메뉴 건너뛰기




Volumn 6, Issue 4, 2011, Pages

Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of lewy body disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; ALPHA SYNUCLEIN MONOCLONAL ANTIBODY; CALPAIN; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG;

EID: 79955757052     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019338     Document Type: Article
Times cited : (365)

References (63)
  • 1
    • 0034518238 scopus 로고    scopus 로고
    • Spectrum of Parkinson's disease, Parkinson's dementia, and Lewy body dementia
    • McKeith IG, (2000) Spectrum of Parkinson's disease, Parkinson's dementia, and Lewy body dementia. Neurol Clin 18: 865-902.
    • (2000) Neurol Clin , vol.18 , pp. 865-902
    • McKeith, I.G.1
  • 2
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb P, Zhen W, Poon A, Conway K, Lansbury PJ, (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochem 35: 13709-13715.
    • (1996) Biochem , vol.35 , pp. 13709-13715
    • Weinreb, P.1    Zhen, W.2    Poon, A.3    Conway, K.4    Lansbury, P.J.5
  • 3
    • 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, et al. (1995) The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 14: 467-475.
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.4    Flanagan, L.5
  • 4
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy DD, Rueter SM, Trojanowski JQ, Lee VM, (2000) Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J Neurosci 20: 3214-3220.
    • (2000) J Neurosci , vol.20 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 5
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M, Hsu LJ, Xia Y, Takeda A, Sisk A, et al. (1999) Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport 10: 717-721.
    • (1999) Neuroreport , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5
  • 6
    • 0029866793 scopus 로고    scopus 로고
    • Purification and characterization of Lewy bodies from brains of patients with diffuse Lewy body disease
    • Iwatsubo T, Yamaguchi H, Fujimuro M, Yokosawa H, Ihara Y, et al. (1996) Purification and characterization of Lewy bodies from brains of patients with diffuse Lewy body disease. AmJPathol 148: 1517-1529.
    • (1996) AmJPathol , vol.148 , pp. 1517-1529
    • Iwatsubo, T.1    Yamaguchi, H.2    Fujimuro, M.3    Yokosawa, H.4    Ihara, Y.5
  • 7
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury PT Jr, (1999) Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc Natl Acad Sci U S A 96: 3342-3344.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3342-3344
    • Lansbury Jr., P.T.1
  • 8
    • 0031910093 scopus 로고    scopus 로고
    • Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: implications for the pathogenesis of Parkinson disease and Lewy body dementia
    • Trojanowski JQ, Lee VM, (1998) Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: implications for the pathogenesis of Parkinson disease and Lewy body dementia. Arch Neurol 55: 151-152.
    • (1998) Arch Neurol , vol.55 , pp. 151-152
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 9
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
    • Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, et al. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc Natl Acad Sci U S A 97: 571-576.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5
  • 10
    • 33947210032 scopus 로고    scopus 로고
    • Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein
    • Tsigelny IF, Bar-On P, Sharikov Y, Crews L, Hashimoto M, et al. (2007) Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein. Febs J 274: 1862-1877.
    • (2007) Febs J , vol.274 , pp. 1862-1877
    • Tsigelny, I.F.1    Bar-On, P.2    Sharikov, Y.3    Crews, L.4    Hashimoto, M.5
  • 12
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy
    • In press
    • Crews L, Spencer B, Desplats P, Patrick C, Paulino A, et al. (2010) Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy. PLoS ONE In press.
    • (2010) PLoS ONE
    • Crews, L.1    Spencer, B.2    Desplats, P.3    Patrick, C.4    Paulino, A.5
  • 14
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D, (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305: 1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 15
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • Spencer B, Potkar R, Trejo M, Rockenstein E, Patrick C, et al. (2009) Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases. J Neurosci 29: 13578-13588.
    • (2009) J Neurosci , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5
  • 16
    • 33645755812 scopus 로고    scopus 로고
    • The Parkinson's complex: parkinsonism is just the tip of the iceberg
    • Langston JW, (2006) The Parkinson's complex: parkinsonism is just the tip of the iceberg. Ann Neurol 59: 591-596.
    • (2006) Ann Neurol , vol.59 , pp. 591-596
    • Langston, J.W.1
  • 17
    • 20444413356 scopus 로고    scopus 로고
    • Effects of alpha-Synuclein Immunization in a Mouse Model of Parkinson's Disease
    • Masliah E, Rockenstein E, Adame A, Alford M, Crews L, et al. (2005) Effects of alpha-Synuclein Immunization in a Mouse Model of Parkinson's Disease. Neuron 46: 857-868.
    • (2005) Neuron , vol.46 , pp. 857-868
    • Masliah, E.1    Rockenstein, E.2    Adame, A.3    Alford, M.4    Crews, L.5
  • 18
    • 10344257196 scopus 로고    scopus 로고
    • A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed alpha-synuclein
    • Zhou C, Emadi S, Sierks MR, Messer A, (2004) A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed alpha-synuclein. Mol Ther 10: 1023-1031.
    • (2004) Mol Ther , vol.10 , pp. 1023-1031
    • Zhou, C.1    Emadi, S.2    Sierks, M.R.3    Messer, A.4
  • 19
    • 1542357652 scopus 로고    scopus 로고
    • Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments
    • Emadi S, Liu R, Yuan B, Schulz P, McAllister C, et al. (2004) Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments. Biochemistry 43: 2871-2878.
    • (2004) Biochemistry , vol.43 , pp. 2871-2878
    • Emadi, S.1    Liu, R.2    Yuan, B.3    Schulz, P.4    McAllister, C.5
  • 21
    • 52349111812 scopus 로고    scopus 로고
    • Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases
    • Tsigelny IF, Crews L, Desplats P, Shaked GM, Sharikov Y, et al. (2008) Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases. PLoS ONE 3: e3135.
    • (2008) PLoS ONE , vol.3
    • Tsigelny, I.F.1    Crews, L.2    Desplats, P.3    Shaked, G.M.4    Sharikov, Y.5
  • 22
    • 55949104903 scopus 로고    scopus 로고
    • Mechanism of alpha-synuclein oligomerization and membrane interaction: theoretical approach to unstructured proteins studies
    • Tsigelny IF, Sharikov Y, Miller MA, Masliah E, (2008) Mechanism of alpha-synuclein oligomerization and membrane interaction: theoretical approach to unstructured proteins studies. Nanomedicine 4: 350-357.
    • (2008) Nanomedicine , vol.4 , pp. 350-357
    • Tsigelny, I.F.1    Sharikov, Y.2    Miller, M.A.3    Masliah, E.4
  • 23
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of alpha-synuclein and its aggregates
    • Lee HJ, Patel S, Lee SJ, (2005) Intravesicular localization and exocytosis of alpha-synuclein and its aggregates. J Neurosci 25: 6016-6024.
    • (2005) J Neurosci , vol.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 24
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein
    • Desplats P, Lee HJ, Bae EJ, Patrick C, Rockenstein E, et al. (2009) Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci U S A 106: 13010-13015.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.J.3    Patrick, C.4    Rockenstein, E.5
  • 25
    • 0034674376 scopus 로고    scopus 로고
    • Full length alpha-synuclein is present in cerebrospinal fluid from Parkinson's disease and normal subjects
    • Borghi R, Marchese R, Negro A, Marinelli L, Forloni G, et al. (2000) Full length alpha-synuclein is present in cerebrospinal fluid from Parkinson's disease and normal subjects. Neurosci Lett 287: 65-67.
    • (2000) Neurosci Lett , vol.287 , pp. 65-67
    • Borghi, R.1    Marchese, R.2    Negro, A.3    Marinelli, L.4    Forloni, G.5
  • 26
    • 58149374375 scopus 로고    scopus 로고
    • CSF alpha-synuclein levels in dementia with Lewy bodies and Alzheimer's disease
    • Noguchi-Shinohara M, Tokuda T, Yoshita M, Kasai T, Ono K, et al. (2009) CSF alpha-synuclein levels in dementia with Lewy bodies and Alzheimer's disease. Brain Res 1251: 1-6.
    • (2009) Brain Res , vol.1251 , pp. 1-6
    • Noguchi-Shinohara, M.1    Tokuda, T.2    Yoshita, M.3    Kasai, T.4    Ono, K.5
  • 27
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • Masliah E, Rockenstein E, Veinbergs I, Mallory M, Hashimoto M, et al. (2000) Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders. Science 287: 1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5
  • 28
    • 0036605566 scopus 로고    scopus 로고
    • Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters
    • Rockenstein E, Mallory M, Hashimoto M, Song D, Shults CW, et al. (2002) Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters. J Neurosci Res 68: 568-578.
    • (2002) J Neurosci Res , vol.68 , pp. 568-578
    • Rockenstein, E.1    Mallory, M.2    Hashimoto, M.3    Song, D.4    Shults, C.W.5
  • 29
    • 0035834076 scopus 로고    scopus 로고
    • beta-amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease
    • Masliah E, Rockenstein E, Veinbergs I, Sagara Y, Mallory M, et al. (2001) beta-amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease. Proc Natl Acad Sci U S A 98: 12245-12250.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12245-12250
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Sagara, Y.4    Mallory, M.5
  • 30
    • 35348932113 scopus 로고    scopus 로고
    • Transgenic animal models of neurodegenerative diseases and their application to treatment development
    • Rockenstein E, Crews L, Masliah E, (2007) Transgenic animal models of neurodegenerative diseases and their application to treatment development. Adv Drug Deliv Rev 59: 1093-1102.
    • (2007) Adv Drug Deliv Rev , vol.59 , pp. 1093-1102
    • Rockenstein, E.1    Crews, L.2    Masliah, E.3
  • 31
    • 84940364788 scopus 로고    scopus 로고
    • Alpha-synuclein and the Lewy body disorders
    • Dickson DW, (2001) Alpha-synuclein and the Lewy body disorders. Curr Opin Neurol 14: 423-432.
    • (2001) Curr Opin Neurol , vol.14 , pp. 423-432
    • Dickson, D.W.1
  • 32
    • 34250832784 scopus 로고    scopus 로고
    • Calpain-Cleavage of {alpha}-Synuclein: Connecting Proteolytic Processing to Disease-Linked Aggregation
    • Dufty BM, Warner LR, Hou ST, Jiang SX, Gomez-Isla T, et al. (2007) Calpain-Cleavage of {alpha}-Synuclein: Connecting Proteolytic Processing to Disease-Linked Aggregation. Am J Pathol 170: 1725-1738.
    • (2007) Am J Pathol , vol.170 , pp. 1725-1738
    • Dufty, B.M.1    Warner, L.R.2    Hou, S.T.3    Jiang, S.X.4    Gomez-Isla, T.5
  • 33
    • 0035889404 scopus 로고    scopus 로고
    • Early formation of mature amyloid-b proteins deposits in a mutant APP transgenic model depends on levels of Ab1-42
    • Rockenstein E, Mallory M, Mante M, Sisk A, Masliah E, (2001) Early formation of mature amyloid-b proteins deposits in a mutant APP transgenic model depends on levels of Ab1-42. J neurosci Res 66: 573-582.
    • (2001) J Neurosci Res , vol.66 , pp. 573-582
    • Rockenstein, E.1    Mallory, M.2    Mante, M.3    Sisk, A.4    Masliah, E.5
  • 34
    • 0020465735 scopus 로고
    • Utilization of ketone bodies and glucose by established neural cell lines
    • Roeder LM, Poduslo SE, Tildon JT, (1982) Utilization of ketone bodies and glucose by established neural cell lines. J Neurosci Res 8: 671-682.
    • (1982) J Neurosci Res , vol.8 , pp. 671-682
    • Roeder, L.M.1    Poduslo, S.E.2    Tildon, J.T.3
  • 35
    • 0035151038 scopus 로고    scopus 로고
    • Reduced neuritic outgrowth and cell adhesion in neuronal cells transfected with human a-synuclein
    • Takenouchi T, Hashimoto M, Hsu L, Mackowski B, Rockenstein E, et al. (2001) Reduced neuritic outgrowth and cell adhesion in neuronal cells transfected with human a-synuclein. MolCell Neurosci 17: 141-150.
    • (2001) MolCell Neurosci , vol.17 , pp. 141-150
    • Takenouchi, T.1    Hashimoto, M.2    Hsu, L.3    Mackowski, B.4    Rockenstein, E.5
  • 36
    • 0038472472 scopus 로고    scopus 로고
    • Alpha-synuclein up-regulates expression of caveolin-1 and down-regulates extracellular signal-regulated kinase activity in B103 neuroblastoma cells: role in the pathogenesis of Parkinson's disease
    • Hashimoto M, Takenouchi T, Rockenstein E, Masliah E, (2003) Alpha-synuclein up-regulates expression of caveolin-1 and down-regulates extracellular signal-regulated kinase activity in B103 neuroblastoma cells: role in the pathogenesis of Parkinson's disease. J Neurochem 85: 1468-1479.
    • (2003) J Neurochem , vol.85 , pp. 1468-1479
    • Hashimoto, M.1    Takenouchi, T.2    Rockenstein, E.3    Masliah, E.4
  • 37
    • 45749114895 scopus 로고    scopus 로고
    • The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice
    • Pickford F, Masliah E, Britschgi M, Lucin K, Narasimhan R, et al. (2008) The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice. J Clin Invest 118: 2190-2199.
    • (2008) J Clin Invest , vol.118 , pp. 2190-2199
    • Pickford, F.1    Masliah, E.2    Britschgi, M.3    Lucin, K.4    Narasimhan, R.5
  • 38
    • 73949132010 scopus 로고    scopus 로고
    • Lovastatin ameliorates alpha-synuclein accumulation and oxidation in transgenic mouse models of alpha-synucleinopathies
    • Koob AO, Ubhi K, Paulsson JF, Kelly J, Rockenstein E, et al. (2010) Lovastatin ameliorates alpha-synuclein accumulation and oxidation in transgenic mouse models of alpha-synucleinopathies. Exp Neurol 221: 267-274.
    • (2010) Exp Neurol , vol.221 , pp. 267-274
    • Koob, A.O.1    Ubhi, K.2    Paulsson, J.F.3    Kelly, J.4    Rockenstein, E.5
  • 39
    • 77951185469 scopus 로고    scopus 로고
    • Genome-wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for Parkinson disease
    • Edwards TL, Scott WK, Almonte C, Burt A, Powell EH, et al. (2010) Genome-wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for Parkinson disease. Ann Hum Genet 74: 97-109.
    • (2010) Ann Hum Genet , vol.74 , pp. 97-109
    • Edwards, T.L.1    Scott, W.K.2    Almonte, C.3    Burt, A.4    Powell, E.H.5
  • 41
    • 13844320376 scopus 로고    scopus 로고
    • Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations
    • Li W, West N, Colla E, Pletnikova O, Troncoso JC, et al. (2005) Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proc Natl Acad Sci U S A 102: 2162-2167.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2162-2167
    • Li, W.1    West, N.2    Colla, E.3    Pletnikova, O.4    Troncoso, J.C.5
  • 42
    • 8544264002 scopus 로고    scopus 로고
    • Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro
    • Hoyer W, Cherny D, Subramaniam V, Jovin TM, (2004) Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro. Biochemistry 43: 16233-16242.
    • (2004) Biochemistry , vol.43 , pp. 16233-16242
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 43
    • 0031661141 scopus 로고    scopus 로고
    • Abnormal distribution of the non-Ab component of Alzheimer's disease amyloid precursor/a-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment
    • Takeda A, Hashimoto M, Mallory M, Sundsmo M, Hansen L, et al. (1998) Abnormal distribution of the non-Ab component of Alzheimer's disease amyloid precursor/a-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment. LabInvest 78: 1169-1177.
    • (1998) LabInvest , vol.78 , pp. 1169-1177
    • Takeda, A.1    Hashimoto, M.2    Mallory, M.3    Sundsmo, M.4    Hansen, L.5
  • 44
    • 28044461467 scopus 로고    scopus 로고
    • Neural activity controls the synaptic accumulation of alpha-synuclein
    • Fortin DL, Nemani VM, Voglmaier SM, Anthony MD, Ryan TA, et al. (2005) Neural activity controls the synaptic accumulation of alpha-synuclein. J Neurosci 25: 10913-10921.
    • (2005) J Neurosci , vol.25 , pp. 10913-10921
    • Fortin, D.L.1    Nemani, V.M.2    Voglmaier, S.M.3    Anthony, M.D.4    Ryan, T.A.5
  • 45
    • 33846997878 scopus 로고    scopus 로고
    • Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies
    • Kramer ML, Schulz-Schaeffer WJ, (2007) Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies. J Neurosci 27: 1405-1410.
    • (2007) J Neurosci , vol.27 , pp. 1405-1410
    • Kramer, M.L.1    Schulz-Schaeffer, W.J.2
  • 46
    • 33749028479 scopus 로고    scopus 로고
    • Conformational properties of the SDS-bound state of alpha-synuclein probed by limited proteolysis: unexpected rigidity of the acidic C-terminal tail
    • de Laureto PP, Tosatto L, Frare E, Marin O, Uversky VN, et al. (2006) Conformational properties of the SDS-bound state of alpha-synuclein probed by limited proteolysis: unexpected rigidity of the acidic C-terminal tail. Biochemistry 45: 11523-11531.
    • (2006) Biochemistry , vol.45 , pp. 11523-11531
    • de Laureto, P.P.1    Tosatto, L.2    Frare, E.3    Marin, O.4    Uversky, V.N.5
  • 47
    • 72249104472 scopus 로고    scopus 로고
    • Structural properties of pore-forming oligomers of alpha-synuclein
    • Kim HY, Cho MK, Kumar A, Maier E, Siebenhaar C, et al. (2009) Structural properties of pore-forming oligomers of alpha-synuclein. J Am Chem Soc 131: 17482-17489.
    • (2009) J Am Chem Soc , vol.131 , pp. 17482-17489
    • Kim, H.Y.1    Cho, M.K.2    Kumar, A.3    Maier, E.4    Siebenhaar, C.5
  • 48
    • 54849417407 scopus 로고    scopus 로고
    • Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing
    • van Rooijen BD, Claessens MM, Subramaniam V, (2008) Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing. FEBS Lett 582: 3788-3792.
    • (2008) FEBS Lett , vol.582 , pp. 3788-3792
    • van Rooijen, B.D.1    Claessens, M.M.2    Subramaniam, V.3
  • 49
    • 65549114936 scopus 로고    scopus 로고
    • Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core
    • van Rooijen BD, Claessens MM, Subramaniam V, (2009) Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core. Biochim Biophys Acta 1788: 1271-1278.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1271-1278
    • van Rooijen, B.D.1    Claessens, M.M.2    Subramaniam, V.3
  • 50
    • 44749083979 scopus 로고    scopus 로고
    • Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein
    • Lee HJ, Suk JE, Bae EJ, Lee JH, Paik SR, et al. (2008) Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein. Int J Biochem Cell Biol 40: 1835-1849.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1835-1849
    • Lee, H.J.1    Suk, J.E.2    Bae, E.J.3    Lee, J.H.4    Paik, S.R.5
  • 51
    • 44749090147 scopus 로고    scopus 로고
    • Clearance and deposition of extracellular alpha-synuclein aggregates in microglia
    • Lee HJ, Suk JE, Bae EJ, Lee SJ, (2008) Clearance and deposition of extracellular alpha-synuclein aggregates in microglia. Biochem Biophys Res Commun 372: 423-428.
    • (2008) Biochem Biophys Res Commun , vol.372 , pp. 423-428
    • Lee, H.J.1    Suk, J.E.2    Bae, E.J.3    Lee, S.J.4
  • 52
    • 40749094842 scopus 로고    scopus 로고
    • Origins and effects of extracellular alpha-synuclein: implications in Parkinson's disease
    • Lee SJ, (2008) Origins and effects of extracellular alpha-synuclein: implications in Parkinson's disease. J Mol Neurosci 34: 17-22.
    • (2008) J Mol Neurosci , vol.34 , pp. 17-22
    • Lee, S.J.1
  • 53
    • 34548496276 scopus 로고    scopus 로고
    • An investigation into the lipid-binding properties of alpha-, beta- and gamma-synucleins in human brain and cerebrospinal fluid
    • Salem SA, Allsop D, Mann DM, Tokuda T, El-Agnaf OM, (2007) An investigation into the lipid-binding properties of alpha-, beta- and gamma-synucleins in human brain and cerebrospinal fluid. Brain Res 1170: 103-111.
    • (2007) Brain Res , vol.1170 , pp. 103-111
    • Salem, S.A.1    Allsop, D.2    Mann, D.M.3    Tokuda, T.4    El-Agnaf, O.M.5
  • 54
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri M, Vogiatzi T, Vekrellis K, Park D, Stefanis L, (2009) Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS ONE 4: e5515.
    • (2009) PLoS ONE , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5
  • 55
    • 53549118274 scopus 로고    scopus 로고
    • alpha-synuclein degradation by autophagic pathways: a potential key to Parkinson's disease pathogenesis
    • Xilouri M, Vogiatzi T, Vekrellis K, Stefanis L, (2008) alpha-synuclein degradation by autophagic pathways: a potential key to Parkinson's disease pathogenesis. Autophagy 4: 917-919.
    • (2008) Autophagy , vol.4 , pp. 917-919
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Stefanis, L.4
  • 56
    • 4344565054 scopus 로고    scopus 로고
    • Morphological characterization of Thioflavin-S-positive amyloid plaques in transgenic Alzheimer mice and effect of passive Abeta immunotherapy on their clearance
    • Bussiere T, Bard F, Barbour R, Grajeda H, Guido T, et al. (2004) Morphological characterization of Thioflavin-S-positive amyloid plaques in transgenic Alzheimer mice and effect of passive Abeta immunotherapy on their clearance. Am J Pathol 165: 987-995.
    • (2004) Am J Pathol , vol.165 , pp. 987-995
    • Bussiere, T.1    Bard, F.2    Barbour, R.3    Grajeda, H.4    Guido, T.5
  • 57
    • 27144511230 scopus 로고    scopus 로고
    • Beta-amyloid immunotherapy prevents synaptic degeneration in a mouse model of Alzheimer's disease
    • Buttini M, Masliah E, Barbour R, Grajeda H, Motter R, et al. (2005) Beta-amyloid immunotherapy prevents synaptic degeneration in a mouse model of Alzheimer's disease. J Neurosci 25: 9096-9101.
    • (2005) J Neurosci , vol.25 , pp. 9096-9101
    • Buttini, M.1    Masliah, E.2    Barbour, R.3    Grajeda, H.4    Motter, R.5
  • 58
    • 33646066257 scopus 로고    scopus 로고
    • Amyloid-beta immunotherapy for the prevention and treatment of Alzheimer disease: lessons from mice, monkeys, and humans
    • Lemere CA, Maier M, Jiang L, Peng Y, Seabrook TJ, (2006) Amyloid-beta immunotherapy for the prevention and treatment of Alzheimer disease: lessons from mice, monkeys, and humans. Rejuvenation Res 9: 77-84.
    • (2006) Rejuvenation Res , vol.9 , pp. 77-84
    • Lemere, C.A.1    Maier, M.2    Jiang, L.3    Peng, Y.4    Seabrook, T.J.5
  • 59
    • 33744471433 scopus 로고    scopus 로고
    • A beta immunotherapy: Lessons learned for potential treatment of Alzheimer's disease
    • Schenk DB, Seubert P, Grundman M, Black R, (2005) A beta immunotherapy: Lessons learned for potential treatment of Alzheimer's disease. Neurodegener Dis 2: 255-260.
    • (2005) Neurodegener Dis , vol.2 , pp. 255-260
    • Schenk, D.B.1    Seubert, P.2    Grundman, M.3    Black, R.4
  • 60
    • 54249156984 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies
    • Sigurdsson EM, (2008) Immunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies. J Alzheimers Dis 15: 157-168.
    • (2008) J Alzheimers Dis , vol.15 , pp. 157-168
    • Sigurdsson, E.M.1
  • 61
    • 70249127559 scopus 로고    scopus 로고
    • Tau-focused immunotherapy for Alzheimer's disease and related tauopathies
    • Sigurdsson EM, (2009) Tau-focused immunotherapy for Alzheimer's disease and related tauopathies. Curr Alzheimer Res 6: 446-450.
    • (2009) Curr Alzheimer Res , vol.6 , pp. 446-450
    • Sigurdsson, E.M.1
  • 62
    • 33744478405 scopus 로고    scopus 로고
    • Clearance and prevention of prion infection in cell culture by anti-PrP antibodies
    • Pankiewicz J, Prelli F, Sy MS, Kascsak RJ, Kascsak RB, et al. (2006) Clearance and prevention of prion infection in cell culture by anti-PrP antibodies. Eur J Neurosci 23: 2635-2647.
    • (2006) Eur J Neurosci , vol.23 , pp. 2635-2647
    • Pankiewicz, J.1    Prelli, F.2    Sy, M.S.3    Kascsak, R.J.4    Kascsak, R.B.5
  • 63
    • 23844543718 scopus 로고    scopus 로고
    • Suppression of Huntington's disease pathology in Drosophila by human single-chain Fv antibodies
    • Wolfgang WJ, Miller TW, Webster JM, Huston JS, Thompson LM, et al. (2005) Suppression of Huntington's disease pathology in Drosophila by human single-chain Fv antibodies. Proc Natl Acad Sci U S A 102: 11563-11568.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 11563-11568
    • Wolfgang, W.J.1    Miller, T.W.2    Webster, J.M.3    Huston, J.S.4    Thompson, L.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.