2, pp. 560-577, 2008.
    • (2008) Journal of Neurochemistry , vol.106 , Issue.2 , pp. 560-577
    • Bellucci, A.1    Collo, G.2    Sarnico, I.3    Battistin, L.4    Missale, C.5    Spano, P.6
  • 42
    • 82855172161 scopus 로고    scopus 로고
    • Redistribution of DAT/α-synuclein complexes visualized by in situ proximity ligation assay in transgenic mice modelling early Parkinsons disease
    • Article IDe27959
    • A. Bellucci, L. Navarria, E. Falarti et al. , "Redistribution of DAT/α-synuclein complexes visualized by in situ proximity ligation assay in transgenic mice modelling early Parkinsons disease," PLoS ONE, vol. 6, no. 12, Article IDe27959, 2011.
    • (2011) PLoS ONE , vol.6 , Issue.12
    • Bellucci, A.1    Navarria, L.2    Falarti, E.3
  • 43
    • 2342496196 scopus 로고    scopus 로고
    • α-Synuclein regulation of the dopaminergic transporter: A possible role in the pathogenesis of Parkinsons disease
    • A. Sidhu, C. Wersinger, and P. Vernier, "α-Synuclein regulation of the dopaminergic transporter: a possible role in the pathogenesis of Parkinsons disease," FEBS Letters, vol. 565, no. 1-3, pp. 1-5, 2004.
    • (2004) FEBS Letters , vol.565 , Issue.1-3 , pp. 1-5
    • Sidhu, A.1    Wersinger, C.2    Vernier, P.3
  • 44
    • 53149130592 scopus 로고    scopus 로고
    • Nigral burden of α-synuclein correlates with striatal dopamine deficit
    • G. G. Kovacs, I. J. Milenkovic, M. Preusser, and H. Budka, "Nigral burden of α-synuclein correlates with striatal dopamine deficit," Movement Disorders, vol. 23,no. 11, pp. 1608-1612, 2008.
    • (2008) Movement Disorders , vol.23 , Issue.11 , pp. 1608-1612
    • Kovacs, G.G.1    Milenkovic, I.J.2    Preusser, M.3    Budka, H.4
  • 45
    • 77954379317 scopus 로고    scopus 로고
    • SNARE protein redistribution and synaptic failure in a transgenic mouse model of Parkinsons disease
    • P. Garcia-Reitbock, O. Anichtchik, A. Bellucci et al. , "SNARE protein redistribution and synaptic failure in a transgenic mouse model of Parkinsons disease," Brain, vol. 133, part 7, pp. 2032-2044, 2010.
    • (2010) Brain , vol.133 , Issue.PART 7 , pp. 2032-2044
    • Garcia-Reitbock, P.1    Anichtchik, O.2    Bellucci, A.3
  • 47
    • 10944243102 scopus 로고    scopus 로고
    • Role of alpha-synuclein in presynaptic dopamine recruitment
    • L. Yavich, H. Tanila, S. Vepsalainen, and P. Jakala, "Role of alpha-synuclein in presynaptic dopamine recruitment," Journal of Neuroscience, vol. 24, no. 49, pp. 11165-11170, 2004.
    • (2004) Journal of Neuroscience , vol.24 , Issue.49 , pp. 11165-11170
    • Yavich, L.1    Tanila, H.2    Vepsalainen, S.3    Jakala, P.4
  • 48
    • 27544507306 scopus 로고    scopus 로고
    • α-synuclein cooperates with CSPα in preventing neurodegeneration
    • S. Chandra, G. Gallardo, R. Fernandez-Chacon, O. M. Schluter, and T. C. Sudhof, "α-synuclein cooperates with CSPα in preventing neurodegeneration," Cell, vol. 123, no. 3, pp. 383-396, 2005.
    • (2005) Cell , vol.123 , Issue.3 , pp. 383-396
    • Chandra, S.1    Gallardo, G.2    Fernandez-Chacon, R.3    Schluter, O.M.4    Sudhof, T.C.5
  • 49
    • 84866918574 scopus 로고    scopus 로고
    • From α-synuclein to synaptic dysfunctions: New insights into the pathophysiology of Parkinsons disease
    • A. Bellucci, M. Zaltieri, L. Navarria, J. Grigoletto, C. Missale, and P. Spano, "From α-synuclein to synaptic dysfunctions: new insights into the pathophysiology of Parkinsons disease," Brain Research, vol. 1476, pp. 183-202, 2012.
    • (2012) Brain Research , vol.1476 , pp. 183-202
    • Bellucci, A.1    Zaltieri, M.2    Navarria, L.3    Grigoletto, J.4    Missale, C.5    Spano, P.6
  • 50
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinsons disease
    • M. R. Cookson, "The biochemistry of Parkinsons disease," Annual Review of Biochemistry, vol. 74, pp. 29-52, 2005.
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 51
    • 84874510614 scopus 로고    scopus 로고
    • Axonopathy in an α-synuclein transgenic model of Lewy body disease is associated with extensive accumulation of c-terminal-truncated α-synuclein
    • D. Games, P. Seubert, E. Rockenstein et al. , "Axonopathy in an α-synuclein transgenic model of Lewy body disease is associated with extensive accumulation of c-terminal-truncated α-synuclein," American Journal of Pathology, vol. 182, no. 3, pp. 940-953, 2013.
    • (2013) American Journal of Pathology , vol.182 , Issue.3 , pp. 940-953
    • Games, D.1    Seubert, P.2    Rockenstein, E.3
  • 53
    • 84862646368 scopus 로고    scopus 로고
    • Nigrostriatal overabundance of α-synuclein leads to decreased vesicle density and deficits in dopamine release that correlate with reduced motor activity
    • M. N. Gaugler, O. Genc, W. Bobela et al. , "Nigrostriatal overabundance of α-synuclein leads to decreased vesicle density and deficits in dopamine release that correlate with reduced motor activity," Acta Neuropathologica, vol. 123, no. 5, pp. 653-669, 2012.
    • (2012) Acta Neuropathologica , vol.123 , Issue.5 , pp. 653-669
    • Gaugler, M.N.1    Genc, O.2    Bobela, W.3
  • 54
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of α-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • V. M. Nemani, W. Lu, V. Berge et al., "Increased expression of α-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis," Neuron, vol. 65, no. 1, pp. 66-79, 2010.
    • (2010) Neuron , vol.65 , Issue.1 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3
  • 55
    • 84911422499 scopus 로고    scopus 로고
    • Protective glove use and hygiene habits modify the associations of specific pesticides with Parkinsons disease
    • M. Furlong, C. M. Tanner, S. M. Goldman et al. , "Protective glove use and hygiene habits modify the associations of specific pesticides with Parkinsons disease," Environment International, vol. 75, pp. 144-150, 2015.
    • (2015) Environment International , vol.75 , pp. 144-150
    • Furlong, M.1    Tanner, C.M.2    Goldman, S.M.3
  • 56
    • 79955557808 scopus 로고    scopus 로고
    • Rotenone, paraquat, and Parkinsons disease
    • C. M. Tanner, F. Kame, G. W. Ross et al. , "Rotenone, paraquat, and Parkinsons disease," EnvironmentalHealth Perspectives, vol. 119, no. 6, pp. 866-872, 2011.
    • (2011) EnvironmentalHealth Perspectives , vol.119 , Issue.6 , pp. 866-872
    • Tanner, C.M.1    Kame, F.2    Ross, G.W.3
  • 57
    • 0005444118 scopus 로고
    • Parkinsons disease in a chemist working with 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
    • article 310
    • J. W. Langston and P. A. Ballard Jr. , "Parkinsons disease in a chemist working with 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine," The New England Journal of Medicine, vol. 309, no. 5, article 310, 1983.
    • (1983) The New England Journal of Medicine , vol.309 , Issue.5
    • Langston, J.W.1    Ballard, P.A.2
  • 58
    • 84919948946 scopus 로고    scopus 로고
    • Tea polyphenols alleviate motor impairments, dopaminergic neuronal injury, and cerebral α-synuclein aggregation inMPTP-intoxicated parkinsonianmonkeys
    • M. Chen, T. Wang, F. Yue et al. , "Tea polyphenols alleviate motor impairments, dopaminergic neuronal injury, and cerebral α-synuclein aggregation inMPTP-intoxicated parkinsonianmonkeys," Neuroscience, vol. 286, pp. 383-392, 2015.
    • (2015) Neuroscience , vol.286 , pp. 383-392
    • Chen, M.1    Wang, T.2    Yue, F.3
  • 60
    • 84864023125 scopus 로고    scopus 로고
    • Loss of spinal motor neurons and alteration of alpha-synuclein immunostaining in MPTP induced Parkinsonism in mice
    • G. Vivacqua, F. Biagioni, S. Yu et al. , "Loss of spinal motor neurons and alteration of alpha-synuclein immunostaining in MPTP induced Parkinsonism in mice," Journal of Chemical Neuroanatomy, vol. 44, no. 2, pp. 76-85, 2012.
    • (2012) Journal of Chemical Neuroanatomy , vol.44 , Issue.2 , pp. 76-85
    • Vivacqua, G.1    Biagioni, F.2    Yu, S.3
  • 61
    • 0033600443 scopus 로고    scopus 로고
    • Possible relation of atypical parkinsonism in the French West Indies with consumption of tropical plants: A case-control study
    • Caribbean Parkinsonism Study Group
    • D. Caparros-Lefebvre and A. Elbaz, "Possible relation of atypical parkinsonism in the French West Indies with consumption of tropical plants: a case-control study. Caribbean Parkinsonism Study Group," The Lancet, vol. 354, no. 9175, pp. 281-286, 1999.
    • (1999) The Lancet , vol.354 , Issue.9175 , pp. 281-286
    • Caparros-Lefebvre, D.1    Elbaz, A.2
  • 62
    • 9144275011 scopus 로고    scopus 로고
    • Annonacin, a lipophilic inhibitor of mitochondrial complex I, induces nigral and striatal neurodegeneration in rats: Possible relevance for atypical parkinsonism in Guadeloupe
    • P. Champy, G. U. Hoglinger, J. Feger et al. , "Annonacin, a lipophilic inhibitor of mitochondrial complex I, induces nigral and striatal neurodegeneration in rats: possible relevance for atypical parkinsonism in Guadeloupe," Journal of Neurochemistry, vol. 88, no. 1, pp. 63-69, 2004.
    • (2004) Journal of Neurochemistry , vol.88 , Issue.1 , pp. 63-69
    • Champy, P.1    Hoglinger, G.U.2    Feger, J.3
  • 63
    • 84867230531 scopus 로고    scopus 로고
    • Pesticide exposure and Parkinsons disease: Epidemiological evidence of association
    • C. Freire and S. Koifman, "Pesticide exposure and Parkinsons disease: epidemiological evidence of association," NeuroToxicology, vol. 33, no. 5, pp. 947-971, 2012.
    • (2012) NeuroToxicology , vol.33 , Issue.5 , pp. 947-971
    • Freire, C.1    Koifman, S.2
  • 64
    • 0042160300 scopus 로고    scopus 로고
    • The rotenone model of Parkinsons disease: Genes, environment and mitochondria
    • J. T. Greenamyre, R. Betarbet, and T. B. Sherer, "The rotenone model of Parkinsons disease: genes, environment and mitochondria," Parkinsonism and Related Disorders, vol. 9, supplement 2, pp. S59-S64, 2003.
    • (2003) Parkinsonism and Related Disorders , vol.9 , pp. S59-S64
    • Greenamyre, J.T.1    Betarbet, R.2    Sherer, T.B.3
  • 65
    • 78951472329 scopus 로고    scopus 로고
    • Parkinsonian rotenone mouse model: Reevaluation of long-term administration of rotenone in C57BL/6 mice
    • M. Inden, Y. Kitamura, M. Abe, A. Tamaki, K. Takata, and T. Taniguchi, "Parkinsonian rotenone mouse model: reevaluation of long-term administration of rotenone in C57BL/6 mice," Biological and Pharmaceutical Bulletin, vol. 34, no. 1, pp. 92-96, 2011.
    • (2011) Biological and Pharmaceutical Bulletin , vol.34 , Issue.1 , pp. 92-96
    • Inden, M.1    Kitamura, Y.2    Abe, M.3    Tamaki, A.4    Takata, K.5    Taniguchi, T.6
  • 66
    • 0141533187 scopus 로고    scopus 로고
    • Themitochondrial complex i inhibitor annonacin is toxic to mesencephalic dopaminergic neurons by impairment of energy metabolism
    • A. Lannuzel, P. P. Michel, G. U. Hoglinger et al. , "Themitochondrial complex I inhibitor annonacin is toxic to mesencephalic dopaminergic neurons by impairment of energy metabolism," Neuroscience, vol. 121, no. 2, pp. 287-296, 2003.
    • (2003) Neuroscience , vol.121 , Issue.2 , pp. 287-296
    • Lannuzel, A.1    Michel, P.P.2    Hoglinger, G.U.3
  • 67
    • 77956213267 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinsons disease
    • J. Zhu and C. T. Chu, "Mitochondrial dysfunction in Parkinsons disease," Journal of Alzheimers Disease, vol. 20, supplement 2, pp. S325-S334, 2010.
    • (2010) Journal of Alzheimers Disease , vol.20 , pp. S325-S334
    • Zhu, J.1    Chu, C.T.2
  • 68
    • 0016772917 scopus 로고
    • Ultrastructure of skeletal muscle in patients with Parkinsons disease and upper motor lesions
    • G. Ahlqvist, S. Landin, and R. Wroblewski, "Ultrastructure of skeletal muscle in patients with Parkinsons disease and upper motor lesions," Laboratory Investigation, vol. 32, no. 5, pp. 673-679, 1975.
    • (1975) Laboratory Investigation , vol.32 , Issue.5 , pp. 673-679
    • Ahlqvist, G.1    Landin, S.2    Wroblewski, R.3
  • 70
    • 0031031845 scopus 로고    scopus 로고
    • Platelet mitochondrial respiratory chain function in Parkinsons disease
    • C. I. Blake, E. Spitz, M. Leehey, B. J. Hoffer, and S. J. Boyson, "Platelet mitochondrial respiratory chain function in Parkinsons disease," Movement Disorders, vol. 12, no. 1, pp. 3-8, 1997.
    • (1997) Movement Disorders , vol.12 , Issue.1 , pp. 3-8
    • Blake, C.I.1    Spitz, E.2    Leehey, M.3    Hoffer, B.J.4    Boyson, S.J.5
  • 71
    • 84868298266 scopus 로고    scopus 로고
    • The use of primary human fibroblasts for monitoring mitochondrial phenotypes in the field of Parkinsons disease
    • Article ID e4228
    • L. F. Burbulla and R. Kruger, "The use of primary human fibroblasts for monitoring mitochondrial phenotypes in the field of Parkinsons disease," Journal of Visualized Experiments, no. 68,Article ID e4228, 2012.
    • (2012) Journal of Visualized Experiments , Issue.68
    • Burbulla, L.F.1    Kruger, R.2
  • 72
    • 0029050583 scopus 로고
    • Low platelet mitochondrial complex i and complex II/III activity in early untreated Parkinsons disease
    • R. H. Haas, F. Nasirian, K. Nakano et al. , "Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinsons disease," Annals of Neurology, vol. 37, no. 6, pp. 714-722, 1995.
    • (1995) Annals of Neurology , vol.37 , Issue.6 , pp. 714-722
    • Haas, R.H.1    Nasirian, F.2    Nakano, K.3
  • 73
    • 33646948530 scopus 로고    scopus 로고
    • Parkinsons disease brain mitochondrial complex i has oxidatively damaged subunits and is functionally impaired and misassembled
    • P. M. Keeney, J. Xie, R. A. Capaldi, and J. P. Bennett Jr. , "Parkinsons disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled," The Journal of Neuroscience, vol. 26, no. 19, pp. 5256-5264, 2006.
    • (2006) The Journal of Neuroscience , vol.26 , Issue.19 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett, J.P.4
  • 74
    • 4544326057 scopus 로고    scopus 로고
    • Mitochondrial complex i and IV activities in leukocytes from patients with parkin mutations
    • M. Muftuoglu, B. Elibol, O. Dalmizrak et al. , "Mitochondrial complex I and IV activities in leukocytes from patients with parkin mutations," Movement Disorders, vol. 19, no. 5, pp. 544-548, 2004.
    • (2004) Movement Disorders , vol.19 , Issue.5 , pp. 544-548
    • Muftuoglu, M.1    Elibol, B.2    Dalmizrak, O.3
  • 75
    • 84899920605 scopus 로고    scopus 로고
    • Mitochondrial impairment observed in fibroblasts fromSouth African Parkinsons disease patients with parkin mutations
    • C. van der Merwe, B. Loos, C. Swart et al. , "Mitochondrial impairment observed in fibroblasts fromSouth African Parkinsons disease patients with parkin mutations," Biochemical and Biophysical Research Communications, vol. 447, no. 2, pp. 334-340, 2014.
    • (2014) Biochemical and Biophysical Research Communications , vol.447 , Issue.2 , pp. 334-340
    • Merwe Der C.Van1    Loos, B.2    Swart, C.3
  • 77
    • 84871005673 scopus 로고    scopus 로고
    • The pathways of mitophagy for quality control and clearance of mitochondria
    • G. Ashrafi and T. L. Schwarz, "The pathways of mitophagy for quality control and clearance of mitochondria," Cell Death and Differentiation, vol. 20, no. 1, pp. 31-42, 2013.
    • (2013) Cell Death and Differentiation , vol.20 , Issue.1 , pp. 31-42
    • Ashrafi, G.1    Schwarz, T.L.2
  • 79
    • 84864471700 scopus 로고    scopus 로고
    • PINK1 as a molecular checkpoint in the maintenance of mitochondrial function and integrity
    • H. Koh and J. Chung, "PINK1 as a molecular checkpoint in the maintenance of mitochondrial function and integrity," Molecules and Cells, vol. 34, no. 1, pp. 7-13, 2012.
    • (2012) Molecules and Cells , vol.34 , Issue.1 , pp. 7-13
    • Koh, H.1    Chung, J.2
  • 80
    • 84868575932 scopus 로고    scopus 로고
    • Mitochondrial quality control mediated by PINK1 and Parkin: Links to parkinsonism
    • D. Narendra, J. E. Walker, and R. Youle, "Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism," Cold Spring Harbor Perspectives in Biology, vol. 4, no. 11, 2012.
    • (2012) Cold Spring Harbor Perspectives in Biology , vol.4 , Issue.11
    • Narendra, D.1    Walker, J.E.2    Youle, R.3
  • 81
    • 33750598457 scopus 로고    scopus 로고
    • A heterozygous effect for PINK1 mutations in Parkinsons disease?
    • P. M. Abou-Sleiman, M. M. K. Muqit, N. Q. McDonald et al. , "A heterozygous effect for PINK1 mutations in Parkinsons disease?" Annals of Neurology, vol. 60, no. 4, pp. 414-419, 2006.
    • (2006) Annals of Neurology , vol.60 , Issue.4 , pp. 414-419
    • Abou-Sleiman, P.M.1    Muqit, M.M.K.2    McDonald, N.Q.3
  • 82
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinsons disease caused by mutations in PINK1
    • E. M. Valente, P. M. Abou-Sleiman, V. Caputo et al. , "Hereditary early-onset Parkinsons disease caused by mutations in PINK1," Science, vol. 304, no. 5674, pp. 1158-1160, 2004.
    • (2004) Science , vol.304 , Issue.5674 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3
  • 83
    • 0025942723 scopus 로고
    • Immunohistochemical studies on complexes I, II, III, and IV of mitochondria in Parkinsons disease
    • N. Hattori, M. Tanaka, T. Ozawa, and Y. Mizuno, "Immunohistochemical studies on complexes I, II, III, and IV of mitochondria in Parkinsons disease," Annals of Neurology, vol. 30, no. 4, pp. 563-571, 1991.
    • (1991) Annals of Neurology , vol.30 , Issue.4 , pp. 563-571
    • Hattori, N.1    Tanaka, M.2    Ozawa, T.3    Mizuno, Y.4
  • 85
    • 41749104745 scopus 로고    scopus 로고
    • Complex i deficiency in Parkinsons disease frontal cortex
    • W. D. Parker Jr. , J. K. Parks, and R. H. Swerdlow, "Complex I deficiency in Parkinsons disease frontal cortex," Brain Research, vol. 1189, no. 1, pp. 215-218, 2008.
    • (2008) Brain Research , vol.1189 , Issue.1 , pp. 215-218
    • Parker, W.D.1    Parks, J.K.2    Swerdlow, R.H.3
  • 86
    • 0028274216 scopus 로고
    • Evidence for mitochondrial dysfunction in Parkinsons disease-a critical appraisal
    • A. H. V. Schapira, "Evidence for mitochondrial dysfunction in Parkinsons disease-a critical appraisal," Movement Disorders, vol. 9, no. 2, pp. 125-138, 1994.
    • (1994) Movement Disorders , vol.9 , Issue.2 , pp. 125-138
    • Schapira, A.H.V.1
  • 87
    • 0029758888 scopus 로고    scopus 로고
    • Determination of regional rate constants from dynamic FDG-PET studies in Parkinsons disease
    • M. Piert, R. A. Koeppe, B. Giordani, S. Minoshima, and D. E. Kuhl, "Determination of regional rate constants from dynamic FDG-PET studies in Parkinsons disease," Journal of Nuclear Medicine, vol. 37, no. 7, pp. 1115-1122, 1996.
    • (1996) Journal of Nuclear Medicine , vol.37 , Issue.7 , pp. 1115-1122
    • Piert, M.1    Koeppe, R.A.2    Giordani, B.3    Minoshima, S.4    Kuhl, D.E.5
  • 88
    • 31444433505 scopus 로고    scopus 로고
    • Parkinsons disease and brain mitochondrial dysfunction: A functional phosphorus magnetic resonance spectroscopy study
    • M. Rango, C. Bonifati, and N. Bresolin, "Parkinsons disease and brain mitochondrial dysfunction: a functional phosphorus magnetic resonance spectroscopy study," Journal of Cerebral Blood Flow and Metabolism, vol. 26, no. 2, pp. 283-290, 2006.
    • (2006) Journal of Cerebral Blood Flow and Metabolism , vol.26 , Issue.2 , pp. 283-290
    • Rango, M.1    Bonifati, C.2    Bresolin, N.3
  • 90
    • 80053605315 scopus 로고    scopus 로고
    • Evaluation of striatal oxidative stress in patients with Parkinsons disease using [62Cu]ATSM PET
    • M. Ikawa, H. Okazawa, T. Kudo, M. Kuriyama, Y. Fujibayashi, and M. Yoneda, "Evaluation of striatal oxidative stress in patients with Parkinsons disease using [62Cu]ATSM PET," Nuclear Medicine and Biology, vol. 38, no. 7, pp. 945-951, 2011.
    • (2011) Nuclear Medicine and Biology , vol.38 , Issue.7 , pp. 945-951
    • Ikawa, M.1    Okazawa, H.2    Kudo, T.3    Kuriyama, M.4    Fujibayashi, Y.5    Yoneda, M.6
  • 91
    • 84894150737 scopus 로고    scopus 로고
    • Activity-driven local ATP synthesis is required for synaptic function
    • V. Rangaraju,N. Calloway, and T. A. Ryan, "Activity-driven local ATP synthesis is required for synaptic function," Cell, vol. 156, no. 4, pp. 825-835, 2014.
    • (2014) Cell , vol.156 , Issue.4 , pp. 825-835
    • Rangaraju, V.1    Calloway, N.2    Ryan, T.A.3
  • 92
    • 84891645843 scopus 로고    scopus 로고
    • The role of oxidative stress in parkinsons disease
    • V. Dias, E. Junn, and M. M. Mouradian, "The role of oxidative stress in parkinsons disease," Journal of Parkinsons Disease, vol. 3, no. 4, pp. 461-491, 2013.
    • (2013) Journal of Parkinsons Disease , vol.3 , Issue.4 , pp. 461-491
    • Dias, V.1    Junn, E.2    Mouradian, M.M.3
  • 93
    • 84876293052 scopus 로고    scopus 로고
    • Potassium depolarization and raised calcium induces alpha-synuclein aggregates
    • J. Follett, B. Darlow, M. B. Wong, J. Goodwin, and D. L. Pountney, "Potassium depolarization and raised calcium induces alpha-synuclein aggregates," Neurotoxicity Research, vol. 23, no. 4, pp. 378-392, 2013.
    • (2013) Neurotoxicity Research , vol.23 , Issue.4 , pp. 378-392
    • Follett, J.1    Darlow, B.2    Wong, M.B.3    Goodwin, J.4    Pountney, D.L.5
  • 94
    • 84875752373 scopus 로고    scopus 로고
    • Raised calcium and oxidative stress cooperatively promote alpha-synuclein aggregate formation
    • J. Goodwin, S. Nath, Y. Engelborghs, and D. L. Pountney, "Raised calcium and oxidative stress cooperatively promote alpha-synuclein aggregate formation," Neurochemistry International, vol. 62, no. 5, pp. 703-711, 2013.
    • (2013) Neurochemistry International , vol.62 , Issue.5 , pp. 703-711
    • Goodwin, J.1    Nath, S.2    Engelborghs, Y.3    Pountney, D.L.4
  • 96
    • 84861554724 scopus 로고    scopus 로고
    • α-synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions
    • T. Cali, D. Ottolini, A. Negro, and M. Brini, "α-synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions," The Journal of Biological Chemistry, vol. 287, no. 22, pp. 17914-17929, 2012.
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.22 , pp. 17914-17929
    • Cali, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 97
    • 34548172773 scopus 로고    scopus 로고
    • Different species of α-synuclein oligomers induce calcium influx and seeding
    • K. M. Danzer, D. Haasen, A. R. Karow et al. , "Different species of α-synuclein oligomers induce calcium influx and seeding," The Journal of Neuroscience, vol. 27, no. 34, pp. 9220-9232, 2007.
    • (2007) The Journal of Neuroscience , vol.27 , Issue.34 , pp. 9220-9232
    • Danzer, K.M.1    Haasen, D.2    Karow, A.R.3
  • 98
    • 27644578107 scopus 로고    scopus 로고
    • Mitochondrial lipid abnormality and electron transport chain impairment in mice lacking α-synuclein
    • C. E. Ellis, E. J. Murphy, D. C. Mitchell et al. , "Mitochondrial lipid abnormality and electron transport chain impairment in mice lacking α-synuclein," Molecular and Cellular Biology, vol. 25, no. 22, pp. 10190-10201, 2005.
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.22 , pp. 10190-10201
    • Ellis, C.E.1    Murphy, E.J.2    Mitchell, D.C.3
  • 99
    • 79956196722 scopus 로고    scopus 로고
    • Neuropathology of sporadic Parkinson disease before the appearance of parkinsonism: Preclinical Parkinson disease
    • I. Ferrer, A. Martinez, R. Blanco, E. Dalfo, and M. Carmona, "Neuropathology of sporadic Parkinson disease before the appearance of parkinsonism: preclinical Parkinson disease," Journal of Neural Transmission, vol. 118, no. 5, pp. 821-839, 2011.
    • (2011) Journal of Neural Transmission , vol.118 , Issue.5 , pp. 821-839
    • Ferrer, I.1    Martinez, A.2    Blanco, R.3    Dalfo, E.4    Carmona, M.5
  • 100
    • 84878920856 scopus 로고    scopus 로고
    • Lewy body pathology is associated with mitochondrial DNA damage in Parkinsons disease
    • S. K. Muller, A. Bender, C. Laub et al. , "Lewy body pathology is associated with mitochondrial DNA damage in Parkinsons disease," Neurobiology of Aging, vol. 34, no. 9, pp. 2231-2233, 2013.
    • (2013) Neurobiology of Aging , vol.34 , Issue.9 , pp. 2231-2233
    • Muller, S.K.1    Bender, A.2    Laub, C.3
  • 101
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of α-synuclein impair complex i in human dopaminergic neuronal cultures and Parkinson disease brain
    • L. Devi, V. Raghavendran, B. M. Prabhu, N. G. Avadhani, and H. K. Anandatheerthavarada, "Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain," The Journal of Biological Chemistry, vol. 283, no. 14, pp. 9089-9100, 2008.
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.14 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 102
    • 0033890821 scopus 로고    scopus 로고
    • Alpha-synuclein promotes mitochondrial deficit and oxidative stress
    • L. J. Hsu, Y. Sagara, A. Arroyo et al. , "alpha-synuclein promotes mitochondrial deficit and oxidative stress," The American Journal of Pathology, vol. 157, no. 2, pp. 401-410, 2000.
    • (2000) The American Journal of Pathology , vol.157 , Issue.2 , pp. 401-410
    • Hsu, L.J.1    Sagara, Y.2    Arroyo, A.3
  • 103
    • 79957974579 scopus 로고    scopus 로고
    • Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein α-synuclein
    • K. Nakamura, V. M. Nemani, F. Azarbal et al. , "Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein α-synuclein," The Journal of Biological Chemistry, vol. 286, no. 23, pp. 20710-20726, 2011.
    • (2011) The Journal of Biological Chemistry , vol.286 , Issue.23 , pp. 20710-20726
    • Nakamura, K.1    Nemani, V.M.2    Azarbal, F.3
  • 104
    • 77958450202 scopus 로고    scopus 로고
    • Inhibition ofmitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1
    • F. Kamp,N. Exner, A. K. Lutz et al. , "Inhibition ofmitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1," EMBO Journal, vol. 29, no. 20, pp. 3571-3589, 2010.
    • (2010) EMBO Journal , vol.29 , Issue.20 , pp. 3571-3589
    • Kamp, F.1    Exner, N.2    Lutz, A.K.3
  • 105
    • 84891410019 scopus 로고    scopus 로고
    • α-synuclein is localized to mitochondria-associated ER membranes
    • C. Guardia-Laguarta, E. Area-Gomez, C. Rub et al. , "α-synuclein is localized to mitochondria-associated ER membranes," The Journal of Neuroscience, vol. 34, no. 1, pp. 249-259, 2014.
    • (2014) The Journal of Neuroscience , vol.34 , Issue.1 , pp. 249-259
    • Guardia-Laguarta, C.1    Area-Gomez, E.2    Rub, C.3
  • 106
    • 84860471851 scopus 로고    scopus 로고
    • Role of alpha-synuclein protein levels in mitochondrial morphology and cell survival in cell lines
    • Article ID e36377
    • M. Zhu,W. Li, and C. Lu, "Role of alpha-synuclein protein levels in mitochondrial morphology and cell survival in cell lines," PLoS ONE, vol. 7, no. 4,Article ID e36377, 2012.
    • (2012) PLoS ONE , vol.7 , Issue.4
    • Zhu, M.1    Li, W.2    Lu, C.3
  • 107
    • 84918777743 scopus 로고    scopus 로고
    • α-synuclein-induced mitochondrial dysfunction in isolated preparation and intact cells: Implications in the pathogenesis of Parkinsons disease
    • A. Bir, O. Sen, S. Anand et al. , "α-synuclein-induced mitochondrial dysfunction in isolated preparation and intact cells: implications in the pathogenesis of Parkinsons disease," Journal of Neurochemistry, vol. 131, no. 6, pp. 868-877, 2014.
    • (2014) Journal of Neurochemistry , vol.131 , Issue.6 , pp. 868-877
    • Bir, A.1    Sen, O.2    An, S.3
  • 108
    • 84906751686 scopus 로고    scopus 로고
    • Linking alpha-synuclein phosphorylation to reactive oxygen species formation and mitochondrial dysfunction in SH-SY5Y cells
    • R. Perfeito, D. F. Lazaro, T. F. Outeiro, and A. C. Rego, "Linking alpha-synuclein phosphorylation to reactive oxygen species formation and mitochondrial dysfunction in SH-SY5Y cells," Molecular and Cellular Neuroscience, vol. 62, pp. 51-59, 2014.
    • (2014) Molecular and Cellular Neuroscience , vol.62 , pp. 51-59
    • Perfeito, R.1    Lazaro, D.F.2    Outeiro, T.F.3    Rego, A.C.4
  • 109
    • 84893521264 scopus 로고    scopus 로고
    • Human A53T α-synuclein causes reversible deficits in mitochondrial function and dynamics in primary mouse cortical neurons
    • Article ID e85815
    • L. Li, S. Nadanaciva, Z. Berger et al. , "Human A53T α-synuclein causes reversible deficits in mitochondrial function and dynamics in primary mouse cortical neurons," PLoS ONE, vol. 8, no. 12, Article ID e85815, 2013.
    • (2013) PLoS ONE , vol.8 , Issue.12
    • Li, L.1    Nadanaciva, S.2    Berger, Z.3
  • 110
    • 84876561267 scopus 로고    scopus 로고
    • TOM40 mediates mitochondrial dysfunction induced by α-synuclein accumulation in Parkinsons disease
    • Article ID e62277
    • A. Bender, P. Desplats, B. Spencer et al. , "TOM40 mediates mitochondrial dysfunction induced by α-synuclein accumulation in Parkinsons disease," PLoS ONE, vol. 8, no. 4, Article ID e62277, 2013.
    • (2013) PLoS ONE , vol.8 , Issue.4
    • Bender, A.1    Desplats, P.2    Spencer, B.3
  • 111
    • 84904749389 scopus 로고    scopus 로고
    • Region specific mitochondrial impairment in mice with widespread overexpression of alpha-synuclein
    • S. R. Subramaniam, L. Vergnes, N. R. Franich, K. Reue, and M. Chesselet, "Region specific mitochondrial impairment in mice with widespread overexpression of alpha-synuclein," Neurobiology of Disease, vol. 70, pp. 204-213, 2014.
    • (2014) Neurobiology of Disease , vol.70 , pp. 204-213
    • Subramaniam, S.R.1    Vergnes, L.2    Franich, N.R.3    Reue, K.4    Chesselet, M.5
  • 113
    • 33244460534 scopus 로고    scopus 로고
    • Mice lacking alphasynuclein are resistant to mitochondrial toxins
    • P. Klivenyi, D. Siwek, G. Gardian et al. , "Mice lacking alphasynuclein are resistant to mitochondrial toxins," Neurobiology of Disease, vol. 21, no. 3, pp. 541-548, 2006.
    • (2006) Neurobiology of Disease , vol.21 , Issue.3 , pp. 541-548
    • Klivenyi, P.1    Siwek, D.2    Gardian, G.3
  • 114
    • 0038404962 scopus 로고    scopus 로고
    • Role of α-synuclein in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridineinduced Parkinsonism in mice
    • O. M. Schluter, F. Fornai, M. G. Alessandri et al. , "Role of α-synuclein in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridineinduced Parkinsonism in mice," Neuroscience, vol. 118, no. 4, pp. 985-1002, 2003.
    • (2003) Neuroscience , vol.118 , Issue.4 , pp. 985-1002
    • Schluter, O.M.1    Fornai, F.2    Alessandri, M.G.3
  • 115
    • 84867031150 scopus 로고    scopus 로고
    • Mitochondrial dysfunction associated with increased oxidative stress and α-synuclein accumulation in PARK2 iPSC-derived neurons and postmortem brain tissue
    • article 35
    • Y. Imaizumi, Y. Okada, W. Akamatsu et al. , "Mitochondrial dysfunction associated with increased oxidative stress and α-synuclein accumulation in PARK2 iPSC-derived neurons and postmortem brain tissue," Molecular Brain, vol. 5, no. 1, article 35, 2012.
    • (2012) Molecular Brain , vol.5 , Issue.1
    • Imaizumi, Y.1    Okada, Y.2    Akamatsu, W.3
  • 116
    • 30644471051 scopus 로고    scopus 로고
    • Parkinsons disease α-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death
    • L. J. Martin, Y. Pan, A. C. Price et al. , "Parkinsons disease α-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death," The Journal of Neuroscience, vol. 26, no. 1, pp. 41-50, 2006.
    • (2006) The Journal of Neuroscience , vol.26 , Issue.1 , pp. 41-50
    • Martin, L.J.1    Pan, Y.2    Price, A.C.3
  • 118
    • 84887706170 scopus 로고    scopus 로고
    • The rescue of microtubule-dependent traffic recoversmitochondrial function in Parkinsons disease
    • A. R. Esteves, I. Gozes, and S. M. Cardoso, "The rescue of microtubule-dependent traffic recoversmitochondrial function in Parkinsons disease," Biochimica et Biophysica Acta:Molecular Basis of Disease, vol. 1842, no. 1, pp. 7-21, 2014.
    • (2014) Biochimica et Biophysica Acta:Molecular Basis of Disease , vol.1842 , Issue.1 , pp. 7-21
    • Esteves, A.R.1    Gozes, I.2    Cardoso, S.M.3
  • 119
    • 85005916286 scopus 로고    scopus 로고
    • The small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity
    • O. Chutna, S. Goncalves, A. Villar-Pique et al. , "The small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity," Human Molecular Genetics, vol. 23, no. 25, pp. 6732-6745, 2014.
    • (2014) Human Molecular Genetics , vol.23 , Issue.25 , pp. 6732-6745
    • Chutna, O.1    Goncalves, S.2    Villar-Pique, A.3
  • 120
    • 18044381951 scopus 로고    scopus 로고
    • Alpha-synuclein binding to rab3a in multiple system atrophy
    • E. Dalfo and I. Ferrer, "Alpha-synuclein binding to rab3a in multiple system atrophy," Neuroscience Letters, vol. 380, no. 1-2, pp. 170-175, 2005.
    • (2005) Neuroscience Letters , vol.380 , Issue.1-2 , pp. 170-175
    • Dalfo, E.1    Ferrer, I.2
  • 121
    • 0034091659 scopus 로고    scopus 로고
    • Expression of the endocytosis regulatory proteins Rab5 and Rabaptin-5 in glial cytoplasmic inclusions from brains with multiple system atrophy
    • S. Nakamura, Y. Kawamoto, S. Nakano, and I. Akiguchi, "Expression of the endocytosis regulatory proteins Rab5 and Rabaptin-5 in glial cytoplasmic inclusions from brains with multiple system atrophy," Clinical Neuropathology, vol. 19, no. 2, pp. 51-56, 2000.
    • (2000) Clinical Neuropathology , vol.19 , Issue.2 , pp. 51-56
    • Nakamura, S.1    Kawamoto, Y.2    Nakano, S.3    Akiguchi, I.4
  • 122
    • 0028107932 scopus 로고
    • Rab GTPases: Master regulators of membrane trafficking
    • S. R. Pfeffer, "Rab GTPases: master regulators of membrane trafficking," Current Opinion in Cell Biology, vol. 6, no. 4, pp. 522-526, 1994.
    • (1994) Current Opinion in Cell Biology , vol.6 , Issue.4 , pp. 522-526
    • Pfeffer, S.R.1
  • 124
    • 0027538111 scopus 로고
    • An early cytoplasmic change before Lewy body maturation: An ultrastructural study of the substantia nigra from an autopsy case of juvenile parkinsonism
    • K. Hayashida, S. Oyanagi, Y. Mizutani, and M. Yokochi, "An early cytoplasmic change before Lewy body maturation: an ultrastructural study of the substantia nigra from an autopsy case of juvenile parkinsonism," Acta Neuropathologica, vol. 85, no. 4, pp. 445-448, 1993.
    • (1993) Acta Neuropathologica , vol.85 , Issue.4 , pp. 445-448
    • Hayashida, K.1    Oyanagi, S.2    Mizutani, Y.3    Yokochi, M.4
  • 126
    • 69749124032 scopus 로고    scopus 로고
    • Chronic rotenone exposure reproduces Parkinsons disease gastrointestinal neuropathology
    • R. E. Drolet, J. R. Cannon, L. Montero, and J. T. Greenamyre, "Chronic rotenone exposure reproduces Parkinsons disease gastrointestinal neuropathology," Neurobiology of Disease, vol. 36, no. 1, pp. 96-102, 2009.
    • (2009) Neurobiology of Disease , vol.36 , Issue.1 , pp. 96-102
    • Drolet, R.E.1    Cannon, J.R.2    Montero, L.3    Greenamyre, J.T.4
  • 127
    • 1842621154 scopus 로고    scopus 로고
    • Iron and α-synuclein in the substantia nigra ofMPTP-treated mice: Effect of neuroprotective drugs R-apomorphine and green tea polyphenol (-)-epigallocatechin-3-gallate
    • S. Mandel, G. Maor, and M. B. H. Youdim, "Iron and α-synuclein in the substantia nigra ofMPTP-treated mice: effect of neuroprotective drugs R-apomorphine and green tea polyphenol (-)-epigallocatechin-3-gallate," Journal ofMolecular Neuroscience, vol. 24, no. 3, pp. 401-416, 2004.
    • (2004) Journal OfMolecular Neuroscience , vol.24 , Issue.3 , pp. 401-416
    • Mandel, S.1    Maor, G.2    Youdim, M.B.H.3
  • 128
    • 84870769168 scopus 로고    scopus 로고
    • Environmental toxins trigger PD-like progression via increased alphasynuclein release from enteric neurons in mice
    • article 898
    • F. Pan-Montojo, M. Schwarz, C. Winkler et al. , "Environmental toxins trigger PD-like progression via increased alphasynuclein release from enteric neurons in mice," Scientific Reports, vol. 2, article 898, 2012.
    • (2012) Scientific Reports , vol.2
    • Pan-Montojo, F.1    Schwarz, M.2    Winkler, C.3
  • 129
    • 80055106119 scopus 로고    scopus 로고
    • Oral administration of rotenone using a gavage and image analysis of alpha-synuclein inclusions in the enteric nervous system
    • article 2123
    • F. J. Pan-Montojo and R. H. W. Funk, "Oral administration of rotenone using a gavage and image analysis of alpha-synuclein inclusions in the enteric nervous system," Journal of Visualized Experiments, no. 44, article 2123, 2010.
    • (2010) Journal of Visualized Experiments , Issue.44
    • Pan-Montojo, F.J.1    Funk, R.H.W.2
  • 130
    • 84886095184 scopus 로고    scopus 로고
    • Evaluation of nigrostriatal neurodegeneration and neuroinflammation following repeated intranasal 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) administration in mice, an experimental model of Parkinsons disease
    • F. S. M. Tristao, M. Amar, I. Latrous, E. A. Del-Bel, R. D. Prediger, and R. Raisman-Vozari, "Evaluation of nigrostriatal neurodegeneration and neuroinflammation following repeated intranasal 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) administration in mice, an experimental model of Parkinsons disease," Neurotoxicity Research, vol. 25, no. 1, pp. 24-32, 2014.
    • (2014) Neurotoxicity Research , vol.25 , Issue.1 , pp. 24-32
    • Tristao, F.S.M.1    Amar, M.2    Latrous, I.3    Del-Bel, E.A.4    Prediger, R.D.5    Raisman-Vozari, R.6
  • 131
    • 84862705469 scopus 로고    scopus 로고
    • UCP4 is a target effector of the NF-κB c-Rel prosurvival pathway against oxidative stress
    • J. Wing-Man Ho, P. Wing-Lok Ho, H.-F. Liu et al. , "UCP4 is a target effector of the NF-κB c-Rel prosurvival pathway against oxidative stress," Free Radical Biology and Medicine, vol. 53, no. 2, pp. 383-394, 2012.
    • (2012) Free Radical Biology and Medicine , vol.53 , Issue.2 , pp. 383-394
    • Wing-Man Ho, J.1    Wing-Lok Ho, P.2    Liu, H.-F.3
  • 132
    • 84866377694 scopus 로고    scopus 로고
    • Late-onset Parkinsonism in NFkappaB/c-Rel-deficient mice
    • C. Baiguera, M. Alghisi, A. Pinna et al. , "Late-onset Parkinsonism in NFkappaB/c-Rel-deficient mice," Brain, vol. 135, no. 9, pp. 2750-2765, 2012.
    • (2012) Brain , vol.135 , Issue.9 , pp. 2750-2765
    • Baiguera, C.1    Alghisi, M.2    Pinna, A.3
  • 133
    • 84907695054 scopus 로고    scopus 로고
    • In vivo mitochondrial inhibition alters corticostriatal synaptic function and the modulatory effects of neurotrophins
    • E. Mendoza, J. Miranda-Barrientos, R. Vazquez-Roque et al. , "In vivo mitochondrial inhibition alters corticostriatal synaptic function and the modulatory effects of neurotrophins," Neuroscience, vol. 280, pp. 156-170, 2014.
    • (2014) Neuroscience , vol.280 , pp. 156-170
    • Mendoza, E.1    Miranda-Barrientos, J.2    Vazquez-Roque, R.3
  • 134
    • 84870231777 scopus 로고    scopus 로고
    • Accumulation of α-synuclein triggered by presynaptic dysfunction
    • Y. Nakata, T. Yasuda, M. Fukaya et al. , "Accumulation of α-synuclein triggered by presynaptic dysfunction," The Journal of Neuroscience, vol. 32, no. 48, pp. 17186-17196, 2012.
    • (2012) The Journal of Neuroscience , vol.32 , Issue.48 , pp. 17186-17196
    • Nakata, Y.1    Yasuda, T.2    Fukaya, M.3
  • 135
    • 84881311235 scopus 로고    scopus 로고
    • Regulation of mitochondrial dynamics and distribution by synapse position and neuronal activity in the axon
    • K. Obashi and S. Okabe, "Regulation of mitochondrial dynamics and distribution by synapse position and neuronal activity in the axon," European Journal of Neuroscience, vol. 38, no. 3, pp. 2350-2363, 2013.
    • (2013) European Journal of Neuroscience , vol.38 , Issue.3 , pp. 2350-2363
    • Obashi, K.1    Okabe, S.2
  • 136
    • 68249087424 scopus 로고    scopus 로고
    • Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice
    • N. Ishihara,M. Nomura, A. Jofuku et al. , "Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice," Nature Cell Biology, vol. 11, no. 8, pp. 958-966, 2009.
    • (2009) Nature Cell Biology , vol.11 , Issue.8 , pp. 958-966
    • Ishihara, N.1    Nomura, M.2    Jofuku, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.