메뉴 건너뛰기




Volumn 138, Issue 6, 2015, Pages 1642-1657

Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain

Author keywords

Alpha synuclein; Oligomers; Parkinson's disease; Pathology

Indexed keywords

ALPHA SYNUCLEIN; OLIGOMER; PROTEINASE K;

EID: 84938704559     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/awv040     Document Type: Article
Times cited : (224)

References (70)
  • 1
    • 28844441969 scopus 로고    scopus 로고
    • Secondary structure of alpha-synuclein oligomers: Characterization by raman and atomic force microscopy
    • Apetri MM, Maiti NC, Zagorski MG, Carey PR, Anderson VE Secondary structure of alpha-synuclein oligomers: characterization by raman and atomic force microscopy. J Mol Biol 2006; 355: 63-71
    • (2006) J Mol Biol , vol.355 , pp. 63-71
    • Apetri, M.M.1    Maiti, N.C.2    Zagorski, M.G.3    Carey, P.R.4    Anderson, V.E.5
  • 2
    • 0344808098 scopus 로고    scopus 로고
    • Immunoelectron-microscopic demonstration of NACP/alpha-synuclein-epitopes on the filamentous component of Lewy bodies in Parkinson's disease and in dementia with Lewy bodies
    • Arima K, Ueda K, Sunohara N, Hirai S, Izumiyama Y, Tonozuka-Uehara H, et al. Immunoelectron-microscopic demonstration of NACP/alpha-synuclein-epitopes on the filamentous component of Lewy bodies in Parkinson's disease and in dementia with Lewy bodies. Brain Res 1998; 808: 93-100
    • (1998) Brain Res , vol.808 , pp. 93-100
    • Arima, K.1    Ueda, K.2    Sunohara, N.3    Hirai, S.4    Izumiyama, Y.5    Tonozuka-Uehara, H.6
  • 3
    • 77956550866 scopus 로고    scopus 로고
    • In situ proximity ligation detection of c-Jun/AP-1 dimers reveals increased levels of c-Jun/Fra1 complexes in aggressive breast cancer cell lines in vitro and in vivo
    • Baan B, Pardali E, ten Dijke P, van Dam H. In situ proximity ligation detection of c-Jun/AP-1 dimers reveals increased levels of c-Jun/Fra1 complexes in aggressive breast cancer cell lines in vitro and in vivo Mol Cell Proteomics 2010; 9: 1982-90
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1982-1990
    • Baan, B.1    Pardali, E.2    Ten Dijke, P.3    Van Dam, H.4
  • 4
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels T, Choi JG, Selkoe DJ. Alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 2011; 477: 107-10
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 5
    • 84864742403 scopus 로고    scopus 로고
    • Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis
    • Bosco DA, Lavoie MJ, Petsko GA, Ringe D. Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis Cold Spring Harb Perspect Biol 2011; 3: a007500
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. a007500
    • Bosco, D.A.1    Lavoie, M.J.2    Petsko, G.A.3    Ringe, D.4
  • 7
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 2010; 11: 301-7
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 8
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002; 416: 507-11
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 9
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003; 26: 267-98
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 10
    • 84860110592 scopus 로고    scopus 로고
    • Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure
    • Celej MS, Sarroukh R, Goormaghtigh E, Fidelio GD, Ruysschaert JM, Raussens V. Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure. Biochem J 2012; 443: 719-26
    • (2012) Biochem J , vol.443 , pp. 719-726
    • Celej, M.S.1    Sarroukh, R.2    Goormaghtigh, E.3    Fidelio, G.D.4    Ruysschaert, J.M.5    Raussens, V.6
  • 12
    • 84874611934 scopus 로고    scopus 로고
    • Large alpha-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking
    • Choi BK, Choi MG, Kim JY, Yang Y, Lai Y, Kweon DH, et al. Large alpha-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking. Proc Natl Acad Sci USA 2013; 110: 4087-92
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 4087-4092
    • Choi, B.K.1    Choi, M.G.2    Kim, J.Y.3    Yang, Y.4    Lai, Y.5    Kweon, D.H.6
  • 13
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo
    • Colla E, Jensen PH, Pletnikova O, Troncoso JC, Glabe C, Lee MK Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo. J Neurosci 2012; 32: 3301-5
    • (2012) J Neurosci , vol.32 , pp. 3301-3305
    • Colla, E.1    Jensen, P.H.2    Pletnikova, O.3    Troncoso, J.C.4    Glabe, C.5    Lee, M.K.6
  • 14
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of alpha-synuclein
    • Cremades N, Cohen SI, Deas E, Abramov AY, Chen AY, Orte A, et al Direct observation of the interconversion of normal and toxic forms of alpha-synuclein. Cell 2012; 149: 1048-59
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1    Cohen, S.I.2    Deas, E.3    Abramov, A.Y.4    Chen, A.Y.5    Orte, A.6
  • 15
  • 17
    • 34548172773 scopus 로고    scopus 로고
    • Different species of alpha-synuclein oligomers induce calcium influx and seeding
    • Danzer KM, Haasen D, Karow AR, Moussaud S, Habeck M, Giese A, et al. Different species of alpha-synuclein oligomers induce calcium influx and seeding. J Neurosci 2007; 27: 9220-32
    • (2007) J Neurosci , vol.27 , pp. 9220-9232
    • Danzer, K.M.1    Haasen, D.2    Karow, A.R.3    Moussaud, S.4    Habeck, M.5    Giese, A.6
  • 18
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-toneuron transmission of alpha-synuclein
    • Desplats P, Lee HJ, Bae EJ, Patrick C, Rockenstein E, Crews L, et al Inclusion formation and neuronal cell death through neuron-toneuron transmission of alpha-synuclein. Proc Natl Acad Sci USA 2009; 106: 13010-5
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.J.3    Patrick, C.4    Rockenstein, E.5    Crews, L.6
  • 19
    • 33645833848 scopus 로고    scopus 로고
    • Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease
    • El-Agnaf OM, Salem SA, Paleologou KE, Curran MD, Gibson MJ, Court JA, et al. Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB J 2006; 20: 419-25
    • (2006) FASEB J , vol.20 , pp. 419-425
    • El-Agnaf, O.M.1    Salem, S.A.2    Paleologou, K.E.3    Curran, M.D.4    Gibson, M.J.5    Court, J.A.6
  • 20
    • 77951976610 scopus 로고    scopus 로고
    • Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome
    • Emmanouilidou E, Stefanis L, Vekrellis K. Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome Neurobiol Aging 2010; 31: 953-68
    • (2010) Neurobiol Aging , vol.31 , pp. 953-968
    • Emmanouilidou, E.1    Stefanis, L.2    Vekrellis, K.3
  • 21
    • 0030469956 scopus 로고    scopus 로고
    • Neurotoxicity of beta-amyloid and prion peptides
    • Forloni G. Neurotoxicity of beta-amyloid and prion peptides. Curr Opin Neurol 1996; 9: 492-500
    • (1996) Curr Opin Neurol , vol.9 , pp. 492-500
    • Forloni, G.1
  • 22
    • 0343527226 scopus 로고    scopus 로고
    • Alpha-synuclein immunoreactivity in dementia with Lewy bodies: Morphological staging and comparison with ubiquitin immunostaining
    • Gomez-Tortosa E, Newell K, Irizarry MC, Sanders JL, Hyman BT Alpha-synuclein immunoreactivity in dementia with Lewy bodies: morphological staging and comparison with ubiquitin immunostaining Acta Neuropathol 2000; 99: 352-7
    • (2000) Acta Neuropathol , vol.99 , pp. 352-357
    • Gomez-Tortosa, E.1    Newell, K.2    Irizarry, M.C.3    Sanders, J.L.4    Hyman, B.T.5
  • 23
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion
    • Gosavi N, Lee HJ, Lee JS, Patel S, Lee SJ. Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J Biol Chem 2002; 277: 48984-92
    • (2002) J Biol Chem , vol.277 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 24
    • 33750021276 scopus 로고    scopus 로고
    • Evidence that loading of cohesin onto chromosomes involves opening of its SMC hinge
    • Gruber S, Arumugam P, Katou Y, Kuglitsch D, Helmhart W, Shirahige K, et al. Evidence that loading of cohesin onto chromosomes involves opening of its SMC hinge. Cell 2006; 127: 523-37
    • (2006) Cell , vol.127 , pp. 523-537
    • Gruber, S.1    Arumugam, P.2    Katou, Y.3    Kuglitsch, D.4    Helmhart, W.5    Shirahige, K.6
  • 25
    • 79551519276 scopus 로고    scopus 로고
    • Alpha-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells
    • Hansen C, Angot E, Bergstrom AL, Steiner JA, Pieri L, Paul G, et al alpha-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells. J Clin Invest 2011; 121: 715-25
    • (2011) J Clin Invest , vol.121 , pp. 715-725
    • Hansen, C.1    Angot, E.2    Bergstrom, A.L.3    Steiner, J.A.4    Pieri, L.5    Paul, G.6
  • 26
    • 0028985267 scopus 로고
    • The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai A, Masliah E, Yoshimoto M, Ge N, Flanagan L, de Silva HA, et al. The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 1995; 14: 467-75
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.4    Flanagan, L.5    De Silva, H.A.6
  • 27
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes R, Spillantini MG, Goedert M. Identification of two distinct synucleins from human brain. FEBS Lett 1994; 345: 27-32
    • (1994) FEBS Lett , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 28
    • 77957260419 scopus 로고    scopus 로고
    • Sensitive detection of Abeta protofibrils by proximity ligation-relevance for Alzheimer's disease
    • Kamali-Moghaddam M, Pettersson FE, Wu D, Englund H, Darmanis S, Lord A, et al. Sensitive detection of Abeta protofibrils by proximity ligation-relevance for Alzheimer's disease. BMC Neurosci 2010; 11: 124
    • (2010) BMC Neurosci , vol.11 , pp. 124
    • Kamali-Moghaddam, M.1    Pettersson, F.E.2    Wu, D.3    Englund, H.4    Darmanis, S.5    Lord, A.6
  • 29
    • 83555166040 scopus 로고    scopus 로고
    • Pale neurites, premature alpha-synuclein aggregates with centripetal extension from axon collaterals
    • Kanazawa T, Adachi E, Orimo S, Nakamura A, Mizusawa H, Uchihara T. Pale neurites, premature alpha-synuclein aggregates with centripetal extension from axon collaterals. Brain Pathol 2012; 22: 67-78
    • (2012) Brain Pathol , vol.22 , pp. 67-78
    • Kanazawa, T.1    Adachi, E.2    Orimo, S.3    Nakamura, A.4    Mizusawa, H.5    Uchihara, T.6
  • 30
    • 0038290644 scopus 로고    scopus 로고
    • Developmental stages of cortical Lewy bodies and their relation to axonal transport blockage in brains of patients with dementia with Lewy bodies
    • Katsuse O, Iseki E, Marui W, Kosaka K. Developmental stages of cortical Lewy bodies and their relation to axonal transport blockage in brains of patients with dementia with Lewy bodies. J Neurol Sci 2003; 211: 29-35
    • (2003) J Neurol Sci , vol.211 , pp. 29-35
    • Katsuse, O.1    Iseki, E.2    Marui, W.3    Kosaka, K.4
  • 31
    • 79956299326 scopus 로고    scopus 로고
    • The parkinsonian mimetic, MPP+, specifically impairs mitochondrial transport in dopamine axons
    • Kim-Han JS, Antenor-Dorsey JA, O'Malley KL. The parkinsonian mimetic, MPP+, specifically impairs mitochondrial transport in dopamine axons. J Neurosci 2011; 31: 7212-21
    • (2011) J Neurosci , vol.31 , pp. 7212-7221
    • Kim-Han, J.S.1    Antenor-Dorsey, J.A.2    O'Malley, K.L.3
  • 33
    • 0018145267 scopus 로고
    • Lewy bodies in cerebral cortex, report of three cases
    • Kosaka K. Lewy bodies in cerebral cortex, report of three cases. Acta Neuropathol 1978; 42: 127-34
    • (1978) Acta Neuropathol , vol.42 , pp. 127-134
    • Kosaka, K.1
  • 34
    • 33846997878 scopus 로고    scopus 로고
    • Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies
    • Kramer ML, Schulz-Schaeffer WJ. Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies. J Neurosci 2007; 27: 1405-10
    • (2007) J Neurosci , vol.27 , pp. 1405-1410
    • Kramer, M.L.1    Schulz-Schaeffer, W.J.2
  • 35
    • 0346460948 scopus 로고    scopus 로고
    • Oxidative dimer formation is the critical ratelimiting step for Parkinson's disease alpha-synuclein fibrillogenesis
    • Krishnan S, Chi EY, Wood SJ, Kendrick BS, Li C, Garzon-Rodriguez W, et al. Oxidative dimer formation is the critical ratelimiting step for Parkinson's disease alpha-synuclein fibrillogenesis Biochemistry 2003; 42: 829-37
    • (2003) Biochemistry , vol.42 , pp. 829-837
    • Krishnan, S.1    Chi, E.Y.2    Wood, S.J.3    Kendrick, B.S.4    Li, C.5    Garzon-Rodriguez, W.6
  • 36
    • 0344305371 scopus 로고    scopus 로고
    • Morphogenesis of lewy bodies: Dissimilar incorporation of alpha-synuclein, ubiquitin, and p62
    • Kuusisto E, Parkkinen L, Alafuzoff I. Morphogenesis of lewy bodies: dissimilar incorporation of alpha-synuclein, ubiquitin, and p62 J Neuropathol Exp Neurol 2003; 62: 1241-53
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 1241-1253
    • Kuusisto, E.1    Parkkinen, L.2    Alafuzoff, I.3
  • 37
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr Neurodegenerative disease: amyloid pores from pathogenic mutations Nature 2002a; 418: 291
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 38
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, et al Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J Mol Biol 2002b; 322: 1089-102
    • (2002) J Mol Biol , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6
  • 39
    • 0037073747 scopus 로고    scopus 로고
    • Characterization of cytoplasmic alpha-synuclein aggregates Fibril formation is tightly linked to the inclusion-forming process in cells
    • Lee HJ, Lee SJ. Characterization of cytoplasmic alpha-synuclein aggregates Fibril formation is tightly linked to the inclusion-forming process in cells. J Biol Chem 2002; 277: 48976-83
    • (2002) J Biol Chem , vol.277 , pp. 48976-48983
    • Lee, H.J.1    Lee, S.J.2
  • 40
    • 84869109864 scopus 로고    scopus 로고
    • Pathological alpha-synuclein transmission initiates Parkinsonlike neurodegeneration in nontransgenic mice
    • Luk KC, Kehm V, Carroll J, Zhang B, O'Brien P, Trojanowski JQ, et al. Pathological alpha-synuclein transmission initiates Parkinsonlike neurodegeneration in nontransgenic mice. Science 2012a; 338: 949-53
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6
  • 41
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice
    • Luk KC, Kehm VM, Zhang B, O'Brien P, Trojanowski JQ, Lee VM Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice. J Exp Med 2012b; 209: 975-86
    • (2012) J Exp Med , vol.209 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3    O'Brien, P.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 43
    • 0034518238 scopus 로고    scopus 로고
    • Spectrum of Parkinson's disease, Parkinson's dementia, and Lewy body dementia
    • McKeith IG. Spectrum of Parkinson's disease, Parkinson's dementia, and Lewy body dementia. Neurol Clin 2000; 18: 865-902
    • (2000) Neurol Clin , vol.18 , pp. 865-902
    • McKeith, I.G.1
  • 44
    • 0037166267 scopus 로고    scopus 로고
    • Biochemical characterization of the core structure of alpha-synuclein filaments
    • Miake H, Mizusawa H, Iwatsubo T, Hasegawa M. Biochemical characterization of the core structure of alpha-synuclein filaments. J Biol Chem 2002; 277: 19213-9
    • (2002) J Biol Chem , vol.277 , pp. 19213-19219
    • Miake, H.1    Mizusawa, H.2    Iwatsubo, T.3    Hasegawa, M.4
  • 45
    • 0037014426 scopus 로고    scopus 로고
    • Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
    • Muchowski PJ. Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron 2002; 35: 9-12
    • (2002) Neuron , vol.35 , pp. 9-12
    • Muchowski, P.J.1
  • 46
    • 0032860819 scopus 로고    scopus 로고
    • Controlled dimerization of ERBB receptors provides evidence for differential signaling by homoand heterodimers
    • Muthuswamy SK, Gilman M, Brugge JS. Controlled dimerization of ErbB receptors provides evidence for differential signaling by homoand heterodimers. Mol Cell Biol 1999; 19: 6845-57
    • (1999) Mol Cell Biol , vol.19 , pp. 6845-6857
    • Muthuswamy, S.K.1    Gilman, M.2    Brugge, J.S.3
  • 47
  • 48
    • 79151470406 scopus 로고    scopus 로고
    • The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of alpha-synuclein oligomers with distinct biochemical, morphological, and functional properties
    • Nasstrom T, Fagerqvist T, Barbu M, Karlsson M, Nikolajeff F, Kasrayan A, et al. The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of alpha-synuclein oligomers with distinct biochemical, morphological, and functional properties. Free Radic Biol Med 2011; 50: 428-37
    • (2011) Free Radic Biol Med , vol.50 , pp. 428-437
    • Nasstrom, T.1    Fagerqvist, T.2    Barbu, M.3    Karlsson, M.4    Nikolajeff, F.5    Kasrayan, A.6
  • 49
    • 10044242402 scopus 로고    scopus 로고
    • Regional distribution of proteinase K-resistant alpha-synuclein correlates with Lewy body disease stage
    • Neumann M, Muller V, Kretzschmar HA, Haass C, Kahle PJ Regional distribution of proteinase K-resistant alpha-synuclein correlates with Lewy body disease stage. J Neuropathol Exp Neurol 2004; 63: 1225-35
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 1225-1235
    • Neumann, M.1    Muller, V.2    Kretzschmar, H.A.3    Haass, C.4    Kahle, P.J.5
  • 50
    • 38649095191 scopus 로고    scopus 로고
    • Evaluation of a novel proximity ligation assay for the sensitive and rapid detection of foot-and-mouth disease virus
    • Nordengrahn A, Gustafsdottir SM, Ebert K, Reid SM, King DP, Ferris NP, et al. Evaluation of a novel proximity ligation assay for the sensitive and rapid detection of foot-and-mouth disease virus Vet Microbiol 2008; 127: 227-36
    • (2008) Vet Microbiol , vol.127 , pp. 227-236
    • Nordengrahn, A.1    Gustafsdottir, S.M.2    Ebert, K.3    Reid, S.M.4    King, D.P.5    Ferris, N.P.6
  • 52
    • 84872458771 scopus 로고    scopus 로고
    • Aggregation and neurotoxicity of recombinant alpha-synuclein aggregates initiated by dimerization
    • Roostaee A, Beaudoin S, Staskevicius A, Roucou X. Aggregation and neurotoxicity of recombinant alpha-synuclein aggregates initiated by dimerization. Mol Neurodegener 2013; 8: 5
    • (2013) Mol Neurodegener , vol.8 , pp. 5
    • Roostaee, A.1    Beaudoin, S.2    Staskevicius, A.3    Roucou, X.4
  • 53
    • 84888093377 scopus 로고    scopus 로고
    • Alpha-synuclein and mitochondrial bioenergetics regulate tetrahydrobiopterin levels in a human dopaminergic model of Parkinson disease
    • Ryan BJ, Lourenco-Venda L, Crabtree MJ, Hale AB, Channon KM, Wade-Martins R. Alpha-synuclein and mitochondrial bioenergetics regulate tetrahydrobiopterin levels in a human dopaminergic model of Parkinson disease. Free Radic Biol Med 2013; 67: 58-68
    • (2013) Free Radic Biol Med , vol.67 , pp. 58-68
    • Ryan, B.J.1    Lourenco-Venda, L.2    Crabtree, M.J.3    Hale, A.B.4    Channon, K.M.5    Wade-Martins, R.6
  • 54
    • 70649100038 scopus 로고    scopus 로고
    • Novel means of viral antigen identification: Improved detection of avian influenza viruses by proximity ligation
    • Schlingemann J, Leijon M, Yacoub A, Schlingemann H, Zohari S, Matyi-Toth A, et al. Novel means of viral antigen identification: improved detection of avian influenza viruses by proximity ligation J Virol Methods 2010; 163: 116-22
    • (2010) J Virol Methods , vol.163 , pp. 116-122
    • Schlingemann, J.1    Leijon, M.2    Yacoub, A.3    Schlingemann, H.4    Zohari, S.5    Matyi-Toth, A.6
  • 55
    • 77957264418 scopus 로고    scopus 로고
    • The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia
    • Schulz-Schaeffer WJ. The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia. Acta Neuropathol 2010; 120: 131-43
    • (2010) Acta Neuropathol , vol.120 , pp. 131-143
    • Schulz-Schaeffer, W.J.1
  • 56
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic alpha-synuclein filaments shows amyloidlike cross-beta conformation
    • Serpell LC, Berriman J, Jakes R, Goedert M, Crowther RA. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloidlike cross-beta conformation. Proc Natl Acad Sci USA 2000; 97: 4897-902
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 58
    • 39049126210 scopus 로고    scopus 로고
    • Protein misfolding and neurodegeneration
    • Soto C, Estrada LD. Protein misfolding and neurodegeneration. Arch Neurol 2008; 65: 184-9
    • (2008) Arch Neurol , vol.65 , pp. 184-189
    • Soto, C.1    Estrada, L.D.2
  • 60
    • 79957673695 scopus 로고    scopus 로고
    • Multiple recognition assay reveals prostasomes as promising plasma biomarkers for prostate cancer
    • Tavoosidana G, Ronquist G, Darmanis S, Yan J, Carlsson L, Wu D, et al. Multiple recognition assay reveals prostasomes as promising plasma biomarkers for prostate cancer. Proc Natl Acad Sci USA 2011; 108: 8809-14
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 8809-8814
    • Tavoosidana, G.1    Ronquist, G.2    Darmanis, S.3    Yan, J.4    Carlsson, L.5    Wu, D.6
  • 62
    • 0242666359 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function
    • Tofaris GK, Razzaq A, Ghetti B, Lilley KS, Spillantini MG Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function. J Biol Chem 2003; 278: 44405-11
    • (2003) J Biol Chem , vol.278 , pp. 44405-44411
    • Tofaris, G.K.1    Razzaq, A.2    Ghetti, B.3    Lilley, K.S.4    Spillantini, M.G.5
  • 63
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • Volles MJ, Lee SJ, Rochet JC, Shtilerman MD, Ding TT, Kessler JC, et al. Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease Biochemistry 2001; 40: 7812-9
    • (2001) Biochemistry , vol.40 , 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
  • 67
    • 28444497467 scopus 로고    scopus 로고
    • Advantages and limitations of clear-native PAGE
    • Wittig I, Schagger H. Advantages and limitations of clear-native PAGE. Proteomics 2005; 5: 4338-46
    • (2005) Proteomics , vol.5 , pp. 4338-4346
    • Wittig, I.1    Schagger, H.2
  • 68
    • 79952846029 scopus 로고    scopus 로고
    • Regulation of AKT phosphorylation at Ser473 and Thr308 by endoplasmic reticulum stress modulates substrate specificity in a severity dependent manner
    • Yung HW, Charnock-Jones DS, Burton GJ. Regulation of AKT phosphorylation at Ser473 and Thr308 by endoplasmic reticulum stress modulates substrate specificity in a severity dependent manner. PLoS One 2011; 6: e17894
    • (2011) PLoS One , vol.6 , pp. e17894
    • Yung, H.W.1    Charnock-Jones, D.S.2    Burton, G.J.3
  • 70
    • 50649112184 scopus 로고    scopus 로고
    • Alpha-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: Understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis
    • Zhang NY, Tang Z, Liu CW. alpha-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis J Biol Chem 2008; 283: 20288-98
    • (2008) J Biol Chem , vol.283 , pp. 20288-20298
    • Zhang, N.Y.1    Tang, Z.2    Liu, C.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.