메뉴 건너뛰기




Volumn 11, Issue 5, 2010, Pages 334-342

Membrane Interactions of Oligomeric Alpha-Synuclein: Potential Role in Parkinson's Disease

Author keywords

synuclein; Amyloid; Disruption; Membrane; Oligomer; Parkinson's disease; Permeabilization; Pore

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; OLIGOMER;

EID: 77957904174     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920310791330659     Document Type: Article
Times cited : (42)

References (164)
  • 3
    • 2542596183 scopus 로고    scopus 로고
    • Parkinson's disease
    • Samii, A.; Nutt, J.G.; Ransom, B.R. Parkinson's disease. Lancet, 2004, 363, 1783-1793.
    • (2004) Lancet , vol.363 , pp. 1783-1793
    • Samii, A.1    Nutt, J.G.2    Ransom, B.R.3
  • 4
    • 0001509014 scopus 로고
    • In Paralysis Agitans
    • Lewandowsski, M.; Ed
    • Lewy, F.H. In Paralysis Agitans. Handbuch der Neurologie; Lewandowsski, M.; Ed. 1912; pp 920-933.
    • (1912) Handbuch Der Neurologie , pp. 920-933
    • Lewy, F.H.1
  • 5
    • 0034973443 scopus 로고    scopus 로고
    • An algorithm (decision tree) for the management of Parkinson's disease: Treatment guidelines
    • Olanow, C.W.; Watts, R.L.; Koller, W.C. An algorithm (decision tree) for the management of Parkinson's disease: treatment guidelines. Neurology, 2001, 56, S1-S88.
    • (2001) Neurology , vol.56 , pp. 1-88
    • Olanow, C.W.1    Watts, R.L.2    Koller, W.C.3
  • 6
    • 0042767676 scopus 로고    scopus 로고
    • Parkinson's disease: Piecing together a genetic jigsaw
    • Dekker, M.C.J.; Bonifati, V.; van Duijn, C.M. Parkinson's disease: piecing together a genetic jigsaw. Brain, 2003, 126, 1722-1733.
    • (2003) Brain , vol.126 , pp. 1722-1733
    • Dekker, M.C.J.1    Bonifati, V.2    van Duijn, C.M.3
  • 7
    • 40749152391 scopus 로고    scopus 로고
    • Parkinson's disease: A genetic perspective
    • Belin, A.C.; Westerlund, M. Parkinson's disease: a genetic perspective. FEBS J., 2008, 275, 1377-1383.
    • (2008) FEBS J , vol.275 , pp. 1377-1383
    • Belin, A.C.1    Westerlund, M.2
  • 9
    • 0031843721 scopus 로고    scopus 로고
    • The risk of Parkinson's disease with exposure to pesticides, farming, well water, and rural living
    • Gorell, J.M.; Johnson, C.C.; Rybicki, B.A.; Peterson, E.L.; Richardson, R.J. The risk of Parkinson's disease with exposure to pesticides, farming, well water, and rural living. Neurology, 1998, 50, 1346-1350.
    • (1998) Neurology , vol.50 , pp. 1346-1350
    • Gorell, J.M.1    Johnson, C.C.2    Rybicki, B.A.3    Peterson, E.L.4    Richardson, R.J.5
  • 16
    • 33748300291 scopus 로고    scopus 로고
    • Behavioral models of Parkinson's disease in rodents: A new look at an old problem
    • Meredith, G.E.; Kang, U.J. Behavioral models of Parkinson's disease in rodents: a new look at an old problem. Mov. Disord., 2006, 21, 1595-1606.
    • (2006) Mov. Disord , vol.21 , pp. 1595-1606
    • Meredith, G.E.1    Kang, U.J.2
  • 17
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany, M.B.; Bender, W.W. A Drosophila model of Parkinson's disease. Nature, 2000, 404, 394-398.
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 19
    • 0032102455 scopus 로고    scopus 로고
    • The synucleins: A family of proteins involved in synaptic function, plasticity, neurodegeneration and disease
    • Clayton, D.F.; George, J.M. The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease. Trends. Neurosci., 1998, 21, 249-254.
    • (1998) Trends. Neurosci , vol.21 , pp. 249-254
    • Clayton, D.F.1    George, J.M.2
  • 21
    • 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.F.; Flanagan, L.; Desilva, H.A.R.; Kittel, A.; Saitoh, T. 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, 467-475.
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.F.4    Flanagan, L.5    Desilva, H.A.R.6    Kittel, A.7    Saitoh, T.8
  • 22
    • 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, D.D.; Rueter, S.M.; Trojanowski, J.Q.; Lee, V.M.Y. Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J. Neurosci., 2000, 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.Y.4
  • 24
    • 33847649977 scopus 로고    scopus 로고
    • Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody
    • Yu, S.; Li, X.; Liu, G.; Han, J.; Zhang, C.; Li, Y.; Xu, S.; Liu, C.; Gao, Y.; Yang, H.; Ueda, K.; Chan, P. Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody. Neuroscience, 2007, 145, 539-555.
    • (2007) Neuroscience , vol.145 , pp. 539-555
    • Yu, S.1    Li, X.2    Liu, G.3    Han, J.4    Zhang, C.5    Li, Y.6    Xu, S.7    Liu, C.8    Gao, Y.9    Yang, H.10    Ueda, K.11    Chan, P.12
  • 26
    • 34548318990 scopus 로고    scopus 로고
    • Physiological and pathological properties of alpha-synuclein
    • Tofaris, G.K.; Spillantini, M.G. Physiological and pathological properties of alpha-synuclein. Cell. Mol. Life Sci., 2007, 64, 2194-2201.
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 2194-2201
    • Tofaris, G.K.1    Spillantini, M.G.2
  • 31
    • 0037451858 scopus 로고    scopus 로고
    • Attenuation of dopamine transporter activity by alpha-synuclein. Neurosci
    • Wersinger, C.; Sidhu, A. Attenuation of dopamine transporter activity by alpha-synuclein. Neurosci. Lett., 2003, 340, 189-192.
    • (2003) Lett , vol.340 , pp. 189-192
    • Wersinger, C.1    Sidhu, A.2
  • 33
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W.S.; Jonas, A.; Clayton, D.F.; George, J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem., 1998, 273, 9443-9449.
    • (1998) J. Biol. Chem , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 34
    • 0037192865 scopus 로고    scopus 로고
    • Alpha-synuclein protects against oxidative stress via inactivation of the c-Jun N-terminal kinase stress- signaling pathway in neuronal cells
    • Hashimoto, M.; Hsu, L.J.; Rockenstein, E.; Takenouchi, T.; Mallory, M.; Masliah, E. alpha-synuclein protects against oxidative stress via inactivation of the c-Jun N-terminal kinase stress- signaling pathway in neuronal cells. J. Biol. Chem., 2002, 277, 11465-11472.
    • (2002) J. Biol. Chem , vol.277 , pp. 11465-11472
    • Hashimoto, M.1    Hsu, L.J.2    Rockenstein, E.3    Takenouchi, T.4    Mallory, M.5    Masliah, E.6
  • 35
    • 33745259502 scopus 로고    scopus 로고
    • Alpha-synuclein is upregulated in neurones in response to chronic oxidative stress and is associated with neuroprotection
    • Quilty, M.C.; King, A.E.; Gai, W.P.; Pountney, D.L.; West, A.K.; Vickers, J.C.; Dickson, T.C. Alpha-synuclein is upregulated in neurones in response to chronic oxidative stress and is associated with neuroprotection. Exp. Neurol., 2006, 199, 249-256.
    • (2006) Exp. Neurol , vol.199 , pp. 249-256
    • Quilty, M.C.1    King, A.E.2    Gai, W.P.3    Pountney, D.L.4    West, A.K.5    Vickers, J.C.6    Dickson, T.C.7
  • 36
    • 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.; Di Monte, D.A. alpha-synuclein overexpression protects against paraquat-induced neurodegeneration. J. Neurosci., 2003, 23, 3095-3099.
    • (2003) J. Neurosci , vol.23 , 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
  • 37
    • 0037185004 scopus 로고    scopus 로고
    • Alpha-Synuclein lowers p53-dependent apoptotic response of neuronal cells - Abolishment by 6-hydroxydopamine and implication for Parkinson's disease
    • da Costa, C.A.; Paitel, E.; Vincent, B.; Checler, F. alpha-Synuclein lowers p53-dependent apoptotic response of neuronal cells - Abolishment by 6-hydroxydopamine and implication for Parkinson's disease. J. Biol. Chem., 2002, 277, 50980-50984.
    • (2002) J. Biol. Chem , vol.277 , pp. 50980-50984
    • da Costa, C.A.1    Paitel, E.2    Vincent, B.3    Checler, F.4
  • 38
    • 33746065340 scopus 로고    scopus 로고
    • Endogenous alpha-synuclein is induced by valproic acid through histone deacetylase inhibition and participates in neuroprotection against glutamate-induced excitotoxicity
    • Leng, Y.; Chuang, D.M. Endogenous alpha-synuclein is induced by valproic acid through histone deacetylase inhibition and participates in neuroprotection against glutamate-induced excitotoxicity. J. Neurosci., 2006, 26, 7502-7512.
    • (2006) J. Neurosci , vol.26 , pp. 7502-7512
    • Leng, Y.1    Chuang, D.M.2
  • 39
    • 0037137224 scopus 로고    scopus 로고
    • Structural and functional implications of C-terminal regions of alpha-synuclein
    • Kim, T.D.; Paik, S.R.; Yang, C.H. Structural and functional implications of C-terminal regions of alpha-synuclein. Biochemistry, 2002, 41, 13782-13790.
    • (2002) Biochemistry , vol.41 , pp. 13782-13790
    • Kim, T.D.1    Paik, S.R.2    Yang, C.H.3
  • 42
    • 0037047371 scopus 로고    scopus 로고
    • Distinct roles of the N-terminal-binding domain and the C- terminal-solubilizing domain of alpha-synuclein, a molecular chaperone
    • Park, S.M.; Jung, H.Y.; Kim, T.D.; Park, J.H.; Yang, C.H.; Kim, J. Distinct roles of the N-terminal-binding domain and the C- terminal-solubilizing domain of alpha-synuclein, a molecular chaperone. J. Biol. Chem., 2002, 277, 28512-28520.
    • (2002) J. Biol. Chem , vol.277 , pp. 28512-28520
    • Park, S.M.1    Jung, H.Y.2    Kim, T.D.3    Park, J.H.4    Yang, C.H.5    Kim, J.6
  • 43
  • 44
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P.H.; Zhen, W.; Poon, A.W.; Conway, K.A.; Lansbury, P.T. Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry, 1996, 35, 13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr, P.T.5
  • 45
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re- assessing the protein structure-function paradigm
    • Wright, P.E.; Dyson, H.J. Intrinsically unstructured proteins: Re- assessing the protein structure-function paradigm. J. Mol. Biol., 1999, 293, 321-331.
    • (1999) J. Mol. Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 46
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded proteins unstructured under physiologic conditions? Proteins-Struct. Funct
    • Uversky, V.N.; Gillespie, J.R.; Fink, A.L. Why are natively unfolded proteins unstructured under physiologic conditions? Proteins-Struct. Funct. Genet., 2000, 41, 415-427.
    • (2000) Genet , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 47
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J.; Wright, P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol., 2005, 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 48
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegene- rative disorders
    • Uversky, V.N. A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegene- rative disorders. J. Biomol. Struct. Dyn., 2003, 21, 211-234.
    • (2003) J. Biomol. Struct. Dyn , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 49
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid- associated states
    • Eliezer, D.; Kutluay, E.; Bussell, R. Jr.; Browne, G. Conformational properties of alpha-synuclein in its free and lipid- associated states. J. Mol. Biol., 2001, 307, 1061-1073.
    • (2001) J. Mol. Biol , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell Jr., R.3    Browne, G.4
  • 50
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis
    • Perrin, R.J.; Woods, W.S.; Clayton, D.F.; George, J.M. Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J. Biol. Chem., 2000, 275, 34393-34398.
    • (2000) J. Biol. Chem , vol.275 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 51
    • 2942555022 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling
    • Jao, C.C.; Der-Sarkissian, A.; Chen, J.; Langen, R. Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc. Natl. Acad. Sci. USA, 2004, 101, 8331-8336.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8331-8336
    • Jao, C.C.1    Der-Sarkissian, A.2    Chen, J.3    Langen, R.4
  • 53
    • 64849109238 scopus 로고    scopus 로고
    • Alpha-Synuclein binds large unilamellar vesicles as an extended helix
    • Trexler, A.J.; Rhoades, E. alpha-Synuclein binds large unilamellar vesicles as an extended helix. Biochemistry, 2009, 48, 2304-2306.
    • (2009) Biochemistry , vol.48 , pp. 2304-2306
    • Trexler, A.J.1    Rhoades, E.2
  • 54
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles
    • Georgieva, E.R.; Ramlall, T.F.; Borbat, P.P.; Freed, J.H.; Eliezer, D. Membrane-bound alpha-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles. J. Am. Chem. Soc., 2008, 130, 12856-12857.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 12856-12857
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 56
    • 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, 19213-19219.
    • (2002) J. Biol. Chem , vol.277 , pp. 19213-19219
    • Miake, H.1    Mizusawa, H.2    Iwatsubo, T.3    Hasegawa, M.4
  • 57
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • Giasson, B.I.; Murray, I.V.J.; Trojanowski, J.Q.; Lee, V.M.Y. A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J. Biol. Chem., 2001, 276, 2380-2386.
    • (2001) J. Biol. Chem , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.J.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 58
    • 0029257497 scopus 로고
    • The core alzheimers peptide nac forms amyloid fibrils which seed and are seeded by beta-amyloid - is nac a common trigger or target in neurodegenerative disease
    • Han, H.Y.; Weinreb, P.H.; Lansbury, P.T. The core alzheimers peptide nac forms amyloid fibrils which seed and are seeded by beta-amyloid - is nac a common trigger or target in neurodegenerative disease. Chem. Biol., 1995, 2, 163-169.
    • (1995) Chem. Biol , vol.2 , pp. 163-169
    • Han, H.Y.1    Weinreb, P.H.2    Lansbury, P.T.3
  • 59
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR
    • Heise, H.; Hoyer, W.; Becker, S.; Andronesi, O.C.; Riedel, D.; Baldus, M. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. USA, 2005, 102, 15871-15876.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 61
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimers-disease - synapse loss is the major correlate of cognitive impairment
    • Terry, R.D.; Masliah, E.; Salmon, D.P.; Butters, N.; Deteresa, R.; Hill, R.; Hansen, L.A.; Katzman, R. Physical basis of cognitive alterations in Alzheimers-disease - synapse loss is the major correlate of cognitive impairment. Ann. Neurol., 1991, 30, 572-580.
    • (1991) Ann. Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 62
    • 0033501744 scopus 로고    scopus 로고
    • Behavioral disturbances in transgenic mice overexpressing the V717F beta-amyloid precursor protein
    • Dodart, J.C.; Meziane, H.; Mathis, C.; Bales, K.R.; Paul, S.M.; Ungerer, A. Behavioral disturbances in transgenic mice overexpressing the V717F beta-amyloid precursor protein. Behav. Neurosci., 1999, 113, 982-990.
    • (1999) Behav. Neurosci , vol.113 , pp. 982-990
    • Dodart, J.C.1    Meziane, H.2    Mathis, C.3    Bales, K.R.4    Paul, S.M.5    Ungerer, A.6
  • 65
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M.; Mitra, S.; Schweitzer, E.S.; Segal, M.R.; Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature, 2004, 431, 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 66
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel, H.A.; Lansbury, P.T. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q. Rev. Biophys., 2006, 39, 167-201.
    • (2006) Q. Rev. Biophys , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, P.T.2
  • 67
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neuro degenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze, M.D.; Bitan, G.; Teplow, D.B. Paradigm shifts in Alzheimer's disease and other neuro degenerative disorders: The emerging role of oligomeric assemblies. J. Neurosci. Res., 2002, 69, 567-577.
    • (2002) J. Neurosci. Res , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 68
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg, M.S.; Lansbury, P.T. Jr. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat. Cell Biol., 2000, 2, E115-E119.
    • (2000) Nat. Cell Biol , vol.2 , pp. 115-119
    • Goldberg, M.S.1    Lansbury Jr, P.T.2
  • 70
    • 70449532484 scopus 로고    scopus 로고
    • A stable proportion of Lewy body bearing neurons in the substantia nigra suggests a model in which the Lewy body causes neuronal death
    • Greffard, S.; Verny, M.; Bonnet, A.-M.; Seilhean, D.; Hauw, J.-J.; Duyckaerts, C. A stable proportion of Lewy body bearing neurons in the substantia nigra suggests a model in which the Lewy body causes neuronal death. Neurobiol. Aging, 2010, 31, 99-103.
    • (2010) Neurobiol. Aging , vol.31 , pp. 99-103
    • Greffard, S.1    Verny, M.2    Bonnet, A.-M.3    Seilhean, D.4    Hauw, J.-J.5    Duyckaerts, C.6
  • 71
    • 68649095418 scopus 로고    scopus 로고
    • Molecular mechanisms of alpha- synuclein neurodegeneration
    • Waxman, E.A.; Giasson, B.I. Molecular mechanisms of alpha- synuclein neurodegeneration. Biochim. Biophys. Acta-Mol. Basis Dis., 2009, 1792, 616-624.
    • (2009) Biochim. Biophys. Acta-Mol. Basis Dis , vol.1792 , pp. 616-624
    • Waxman, E.A.1    Giasson, B.I.2
  • 72
    • 57749095477 scopus 로고    scopus 로고
    • A critical evaluation of the braak staging scheme for Parkinson's disease
    • Burke, R.E.; Dauer, W.T.; Vonsattel, J.P.G. A critical evaluation of the braak staging scheme for Parkinson's disease. Ann. Neurol., 2008, 64, 485-491.
    • (2008) Ann. Neurol , vol.64 , pp. 485-491
    • Burke, R.E.1    Dauer, W.T.2    Vonsattel, J.P.G.3
  • 73
    • 11144241275 scopus 로고    scopus 로고
    • Alpha-Synuclein pathology does not predict extrapyramidal symptoms or dementia
    • Parkkinen, L.; Kauppinen, T.; Pirttila, T.; Autere, J.M.; Alafuzoff, I. alpha-Synuclein pathology does not predict extrapyramidal symptoms or dementia. Ann. Neurol., 2005, 57, 82-91.
    • (2005) Ann. Neurol , vol.57 , pp. 82-91
    • Parkkinen, L.1    Kauppinen, T.2    Pirttila, T.3    Autere, J.M.4    Alafuzoff, I.5
  • 74
    • 68349109646 scopus 로고    scopus 로고
    • Absence of alpha-synuclein pathology in postencephalitic parkinsonism
    • Jellinger, K.A. Absence of alpha-synuclein pathology in postencephalitic parkinsonism. Acta Neuropathol., 2009, 118, 371-379
    • (2009) Acta Neuropathol , vol.118 , pp. 371-379
    • Jellinger, K.A.1
  • 75
    • 69549116777 scopus 로고    scopus 로고
    • Formation and development of Lewy pathology: A critical update
    • Jellinger, K.A. Formation and development of Lewy pathology: a critical update. J. Neurol., 2009, 256 (Suppl 3), 270-279.
    • (2009) J. Neurol , vol.256 , Issue.SUPPL. 3 , pp. 270-279
    • Jellinger, K.A.1
  • 77
    • 0031474418 scopus 로고    scopus 로고
    • Contribution of somal Lewy bodies to neuronal death
    • Tompkins, M.M.; Hill, W.D. Contribution of somal Lewy bodies to neuronal death. Brain Res., 1997, 775, 24-29.
    • (1997) Brain Res , vol.775 , pp. 24-29
    • Tompkins, M.M.1    Hill, W.D.2
  • 78
    • 0036550101 scopus 로고    scopus 로고
    • Parkinson-like neurodegeneration induced by targeted overexpression of alpha- synuclein in the nigrostriatal system
    • Kirik, D.; Rosenblad, C.; Burer, C.; Lundberg, C.; Johansen, T.E.; Muzyczka, N.; Mandel, R.J.; Björklund, A. Parkinson-like neurodegeneration induced by targeted overexpression of alpha- synuclein in the nigrostriatal system. J. Neurosci., 2002, 22, 2780-2791.
    • (2002) J. Neurosci , vol.22 , pp. 2780-2791
    • Kirik, D.1    Rosenblad, C.2    Burer, C.3    Lundberg, C.4    Johansen, T.E.5    Muzyczka, N.6    Mandel, R.J.7    Björklund, A.8
  • 82
    • 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, H.J.; Lee, J.S.; Patel, S.; Lee, S.J. Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J. Biol. Chem., 2002, 277, 48984-48992.
    • (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
  • 83
    • 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.; Mouradian, M.M. Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. J. Biol. Chem., 2004, 279, 4625-4631.
    • (2004) J. Biol. Chem , vol.279 , pp. 4625-4631
    • Tanaka, M.1    Kim, Y.M.2    Lee, G.3    Junn, E.4    Iwatsubo, T.5    Mouradian, M.M.6
  • 85
    • 66449097646 scopus 로고    scopus 로고
    • Detecting morphologically distinct oligomeric forms of alpha- synuclein
    • Emadi, S.; Kasturirangan, S.; Wang, M.S.; Schulz, P.; Sierks, M.R. Detecting morphologically distinct oligomeric forms of alpha-synuclein. J. Biol. Chem., 2009, 284, 11048-11058.
    • (2009) J. Biol. Chem , vol.284 , pp. 11048-11058
    • Emadi, S.1    Kasturirangan, S.2    Wang, M.S.3    Schulz, P.4    Sierks, M.R.5
  • 86
    • 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, K.A.; Lee, S.J.; Rochet, J.C.; Ding, T.T.; Williamson, R.E.; Lansbury, P.T. Jr. 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. USA, 2000, 97, 571-576.
    • (2000) Proc. Natl. Acad. Sci. USA , 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    Lansbury Jr, P.T.6
  • 88
    • 33749507375 scopus 로고    scopus 로고
    • In: Conformation-dependent anti-amyloid oligomer antibodies
    • Elsevier Academic Press Inc: San Diego
    • [88] Kayed, R.; Glabe, C.G. In: Conformation-dependent anti-amyloid oligomer antibodies. Amyloid, Prions, and other Protein Aggregates, Pt C; Elsevier Academic Press Inc: San Diego, 2006; Vol. 413, pp 326-344.
    • (2006) Amyloid, Prions, and Other Protein Aggregates, Pt C , vol.413 , pp. 326-344
    • Kayed, R.1    Glabe, C.G.2
  • 91
    • 68849102707 scopus 로고    scopus 로고
    • Unique copper-induced oligomers mediate alpha-synuclein toxicity
    • Wright, J.A.; Wang, X.; Brown, D.R. Unique copper-induced oligomers mediate alpha-synuclein toxicity. FASEB J., 2009, 23, 2384-2393.
    • (2009) FASEB J , vol.23 , pp. 2384-2393
    • Wright, J.A.1    Wang, X.2    Brown, D.R.3
  • 92
  • 93
    • 34147130637 scopus 로고    scopus 로고
    • Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity
    • Emadi, S.; Barkhordarian, H.; Wang, M.S.; Schulz, P.; Sierks, M.R. Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity. J. Mol. Biol., 2007, 368, 1132-1144.
    • (2007) J. Mol. Biol , vol.368 , pp. 1132-1144
    • Emadi, S.1    Barkhordarian, H.2    Wang, M.S.3    Schulz, P.4    Sierks, M.R.5
  • 94
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology
    • Danzer, K.M.; Krebs, S.K.; Wolff, M.; Birk, G.; Hengerer, B. Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J. Neurochem., 2009, 111, 192-203.
    • (2009) J. Neurochem , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 95
    • 65749095912 scopus 로고    scopus 로고
    • Intracellular targeting and clearance of oligomeric alpha-synuclein alleviates toxicity in mammalian cells
    • Yuan, B.; Sierks, M.R. Intracellular targeting and clearance of oligomeric alpha-synuclein alleviates toxicity in mammalian cells. Neurosci. Lett., 2009, 459, 16-8.
    • (2009) Neurosci. Lett , vol.459 , pp. 16-18
    • Yuan, B.1    Sierks, M.R.2
  • 96
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta- protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin, A.; Chung, D.S.; Benedek, G.B.; Kirschner, D.A.; Teplow, D.B. On the nucleation and growth of amyloid beta- protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA, 1996, 93, 1125-1129.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 97
    • 0033538541 scopus 로고    scopus 로고
    • Alpha-synuclein fibrillogenesis is nucleation-dependent - Implications for the pathogenesis of Parkinson's disease
    • Wood, S.J.; Wypych, J.; Steavenson, S.; Louis, J.C.; Citron, M.; Biere, A.L. alpha-synuclein fibrillogenesis is nucleation-dependent - Implications for the pathogenesis of Parkinson's disease. J. Biol. Chem., 1999, 274, 19509-19512.
    • (1999) J. Biol. Chem , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6
  • 98
    • 36248965693 scopus 로고    scopus 로고
    • Role of different regions of alpha-synuclein in the assembly of fibrils
    • Qin, Z.; Hu, D.; Han, S.; Hong, D.P.; Fink, A.L. Role of different regions of alpha-synuclein in the assembly of fibrils. Biochemistry, 2007, 46, 13322-13330.
    • (2007) Biochemistry , vol.46 , pp. 13322-13330
    • Qin, Z.1    Hu, D.2    Han, S.3    Hong, D.P.4    Fink, A.L.5
  • 99
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level
    • Del Mar, C.; Greenbaum, E.A.; Mayne, L.; Englander, S.W.; Woods, V.L. Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level. Proc. Natl. Acad. Sci. USA, 2005, 102, 15477-15482.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15477-15482
    • del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 100
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling
    • Der-Sarkissian, A.; Jao, C.C.; Chen, J.; Langen, R. Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling. J. Biol. Chem., 2003, 278, 37530-37535.
    • (2003) J. Biol. Chem , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 101
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation
    • Serpell, L.C.; Berriman, J.; Jakes, R.; Goedert, M.; Crowther, R.A. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc. Natl. Acad. Sci. USA, 2000, 97, 4897-4902.
    • (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
  • 102
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky, V.N.; Li, J.; Fink, A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem., 2001, 276, 10737-10744.
    • (2001) J. Biol. Chem , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 104
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the aggregation kinetics of amyloid peptides
    • Pellarin, R.; Caflisch, A. Interpreting the aggregation kinetics of amyloid peptides. J. Mol. Biol., 2006, 360, 882-892.
    • (2006) J. Mol. Biol , vol.360 , pp. 882-892
    • Pellarin, R.1    Caflisch, A.2
  • 105
    • 57149102288 scopus 로고    scopus 로고
    • A Generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates
    • [105] Auer, S.; Meersman, F.; Dobson, C.M.; Vendruscolo, M. A Generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates. PLoS Comput. Biol., 2008, 4(11), e1000222.
    • (2008) PLoS Comput. Biol , vol.4 , Issue.11 , pp. 1000222
    • Auer, S.1    Meersman, F.2    Dobson, C.M.3    Vendruscolo, M.4
  • 106
    • 34848929022 scopus 로고    scopus 로고
    • Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    • Cheon, M.; Chang, I.; Mohanty, S.; Luheshi, L.M.; Dobson, C.M.; Vendruscolo, M.; Favrin, G. Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils. PLoS Comput. Biol., 2007, 3, 1727-1738.
    • (2007) PLoS Comput. Biol , vol.3 , pp. 1727-1738
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5    Vendruscolo, M.6    Favrin, G.7
  • 107
    • 35748943830 scopus 로고    scopus 로고
    • Pathways and intermediates of amyloid fibril formation
    • Pellarin, R.; Guarnera, E.; Caflisch, A. Pathways and intermediates of amyloid fibril formation. J. Mol. Biol., 2007, 374, 917-924.
    • (2007) J. Mol. Biol , vol.374 , pp. 917-924
    • Pellarin, R.1    Guarnera, E.2    Caflisch, A.3
  • 108
    • 45849128342 scopus 로고    scopus 로고
    • Fluorescent N Arylaminonaphthalene sulfonate probes for amyloid aggregation of alpha-synuclein
    • Celej, M.S.; Jares-Erijman, E.A.; Jovin, T.M. Fluorescent N- arylaminonaphthalene sulfonate probes for amyloid aggregation of alpha-synuclein. Biophys. J., 2008, 94, 4867-4879.
    • (2008) Biophys. J , vol.94 , pp. 4867-4879
    • Celej, M.S.1    Jares-Erijman, E.A.2    Jovin, T.M.3
  • 109
    • 22244456042 scopus 로고    scopus 로고
    • Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy
    • Lindgren, M.; Sörgjerd, K.; Hammarström, P. Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy. Biophys. J., 2005, 88, 4200-4212.
    • (2005) Biophys. J , vol.88 , pp. 4200-4212
    • Lindgren, M.1    Sörgjerd, K.2    Hammarström, P.3
  • 110
    • 33644527256 scopus 로고    scopus 로고
    • Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence
    • Dusa, A.; Kaylor, J.; Edridge, S.; Bodner, N.; Hong, D.P.; Fink, A.L. Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence. Biochemistry, 2006, 45, 2752-2760.
    • (2006) Biochemistry , vol.45 , pp. 2752-2760
    • Dusa, A.1    Kaylor, J.2    Edridge, S.3    Bodner, N.4    Hong, D.P.5    Fink, A.L.6
  • 111
    • 61449135187 scopus 로고    scopus 로고
    • Real-time analysis of amyloid fibril formation of alpha-synuclein using a fibrillation-state-specific fluorescent probe of JC-1
    • Lee, J.H.; Lee, I.H.; Choe, Y.J.; Kang, S.; Kim, H.Y.; Gai, W.P.; Hahn, J.S.; Paik, S.R. Real-time analysis of amyloid fibril formation of alpha-synuclein using a fibrillation-state-specific fluorescent probe of JC-1. Biochem. J., 2009, 418, 311-323.
    • (2009) Biochem. J , vol.418 , pp. 311-323
    • Lee, J.H.1    Lee, I.H.2    Choe, Y.J.3    Kang, S.4    Kim, H.Y.5    Gai, W.P.6    Hahn, J.S.7    Paik, S.R.8
  • 112
    • 35848966149 scopus 로고    scopus 로고
    • Sensitive fluorescence polarization technique for rapid screening of alpha- synuclein oligomerization/fibrillization inhibitors
    • Luk, K.C.; Hyde, E.G.; Trojanowski, J.Q.; Lee, V.M. Sensitive fluorescence polarization technique for rapid screening of alpha- synuclein oligomerization/fibrillization inhibitors. Biochemistry, 2007, 46, 12522-12529.
    • (2007) Biochemistry , vol.46 , pp. 12522-12529
    • Luk, K.C.1    Hyde, E.G.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 113
    • 42649135877 scopus 로고    scopus 로고
    • Multiparametric fluorescence detection of early stages in the amyloid protein aggregation of pyrene-labeled alpha-synuclein
    • Thirunavukkuarasu, S.; Jares-Erijman, E.A.; Jovin, T.M. Multiparametric fluorescence detection of early stages in the amyloid protein aggregation of pyrene-labeled alpha-synuclein. J. Mol. Biol., 2008, 378, 1064-1073.
    • (2008) J. Mol. Biol , vol.378 , pp. 1064-1073
    • Thirunavukkuarasu, S.1    Jares-Erijman, E.A.2    Jovin, T.M.3
  • 114
    • 25444433798 scopus 로고    scopus 로고
    • Characterization of oligomeric intermediates in alpha- synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F alpha-synuclein
    • Kaylor, J.; Bodner, N.; Edridge, S.; Yamin, G.; Hong, D.P.; Fink, A.L. Characterization of oligomeric intermediates in alpha- synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F alpha-synuclein. J. Mol. Biol., 2005, 353, 357-372.
    • (2005) J. Mol. Biol , vol.353 , pp. 357-372
    • Kaylor, J.1    Bodner, N.2    Edridge, S.3    Yamin, G.4    Hong, D.P.5    Fink, A.L.6
  • 115
    • 0037072284 scopus 로고    scopus 로고
    • Annular alpha- synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • Ding, T.T.; Lee, S.J.; Rochet, J.C.; Lansbury, P.T. Annular alpha- synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry, 2002, 41, 10209-10217.
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Rochet, J.C.3    Lansbury, P.T.4
  • 116
    • 58649100263 scopus 로고    scopus 로고
    • Granular assembly of alpha-synuclein leading to the accelerated amyloid fibril formation with shear stress
    • Bhak, G.; Lee, J.H.; Hahn, J.S.; Paik, S.R. Granular assembly of alpha-synuclein leading to the accelerated amyloid fibril formation with shear stress. PLoS One, 2009, 4, e4177.
    • (2009) PLoS One , Issue.4
    • Bhak, G.1    Lee, J.H.2    Hahn, J.S.3    Paik, S.R.4
  • 118
    • 47749146102 scopus 로고    scopus 로고
    • Instantaneous amyloid fibril formation of alpha-synuclein from the oligomeric granular structures in the presence of hexane
    • Lee, J.H.; Bhak, G.; Lee, S.G.; Paik, S.R. Instantaneous amyloid fibril formation of alpha-synuclein from the oligomeric granular structures in the presence of hexane. Biophys. J., 2008, 95, L16-8.
    • (2008) Biophys. J , vol.95
    • Lee, J.H.1    Bhak, G.2    Lee, S.G.3    Paik, S.R.4
  • 119
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins, S.R.; Douglass, A.; Vale, R.D.; Weissman, J.S. Mechanism of prion propagation: Amyloid growth occurs by monomer addition. PLoS Biol., 2004, 2, 1582-1590.
    • (2004) PLoS Biol , vol.2 , pp. 1582-1590
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 120
    • 0037076539 scopus 로고    scopus 로고
    • Growth of beta- amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy
    • Nichols, M.R.; Moss, M.A.; Reed, D.K.; Lin, W.L.; Mukhopadhyay, R.; Hoh, J.H.; Rosenberry, T.L. Growth of beta- amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy. Biochemistry, 2002, 41, 6115-6127.
    • (2002) Biochemistry , vol.41 , pp. 6115-6127
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Lin, W.L.4    Mukhopadhyay, R.5    Hoh, J.H.6    Rosenberry, T.L.7
  • 121
    • 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.; Lansbury, P.T. Jr. Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry, 2001, 40, 7812-7819.
    • (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    Lansbury Jr, P.T.7
  • 122
    • 28844441969 scopus 로고    scopus 로고
    • Secondary structure of alpha-synuclein oligomers: Characterization by Raman and atomic force microscopy
    • Apetri, M.M.; Maiti, N.C.; Zagorski, M.G.; Carey, P.R.; Anderson, V.E. 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
  • 126
    • 33750117120 scopus 로고    scopus 로고
    • Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging
    • Klucken, J.; Outeiro, T.F.; Nguyen, P.; McLean, P.J.; Hyman, B.T. Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging. FASEB J., 2006, 20, 2050-2057.
    • (2006) FASEB J , vol.20 , pp. 2050-2057
    • Klucken, J.1    Outeiro, T.F.2    Nguyen, P.3    McLean, P.J.4    Hyman, B.T.5
  • 129
    • 0037456578 scopus 로고    scopus 로고
    • The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease
    • Sharon, R.; Bar-Joseph, I.; Frosch, M.P.; Walsh, D.M.; Hamilton, J.A.; Selkoe, D.J. The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron, 2003, 37, 583-595.
    • (2003) Neuron , vol.37 , pp. 583-595
    • Sharon, R.1    Bar-Joseph, I.2    Frosch, M.P.3    Walsh, D.M.4    Hamilton, J.A.5    Selkoe, D.J.6
  • 131
    • 9344233839 scopus 로고    scopus 로고
    • Calcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain
    • Lowe, R.; Pountney, D.L.; Jensen, P.H.; Gai, W.P.; Voelcker, N.H. Calcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain. Protein Sci., 2004, 13, 3245-3252.
    • (2004) Protein Sci , vol.13 , pp. 3245-3252
    • Lowe, R.1    Pountney, D.L.2    Jensen, P.H.3    Gai, W.P.4    Voelcker, N.H.5
  • 132
    • 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, 953-968.
    • (2010) Neurobiol. Aging , vol.31 , pp. 953-968
    • Emmanouilidou, E.1    Stefanis, L.2    Vekrellis, K.3
  • 133
    • 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, K.E.; Kragh, C.L.; Mann, D.M.; Salem, S.A.; Al-Shami, R.; Allsop, D.; Hassan, A.H.; Jensen, P.H.; El-Agnaf, O.M. Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies. Brain, 2009, 132, 1093-1101.
    • (2009) Brain , vol.132 , pp. 1093-1101
    • Paleologou, K.E.1    Kragh, C.L.2    Mann, D.M.3    Salem, S.A.4    Al-Shami, R.5    Allsop, D.6    Hassan, A.H.7    Jensen, P.H.8    El-Agnaf, O.M.9
  • 134
    • 3142664614 scopus 로고    scopus 로고
    • Annular alpha-synuclein species from purified multiple system atrophy inclusions
    • Pountney, D.L.; Lowe, R.; Quilty, M.; Vickers, J.C.; Voelcker, N.H.; Gai, W.P. Annular alpha-synuclein species from purified multiple system atrophy inclusions. J. Neurochem., 2004, 90, 502-512.
    • (2004) J. Neurochem , vol.90 , pp. 502-512
    • Pountney, D.L.1    Lowe, R.2    Quilty, M.3    Vickers, J.C.4    Voelcker, N.H.5    Gai, W.P.6
  • 135
    • 0035958973 scopus 로고    scopus 로고
    • Muscarinic receptor stimulation induces translocation of an alpha-synuclein oligomer from plasma membrane to a light vesicle fraction in cytoplasm
    • Leng, Y.; Chase, T.N.; Bennett, M.C. Muscarinic receptor stimulation induces translocation of an alpha-synuclein oligomer from plasma membrane to a light vesicle fraction in cytoplasm. J. Biol. Chem., 2001, 276, 28212-28218.
    • (2001) J. Biol. Chem , vol.276 , pp. 28212-28218
    • Leng, Y.1    Chase, T.N.2    Bennett, M.C.3
  • 136
  • 139
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as aubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro, A.; Mina, E.; Kayed, R.; Milton, S.C.; Parker, I.; Glabe, C.G. Calcium dysregulation and membrane disruption as aubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem., 2005, 280, 17294-17300.
    • (2005) J. Biol. Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 140
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed, R.; Sokolov, Y.; Edmonds, B.; McIntire, T.M.; Milton, S.C.; Hall, J.E.; Glabe, C.G. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem., 2004, 279, 46363-46366.
    • (2004) J. Biol. Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 141
    • 0036381074 scopus 로고    scopus 로고
    • Ion channel formation and membrane- linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules
    • Kourie, J.I.; Henry, C.L. Ion channel formation and membrane- linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules. Clin. Exp. Pharmacol. Physiol., 2002, 29, 741-753.
    • (2002) Clin. Exp. Pharmacol. Physiol , vol.29 , pp. 741-753
    • Kourie, J.I.1    Henry, C.L.2
  • 142
    • 0027508926 scopus 로고
    • Alzheimer-disease amyloid beta-protein forms calcium channels in bilayer-membranes - blockade by tromethamine and aluminum
    • Arispe, N.; Rojas, E.; Pollard, H.B. Alzheimer-disease amyloid beta-protein forms calcium channels in bilayer-membranes - blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci USA, 1993, 90, 567-571.
    • (1993) Proc. Natl. Acad. Sci USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 143
    • 22844447715 scopus 로고    scopus 로고
    • In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein
    • Lashuel, H.A.; Grillo-Bosch, D. In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein. Methods Mol. Biol., 2005, 299, 19-33.
    • (2005) Methods Mol. Biol , vol.299 , pp. 19-33
    • Lashuel, H.A.1    Grillo-Bosch, D.2
  • 144
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel, H.A.; Petre, B.M.; Wall, J.; Simon, M.; Nowak, R.J.; Walz, T.; Lansbury, P.T. Jr. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol., 2002, 322, 1089-1102.
    • (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    Lansbury Jr, P.T.7
  • 145
    • 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.; Lansbury, P.T. Jr. Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease- linked mutations and occurs by a pore-like mechanism. Biochemistry, 2002, 41, 4595-4602.
    • (2002) Biochemistry , vol.41 , pp. 4595-4602
    • Volles, M.J.1    Lansbury Jr, P.T.2
  • 146
    • 33751516396 scopus 로고    scopus 로고
    • Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure
    • Sokolov, Y.; Kozak, J.A.; Kayed, R.; Chanturiya, A.; Glabe, C.; Hall, J.E. Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure. J. Gen. Physiol., 2006, 128, 637-647.
    • (2006) J. Gen. Physiol , vol.128 , pp. 637-647
    • Sokolov, Y.1    Kozak, J.A.2    Kayed, R.3    Chanturiya, A.4    Glabe, C.5    Hall, J.E.6
  • 150
    • 3242879787 scopus 로고    scopus 로고
    • Alpha-Synuclein-synaptosomal membrane interactions: Implications for fibrillogenesis
    • Jo, E.; Darabie, A.A.; Han, K.; Tandon, A.; Fraser, P.E.; McLaurin, J. alpha-Synuclein-synaptosomal membrane interactions: implications for fibrillogenesis. Eur. J. Biochem., 2004, 271, 3180-3189.
    • (2004) Eur. J. Biochem , vol.271 , pp. 3180-3189
    • Jo, E.1    Darabie, A.A.2    Han, K.3    Tandon, A.4    Fraser, P.E.5    McLaurin, J.6
  • 151
    • 0037016741 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form
    • Lee, H.J.; Choi, C.; Lee, S.J. Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. J. Biol. Chem., 2002, 277, 671-678.
    • (2002) J. Biol. Chem , vol.277 , pp. 671-678
    • Lee, H.J.1    Choi, C.2    Lee, S.J.3
  • 152
    • 0141891097 scopus 로고    scopus 로고
    • The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation
    • Zhu, M.; Li, J.; Fink, A.L. The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation. J. Biol. Chem., 2003, 278, 40186-40197.
    • (2003) J. Biol. Chem , vol.278 , pp. 40186-40197
    • Zhu, M.1    Li, J.2    Fink, A.L.3
  • 155
    • 65549114936 scopus 로고    scopus 로고
    • Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core
    • van Rooijen, B.D.; Claessens, M.M.A.E.; Subramaniam, V. Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core. Biochim. Biophys. Acta, 2009, 1788, 1271-1278.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1271-1278
    • van Rooijen, B.D.1    Claessens, M.M.A.E.2    Subramaniam, V.3
  • 157
    • 0033669319 scopus 로고    scopus 로고
    • In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies
    • Gai, W.P.; Yuan, H.X.; Li, X.Q.; Power, J.T.H.; Blumbergs, P.C.; Jensen, P.H. In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies. Exp. Neurol., 2000, 166, 324-333.
    • (2000) Exp. Neurol , vol.166 , pp. 324-333
    • Gai, W.P.1    Yuan, H.X.2    Li, X.Q.3    Power, J.T.H.4    Blumbergs, P.C.5    Jensen, P.H.6
  • 158
    • 54849417407 scopus 로고    scopus 로고
    • Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing
    • van Rooijen, B.D.; Claessens, M.M.A.E.; Subramaniam, V. Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing. FEBS Lett., 2008, 582, 3788-3792.
    • (2008) FEBS Lett , vol.582 , pp. 3788-3792
    • van Rooijen, B.D.1    Claessens, M.M.A.E.2    Subramaniam, V.3
  • 159
    • 2542461043 scopus 로고    scopus 로고
    • Alpha-synuclein has a high affinity for packing defects in a bilayer membrane - A thermodynamics study
    • Nuscher, B.; Kamp, F.; Mehnert, T.; Odoy, S.; Haass, C.; Kahle, P.J.; Beyer, K. alpha-synuclein has a high affinity for packing defects in a bilayer membrane - A thermodynamics study. J. Biol. Chem., 2004, 279, 21966-21975.
    • (2004) J. Biol. Chem , vol.279 , pp. 21966-21975
    • Nuscher, B.1    Kamp, F.2    Mehnert, T.3    Odoy, S.4    Haass, C.5    Kahle, P.J.6    Beyer, K.7
  • 160
    • 0029125354 scopus 로고
    • Interaction of partially structured states of acidic fibroblast growth-factor with phospholipid-membranes
    • Mach, H.; Middaugh, C.R. Interaction of partially structured states of acidic fibroblast growth-factor with phospholipid-membranes. Biochemistry, 1995, 34, 9913-9920.
    • (1995) Biochemistry , vol.34 , pp. 9913-9920
    • Mach, H.1    Middaugh, C.R.2
  • 161
    • 20344374426 scopus 로고    scopus 로고
    • Conformational flexibility of alpha-lactalbumin related to its membrane binding capacity
    • Halskau, O.; Underhaug, J.; Frøystein, N.A.; Martínez, A. Conformational flexibility of alpha-lactalbumin related to its membrane binding capacity. J. Mol. Biol., 2005, 349, 1072-1086.
    • (2005) J. Mol. Biol , vol.349 , pp. 1072-1086
    • Halskau, O.1    Underhaug, J.2    Frøystein, N.A.3    Martínez, A.4
  • 162
    • 0035874472 scopus 로고    scopus 로고
    • Molten-globule structure and membrane binding of the N-terminal protease-resistant domain (63-193) of the steroidogenic acute regulatory protein (StAR)
    • Song, M.S.; Shao, H.Y.; Mujeeb, A.; James, M.L.; Miller, W.L. Molten-globule structure and membrane binding of the N-terminal protease-resistant domain (63-193) of the steroidogenic acute regulatory protein (StAR). Biochem. J., 2001, 356, 151-158.
    • (2001) Biochem. J , vol.356 , pp. 151-158
    • Song, M.S.1    Shao, H.Y.2    Mujeeb, A.3    James, M.L.4    Miller, W.L.5
  • 163
    • 38849179462 scopus 로고    scopus 로고
    • Formation of a high affinity lipid- binding intermediate during the early aggregation phase of alpha- synuclein
    • Smith, D.P.; Tew, D.J.; Hill, A.F.; Bottomley, S.P.; Masters, C.L.; Barnham, K.J.; Cappai, R. Formation of a high affinity lipid- binding intermediate during the early aggregation phase of alpha- synuclein. Biochemistry, 2008, 47, 1425-1434.
    • (2008) Biochemistry , vol.47 , pp. 1425-1434
    • Smith, D.P.1    Tew, D.J.2    Hill, A.F.3    Bottomley, S.P.4    Masters, C.L.5    Barnham, K.J.6    Cappai, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.