메뉴 건너뛰기




Volumn 55, Issue 5, 2018, Pages 3916-3930

Prion-Like Seeding of Misfolded α-Synuclein in the Brains of Dementia with Lewy Body Patients in RT-QUIC

Author keywords

Dementia with Lewy bodies (DLB); Prion; Real time quaking induced conversion (RT QUIC); synuclein

Indexed keywords

ALPHA SYNUCLEIN; OLIGOMER; RECOMBINANT ALPHA SYNUCLEIN; SERINE; UNCLASSIFIED DRUG; PHOSPHOSERINE; PROTEIN AGGREGATE; RECOMBINANT PROTEIN;

EID: 85019740998     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-017-0624-1     Document Type: Article
Times cited : (64)

References (43)
  • 1
    • 0036174010 scopus 로고    scopus 로고
    • Alpha-synuclein is phosphorylated in synucleinopathy lesions
    • COI: 1:CAS:528:DC%2BD38XhsVKnur4%3D, PID: 11813001
    • Fujiwara H, Hasegawa M, Dohmae N et al (2002) Alpha-synuclein is phosphorylated in synucleinopathy lesions. Nat Cell Biol 4:160–164
    • (2002) Nat Cell Biol , vol.4 , pp. 160-164
    • Fujiwara, H.1    Hasegawa, M.2    Dohmae, N.3
  • 2
    • 20444416315 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation enhances eosinophilic cytoplasmic inclusion formation in SH-SY5Y cells
    • COI: 1:CAS:528:DC%2BD2MXlsFWhtbg%3D
    • Smith WW, Margolis RL, Li X et al (2005) Alpha-synuclein phosphorylation enhances eosinophilic cytoplasmic inclusion formation in SH-SY5Y cells. J Neurosci: the official journal of the Society for Neuroscience 25:5544–5552
    • (2005) J Neurosci: the official journal of the Society for Neuroscience , vol.25 , pp. 5544-5552
    • Smith, W.W.1    Margolis, R.L.2    Li, X.3
  • 3
    • 47749107973 scopus 로고    scopus 로고
    • Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein
    • COI: 1:CAS:528:DC%2BD1cXmslOitLo%3D, PID: 18343814
    • Paleologou KE, Schmid AW, Rospigliosi CC et al (2008) Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein. J Biol Chem 283:16895–16905
    • (2008) J Biol Chem , vol.283 , pp. 16895-16905
    • Paleologou, K.E.1    Schmid, A.W.2    Rospigliosi, C.C.3
  • 4
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • COI: 1:CAS:528:DC%2BD2MXjsFyktL0%3D, PID: 15834418
    • Chen L, Feany MB (2005) Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat Neurosci 8:657–663
    • (2005) Nat Neurosci , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 5
    • 38649084032 scopus 로고    scopus 로고
    • The phosphorylation state of Ser-129 in human alpha-synuclein determines neurodegeneration in a rat model of Parkinson disease
    • COI: 1:CAS:528:DC%2BD1cXpvFOqtA%3D%3D, PID: 18178617
    • Gorbatyuk OS, Li S, Sullivan LF et al (2008) The phosphorylation state of Ser-129 in human alpha-synuclein determines neurodegeneration in a rat model of Parkinson disease. Proc Natl Acad Sci U S A 105:763–768
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 763-768
    • Gorbatyuk, O.S.1    Li, S.2    Sullivan, L.F.3
  • 6
    • 60549109895 scopus 로고    scopus 로고
    • Phosphorylation does not prompt, nor prevent, the formation of alpha-synuclein toxic species in a rat model of Parkinson’s disease
    • COI: 1:CAS:528:DC%2BD1MXhvV2jtL4%3D, PID: 19074459
    • Azeredo da Silveira S, Schneider BL, Cifuentes-Diaz C et al (2009) Phosphorylation does not prompt, nor prevent, the formation of alpha-synuclein toxic species in a rat model of Parkinson’s disease. Hum Mol Genet 18:872–887
    • (2009) Hum Mol Genet , vol.18 , pp. 872-887
    • Azeredo da Silveira, S.1    Schneider, B.L.2    Cifuentes-Diaz, C.3
  • 7
    • 70149118325 scopus 로고    scopus 로고
    • Alpha-synuclein S129 phosphorylation mutants do not alter nigrostriatal toxicity in a rat model of Parkinson disease
    • COI: 1:CAS:528:DC%2BD1MXltFOqsr4%3D, PID: 19525899
    • McFarland NR, Fan Z, Xu K et al (2009) Alpha-synuclein S129 phosphorylation mutants do not alter nigrostriatal toxicity in a rat model of Parkinson disease. J Neuropathol Exp Neurol 68:515–524
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 515-524
    • McFarland, N.R.1    Fan, Z.2    Xu, K.3
  • 8
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson’s disease
    • PID: 12498954
    • Braak H, Del Tredici K, Rub U et al (2003) Staging of brain pathology related to sporadic Parkinson’s disease. Neurobiol Aging 24:197–211
    • (2003) Neurobiol Aging , vol.24 , pp. 197-211
    • Braak, H.1    Del Tredici, K.2    Rub, U.3
  • 9
    • 17644426053 scopus 로고    scopus 로고
    • Cognitive status correlates with neuropathologic stage in Parkinson disease
    • COI: 1:STN:280:DC%2BD2M3hsleruw%3D%3D, PID: 15851731
    • Braak H, Rub U, Jansen Steur EN et al (2005) Cognitive status correlates with neuropathologic stage in Parkinson disease. Neurology 64:1404–1410
    • (2005) Neurology , vol.64 , pp. 1404-1410
    • Braak, H.1    Rub, U.2    Jansen Steur, E.N.3
  • 10
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson’s disease
    • COI: 1:CAS:528:DC%2BD1cXlsFCmsrg%3D, PID: 18391962
    • Kordower JH, Chu Y, Hauser RA et al (2008) Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson’s disease. Nat Med 14:504–506
    • (2008) Nat Med , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3
  • 11
    • 43249110200 scopus 로고    scopus 로고
    • Lewy bodies in grafted neurons in subjects with Parkinson’s disease suggest host-to-graft disease propagation
    • COI: 1:CAS:528:DC%2BD1cXlsFCmsrs%3D, PID: 18391963
    • Li JY, Englund E, Holton JL et al (2008) Lewy bodies in grafted neurons in subjects with Parkinson’s disease suggest host-to-graft disease propagation. Nat Med 14:501–503
    • (2008) Nat Med , vol.14 , pp. 501-503
    • Li, J.Y.1    Englund, E.2    Holton, J.L.3
  • 12
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice
    • COI: 1:CAS:528:DC%2BC38Xmsl2itb8%3D, PID: 22508839
    • Luk KC, Kehm VM, Zhang B et al (2012) Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice. J Exp Med 209:975–986
    • (2012) J Exp Med , vol.209 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3
  • 13
    • 84863433677 scopus 로고    scopus 로고
    • Prion-like acceleration of a synucleinopathy in a transgenic mouse model
    • COI: 1:CAS:528:DC%2BC38XhtVSgurfP, PID: 21813214
    • Mougenot AL, Nicot S, Bencsik A et al (2012) Prion-like acceleration of a synucleinopathy in a transgenic mouse model. Neurobiol Aging 33:2225–2228
    • (2012) Neurobiol Aging , vol.33 , pp. 2225-2228
    • Mougenot, A.L.1    Nicot, S.2    Bencsik, A.3
  • 14
    • 84888349390 scopus 로고    scopus 로고
    • Transmission of multiple system atrophy prions to transgenic mice
    • COI: 1:CAS:528:DC%2BC3sXhvFemurnM, PID: 24218576
    • Watts JC, Giles K, Oehler A et al (2013) Transmission of multiple system atrophy prions to transgenic mice. Proc Natl Acad Sci U S A 110:19555–19560
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 19555-19560
    • Watts, J.C.1    Giles, K.2    Oehler, A.3
  • 16
    • 80053613574 scopus 로고    scopus 로고
    • Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death
    • COI: 1:CAS:528:DC%2BC3MXht12kt7bP, PID: 21982369
    • Volpicelli-Daley LA, Luk KC, Patel TP et al (2011) Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron 72:57–71
    • (2011) Neuron , vol.72 , pp. 57-71
    • Volpicelli-Daley, L.A.1    Luk, K.C.2    Patel, T.P.3
  • 17
    • 84869109864 scopus 로고    scopus 로고
    • Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • COI: 1:CAS:528:DC%2BC38Xhs1GntL7L
    • Luk KC, Kehm V, Carroll J et al (2012) Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science (New York, NY) 338:949–953
    • (2012) Science (New York, NY) , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3
  • 18
    • 79751535822 scopus 로고    scopus 로고
    • Ultrasensitive human prion detection in cerebrospinal fluid by real-time quaking-induced conversion
    • COI: 1:CAS:528:DC%2BC3MXht12msrs%3D, PID: 21278748
    • Atarashi R, Satoh K, Sano K et al (2011) Ultrasensitive human prion detection in cerebrospinal fluid by real-time quaking-induced conversion. Nat Med 17:175–178
    • (2011) Nat Med , vol.17 , pp. 175-178
    • Atarashi, R.1    Satoh, K.2    Sano, K.3
  • 19
    • 84907440608 scopus 로고    scopus 로고
    • Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion
    • PID: 25078700
    • Sano K, Atarashi R, Ishibashi D et al (2014) Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. J Virol 88:11791–11801
    • (2014) J Virol , vol.88 , pp. 11791-11801
    • Sano, K.1    Atarashi, R.2    Ishibashi, D.3
  • 20
    • 85033548081 scopus 로고    scopus 로고
    • Alpha-synuclein RT-QuIC in the CSF of patients with alpha-synucleinopathies
    • COI: 1:CAS:528:DC%2BC28Xhs1SjtrjN, PID: 27752516
    • Fairfoul G, McGuire LI, Pal S et al (2016) Alpha-synuclein RT-QuIC in the CSF of patients with alpha-synucleinopathies. Ann Clin Transl Neurol 3:812–818
    • (2016) Ann Clin Transl Neurol , vol.3 , pp. 812-818
    • Fairfoul, G.1    McGuire, L.I.2    Pal, S.3
  • 21
    • 80055078029 scopus 로고    scopus 로고
    • A soluble alpha-synuclein construct forms a dynamic tetramer
    • COI: 1:CAS:528:DC%2BC3MXhsVGksLrE, PID: 22006323
    • Wang W, Perovic I, Chittuluru J et al (2011) A soluble alpha-synuclein construct forms a dynamic tetramer. Proc Natl Acad Sci U S A 108:17797–17802
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 17797-17802
    • Wang, W.1    Perovic, I.2    Chittuluru, J.3
  • 22
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • COI: 1:CAS:528:DC%2BC3MXhtFWku7nM, PID: 21841800
    • Bartels T, Choi JG, Selkoe DJ (2011) Alpha-synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477:107–110
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 23
    • 78651249792 scopus 로고    scopus 로고
    • Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays
    • PID: 21152012
    • Wilham JM, Orru CD, Bessen RA et al (2010) Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays. PLoS Pathog 6:e1001217
    • (2010) PLoS Pathog , vol.6
    • Wilham, J.M.1    Orru, C.D.2    Bessen, R.A.3
  • 25
    • 77749341497 scopus 로고    scopus 로고
    • Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions
    • COI: 1:CAS:528:DC%2BC3cXjtFahtLo%3D
    • Paleologou KE, Oueslati A, Shakked G et al (2010) Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions. J Neurosci: the official journal of the Society for Neuroscience 30:3184–3198
    • (2010) J Neurosci: the official journal of the Society for Neuroscience , vol.30 , pp. 3184-3198
    • Paleologou, K.E.1    Oueslati, A.2    Shakked, G.3
  • 26
    • 83355175639 scopus 로고    scopus 로고
    • Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson’s disease protein alpha-synuclein as revealed by ion mobility mass spectrometry
    • COI: 1:CAS:528:DC%2BC3MXhsVWlsrjK, PID: 22162214
    • Vlad C, Lindner K, Karreman C et al (2011) Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson’s disease protein alpha-synuclein as revealed by ion mobility mass spectrometry. Chembiochem: a European journal of chemical biology 12:2740–2744
    • (2011) Chembiochem: a European journal of chemical biology , vol.12 , pp. 2740-2744
    • Vlad, C.1    Lindner, K.2    Karreman, C.3
  • 27
    • 67651087325 scopus 로고    scopus 로고
    • Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils
    • COI: 1:CAS:528:DC%2BD1MXptVWhurc%3D, PID: 19564620
    • Chatani E, Lee YH, Yagi H et al (2009) Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils. Proc Natl Acad Sci U S A 106:11119–11124
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 11119-11124
    • Chatani, E.1    Lee, Y.H.2    Yagi, H.3
  • 28
    • 71749089460 scopus 로고    scopus 로고
    • Fibril fragmentation enhances amyloid cytotoxicity
    • COI: 1:CAS:528:DC%2BD1MXhsVymu7fK, PID: 19808677
    • Xue WF, Hellewell AL, Gosal WS et al (2009) Fibril fragmentation enhances amyloid cytotoxicity. J Biol Chem 284:34272–34282
    • (2009) J Biol Chem , vol.284 , pp. 34272-34282
    • Xue, W.F.1    Hellewell, A.L.2    Gosal, W.S.3
  • 29
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology
    • COI: 1:CAS:528:DC%2BD1MXht1ertLbP, PID: 19686384
    • Danzer KM, Krebs SK, Wolff M et al (2009) Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J Neurochem 111:192–203
    • (2009) J Neurochem , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3
  • 31
    • 77953575526 scopus 로고    scopus 로고
    • Oligomeric alpha-synuclein and its role in neuronal death
    • COI: 1:CAS:528:DC%2BC3cXkvFegtLc%3D, PID: 20209636
    • Brown DR (2010) Oligomeric alpha-synuclein and its role in neuronal death. IUBMB life 62:334–339
    • (2010) IUBMB life , vol.62 , pp. 334-339
    • Brown, D.R.1
  • 32
    • 80054755695 scopus 로고    scopus 로고
    • Pathological roles of alpha-synuclein in neurological disorders
    • COI: 1:CAS:528:DC%2BC3MXhtlOks7jI, PID: 22014436
    • Vekrellis K, Xilouri M, Emmanouilidou E et al (2011) Pathological roles of alpha-synuclein in neurological disorders. Lancet Neurol 10:1015–1025
    • (2011) Lancet Neurol , vol.10 , pp. 1015-1025
    • Vekrellis, K.1    Xilouri, M.2    Emmanouilidou, E.3
  • 33
    • 65249162241 scopus 로고    scopus 로고
    • Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies
    • Paleologou KE, Kragh CL, Mann DM et al (2009) Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies. Brain: a journal of neurology 132:1093–1101
    • (2009) Brain: a journal of neurology , vol.132 , pp. 1093-1101
    • Paleologou, K.E.1    Kragh, C.L.2    Mann, D.M.3
  • 34
    • 84898026266 scopus 로고    scopus 로고
    • Detection of misfolded Abeta oligomers for sensitive biochemical diagnosis of Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC2cXks1OmsL0%3D, PID: 24656814
    • Salvadores N, Shahnawaz M, Scarpini E et al (2014) Detection of misfolded Abeta oligomers for sensitive biochemical diagnosis of Alzheimer’s disease. Cell Rep 7:261–268
    • (2014) Cell Rep , vol.7 , pp. 261-268
    • Salvadores, N.1    Shahnawaz, M.2    Scarpini, E.3
  • 35
    • 1042266326 scopus 로고    scopus 로고
    • Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
    • COI: 1:CAS:528:DC%2BD2cXps12ksw%3D%3D, PID: 14627698
    • Tanaka M, Kim YM, Lee G et al (2004) Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. J Biol Chem 279:4625–4631
    • (2004) J Biol Chem , vol.279 , pp. 4625-4631
    • Tanaka, M.1    Kim, Y.M.2    Lee, G.3
  • 36
    • 84867581207 scopus 로고    scopus 로고
    • Biochemical increase in phosphorylated alpha-synuclein precedes histopathology of Lewy-type synucleinopathies
    • COI: 1:CAS:528:DC%2BC3sXhsFalsg%3D%3D
    • Lue LF, Walker DG, Adler CH et al (2012) Biochemical increase in phosphorylated alpha-synuclein precedes histopathology of Lewy-type synucleinopathies. Brain Pathol (Zurich, Switzerland) 22:745–756
    • (2012) Brain Pathol (Zurich, Switzerland) , vol.22 , pp. 745-756
    • Lue, L.F.1    Walker, D.G.2    Adler, C.H.3
  • 37
    • 84906751686 scopus 로고    scopus 로고
    • Linking alpha-synuclein phosphorylation to reactive oxygen species formation and mitochondrial dysfunction in SH-SY5Y cells
    • COI: 1:CAS:528:DC%2BC2cXhtleitbbP, PID: 25109238
    • Perfeito R, Lazaro DF, Outeiro TF et al (2014) Linking alpha-synuclein phosphorylation to reactive oxygen species formation and mitochondrial dysfunction in SH-SY5Y cells. Mol Cell Neurosci 62:51–59
    • (2014) Mol Cell Neurosci , vol.62 , pp. 51-59
    • Perfeito, R.1    Lazaro, D.F.2    Outeiro, T.F.3
  • 38
    • 67650496503 scopus 로고    scopus 로고
    • Relationship between alpha synuclein phosphorylation, proteasomal inhibition and cell death: relevance to Parkinson’s disease pathogenesis
    • COI: 1:CAS:528:DC%2BD1MXptlensLo%3D, PID: 19493164
    • Chau KY, Ching HL, Schapira AH et al (2009) Relationship between alpha synuclein phosphorylation, proteasomal inhibition and cell death: relevance to Parkinson’s disease pathogenesis. J Neurochem 110:1005–1013
    • (2009) J Neurochem , vol.110 , pp. 1005-1013
    • Chau, K.Y.1    Ching, H.L.2    Schapira, A.H.3
  • 39
    • 84857693190 scopus 로고    scopus 로고
    • Phosphorylation of alpha-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans
    • COI: 1:CAS:528:DC%2BC38XjtFyltb8%3D, PID: 22232559
    • Kuwahara T, Tonegawa R, Ito G et al (2012) Phosphorylation of alpha-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans. J Biol Chem 287:7098–7109
    • (2012) J Biol Chem , vol.287 , pp. 7098-7109
    • Kuwahara, T.1    Tonegawa, R.2    Ito, G.3
  • 40
    • 84884683227 scopus 로고    scopus 로고
    • Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases
    • COI: 1:CAS:528:DC%2BC3sXhsFOntLzL, PID: 24068917
    • Morales R, Moreno-Gonzalez I, Soto C (2013) Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. PLoS Pathog 9:e1003537
    • (2013) PLoS Pathog , vol.9
    • Morales, R.1    Moreno-Gonzalez, I.2    Soto, C.3
  • 41
    • 84874894136 scopus 로고    scopus 로고
    • Alpha-synuclein as CSF and blood biomarker of dementia with Lewy bodies
    • PID: 23056991
    • Kasuga K, Nishizawa M, Ikeuchi T (2012) Alpha-synuclein as CSF and blood biomarker of dementia with Lewy bodies. Int J Alzheimers Dis 2012:437025
    • (2012) Int J Alzheimers Dis , vol.2012 , pp. 437025
    • Kasuga, K.1    Nishizawa, M.2    Ikeuchi, T.3
  • 42
    • 78649990079 scopus 로고    scopus 로고
    • Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease
    • COI: 1:CAS:528:DC%2BC3cXhsVans7vF, PID: 20962290
    • Tokuda T, Qureshi MM, Ardah MT et al (2010) Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease. Neurology 75:1766–1772
    • (2010) Neurology , vol.75 , pp. 1766-1772
    • Tokuda, T.1    Qureshi, M.M.2    Ardah, M.T.3
  • 43
    • 84989182833 scopus 로고    scopus 로고
    • Levels of cerebrospinal fluid alpha-synuclein oligomers are increased in Parkinson’s disease with dementia and dementia with Lewy bodies compared to Alzheimer’s disease
    • PID: 24987465
    • Hansson O, Hall S, Ohrfelt A et al (2014) Levels of cerebrospinal fluid alpha-synuclein oligomers are increased in Parkinson’s disease with dementia and dementia with Lewy bodies compared to Alzheimer’s disease. Alzheimers Res Ther 6:25
    • (2014) Alzheimers Res Ther , vol.6 , pp. 25
    • Hansson, O.1    Hall, S.2    Ohrfelt, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.