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Volumn 114, Issue 3, 2007, Pages 327-344

Environmental neurotoxic chemicals-induced ubiquitin proteasome system dysfunction in the pathogenesis and progression of Parkinson's disease

Author keywords

Synuclein; Dieldrin; Neurotoxicants; Neurotoxicity; Oxidative stess; Parkinson's disease; Proteasome; UPS

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; ALPHA SYNUCLEIN; BORTEZOMIB; CURCUMIN; DIELDRIN; DOPAMINE; EPOXOMICIN; IRON; LACTACYSTIN; LACTONE; MANEB; MANGANESE; NEUROTOXIN; PARAQUAT; PROTEASOME; REPINOTAN; ROTENONE; UBIQUITIN;

EID: 34249681825     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2007.04.001     Document Type: Review
Times cited : (59)

References (212)
  • 1
    • 0034077041 scopus 로고    scopus 로고
    • Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system
    • Abeliovich A., Schmitz Y., Farinas I., Choi-Lundberg D., Ho W.H., Castillo P.E., et al. Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron 25 1 (2000) 239-252
    • (2000) Neuron , vol.25 , Issue.1 , pp. 239-252
    • Abeliovich, A.1    Schmitz, Y.2    Farinas, I.3    Choi-Lundberg, D.4    Ho, W.H.5    Castillo, P.E.6
  • 2
    • 0036932955 scopus 로고    scopus 로고
    • Effect of neurotoxic metal ions on the proteolytic activities of the 20S proteasome from bovine brain
    • Amici M., Forti K., Nobili C., Lupidi G., Angeletti M., Fioretti E., et al. Effect of neurotoxic metal ions on the proteolytic activities of the 20S proteasome from bovine brain. J Biol Inorg Chem 7 7-8 (2002) 750-756
    • (2002) J Biol Inorg Chem , vol.7 , Issue.7-8 , pp. 750-756
    • Amici, M.1    Forti, K.2    Nobili, C.3    Lupidi, G.4    Angeletti, M.5    Fioretti, E.6
  • 3
    • 27244437782 scopus 로고    scopus 로고
    • Effect of metals on herbicides-alpha-synuclein association: a possible factor in neurodegenerative disease studied by capillary electrophoresis
    • Andre C., Truong T.T., Robert J.F., and Guillaume Y.C. Effect of metals on herbicides-alpha-synuclein association: a possible factor in neurodegenerative disease studied by capillary electrophoresis. Electrophoresis 26 17 (2005) 3256-3264
    • (2005) Electrophoresis , vol.26 , Issue.17 , pp. 3256-3264
    • Andre, C.1    Truong, T.T.2    Robert, J.F.3    Guillaume, Y.C.4
  • 4
    • 5644246423 scopus 로고    scopus 로고
    • The role of ubiquitin-protein ligases in neurodegenerative disease
    • Ardley H.C., and Robinson P.A. The role of ubiquitin-protein ligases in neurodegenerative disease. Neurodegener Dis 1 (2004) 71-87
    • (2004) Neurodegener Dis , vol.1 , pp. 71-87
    • Ardley, H.C.1    Robinson, P.A.2
  • 5
    • 0242531029 scopus 로고    scopus 로고
    • Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin
    • Ardley H.C., Scott G.B., Rose S.A., Tan N.G., Markham A.F., and Robinson P.A. Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin. Mol Biol Cell 14 11 (2003) 4541-4556
    • (2003) Mol Biol Cell , vol.14 , Issue.11 , pp. 4541-4556
    • Ardley, H.C.1    Scott, G.B.2    Rose, S.A.3    Tan, N.G.4    Markham, A.F.5    Robinson, P.A.6
  • 6
    • 3142724742 scopus 로고    scopus 로고
    • UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease
    • Ardley H.C., Scott G.B., Rose S.A., Tan N.G., and Robinson P.A. UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease. J Neurochem 90 2 (2004) 379-391
    • (2004) J Neurochem , vol.90 , Issue.2 , pp. 379-391
    • Ardley, H.C.1    Scott, G.B.2    Rose, S.A.3    Tan, N.G.4    Robinson, P.A.5
  • 7
    • 9144245594 scopus 로고    scopus 로고
    • Quinone formation as dopaminergic neuron-specific oxidative stress in the pathogenesis of sporadic Parkinson's disease and neurotoxin-induced parkinsonism
    • Asanuma M., Miyazaki I., Diaz-Corrales F.J., and Ogawa N. Quinone formation as dopaminergic neuron-specific oxidative stress in the pathogenesis of sporadic Parkinson's disease and neurotoxin-induced parkinsonism. Acta Med Okayama 58 5 (2004) 221-233
    • (2004) Acta Med Okayama , vol.58 , Issue.5 , pp. 221-233
    • Asanuma, M.1    Miyazaki, I.2    Diaz-Corrales, F.J.3    Ogawa, N.4
  • 8
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck P.K., Chan H.Y., Trojanowski J.Q., Lee V.M., and Bonini N.M. Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295 5556 (2002) 865-868
    • (2002) Science , vol.295 , Issue.5556 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 9
    • 13244267202 scopus 로고    scopus 로고
    • Mechanisms of suppression of α-synuclein neurotoxicity by geldanamycin in Drosophila
    • Auluck P.K., Meulener M.C., and Bonini N.M. Mechanisms of suppression of α-synuclein neurotoxicity by geldanamycin in Drosophila. J Biol Chem 280 4 (2005) 2873-2878
    • (2005) J Biol Chem , vol.280 , Issue.4 , pp. 2873-2878
    • Auluck, P.K.1    Meulener, M.C.2    Bonini, N.M.3
  • 10
    • 24644448584 scopus 로고    scopus 로고
    • Synphilin-1 and parkin show overlapping expression patterns in human brain and form aggresomes in response to proteasomal inhibition
    • Bandopadhyay R., Kingsbury A.E., Muqit M.M., Harvey K., Reid A.R., Kilford L., et al. Synphilin-1 and parkin show overlapping expression patterns in human brain and form aggresomes in response to proteasomal inhibition. Neurobiol Dis 20 2 (2005) 401-411
    • (2005) Neurobiol Dis , vol.20 , Issue.2 , pp. 401-411
    • Bandopadhyay, R.1    Kingsbury, A.E.2    Muqit, M.M.3    Harvey, K.4    Reid, A.R.5    Kilford, L.6
  • 11
    • 0034844226 scopus 로고    scopus 로고
    • Is there a rationale for neuroprotection against dopamine toxicity in Parkinson's disease?
    • Barzilai A., Melamed E., and Shirvan A. Is there a rationale for neuroprotection against dopamine toxicity in Parkinson's disease?. Cell Mol Neurobiol 21 3 (2001) 215-235
    • (2001) Cell Mol Neurobiol , vol.21 , Issue.3 , pp. 215-235
    • Barzilai, A.1    Melamed, E.2    Shirvan, A.3
  • 12
    • 14344263884 scopus 로고    scopus 로고
    • The role of alpha-synuclein in neurodegenerative diseases
    • Bennett M.C. The role of alpha-synuclein in neurodegenerative diseases. Pharmacol Ther 105 3 (2005) 311-331
    • (2005) Pharmacol Ther , vol.105 , Issue.3 , pp. 311-331
    • Bennett, M.C.1
  • 14
    • 11344262265 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and Parkinson's diseases
    • Betarbet R., Sherer T.B., and Greenamyre J.T. Ubiquitin-proteasome system and Parkinson's diseases. Exp Neurol 191 Suppl 1 (2005) S17-S27
    • (2005) Exp Neurol , vol.191 , Issue.SUPPL. 1
    • Betarbet, R.1    Sherer, T.B.2    Greenamyre, J.T.3
  • 15
    • 33745612296 scopus 로고    scopus 로고
    • Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system
    • Betarbet R., Canet-Aviles R.M., Sherer T.B., Mastroberardino P.G., McLendon C., Kim J.H., et al. Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system. Neurobiol Dis 22 2 (2006) 404-420
    • (2006) Neurobiol Dis , vol.22 , Issue.2 , pp. 404-420
    • Betarbet, R.1    Canet-Aviles, R.M.2    Sherer, T.B.3    Mastroberardino, P.G.4    McLendon, C.5    Kim, J.H.6
  • 16
    • 29444455075 scopus 로고    scopus 로고
    • Drosophila as a model for human neurodegenerative disease
    • Bilen J., and Bonini N.M. Drosophila as a model for human neurodegenerative disease. Annu Rev Genet 39 (2005) 153-171
    • (2005) Annu Rev Genet , vol.39 , pp. 153-171
    • Bilen, J.1    Bonini, N.M.2
  • 17
    • 26844505808 scopus 로고    scopus 로고
    • Toxin-induced models of Parkinson's disease
    • Bove J., Prou D., Perier C., and Przedborski S. Toxin-induced models of Parkinson's disease. NeuroRx 2 3 (2005) 484-494
    • (2005) NeuroRx , vol.2 , Issue.3 , pp. 484-494
    • Bove, J.1    Prou, D.2    Perier, C.3    Przedborski, S.4
  • 19
    • 33644499124 scopus 로고    scopus 로고
    • Dopamine in neurotoxicity and neuroprotection: what do D2 receptors have to do with it?
    • Bozzi Y., and Borrelli E. Dopamine in neurotoxicity and neuroprotection: what do D2 receptors have to do with it?. Trends Neurosci 29 3 (2006) 167-174
    • (2006) Trends Neurosci , vol.29 , Issue.3 , pp. 167-174
    • Bozzi, Y.1    Borrelli, E.2
  • 20
    • 0033608811 scopus 로고    scopus 로고
    • Paraquat elicited neurobehavioral syndrome caused by dopaminergic neuron loss
    • Brooks A.I., Chadwick C.A., Gelbard H.A., Cory-Slechta D.A., and Federoff H.J. Paraquat elicited neurobehavioral syndrome caused by dopaminergic neuron loss. Brain Res 823 1-2 (1999) 1-10
    • (1999) Brain Res , vol.823 , Issue.1-2 , pp. 1-10
    • Brooks, A.I.1    Chadwick, C.A.2    Gelbard, H.A.3    Cory-Slechta, D.A.4    Federoff, H.J.5
  • 21
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein
    • Cabin D.E., Shimazu K., Murphy D., Cole N.B., Gottschalk W., McIlwain K.L., et al. Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein. J Neurosci 22 20 (2002) 8797-8807
    • (2002) J Neurosci , vol.22 , Issue.20 , pp. 8797-8807
    • Cabin, D.E.1    Shimazu, K.2    Murphy, D.3    Cole, N.B.4    Gottschalk, W.5    McIlwain, K.L.6
  • 22
    • 23444455247 scopus 로고    scopus 로고
    • Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway
    • Cappai R., Leck S.L., Tew D.J., Williamson N.A., Smith D.P., Galatis D., et al. Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway. FASEB J 19 10 (2005) 1377-1379
    • (2005) FASEB J , vol.19 , Issue.10 , pp. 1377-1379
    • Cappai, R.1    Leck, S.L.2    Tew, D.J.3    Williamson, N.A.4    Smith, D.P.5    Galatis, D.6
  • 24
    • 33845950366 scopus 로고    scopus 로고
    • The fly as a model from neurodegenerative diseases: is it worth the jump?
    • Cauchi R.J., and van den Heuvel M. The fly as a model from neurodegenerative diseases: is it worth the jump?. Neurodegener Dis 3 6 (2006) 338-356
    • (2006) Neurodegener Dis , vol.3 , Issue.6 , pp. 338-356
    • Cauchi, R.J.1    van den Heuvel, M.2
  • 25
    • 32544432029 scopus 로고    scopus 로고
    • Non-motor symptoms of Parkinson's disease: diagnosis and management
    • Chaudhuri K.R., Healy D.G., and Schapira A.H. Non-motor symptoms of Parkinson's disease: diagnosis and management. Lancet Neurol 5 3 (2006) 235-245
    • (2006) Lancet Neurol , vol.5 , Issue.3 , pp. 235-245
    • Chaudhuri, K.R.1    Healy, D.G.2    Schapira, A.H.3
  • 26
    • 9444257518 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta (GSK3beta) mediates 6-hydroxydopamine-induced neuronal death
    • Chen G., Bower K.A., Ma C., Fang S., Thiele C.J., and Luo J. Glycogen synthase kinase 3beta (GSK3beta) mediates 6-hydroxydopamine-induced neuronal death. FASEB J 18 (2004) 1162-1164
    • (2004) FASEB J , vol.18 , pp. 1162-1164
    • Chen, G.1    Bower, K.A.2    Ma, C.3    Fang, S.4    Thiele, C.J.5    Luo, J.6
  • 27
    • 24044516868 scopus 로고    scopus 로고
    • Alpha-synuclein alters proteasome function, protein synthesis, and stationary phase viability
    • Chen Q., Thorpe J., and Keller J.N. Alpha-synuclein alters proteasome function, protein synthesis, and stationary phase viability. J Biol Chem 280 34 (2005) 30009-30017
    • (2005) J Biol Chem , vol.280 , Issue.34 , pp. 30009-30017
    • Chen, Q.1    Thorpe, J.2    Keller, J.N.3
  • 28
    • 33745140532 scopus 로고    scopus 로고
    • Proteasome dysfunction in aged human alpha-synuclein transgenic mice
    • Chen L., Thiruchelvam M.J., Madura K., and Richfield E.K. Proteasome dysfunction in aged human alpha-synuclein transgenic mice. Neurobiol Dis 23 1 (2006) 120-126
    • (2006) Neurobiol Dis , vol.23 , Issue.1 , pp. 120-126
    • Chen, L.1    Thiruchelvam, M.J.2    Madura, K.3    Richfield, E.K.4
  • 29
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J., Levey A.I., Weintraub S.T., Rees H.D., Gearing M., Chin L.S., et al. Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J Biol Chem 279 13 (2004) 13256-13264
    • (2004) J Biol Chem , vol.279 , Issue.13 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6
  • 30
    • 27944510125 scopus 로고    scopus 로고
    • Proteasome dysfunction in mammalian aging: steps and factors involved
    • Chondrogianni N., and Gonos E.S. Proteasome dysfunction in mammalian aging: steps and factors involved. Exp Gerontol 40 (2005) 931-938
    • (2005) Exp Gerontol , vol.40 , pp. 931-938
    • Chondrogianni, N.1    Gonos, E.S.2
  • 31
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease
    • Chung K.K., Zhang Y., Lim K.L., Tanaka Y., Huang H., Gao J., et al. Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat Med 7 10 (2001) 1144-1150
    • (2001) Nat Med , vol.7 , Issue.10 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6
  • 32
    • 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., et al. S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 304 5675 (2004) 1328-1331
    • (2004) Science , vol.304 , Issue.5675 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6
  • 33
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark I.E., Dodson M.W., Jiang C., Cao J.H., Huh J.R., Seol J.H., et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 7097 (2006) 1162-1166
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6
  • 34
    • 15744402739 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments
    • Cole N.B., Murphy D.D., Lebowitz J., Di Noto L., Levine R.L., and Nussbaum R.L. Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments. J Biol Chem 280 10 (2005) 9678-9690
    • (2005) J Biol Chem , vol.280 , Issue.10 , pp. 9678-9690
    • Cole, N.B.1    Murphy, D.D.2    Lebowitz, J.3    Di Noto, L.4    Levine, R.L.5    Nussbaum, R.L.6
  • 35
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway K.A., Rochet J.C., Bieganski R.M., and Lansbury Jr. P.T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294 5545 (2001) 1346-1349
    • (2001) Science , vol.294 , Issue.5545 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 37
    • 10744220754 scopus 로고    scopus 로고
    • The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration
    • Corti O., Hampe C., Koutnikova H., Darios F., Jacquier S., Prigent A., et al. The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration. Hum Mol Genet 12 12 (2003) 1427-1437
    • (2003) Hum Mol Genet , vol.12 , Issue.12 , pp. 1427-1437
    • Corti, O.1    Hampe, C.2    Koutnikova, H.3    Darios, F.4    Jacquier, S.5    Prigent, A.6
  • 38
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • Darios F., Corti O., Lucking C.B., Hampe C., Muriel M.P., Abbas N., et al. Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Hum Mol Genet 12 5 (2003) 517-526
    • (2003) Hum Mol Genet , vol.12 , Issue.5 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lucking, C.B.3    Hampe, C.4    Muriel, M.P.5    Abbas, N.6
  • 39
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: mechanisms and models
    • Dauer W., and Przedborski S. Parkinson's disease: mechanisms and models. Neuron 39 6 (2003) 889-909
    • (2003) Neuron , vol.39 , Issue.6 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 41
    • 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 83 3-4 (2001) 301-310
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 301-310
    • Davies, K.J.1
  • 42
  • 44
    • 0035451913 scopus 로고    scopus 로고
    • Proteasomes and proteasome inhibition in the central nervous system
    • Ding Q., and Keller J.N. Proteasomes and proteasome inhibition in the central nervous system. Free Radic Biol Med 31 (2001) 574-584
    • (2001) Free Radic Biol Med , vol.31 , pp. 574-584
    • Ding, Q.1    Keller, J.N.2
  • 45
    • 0035006792 scopus 로고    scopus 로고
    • Proteasome inhibition in oxidative stress neurotoxicity: implications for heat shock proteins
    • Ding Q., and Keller J.N. Proteasome inhibition in oxidative stress neurotoxicity: implications for heat shock proteins. J Neurochem 77 4 (2001) 1010-1017
    • (2001) J Neurochem , vol.77 , Issue.4 , pp. 1010-1017
    • Ding, Q.1    Keller, J.N.2
  • 46
    • 33644652951 scopus 로고    scopus 로고
    • Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS
    • Ding Q., Dimayuga E., and Keller J.N. Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS. Antioxid Redox Signal 8 (2006) 163-172
    • (2006) Antioxid Redox Signal , vol.8 , pp. 163-172
    • Ding, Q.1    Dimayuga, E.2    Keller, J.N.3
  • 48
    • 0142059791 scopus 로고    scopus 로고
    • Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1
    • Dong Z., Ferger B., Paterna J.C., Vogel D., Furler S., Osinde M., et al. Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1. Proc Natl Acad Sci U S A 100 21 (2003) 12438-12443
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.21 , pp. 12438-12443
    • Dong, Z.1    Ferger, B.2    Paterna, J.C.3    Vogel, D.4    Furler, S.5    Osinde, M.6
  • 49
    • 3542993306 scopus 로고    scopus 로고
    • Mice lacking alpha-synuclein have an attenuated loss of striatal dopamine following prolonged chronic MPTP administration
    • Drolet R.E., Behrouz B., Lookingland K.J., and Goudreau J.L. Mice lacking alpha-synuclein have an attenuated loss of striatal dopamine following prolonged chronic MPTP administration. Neurotoxicology 25 5 (2004) 761-769
    • (2004) Neurotoxicology , vol.25 , Issue.5 , pp. 761-769
    • Drolet, R.E.1    Behrouz, B.2    Lookingland, K.J.3    Goudreau, J.L.4
  • 50
    • 0035567927 scopus 로고    scopus 로고
    • 6-Hydroxydopamine increases ubiquitin-conjugates and protein degradation: implications for the pathogenesis of Parkinson's disease
    • Elkon H., Melamed E., and Offen D. 6-Hydroxydopamine increases ubiquitin-conjugates and protein degradation: implications for the pathogenesis of Parkinson's disease. Cell Mol Neurobiol 21 6 (2001) 771-781
    • (2001) Cell Mol Neurobiol , vol.21 , Issue.6 , pp. 771-781
    • Elkon, H.1    Melamed, E.2    Offen, D.3
  • 51
    • 18044380103 scopus 로고    scopus 로고
    • Oxidative stress, induced by 6-hydroxydopamine, reduces proteasome activities in PC12 cells: implications for the pathogenesis of Parkinson's disease
    • Elkon H., Melamed E., and Offen D. Oxidative stress, induced by 6-hydroxydopamine, reduces proteasome activities in PC12 cells: implications for the pathogenesis of Parkinson's disease. J Mol Neurosci 24 3 (2004) 387-400
    • (2004) J Mol Neurosci , vol.24 , Issue.3 , pp. 387-400
    • Elkon, H.1    Melamed, E.2    Offen, D.3
  • 52
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany M.B., and Bender W.W. A Drosophila model of Parkinson's disease. Nature 404 6776 (2000) 394-398
    • (2000) Nature , vol.404 , Issue.6776 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 53
    • 0028180516 scopus 로고
    • A beta-lactone related to lactacystin induces neurite outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line
    • Fenteany G., Standaert R.F., Reichard G.A., Corey E.J., and Schreiber S.L. A beta-lactone related to lactacystin induces neurite outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line. Proc Natl Acad Sci U S A 91 8 (1994) 3358-3362
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.8 , pp. 3358-3362
    • Fenteany, G.1    Standaert, R.F.2    Reichard, G.A.3    Corey, E.J.4    Schreiber, S.L.5
  • 54
    • 5144234034 scopus 로고    scopus 로고
    • Alpha-synuclein and transgenic mouse models
    • Fernagut P.O., and Chesselet M.F. Alpha-synuclein and transgenic mouse models. Neurobiol Dis 17 2 (2004) 123-130
    • (2004) Neurobiol Dis , vol.17 , Issue.2 , pp. 123-130
    • Fernagut, P.O.1    Chesselet, M.F.2
  • 55
    • 0028339708 scopus 로고
    • Parkinson's disease and brain levels of organochlorine pesticides
    • Fleming L., Mann J.B., Bean J., Briggle T., and Sanchez-Ramos J.R. Parkinson's disease and brain levels of organochlorine pesticides. Ann Neurol 36 1 (1994) 100-103
    • (1994) Ann Neurol , vol.36 , Issue.1 , pp. 100-103
    • Fleming, L.1    Mann, J.B.2    Bean, J.3    Briggle, T.4    Sanchez-Ramos, J.R.5
  • 56
    • 20044385568 scopus 로고    scopus 로고
    • Parkinson-like syndrome induced by continuous MPTP infusion: convergent roles of the ubiquitin-proteasome system and alpha-synuclein
    • Fornai F., Schluter O.M., Lenzi P., Gesi M., Ruffoli R., Ferrucci M., et al. Parkinson-like syndrome induced by continuous MPTP infusion: convergent roles of the ubiquitin-proteasome system and alpha-synuclein. Proc Natl Acad Sci U S A 102 9 (2005) 3413-3418
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.9 , pp. 3413-3418
    • Fornai, F.1    Schluter, O.M.2    Lenzi, P.3    Gesi, M.4    Ruffoli, R.5    Ferrucci, M.6
  • 57
    • 33646120085 scopus 로고    scopus 로고
    • Plasma membrane ion permeability induced by mutant alpha-synuclein contributes to the degeneration of neural cells
    • Furukawa K., Matsuzaki-Kobayashi M., Hasegawa T., Kikuchi A., Sugeno N., Itoyama Y., et al. Plasma membrane ion permeability induced by mutant alpha-synuclein contributes to the degeneration of neural cells. J Neurochem 97 4 (2006) 1071-1077
    • (2006) J Neurochem , vol.97 , Issue.4 , pp. 1071-1077
    • Furukawa, K.1    Matsuzaki-Kobayashi, M.2    Hasegawa, T.3    Kikuchi, A.4    Sugeno, N.5    Itoyama, Y.6
  • 58
    • 0033788434 scopus 로고    scopus 로고
    • Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex
    • Ghee M., Fournier A., and Mallet J. Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex. J Neurochem 75 5 (2000) 2221-2224
    • (2000) J Neurochem , vol.75 , Issue.5 , pp. 2221-2224
    • Ghee, M.1    Fournier, A.2    Mallet, J.3
  • 59
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82 2 (2002) 373-428
    • (2002) Physiol Rev , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 60
    • 0141891953 scopus 로고    scopus 로고
    • Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons
    • Goldberg M.S., Fleming S.M., Palacino J.J., Cepeda C., Lam H.A., Bhatnagar A., et al. Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons. J Biol Chem 278 44 (2003) 43628-43635
    • (2003) J Biol Chem , vol.278 , Issue.44 , pp. 43628-43635
    • Goldberg, M.S.1    Fleming, S.M.2    Palacino, J.J.3    Cepeda, C.4    Lam, H.A.5    Bhatnagar, A.6
  • 61
    • 0037013194 scopus 로고    scopus 로고
    • Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein
    • Golts N., Snyder H., Frasier M., Theisler C., Choi P., and Wolozin B. Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein. J Biol Chem 277 18 (2002) 16116-16123
    • (2002) J Biol Chem , vol.277 , Issue.18 , pp. 16116-16123
    • Golts, N.1    Snyder, H.2    Frasier, M.3    Theisler, C.4    Choi, P.5    Wolozin, B.6
  • 64
    • 9644262422 scopus 로고    scopus 로고
    • Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach
    • Groll M., and Huber R. Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach. Biochim Biophys Acta 1695 1-3 (2004) 33-44
    • (2004) Biochim Biophys Acta , vol.1695 , Issue.1-3 , pp. 33-44
    • Groll, M.1    Huber, R.2
  • 65
    • 33846313981 scopus 로고    scopus 로고
    • Proteasomal dysfunction: a common feature of neurodegenerative diseases? Implications for the environmental origins of neurodegeneration
    • Halliwell B. Proteasomal dysfunction: a common feature of neurodegenerative diseases? Implications for the environmental origins of neurodegeneration. Antioxid Redox Signal 8 (2006) 2007-2019
    • (2006) Antioxid Redox Signal , vol.8 , pp. 2007-2019
    • Halliwell, B.1
  • 66
    • 4544290828 scopus 로고    scopus 로고
    • Protein degradation: recognition of ubiquitinylated substrates
    • Hartmann-Petersen R., and Gordon C. Protein degradation: recognition of ubiquitinylated substrates. Curr Biol 14 18 (2004) R754-R756
    • (2004) Curr Biol , vol.14 , Issue.18
    • Hartmann-Petersen, R.1    Gordon, C.2
  • 67
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M., Hsu L.J., Xia Y., Takeda A., Sisk A., Sundsmo M., et al. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. NeuroReport 10 4 (1999) 717-721
    • (1999) NeuroReport , vol.10 , Issue.4 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6
  • 68
    • 32344444326 scopus 로고    scopus 로고
    • Down-regulation of alpha-synuclein expression can rescue dopaminergic cells from cell death in the substantia nigra of Parkinson's disease rat model
    • Hayashita-Kinoh H., Yamada M., Yokota T., Mizuno Y., and Mochizuki H. Down-regulation of alpha-synuclein expression can rescue dopaminergic cells from cell death in the substantia nigra of Parkinson's disease rat model. Biochem Biophys Res Commun 341 4 (2006) 1088-1095
    • (2006) Biochem Biophys Res Commun , vol.341 , Issue.4 , pp. 1088-1095
    • Hayashita-Kinoh, H.1    Yamada, M.2    Yokota, T.3    Mizuno, Y.4    Mochizuki, H.5
  • 69
    • 2642516493 scopus 로고    scopus 로고
    • Parkin counteracts symptoms in a Drosophila model of Parkinson's disease
    • Haywood A.F., and Staveley B.E. Parkin counteracts symptoms in a Drosophila model of Parkinson's disease. BMC Neurosci 5 14 (2004)
    • (2004) BMC Neurosci , vol.5 , Issue.14
    • Haywood, A.F.1    Staveley, B.E.2
  • 70
    • 33747832846 scopus 로고    scopus 로고
    • Mutant alpha-synuclein-induced degeneration is reduced by parkin in a fly model of Parkinson's disease
    • Haywood A.F., and Staveley B.E. Mutant alpha-synuclein-induced degeneration is reduced by parkin in a fly model of Parkinson's disease. Genome 49 5 (2006) 505-510
    • (2006) Genome , vol.49 , Issue.5 , pp. 505-510
    • Haywood, A.F.1    Staveley, B.E.2
  • 72
    • 0041430614 scopus 로고    scopus 로고
    • Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease
    • Hoglinger G.U., Carrard G., Michel P.P., Medja F., Lombes A., Ruberg M., et al. Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease. J Neurochem 86 5 (2003) 1297-1307
    • (2003) J Neurochem , vol.86 , Issue.5 , pp. 1297-1307
    • Hoglinger, G.U.1    Carrard, G.2    Michel, P.P.3    Medja, F.4    Lombes, A.5    Ruberg, M.6
  • 73
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • Holtz W.A., and O'Malley K.L. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 278 (2003) 19367-19377
    • (2003) J Biol Chem , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 74
    • 0141995596 scopus 로고    scopus 로고
    • The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI
    • Huynh D.P., Scoles D.R., Nguyen D., and Pulst S.M. The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Hum Mol Genet 12 20 (2003) 2587-2597
    • (2003) Hum Mol Genet , vol.12 , Issue.20 , pp. 2587-2597
    • Huynh, D.P.1    Scoles, D.R.2    Nguyen, D.3    Pulst, S.M.4
  • 75
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K.I., and Takahashi R. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell 10 (2002) 55-67
    • (2002) Mol Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6    Takahashi, R.7
  • 76
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome
    • Ishii T., Sakurai T., Usami H., and Uchida K. Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome. Biochemistry 44 42 (2005) 13893-13901
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 77
    • 26844555183 scopus 로고    scopus 로고
    • Molecular genetic pathways in Parkinson's disease: a review
    • Jain H., Wood N.W., and Healy D.G. Molecular genetic pathways in Parkinson's disease: a review. Clin Sci 109 (2005) 355-364
    • (2005) Clin Sci , vol.109 , pp. 355-364
    • Jain, H.1    Wood, N.W.2    Healy, D.G.3
  • 78
    • 4444327827 scopus 로고    scopus 로고
    • Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis
    • Jiang H., Ren Y., Zhao J., and Feng J. Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis. Hum Mol Genet 13 16 (2004) 1745-1754
    • (2004) Hum Mol Genet , vol.13 , Issue.16 , pp. 1745-1754
    • Jiang, H.1    Ren, Y.2    Zhao, J.3    Feng, J.4
  • 79
    • 0033625739 scopus 로고    scopus 로고
    • Molecular mechanism of monoamine toxicity in Parkinson's disease: hypothetical cell death model
    • Jimenez del Rio M., and Velez-Pardo C. Molecular mechanism of monoamine toxicity in Parkinson's disease: hypothetical cell death model. Med Hypotheses 54 2 (2000) 269-274
    • (2000) Med Hypotheses , vol.54 , Issue.2 , pp. 269-274
    • Jimenez del Rio, M.1    Velez-Pardo, C.2
  • 82
    • 0142200985 scopus 로고    scopus 로고
    • Role of proteolytic activation of protein kinase Cdelta in oxidative stress-induced apoptosis
    • Kanthasamy A.G., Kitazawa M., Kanthasamy A., and Anantharam V. Role of proteolytic activation of protein kinase Cdelta in oxidative stress-induced apoptosis. Antioxid Redox Signal 5 5 (2003) 609-620
    • (2003) Antioxid Redox Signal , vol.5 , Issue.5 , pp. 609-620
    • Kanthasamy, A.G.1    Kitazawa, M.2    Kanthasamy, A.3    Anantharam, V.4
  • 83
    • 23844461866 scopus 로고    scopus 로고
    • Dieldrin-induced neurotoxicity: relevance to Parkinson's disease pathogenesis
    • Kanthasamy A.G., Kitazawa M., Kanthasamy A., and Anantharam V. Dieldrin-induced neurotoxicity: relevance to Parkinson's disease pathogenesis. Neurotoxicology 26 4 (2005) 701-719
    • (2005) Neurotoxicology , vol.26 , Issue.4 , pp. 701-719
    • Kanthasamy, A.G.1    Kitazawa, M.2    Kanthasamy, A.3    Anantharam, V.4
  • 85
    • 3042654997 scopus 로고    scopus 로고
    • Does cellular iron dysregulation play a causative role in Parkinson's disease?
    • Kaur D., and Andersen J. Does cellular iron dysregulation play a causative role in Parkinson's disease?. Ageing Res Rev 3 3 (2004) 327-343
    • (2004) Ageing Res Rev , vol.3 , Issue.3 , pp. 327-343
    • Kaur, D.1    Andersen, J.2
  • 86
    • 0034669569 scopus 로고    scopus 로고
    • Dopamine induces proteasome inhibition in neural PC12 cell line
    • Keller J.N., Huang F.F., Dimayuga E.R., and Maragos W.F. Dopamine induces proteasome inhibition in neural PC12 cell line. Free Radic Biol Med 29 10 (2000) 1037-1042
    • (2000) Free Radic Biol Med , vol.29 , Issue.10 , pp. 1037-1042
    • Keller, J.N.1    Huang, F.F.2    Dimayuga, E.R.3    Maragos, W.F.4
  • 87
    • 11444265305 scopus 로고    scopus 로고
    • Dopaminergic dysfunction in unrelated, asymptomatic carriers of a single parkin mutation
    • Khan N.L., Scherfler C., Graham E., Bhatia K.P., Quinn N., Lees A.J., et al. Dopaminergic dysfunction in unrelated, asymptomatic carriers of a single parkin mutation. Neurology 64 1 (2005) 134-136
    • (2005) Neurology , vol.64 , Issue.1 , pp. 134-136
    • Khan, N.L.1    Scherfler, C.2    Graham, E.3    Bhatia, K.P.4    Quinn, N.5    Lees, A.J.6
  • 88
    • 0037469979 scopus 로고    scopus 로고
    • Effect of proteasome inhibitor on cultured mesencephalic dopaminergic neurons
    • Kikuchi S., Shinpo K., Tsuji S., Takeuchi M., Yamagishi S., Makita Z., et al. Effect of proteasome inhibitor on cultured mesencephalic dopaminergic neurons. Brain Res 964 2 (2003) 228-236
    • (2003) Brain Res , vol.964 , Issue.2 , pp. 228-236
    • Kikuchi, S.1    Shinpo, K.2    Tsuji, S.3    Takeuchi, M.4    Yamagishi, S.5    Makita, Z.6
  • 89
    • 23144452492 scopus 로고    scopus 로고
    • Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics
    • Kirkpatrick D.S., Denison C., and Gygi S.P. Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics. Nat Cell Biol 7 8 (2005) 750-757
    • (2005) Nat Cell Biol , vol.7 , Issue.8 , pp. 750-757
    • Kirkpatrick, D.S.1    Denison, C.2    Gygi, S.P.3
  • 90
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: from research tools to drug candidates
    • Kisselev A.F., and Goldberg A.L. Proteasome inhibitors: from research tools to drug candidates. Chem Biol 8 8 (2001) 739-758
    • (2001) Chem Biol , vol.8 , Issue.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 91
    • 0035581423 scopus 로고    scopus 로고
    • Dieldrin-induced oxidative stress and neurochemical changes contribute to apoptopic cell death in dopaminergic cells
    • Kitazawa M., Anantharam V., and Kanthasamy A.G. Dieldrin-induced oxidative stress and neurochemical changes contribute to apoptopic cell death in dopaminergic cells. Free Radic Biol Med 31 11 (2001) 1473-1485
    • (2001) Free Radic Biol Med , vol.31 , Issue.11 , pp. 1473-1485
    • Kitazawa, M.1    Anantharam, V.2    Kanthasamy, A.G.3
  • 92
    • 0038433325 scopus 로고    scopus 로고
    • Dieldrin induces apoptosis by promoting caspase-3-dependent proteolytic cleavage of protein kinase Cdelta in dopaminergic cells: relevance to oxidative stress and dopaminergic degeneration
    • Kitazawa M., Anantharam V., and Kanthasamy A.G. Dieldrin induces apoptosis by promoting caspase-3-dependent proteolytic cleavage of protein kinase Cdelta in dopaminergic cells: relevance to oxidative stress and dopaminergic degeneration. Neuroscience 119 4 (2003) 945-964
    • (2003) Neuroscience , vol.119 , Issue.4 , pp. 945-964
    • Kitazawa, M.1    Anantharam, V.2    Kanthasamy, A.G.3
  • 93
    • 33646408797 scopus 로고    scopus 로고
    • Parkin is protective for substantia nigra dopamine neurons in a tau gene transfer neurodegeneration model
    • Klein R.L., Dayton R.D., Henderson K.M., and Petrucelli L. Parkin is protective for substantia nigra dopamine neurons in a tau gene transfer neurodegeneration model. Neurosci Lett 401 1-2 (2006) 130-135
    • (2006) Neurosci Lett , vol.401 , Issue.1-2 , pp. 130-135
    • Klein, R.L.1    Dayton, R.D.2    Henderson, K.M.3    Petrucelli, L.4
  • 94
    • 33244460534 scopus 로고    scopus 로고
    • Mice lacking alpha-synuclein are resistant to mitochondrial toxins
    • Klivenyi P., Siwek D., Gardian G., Yang L., Starkov A., Cleren C., et al. Mice lacking alpha-synuclein are resistant to mitochondrial toxins. Neurobiol Dis 21 3 (2006) 541-548
    • (2006) Neurobiol Dis , vol.21 , Issue.3 , pp. 541-548
    • Klivenyi, P.1    Siwek, D.2    Gardian, G.3    Yang, L.4    Starkov, A.5    Cleren, C.6
  • 95
    • 24144497601 scopus 로고    scopus 로고
    • Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death
    • Ko H.S., von Coelln R., Sriram S.R., Kim S.W., Chung K.K., Pletnikova O., et al. Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death. J Neurosci 25 35 (2005) 7968-7978
    • (2005) J Neurosci , vol.25 , Issue.35 , pp. 7968-7978
    • Ko, H.S.1    von Coelln, R.2    Sriram, S.R.3    Kim, S.W.4    Chung, K.K.5    Pletnikova, O.6
  • 96
    • 33745220302 scopus 로고    scopus 로고
    • Identification of far upstream element-binding protein-1 as an authentic Parkin substrate
    • Ko H.S., Kim S.W., Sriram S.R., Dawson V.L., and Dawson T.M. Identification of far upstream element-binding protein-1 as an authentic Parkin substrate. J Biol Chem 281 24 (2006) 16193-16196
    • (2006) J Biol Chem , vol.281 , Issue.24 , pp. 16193-16196
    • Ko, H.S.1    Kim, S.W.2    Sriram, S.R.3    Dawson, V.L.4    Dawson, T.M.5
  • 97
    • 0034105791 scopus 로고    scopus 로고
    • TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities
    • Koguchi Y., Kohno J., Nishio M., Takahashi K., Okuda T., Ohnuki T., et al. TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities. J Antibiot (Tokyo) 53 2 (2000) 105-109
    • (2000) J Antibiot (Tokyo) , vol.53 , Issue.2 , pp. 105-109
    • Koguchi, Y.1    Kohno, J.2    Nishio, M.3    Takahashi, K.4    Okuda, T.5    Ohnuki, T.6
  • 98
    • 33746851988 scopus 로고    scopus 로고
    • Failure of proteasome inhibitor administration to provide a model of Parkinson's disease in rats and monkeys
    • Kordower J.H., Kanaan N.M., Chu Y., Suresh Babu R., Stansell III J., Terpstra B.T., et al. Failure of proteasome inhibitor administration to provide a model of Parkinson's disease in rats and monkeys. Ann Neurol 60 2 (2006) 264-268
    • (2006) Ann Neurol , vol.60 , Issue.2 , pp. 264-268
    • Kordower, J.H.1    Kanaan, N.M.2    Chu, Y.3    Suresh Babu, R.4    Stansell III, J.5    Terpstra, B.T.6
  • 99
    • 0036091142 scopus 로고    scopus 로고
    • Occupational and environmental risk factors for Parkinson's disease
    • Lai B.C., Marion S.A., Teschke K., and Tsui J.K. Occupational and environmental risk factors for Parkinson's disease. Parkinsonism Relat Disord 8 5 (2002) 297-309
    • (2002) Parkinsonism Relat Disord , vol.8 , Issue.5 , pp. 297-309
    • Lai, B.C.1    Marion, S.A.2    Teschke, K.3    Tsui, J.K.4
  • 100
    • 0032497504 scopus 로고    scopus 로고
    • Parkinson's disease. First of two parts
    • Lang A.E., and Lozano A.M. Parkinson's disease. First of two parts. N Engl J Med 339 15 (1998) 1044-1053
    • (1998) N Engl J Med , vol.339 , Issue.15 , pp. 1044-1053
    • Lang, A.E.1    Lozano, A.M.2
  • 101
    • 0021239393 scopus 로고
    • Parkinsonism induced by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP): implications for treatment and the pathogenesis of Parkinson's disease
    • Langston J.W., and Ballard P. Parkinsonism induced by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP): implications for treatment and the pathogenesis of Parkinson's disease. Can J Neurol Sci 11 1 Suppl (1984) 160-165
    • (1984) Can J Neurol Sci , vol.11 , Issue.1 SUPPL , pp. 160-165
    • Langston, J.W.1    Ballard, P.2
  • 103
    • 8644263976 scopus 로고    scopus 로고
    • A proteasomal stress response: pre-treatment with proteasome inhibitors increases proteasome activity and reduces neuronal vulnerability to oxidative injury
    • Lee C.S., Tee L.Y., Warmke T., Vinjamoori A., Cai A., Fagan A.M., et al. A proteasomal stress response: pre-treatment with proteasome inhibitors increases proteasome activity and reduces neuronal vulnerability to oxidative injury. J Neurochem 91 4 (2004) 996-1006
    • (2004) J Neurochem , vol.91 , Issue.4 , pp. 996-1006
    • Lee, C.S.1    Tee, L.Y.2    Warmke, T.3    Vinjamoori, A.4    Cai, A.5    Fagan, A.M.6
  • 104
    • 0032190090 scopus 로고    scopus 로고
    • The ubiquitin pathway in Parkinson's disease
    • Leroy E., Boyer R., Auburger G., Leube B., Ulm G., Mezey E., et al. The ubiquitin pathway in Parkinson's disease. Nature 395 6701 (1998) 451-452
    • (1998) Nature , vol.395 , Issue.6701 , pp. 451-452
    • Leroy, E.1    Boyer, R.2    Auburger, G.3    Leube, B.4    Ulm, G.5    Mezey, E.6
  • 105
    • 33646521299 scopus 로고    scopus 로고
    • Proteasomal inhibition hypersensitizes differentiated neuroblastoma cells to oxidative damage
    • Lev N., Melamed E., and Offen D. Proteasomal inhibition hypersensitizes differentiated neuroblastoma cells to oxidative damage. Neurosci Lett 399 1-2 (2006) 27-32
    • (2006) Neurosci Lett , vol.399 , Issue.1-2 , pp. 27-32
    • Lev, N.1    Melamed, E.2    Offen, D.3
  • 106
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and l-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease
    • Li J., Zhu M., Manning-Bog A.B., Di Monte D.A., and Fink A.L. Dopamine and l-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. FASEB J 18 9 (2004) 962-964
    • (2004) FASEB J , vol.18 , Issue.9 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di Monte, D.A.4    Fink, A.L.5
  • 107
    • 1842424791 scopus 로고    scopus 로고
    • Proteasomal inhibition by alpha-synuclein filaments and oligomers
    • Lindersson E., Beedholm R., Hojrup P., Moos T., Gai W., Hendil K.B., et al. Proteasomal inhibition by alpha-synuclein filaments and oligomers. J Biol Chem 279 13 (2004) 12924-12934
    • (2004) J Biol Chem , vol.279 , Issue.13 , pp. 12924-12934
    • Lindersson, E.1    Beedholm, R.2    Hojrup, P.3    Moos, T.4    Gai, W.5    Hendil, K.B.6
  • 108
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
    • Liu Y., Fallon L., Lashuel H.A., Liu Z., and Lansbury Jr. P.T. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility. Cell 111 2 (2002) 209-218
    • (2002) Cell , vol.111 , Issue.2 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury Jr., P.T.5
  • 109
    • 10644281090 scopus 로고    scopus 로고
    • Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an alpha-synuclein rat model of Parkinson's disease
    • Lo Bianco C., Schneider B.L., Bauer M., Sajadi A., Brice A., Iwatsubo T., et al. Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an alpha-synuclein rat model of Parkinson's disease. Proc Natl Acad Sci U S A 101 50 (2004) 17510-17515
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.50 , pp. 17510-17515
    • Lo Bianco, C.1    Schneider, B.L.2    Bauer, M.3    Sajadi, A.4    Brice, A.5    Iwatsubo, T.6
  • 110
    • 0036797552 scopus 로고    scopus 로고
    • Impaired dopamine storage resulting from alpha-synuclein mutations may contribute to the pathogenesis of Parkinson's disease
    • Lotharius J., and Brundin P. Impaired dopamine storage resulting from alpha-synuclein mutations may contribute to the pathogenesis of Parkinson's disease. Hum Mol Genet 11 20 (2002) 2395-2407
    • (2002) Hum Mol Genet , vol.11 , Issue.20 , pp. 2395-2407
    • Lotharius, J.1    Brundin, P.2
  • 111
    • 0037064078 scopus 로고    scopus 로고
    • Effect of mutant alpha-synuclein on dopamine homeostasis in a new human mesencephalic cell line
    • Lotharius J., Barg S., Wiekop P., Lundberg C., Raymon H.K., and Brundin P. Effect of mutant alpha-synuclein on dopamine homeostasis in a new human mesencephalic cell line. J Biol Chem 277 41 (2002) 38884-38894
    • (2002) J Biol Chem , vol.277 , Issue.41 , pp. 38884-38894
    • Lotharius, J.1    Barg, S.2    Wiekop, P.3    Lundberg, C.4    Raymon, H.K.5    Brundin, P.6
  • 112
    • 17844365885 scopus 로고    scopus 로고
    • Symptoms of autonomic failure in Parkinson's disease: prevalence and impact on daily life
    • Magerkurth C., Schnitzer R., and Braune S. Symptoms of autonomic failure in Parkinson's disease: prevalence and impact on daily life. Clin Auton Res 15 2 (2005) 76-82
    • (2005) Clin Auton Res , vol.15 , Issue.2 , pp. 76-82
    • Magerkurth, C.1    Schnitzer, R.2    Braune, S.3
  • 113
    • 0037127197 scopus 로고    scopus 로고
    • The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein
    • Manning-Bog A.B., McCormack A.L., Li J., Uversky V.N., Fink A.L., and Di Monte D.A. The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein. J Biol Chem 277 3 (2002) 1641-1644
    • (2002) J Biol Chem , vol.277 , Issue.3 , pp. 1641-1644
    • Manning-Bog, A.B.1    McCormack, A.L.2    Li, J.3    Uversky, V.N.4    Fink, A.L.5    Di Monte, D.A.6
  • 114
    • 0038334899 scopus 로고    scopus 로고
    • Alpha-synuclein overexpression protects against paraquat-induced neurodegeneration
    • Manning-Bog A.B., McCormack A.L., Purisai M.G., Bolin L.M., and Di Monte D.A. Alpha-synuclein overexpression protects against paraquat-induced neurodegeneration. J Neurosci 23 8 (2003) 3095-3099
    • (2003) J Neurosci , vol.23 , Issue.8 , pp. 3095-3099
    • Manning-Bog, A.B.1    McCormack, A.L.2    Purisai, M.G.3    Bolin, L.M.4    Di Monte, D.A.5
  • 116
    • 0141499226 scopus 로고    scopus 로고
    • The role of alpha-synuclein in Parkinson's disease: insights from animal models
    • Maries E., Dass B., Collier T.J., Kordower J.H., and Steece-Collier K. The role of alpha-synuclein in Parkinson's disease: insights from animal models. Nat Rev Neurosci 4 9 (2003) 727-738
    • (2003) Nat Rev Neurosci , vol.4 , Issue.9 , pp. 727-738
    • Maries, E.1    Dass, B.2    Collier, T.J.3    Kordower, J.H.4    Steece-Collier, K.5
  • 117
    • 0037380982 scopus 로고    scopus 로고
    • Effects of l-dopa and other amino acids against paraquat-induced nigrostriatal degeneration
    • McCormack A.L., and Di Monte D.A. Effects of l-dopa and other amino acids against paraquat-induced nigrostriatal degeneration. J Neurochem 85 1 (2003) 82-86
    • (2003) J Neurochem , vol.85 , Issue.1 , pp. 82-86
    • McCormack, A.L.1    Di Monte, D.A.2
  • 118
    • 0036075892 scopus 로고    scopus 로고
    • Environmental risk factors and Parkinson's disease: selective degeneration of nigral dopaminergic neurons caused by the herbicide paraquat
    • McCormack A.L., Thiruchelvam M., Manning-Bog A.B., Thiffault C., Langston J.W., Cory-Slechta D.A., et al. Environmental risk factors and Parkinson's disease: selective degeneration of nigral dopaminergic neurons caused by the herbicide paraquat. Neurobiol Dis 10 2 (2002) 119-127
    • (2002) Neurobiol Dis , vol.10 , Issue.2 , pp. 119-127
    • McCormack, A.L.1    Thiruchelvam, M.2    Manning-Bog, A.B.3    Thiffault, C.4    Langston, J.W.5    Cory-Slechta, D.A.6
  • 119
    • 33746839220 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced model of Parkinson's disease
    • McNaught K.S., and Olanow C.W. Proteasome inhibitor-induced model of Parkinson's disease. Ann Neurol 60 2 (2006) 243-247
    • (2006) Ann Neurol , vol.60 , Issue.2 , pp. 243-247
    • McNaught, K.S.1    Olanow, C.W.2
  • 120
    • 0037025111 scopus 로고    scopus 로고
    • Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson's disease
    • McNaught K.S., Belizaire R., Jenner P., Olanow C.W., and Isacson O. Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson's disease. Neurosci Lett 326 3 (2002) 155-158
    • (2002) Neurosci Lett , vol.326 , Issue.3 , pp. 155-158
    • McNaught, K.S.1    Belizaire, R.2    Jenner, P.3    Olanow, C.W.4    Isacson, O.5
  • 122
    • 0036316947 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures
    • McNaught K.S., Mytilineou C., Jnobaptiste R., Yabut J., Shashidharan P., Jennert P., et al. Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures. J Neurochem 81 2 (2002) 301-306
    • (2002) J Neurochem , vol.81 , Issue.2 , pp. 301-306
    • McNaught, K.S.1    Mytilineou, C.2    Jnobaptiste, R.3    Yabut, J.4    Shashidharan, P.5    Jennert, P.6
  • 124
    • 3042794162 scopus 로고    scopus 로고
    • Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease
    • McNaught K.S., Perl D.P., Brownell A.L., and Olanow C.W. Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann Neurol 56 1 (2004) 149-162
    • (2004) Ann Neurol , vol.56 , Issue.1 , pp. 149-162
    • McNaught, K.S.1    Perl, D.P.2    Brownell, A.L.3    Olanow, C.W.4
  • 125
    • 33747611218 scopus 로고    scopus 로고
    • Mutational analysis of DJ-1 in Drosophila implicates functional inactivation by oxidative damage and aging
    • Meulener M.C., Xu K., Thomson L., Ischiropoulos H., and Bonini N.M. Mutational analysis of DJ-1 in Drosophila implicates functional inactivation by oxidative damage and aging. Proc Natl Acad Sci U S A 103 33 (2006) 12517-12522
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.33 , pp. 12517-12522
    • Meulener, M.C.1    Xu, K.2    Thomson, L.3    Ischiropoulos, H.4    Bonini, N.M.5
  • 126
    • 18044380520 scopus 로고    scopus 로고
    • Retrograde dopaminergic neuron degeneration following intrastriatal proteasome inhibition
    • Miwa H., Kubo T., Suzuki A., Nishi K., and Kondo T. Retrograde dopaminergic neuron degeneration following intrastriatal proteasome inhibition. Neurosci Lett 380 1-2 (2005) 93-98
    • (2005) Neurosci Lett , vol.380 , Issue.1-2 , pp. 93-98
    • Miwa, H.1    Kubo, T.2    Suzuki, A.3    Nishi, K.4    Kondo, T.5
  • 128
    • 0034967925 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and proteasome inhibitors
    • Myung J., Kim K.B., and Crews C.M. The ubiquitin-proteasome pathway and proteasome inhibitors. Med Res Rev 21 4 (2001) 245-273
    • (2001) Med Res Rev , vol.21 , Issue.4 , pp. 245-273
    • Myung, J.1    Kim, K.B.2    Crews, C.M.3
  • 129
    • 0035918278 scopus 로고    scopus 로고
    • Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo
    • Nam S., Smith D.M., and Dou Q.P. Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo. J Biol Chem 276 16 (2001) 13322-13330
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 13322-13330
    • Nam, S.1    Smith, D.M.2    Dou, Q.P.3
  • 130
    • 0037466510 scopus 로고    scopus 로고
    • Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants
    • Nishikawa K., Li H., Kawamura R., Osaka H., Wang Y.L., Hara Y., et al. Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants. Biochem Biophys Res Commun 304 1 (2003) 176-183
    • (2003) Biochem Biophys Res Commun , vol.304 , Issue.1 , pp. 176-183
    • Nishikawa, K.1    Li, H.2    Kawamura, R.3    Osaka, H.4    Wang, Y.L.5    Hara, Y.6
  • 131
    • 20444401187 scopus 로고    scopus 로고
    • Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations
    • Norris E.H., Giasson B.I., Hodara R., Xu S., Trojanowski J.Q., Ischiropoulos H., et al. Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations. J Biol Chem 280 22 (2005) 21212-21219
    • (2005) J Biol Chem , vol.280 , Issue.22 , pp. 21212-21219
    • Norris, E.H.1    Giasson, B.I.2    Hodara, R.3    Xu, S.4    Trojanowski, J.Q.5    Ischiropoulos, H.6
  • 132
    • 0033588087 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress. Identification of proteasomes as target molecules
    • Okada K., Wangpoengtrakul C., Osawa T., Toyokuni S., Tanaka K., and Uchida K. 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress. Identification of proteasomes as target molecules. J Biol Chem 274 34 (1999) 23787-23793
    • (1999) J Biol Chem , vol.274 , Issue.34 , pp. 23787-23793
    • Okada, K.1    Wangpoengtrakul, C.2    Osawa, T.3    Toyokuni, S.4    Tanaka, K.5    Uchida, K.6
  • 133
    • 1842504319 scopus 로고    scopus 로고
    • Manganese-induced parkinsonism and Parkinson's disease
    • Olanow C.W. Manganese-induced parkinsonism and Parkinson's disease. Ann NY Acad Sci 1012 (2004) 209-223
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 209-223
    • Olanow, C.W.1
  • 135
    • 0034663039 scopus 로고    scopus 로고
    • The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity
    • Ostrerova-Golts N., Petrucelli L., Hardy J., Lee J.M., Farer M., and Wolozin B. The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity. J Neurosci 20 16 (2000) 6048-6054
    • (2000) J Neurosci , vol.20 , Issue.16 , pp. 6048-6054
    • Ostrerova-Golts, N.1    Petrucelli, L.2    Hardy, J.3    Lee, J.M.4    Farer, M.5    Wolozin, B.6
  • 136
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • Palacino J.J., Sagi D., Goldberg M.S., Krauss S., Motz C., Wacker M., et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J Biol Chem 279 18 (2004) 18614-18622
    • (2004) J Biol Chem , vol.279 , Issue.18 , pp. 18614-18622
    • Palacino, J.J.1    Sagi, D.2    Goldberg, M.S.3    Krauss, S.4    Motz, C.5    Wacker, M.6
  • 137
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park J., Lee S.B., Lee S., Kim Y., Song S., Kim S., et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441 7097 (2006) 1157-1161
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6
  • 138
    • 2542579359 scopus 로고    scopus 로고
    • Getting into position: the catalytic mechanisms of protein ubiquitylation
    • Passmore L.A., and Barford D. Getting into position: the catalytic mechanisms of protein ubiquitylation. Biochem J 379 Pt 3 (2004) 513-525
    • (2004) Biochem J , vol.379 , Issue.PART 3 , pp. 513-525
    • Passmore, L.A.1    Barford, D.2
  • 139
    • 10744224951 scopus 로고    scopus 로고
    • Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age
    • Pawlyk A.C., Giasson B.I., Sampathu D.M., Perez F.A., Lim K.L., Dawson V.L., et al. Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age. J Biol Chem 278 48 (2003) 48120-48128
    • (2003) J Biol Chem , vol.278 , Issue.48 , pp. 48120-48128
    • Pawlyk, A.C.1    Giasson, B.I.2    Sampathu, D.M.3    Perez, F.A.4    Lim, K.L.5    Dawson, V.L.6
  • 141
    • 13844313915 scopus 로고    scopus 로고
    • Parkin-deficient mice are not a robust model of parkinsonism
    • Perez F.A., and Palmiter R.D. Parkin-deficient mice are not a robust model of parkinsonism. Proc Natl Acad Sci U S A 102 6 (2005) 2174-2179
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.6 , pp. 2174-2179
    • Perez, F.A.1    Palmiter, R.D.2
  • 142
    • 0037092442 scopus 로고    scopus 로고
    • A role for alpha-synuclein in the regulation of dopamine biosynthesis
    • Perez R.G., Waymire J.C., Lin E., Liu J.J., Guo F., and Zigmond M.J. A role for alpha-synuclein in the regulation of dopamine biosynthesis. J Neurosci 22 8 (2002) 3090-3099
    • (2002) J Neurosci , vol.22 , Issue.8 , pp. 3090-3099
    • Perez, R.G.1    Waymire, J.C.2    Lin, E.3    Liu, J.J.4    Guo, F.5    Zigmond, M.J.6
  • 143
    • 30344450813 scopus 로고    scopus 로고
    • Parkin-deficient mice are not more sensitive to 6-hydroxydopamine or methamphetamine neurotoxicity
    • Perez F.A., Curtis W.R., and Palmiter R.D. Parkin-deficient mice are not more sensitive to 6-hydroxydopamine or methamphetamine neurotoxicity. BMC Neurosci 6 71 (2005)
    • (2005) BMC Neurosci , vol.6 , Issue.71
    • Perez, F.A.1    Curtis, W.R.2    Palmiter, R.D.3
  • 144
    • 28844439032 scopus 로고    scopus 로고
    • Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function
    • Periquet M., Corti O., Jacquier S., and Brice A. Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function. J Neurochem 95 5 (2005) 1259-1276
    • (2005) J Neurochem , vol.95 , Issue.5 , pp. 1259-1276
    • Periquet, M.1    Corti, O.2    Jacquier, S.3    Brice, A.4
  • 145
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli L., O'Farrell C., Lockhart P.J., Baptista M., Kehoe K., Vink L., et al. Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron 36 6 (2002) 1007-1019
    • (2002) Neuron , vol.36 , Issue.6 , pp. 1007-1019
    • Petrucelli, L.1    O'Farrell, C.2    Lockhart, P.J.3    Baptista, M.4    Kehoe, K.5    Vink, L.6
  • 146
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: structures, functions, mechanisms
    • Pickart C.M., and Eddins M.J. Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 1695 1-3 (2004) 55-72
    • (2004) Biochim Biophys Acta , vol.1695 , Issue.1-3 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 147
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: polymeric protein signals
    • Pickart C.M., and Fushman D. Polyubiquitin chains: polymeric protein signals. Curr Opin Chem Biol 8 6 (2004) 610-616
    • (2004) Curr Opin Chem Biol , vol.8 , Issue.6 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 148
    • 17444422182 scopus 로고    scopus 로고
    • Increased levels of ubiquitin in the 6-OHDA-lesioned striatum of rats
    • Pierson J., Svenningsson P., Caprioli R.M., and Andren P.E. Increased levels of ubiquitin in the 6-OHDA-lesioned striatum of rats. J. Proteome Res 4 2 (2005) 223-226
    • (2005) J. Proteome Res , vol.4 , Issue.2 , pp. 223-226
    • Pierson, J.1    Svenningsson, P.2    Caprioli, R.M.3    Andren, P.E.4
  • 149
    • 0347416827 scopus 로고    scopus 로고
    • alpha-Synuclein selectively increases manganese-induced viability loss in SK-N-MC neuroblastoma cells expressing the human dopamine transporter
    • Pifl C., Khorchide M., Kattinger A., Reither H., Hardy J., and Hornykiewicz O. alpha-Synuclein selectively increases manganese-induced viability loss in SK-N-MC neuroblastoma cells expressing the human dopamine transporter. Neurosci Lett 354 1 (2004) 34-37
    • (2004) Neurosci Lett , vol.354 , Issue.1 , pp. 34-37
    • Pifl, C.1    Khorchide, M.2    Kattinger, A.3    Reither, H.4    Hardy, J.5    Hornykiewicz, O.6
  • 150
    • 27744450270 scopus 로고    scopus 로고
    • Alpha-synuclein expression in the substantia nigra of MPTP-lesioned non-human primates
    • Purisai M.G., McCormack A.L., Langston W.J., Johnston L.C., and Di Monte D.A. Alpha-synuclein expression in the substantia nigra of MPTP-lesioned non-human primates. Neurobiol Dis 20 3 (2005) 898-906
    • (2005) Neurobiol Dis , vol.20 , Issue.3 , pp. 898-906
    • Purisai, M.G.1    McCormack, A.L.2    Langston, W.J.3    Johnston, L.C.4    Di Monte, D.A.5
  • 151
    • 33750618682 scopus 로고    scopus 로고
    • Comparison of the neurotoxic effects of proteasomal inhibitors in primary mesencephalic cultures
    • Reaney S.H., Johnston L.C., Langston W.J., and Di Monte D.A. Comparison of the neurotoxic effects of proteasomal inhibitors in primary mesencephalic cultures. Exp Neurol (2006)
    • (2006) Exp Neurol
    • Reaney, S.H.1    Johnston, L.C.2    Langston, W.J.3    Di Monte, D.A.4
  • 152
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M., and Hill C.P. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol 15 1 (2005) 27-33
    • (2005) Trends Cell Biol , vol.15 , Issue.1 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 153
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation
    • Ren Y., Zhao J., and Feng J. Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J Neurosci 23 8 (2003) 3316-3324
    • (2003) J Neurosci , vol.23 , Issue.8 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 154
    • 0036432029 scopus 로고    scopus 로고
    • Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination
    • Rideout H.J., and Stefanis L. Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination. Mol Cell Neurosci 21 2 (2002) 223-238
    • (2002) Mol Cell Neurosci , vol.21 , Issue.2 , pp. 223-238
    • Rideout, H.J.1    Stefanis, L.2
  • 155
    • 8744311814 scopus 로고    scopus 로고
    • alpha-Synuclein is required for the fibrillar nature of ubiquitinated inclusions induced by proteasomal inhibition in primary neurons
    • Rideout H.J., Dietrich P., Wang Q., Dauer W.T., and Stefanis L. alpha-Synuclein is required for the fibrillar nature of ubiquitinated inclusions induced by proteasomal inhibition in primary neurons. J Biol Chem 279 45 (2004) 46915-46920
    • (2004) J Biol Chem , vol.279 , Issue.45 , pp. 46915-46920
    • Rideout, H.J.1    Dietrich, P.2    Wang, Q.3    Dauer, W.T.4    Stefanis, L.5
  • 156
    • 20144381356 scopus 로고    scopus 로고
    • Dopaminergic neurons in rat ventral midbrain cultures undergo selective apoptosis and form inclusions, but do not up-regulate iHSP70, following proteasomal inhibition
    • Rideout H.J., Lang-Rollin I.C., Savalle M., and Stefanis L. Dopaminergic neurons in rat ventral midbrain cultures undergo selective apoptosis and form inclusions, but do not up-regulate iHSP70, following proteasomal inhibition. J Neurochem 93 5 (2005) 1304-1313
    • (2005) J Neurochem , vol.93 , Issue.5 , pp. 1304-1313
    • Rideout, H.J.1    Lang-Rollin, I.C.2    Savalle, M.3    Stefanis, L.4
  • 157
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • Ryu E.J., Harding H.P., Angelastro J.M., Vitolo O.V., Ron D., and Greene L.A. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J Neurosci 22 (2002) 10690-10698
    • (2002) J Neurosci , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 158
    • 0037368598 scopus 로고    scopus 로고
    • Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain
    • Sakata E., Yamaguchi Y., Kurimoto E., Kikuchi J., Yokoyama S., Yamada S., et al. Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain. EMBO Rep 4 3 (2003) 301-306
    • (2003) EMBO Rep , vol.4 , Issue.3 , pp. 301-306
    • Sakata, E.1    Yamaguchi, Y.2    Kurimoto, E.3    Kikuchi, J.4    Yokoyama, S.5    Yamada, S.6
  • 159
    • 17544404713 scopus 로고    scopus 로고
    • Toxicity of dieldrin for dopaminergic neurons in mesencephalic cultures
    • Sanchez-Ramos J., Facca A., Basit A., and Song S. Toxicity of dieldrin for dopaminergic neurons in mesencephalic cultures. Exp Neurol 150 2 (1998) 263-271
    • (1998) Exp Neurol , vol.150 , Issue.2 , pp. 263-271
    • Sanchez-Ramos, J.1    Facca, A.2    Basit, A.3    Song, S.4
  • 160
    • 12144290630 scopus 로고    scopus 로고
    • Proteasome mediates dopaminergic neuronal degeneration, and its inhibition causes alpha-synuclein inclusions
    • Sawada H., Kohno R., Kihara T., Izumi Y., Sakka N., Ibi M., et al. Proteasome mediates dopaminergic neuronal degeneration, and its inhibition causes alpha-synuclein inclusions. J Biol Chem 279 11 (2004) 10710-10719
    • (2004) J Biol Chem , vol.279 , Issue.11 , pp. 10710-10719
    • Sawada, H.1    Kohno, R.2    Kihara, T.3    Izumi, Y.4    Sakka, N.5    Ibi, M.6
  • 162
    • 0242362280 scopus 로고    scopus 로고
    • An inhibitor of mitochondrial complex I, rotenone, inactivates proteasome by oxidative modification and induces aggregation of oxidized proteins in SH-SY5Y cells
    • Shamoto-Nagai M., Maruyama W., Kato Y., Isobe K., Tanaka M., Naoi M., et al. An inhibitor of mitochondrial complex I, rotenone, inactivates proteasome by oxidative modification and induces aggregation of oxidized proteins in SH-SY5Y cells. J Neurosci Res 74 4 (2003) 589-597
    • (2003) J Neurosci Res , vol.74 , Issue.4 , pp. 589-597
    • Shamoto-Nagai, M.1    Maruyama, W.2    Kato, Y.3    Isobe, K.4    Tanaka, M.5    Naoi, M.6
  • 163
    • 33646378453 scopus 로고    scopus 로고
    • Neuromelanin induces oxidative stress in mitochondria through release of iron: mechanism behind the inhibition of 26S proteasome
    • Shamoto-Nagai M., Maruyama W., Yi H., Akao Y., Tribl F., Gerlach M., et al. Neuromelanin induces oxidative stress in mitochondria through release of iron: mechanism behind the inhibition of 26S proteasome. J Neural Transm 113 5 (2006) 633-644
    • (2006) J Neural Transm , vol.113 , Issue.5 , pp. 633-644
    • Shamoto-Nagai, M.1    Maruyama, W.2    Yi, H.3    Akao, Y.4    Tribl, F.5    Gerlach, M.6
  • 164
    • 4043079949 scopus 로고    scopus 로고
    • Mitochondria and dopamine: new insights into recessive parkinsonism
    • Shen J., and Cookson M.R. Mitochondria and dopamine: new insights into recessive parkinsonism. Neuron 43 3 (2004) 301-304
    • (2004) Neuron , vol.43 , Issue.3 , pp. 301-304
    • Shen, J.1    Cookson, M.R.2
  • 165
    • 0035816365 scopus 로고    scopus 로고
    • Carrier-mediated processes in blood-brain barrier penetration and neural uptake of paraquat
    • Shimizu K., Ohtaki K., Matsubara K., Aoyama K., Uezono T., Saito O., et al. Carrier-mediated processes in blood-brain barrier penetration and neural uptake of paraquat. Brain Res 906 1-2 (2001) 135-142
    • (2001) Brain Res , vol.906 , Issue.1-2 , pp. 135-142
    • Shimizu, K.1    Ohtaki, K.2    Matsubara, K.3    Aoyama, K.4    Uezono, T.5    Saito, O.6
  • 166
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H., Hattori N., Kubo S., Mizuno Y., Asakawa S., Minoshima S., et al. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet 25 3 (2000) 302-305
    • (2000) Nat Genet , vol.25 , Issue.3 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3    Mizuno, Y.4    Asakawa, S.5    Minoshima, S.6
  • 167
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease
    • Shimura H., Schlossmacher M.G., Hattori N., Frosch M.P., Trockenbacher A., Schneider R., et al. Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science 293 5528 (2001) 263-269
    • (2001) Science , vol.293 , Issue.5528 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3    Frosch, M.P.4    Trockenbacher, A.5    Schneider, R.6
  • 168
    • 14944348552 scopus 로고    scopus 로고
    • The role of alpha-synuclein in both neuroprotection and neurodegeneration
    • Sidhu A., Wersinger C., Moussa C.E., and Vernier P. The role of alpha-synuclein in both neuroprotection and neurodegeneration. Ann NY Acad Sci 1035 (2004) 250-270
    • (2004) Ann NY Acad Sci , vol.1035 , pp. 250-270
    • Sidhu, A.1    Wersinger, C.2    Moussa, C.E.3    Vernier, P.4
  • 169
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891-894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 170
    • 29644434199 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity
    • Smith W.W., Jiang H., Pei Z., Tanaka Y., Morita H., Sawa A., et al. Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Hum Mol Genet 14 (2005) 3801-3811
    • (2005) Hum Mol Genet , vol.14 , pp. 3801-3811
    • Smith, W.W.1    Jiang, H.2    Pei, Z.3    Tanaka, Y.4    Morita, H.5    Sawa, A.6
  • 171
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and monomeric alpha-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function
    • Snyder H., Mensah K., Theisler C., Lee J., Matouschek A., and Wolozin B. Aggregated and monomeric alpha-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function. J Biol Chem 278 14 (2003) 11753-11759
    • (2003) J Biol Chem , vol.278 , Issue.14 , pp. 11753-11759
    • Snyder, H.1    Mensah, K.2    Theisler, C.3    Lee, J.4    Matouschek, A.5    Wolozin, B.6
  • 172
    • 1542617769 scopus 로고    scopus 로고
    • Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP
    • Song D.D., Shults C.W., Sisk A., Rockenstein E., and Masliah E. Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP. Exp Neurol 186 2 (2004) 158-172
    • (2004) Exp Neurol , vol.186 , Issue.2 , pp. 158-172
    • Song, D.D.1    Shults, C.W.2    Sisk, A.3    Rockenstein, E.4    Masliah, E.5
  • 173
    • 0025347098 scopus 로고
    • Repin, a sesquiterpene lactone from Acroptilon repens possessing exceptional biological activity
    • Stevens K.L., Riopelle R.J., and Wong R.Y. Repin, a sesquiterpene lactone from Acroptilon repens possessing exceptional biological activity. J Nat Prod 53 1 (1990) 218-221
    • (1990) J Nat Prod , vol.53 , Issue.1 , pp. 218-221
    • Stevens, K.L.1    Riopelle, R.J.2    Wong, R.Y.3
  • 174
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun L., and Chen Z.J. The novel functions of ubiquitination in signaling. Curr Opin Cell Biol 16 2 (2004) 119-126
    • (2004) Curr Opin Cell Biol , vol.16 , Issue.2 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 175
    • 25644446864 scopus 로고    scopus 로고
    • Dieldrin induces ubiquitin-proteasome dysfunction in alpha-synuclein overexpressing dopaminergic neuronal cells and enhances susceptibility to apoptotic cell death
    • Sun F., Anantharam V., Latchoumycandane C., Kanthasamy A., and Kanthasamy A.G. Dieldrin induces ubiquitin-proteasome dysfunction in alpha-synuclein overexpressing dopaminergic neuronal cells and enhances susceptibility to apoptotic cell death. J Pharmacol Exp Ther 315 1 (2005) 69-79
    • (2005) J Pharmacol Exp Ther , vol.315 , Issue.1 , pp. 69-79
    • Sun, F.1    Anantharam, V.2    Latchoumycandane, C.3    Kanthasamy, A.4    Kanthasamy, A.G.5
  • 177
    • 0036436244 scopus 로고    scopus 로고
    • Neuroinvasive Nocardia asteroides GUH-2 induces apoptosis in the substantia nigra in vivo and dopaminergic cells in vitro
    • Tam S., Barry D.P., Beaman L., and Beaman B.L. Neuroinvasive Nocardia asteroides GUH-2 induces apoptosis in the substantia nigra in vivo and dopaminergic cells in vitro. Exp Neurol 177 2 (2002) 453-460
    • (2002) Exp Neurol , vol.177 , Issue.2 , pp. 453-460
    • Tam, S.1    Barry, D.P.2    Beaman, L.3    Beaman, B.L.4
  • 178
    • 0035870881 scopus 로고    scopus 로고
    • Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
    • Tanaka Y., Engelender S., Igarashi S., Rao R.K., Wanner T., Tanzi R.E., et al. Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis. Hum Mol Genet 10 9 (2001) 919-926
    • (2001) Hum Mol Genet , vol.10 , Issue.9 , pp. 919-926
    • Tanaka, Y.1    Engelender, S.2    Igarashi, S.3    Rao, R.K.4    Wanner, T.5    Tanzi, R.E.6
  • 179
    • 1042266326 scopus 로고    scopus 로고
    • Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
    • Tanaka M., Kim Y.M., Lee G., Junn E., Iwatsubo T., and Mouradian M.M. Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. J Biol Chem 279 6 (2004) 4625-4631
    • (2004) J Biol Chem , vol.279 , Issue.6 , pp. 4625-4631
    • Tanaka, M.1    Kim, Y.M.2    Lee, G.3    Junn, E.4    Iwatsubo, T.5    Mouradian, M.M.6
  • 180
    • 0037208691 scopus 로고    scopus 로고
    • Is the cause of Parkinson's disease environmental or hereditary? Evidence from twin studies
    • Tanner C.M. Is the cause of Parkinson's disease environmental or hereditary? Evidence from twin studies. Adv Neurol 91 (2003) 133-142
    • (2003) Adv Neurol , vol.91 , pp. 133-142
    • Tanner, C.M.1
  • 181
    • 1542359628 scopus 로고    scopus 로고
    • Risk factors for dopaminergic neuron loss in human alpha-synuclein transgenic mice
    • Thiruchelvam M.J., Powers J.M., Cory-Slechta D.A., and Richfield E.K. Risk factors for dopaminergic neuron loss in human alpha-synuclein transgenic mice. Eur J Neurosci 19 4 (2004) 845-854
    • (2004) Eur J Neurosci , vol.19 , Issue.4 , pp. 845-854
    • Thiruchelvam, M.J.1    Powers, J.M.2    Cory-Slechta, D.A.3    Richfield, E.K.4
  • 182
    • 33645961605 scopus 로고    scopus 로고
    • Natural products inhibiting the ubiquitin-proteasome proteolytic pathway, a target for drug development
    • Tsukamoto S., and Yokosawa H. Natural products inhibiting the ubiquitin-proteasome proteolytic pathway, a target for drug development. Curr Med Chem 13 7 (2006) 745-754
    • (2006) Curr Med Chem , vol.13 , Issue.7 , pp. 745-754
    • Tsukamoto, S.1    Yokosawa, H.2
  • 183
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky V.N., Li J., and Fink A.L. Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J Biol Chem 276 47 (2001) 44284-44296
    • (2001) J Biol Chem , vol.276 , Issue.47 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 184
    • 0035816404 scopus 로고    scopus 로고
    • Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease
    • Uversky V.N., Li J., and Fink A.L. Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease. FEBS Lett 500 3 (2001) 105-108
    • (2001) FEBS Lett , vol.500 , Issue.3 , pp. 105-108
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 185
    • 30044434872 scopus 로고    scopus 로고
    • Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans
    • Ved R., Saha S., Westlund B., Perier C., Burnam L., Sluder A., et al. Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans. J Biol Chem 280 52 (2005) 42655-42668
    • (2005) J Biol Chem , vol.280 , Issue.52 , pp. 42655-42668
    • Ved, R.1    Saha, S.2    Westlund, B.3    Perier, C.4    Burnam, L.5    Sluder, A.6
  • 187
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism
    • Volles M.J., and Lansbury Jr. P.T. Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. Biochemistry 41 14 (2002) 4595-4602
    • (2002) Biochemistry , vol.41 , Issue.14 , pp. 4595-4602
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 188
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease
    • Volles M.J., Lee S.J., Rochet J.C., Shtilerman M.D., Ding T.T., Kessler J.C., et al. Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40 26 (2001) 7812-7819
    • (2001) Biochemistry , vol.40 , Issue.26 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.J.2    Rochet, J.C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6
  • 189
    • 3242695252 scopus 로고    scopus 로고
    • Genes, proteins, and neurotoxins involved in Parkinson's disease
    • von Bohlen und Halbach O., Schober A., and Krieglstein K. Genes, proteins, and neurotoxins involved in Parkinson's disease. Prog Neurobiol 73 3 (2004) 151-177
    • (2004) Prog Neurobiol , vol.73 , Issue.3 , pp. 151-177
    • von Bohlen und Halbach, O.1    Schober, A.2    Krieglstein, K.3
  • 190
    • 33144469102 scopus 로고    scopus 로고
    • The proteasome and proteasome inhibitors in cancer therapy
    • Voorhees P.M., and Orlowski R.Z. The proteasome and proteasome inhibitors in cancer therapy. Annu Rev Pharmacol Toxicol 46 (2006) 189-213
    • (2006) Annu Rev Pharmacol Toxicol , vol.46 , pp. 189-213
    • Voorhees, P.M.1    Orlowski, R.Z.2
  • 191
    • 29644448325 scopus 로고    scopus 로고
    • Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function
    • Wang C., Ko H.S., Thomas B., Tsang F., Chew K.C., Tay S.P., et al. Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function. Hum Mol Genet 14 24 (2005) 3885-3897
    • (2005) Hum Mol Genet , vol.14 , Issue.24 , pp. 3885-3897
    • Wang, C.1    Ko, H.S.2    Thomas, B.3    Tsang, F.4    Chew, K.C.5    Tay, S.P.6
  • 192
    • 33745143950 scopus 로고    scopus 로고
    • Inhibitory effects of pesticides on proteasome activity: implication in Parkinson's disease
    • Wang X.F., Li S., Chou A.P., and Bronstein J.M. Inhibitory effects of pesticides on proteasome activity: implication in Parkinson's disease. Neurobiol Dis 23 1 (2006) 198-205
    • (2006) Neurobiol Dis , vol.23 , Issue.1 , pp. 198-205
    • Wang, X.F.1    Li, S.2    Chou, A.P.3    Bronstein, J.M.4
  • 193
    • 0037379324 scopus 로고    scopus 로고
    • Genetic and environmental factors in the cause of Parkinson's disease
    • (discussion S23--15)
    • Warner T.T., and Schapira A.H. Genetic and environmental factors in the cause of Parkinson's disease. Ann Neurol 53 Suppl 3 (2003) S16-S23 (discussion S23--15)
    • (2003) Ann Neurol , vol.53 , Issue.SUPPL. 3
    • Warner, T.T.1    Schapira, A.H.2
  • 194
    • 0037451858 scopus 로고    scopus 로고
    • Attenuation of dopamine transporter activity by alpha-synuclein
    • Wersinger C., and Sidhu A. Attenuation of dopamine transporter activity by alpha-synuclein. Neurosci Lett 340 3 (2003) 189-192
    • (2003) Neurosci Lett , vol.340 , Issue.3 , pp. 189-192
    • Wersinger, C.1    Sidhu, A.2
  • 195
    • 33644862373 scopus 로고    scopus 로고
    • Drosophila models pioneer a new approach to drug discovery for Parkinson's disease
    • Whitworth A.J., Wes P.D., and Pallanck L.J. Drosophila models pioneer a new approach to drug discovery for Parkinson's disease. Drug Discov Today 11 3-4 (2006) 119-126
    • (2006) Drug Discov Today , vol.11 , Issue.3-4 , pp. 119-126
    • Whitworth, A.J.1    Wes, P.D.2    Pallanck, L.J.3
  • 196
    • 33750720268 scopus 로고    scopus 로고
    • Protein oxidation and degradation during aging: role in skin aging and neurodegeneration
    • Widmer R., Ziaja I., and Grune T. Protein oxidation and degradation during aging: role in skin aging and neurodegeneration. Free Radic Res 40 (2006) 1259-1268
    • (2006) Free Radic Res , vol.40 , pp. 1259-1268
    • Widmer, R.1    Ziaja, I.2    Grune, T.3
  • 197
    • 0036152892 scopus 로고    scopus 로고
    • Iron and Parkinson's disease
    • Wolozin B., and Golts N. Iron and Parkinson's disease. Neuroscientist 8 1 (2002) 22-32
    • (2002) Neuroscientist , vol.8 , Issue.1 , pp. 22-32
    • Wolozin, B.1    Golts, N.2
  • 198
    • 14844303486 scopus 로고    scopus 로고
    • Parkin gene therapy for alpha-synucleinopathy: a rat model of Parkinson's disease
    • Yamada M., Mizuno Y., and Mochizuki H. Parkin gene therapy for alpha-synucleinopathy: a rat model of Parkinson's disease. Hum Gene Ther 16 2 (2005) 262-270
    • (2005) Hum Gene Ther , vol.16 , Issue.2 , pp. 262-270
    • Yamada, M.1    Mizuno, Y.2    Mochizuki, H.3
  • 199
    • 0037468831 scopus 로고    scopus 로고
    • Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila
    • Yang Y., Nishimura I., Imai Y., Takahashi R., and Lu B. Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila. Neuron 37 6 (2003) 911-924
    • (2003) Neuron , vol.37 , Issue.6 , pp. 911-924
    • Yang, Y.1    Nishimura, I.2    Imai, Y.3    Takahashi, R.4    Lu, B.5
  • 200
    • 20044370990 scopus 로고    scopus 로고
    • Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo
    • Yang F., Lim G.P., Begum A.N., Ubeda O.J., Simmons M.R., Ambegaokar S.S., et al. Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem 280 7 (2005) 5892-5901
    • (2005) J Biol Chem , vol.280 , Issue.7 , pp. 5892-5901
    • Yang, F.1    Lim, G.P.2    Begum, A.N.3    Ubeda, O.J.4    Simmons, M.R.5    Ambegaokar, S.S.6
  • 201
    • 26444489693 scopus 로고    scopus 로고
    • Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling
    • Yang Y., Gehrke S., Haque M.E., Imai Y., Kosek J., Yang L., et al. Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling. Proc Natl Acad Sci U S A 102 38 (2005) 13670-13675
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.38 , pp. 13670-13675
    • Yang, Y.1    Gehrke, S.2    Haque, M.E.3    Imai, Y.4    Kosek, J.5    Yang, L.6
  • 202
    • 3242733689 scopus 로고    scopus 로고
    • Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity
    • Yao D., Gu Z., Nakamura T., Shi Z.Q., Ma Y., Gaston B., et al. Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity. Proc Natl Acad Sci U S A 101 29 (2004) 10810-10814
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.29 , pp. 10810-10814
    • Yao, D.1    Gu, Z.2    Nakamura, T.3    Shi, Z.Q.4    Ma, Y.5    Gaston, B.6
  • 203
    • 10944243102 scopus 로고    scopus 로고
    • Role of alpha-synuclein in presynaptic dopamine recruitment
    • Yavich L., Tanila H., Vepsalainen S., and Jakala P. Role of alpha-synuclein in presynaptic dopamine recruitment. J Neurosci 24 49 (2004) 11165-11170
    • (2004) J Neurosci , vol.24 , Issue.49 , pp. 11165-11170
    • Yavich, L.1    Tanila, H.2    Vepsalainen, S.3    Jakala, P.4
  • 204
    • 23844516979 scopus 로고    scopus 로고
    • Proteasome inhibition by lactacystin in primary neuronal cells induces both potentially neuroprotective and pro-apoptotic transcriptional responses: a microarray analysis
    • Yew E.H., Cheung N.S., Choy M.S., Qi R.Z., Lee A.Y., Peng Z.F., et al. Proteasome inhibition by lactacystin in primary neuronal cells induces both potentially neuroprotective and pro-apoptotic transcriptional responses: a microarray analysis. J Neurochem 94 (2005) 943-956
    • (2005) J Neurochem , vol.94 , pp. 943-956
    • Yew, E.H.1    Cheung, N.S.2    Choy, M.S.3    Qi, R.Z.4    Lee, A.Y.5    Peng, Z.F.6
  • 205
    • 13844300068 scopus 로고    scopus 로고
    • l-Dopa and dopamine enhance the formation of aggregates under proteasome inhibition in PC12 cells
    • Yoshimoto Y., Nakaso K., and Nakashima K. l-Dopa and dopamine enhance the formation of aggregates under proteasome inhibition in PC12 cells. FEBS Lett 579 5 (2005) 1197-1202
    • (2005) FEBS Lett , vol.579 , Issue.5 , pp. 1197-1202
    • Yoshimoto, Y.1    Nakaso, K.2    Nakashima, K.3
  • 206
    • 33747624165 scopus 로고    scopus 로고
    • A potential role for cyclized quinones derived from dopamine, DOPA, and 3,4-dihydroxyphenylacetic acid in proteasomal inhibition
    • Zafar K.S., Siegel D., and Ross D. A potential role for cyclized quinones derived from dopamine, DOPA, and 3,4-dihydroxyphenylacetic acid in proteasomal inhibition. Mol Pharmacol 70 3 (2006) 1079-1086
    • (2006) Mol Pharmacol , vol.70 , Issue.3 , pp. 1079-1086
    • Zafar, K.S.1    Siegel, D.2    Ross, D.3
  • 207
    • 17644411438 scopus 로고    scopus 로고
    • Energy status, ubiquitin proteasomal function, and oxidative stress during chronic and acute complex I inhibition with rotenone in mesencephalic cultures
    • Zeevalk G.D., and Bernard L.P. Energy status, ubiquitin proteasomal function, and oxidative stress during chronic and acute complex I inhibition with rotenone in mesencephalic cultures. Antioxid Redox Signal 7 5-6 (2005) 662-672
    • (2005) Antioxid Redox Signal , vol.7 , Issue.5-6 , pp. 662-672
    • Zeevalk, G.D.1    Bernard, L.P.2
  • 208
    • 18844418175 scopus 로고    scopus 로고
    • Proteasomal activity in brain differs between species and brain regions and changes with age
    • Zeng B.Y., Medhurst A.D., Jackson M., Rose S., and Jenner P. Proteasomal activity in brain differs between species and brain regions and changes with age. Mech Ageing Dev 126 (2005) 760-766
    • (2005) Mech Ageing Dev , vol.126 , pp. 760-766
    • Zeng, B.Y.1    Medhurst, A.D.2    Jackson, M.3    Rose, S.4    Jenner, P.5
  • 209
    • 33645450436 scopus 로고    scopus 로고
    • MPTP treatment of common marmosets impairs proteasomal enzyme activity and decreases expression of structural and regulatory elements of the 26S proteasome
    • Zeng B.Y., Iravani M.M., Lin S.T., Irifune M., Kuoppamaki M., Al-Barghouthy G., et al. MPTP treatment of common marmosets impairs proteasomal enzyme activity and decreases expression of structural and regulatory elements of the 26S proteasome. Eur J Neurosci 23 7 (2006) 1766-1774
    • (2006) Eur J Neurosci , vol.23 , Issue.7 , pp. 1766-1774
    • Zeng, B.Y.1    Iravani, M.M.2    Lin, S.T.3    Irifune, M.4    Kuoppamaki, M.5    Al-Barghouthy, G.6
  • 210
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y., Gao J., Chung K.K., Huang H., Dawson V.L., and Dawson T.M. Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci U S A 97 24 (2000) 13354-13359
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.24 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 211
    • 20544465100 scopus 로고    scopus 로고
    • Neuroprotection by iron chelator against proteasome inhibitor-induced nigral degeneration
    • Zhang X., Xie W., Qu S., Pan T., Wang X., and Le W. Neuroprotection by iron chelator against proteasome inhibitor-induced nigral degeneration. Biochem Biophys Res Commun 333 2 (2005) 544-549
    • (2005) Biochem Biophys Res Commun , vol.333 , Issue.2 , pp. 544-549
    • Zhang, X.1    Xie, W.2    Qu, S.3    Pan, T.4    Wang, X.5    Le, W.6
  • 212
    • 4444225471 scopus 로고    scopus 로고
    • Proteasomal inhibition induced by manganese ethylene-bis-dithiocarbamate: relevance to Parkinson's disease
    • Zhou Y., Shie F.S., Piccardo P., Montine T.J., and Zhang J. Proteasomal inhibition induced by manganese ethylene-bis-dithiocarbamate: relevance to Parkinson's disease. Neuroscience 128 2 (2004) 281-291
    • (2004) Neuroscience , vol.128 , Issue.2 , pp. 281-291
    • Zhou, Y.1    Shie, F.S.2    Piccardo, P.3    Montine, T.J.4    Zhang, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.