메뉴 건너뛰기




Volumn 10, Issue 5, 2009, Pages 483-499

Biophysics of Parkinson's disease: Structure and aggregation of α-synuclein

Author keywords

synuclein; Aggregation; Amyloid; Fibril; Intrinsically disordered protein; Neurodegeneration; NMR; Partially folded intermediate; Synucleinopathies

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; ANION; BAICALEIN; BETA SYNUCLEIN; GAMMA SYNUCLEIN; HEAVY METAL; HERBICIDE; LEPROSTATIC AGENT; ORGANIC SOLVENT; PESTICIDE; POLYANION; POLYCATION; RIFAMPICIN; SODIUM CHLORIDE;

EID: 70349503591     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920309789351921     Document Type: Review
Times cited : (282)

References (254)
  • 1
    • 0032936755 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Olanow, C.W.; Tatton, W.G. Etiology and pathogenesis of Parkinson's disease. Annu. Rev. Neurosci., 1999, 22, 123-144.
    • (1999) Annu. Rev. Neurosci , vol.22 , pp. 123-144
    • Olanow, C.W.1    Tatton, W.G.2
  • 2
    • 0028338865 scopus 로고
    • Prevalence of movement disorders in elderly community residents
    • Moghal, S.; Rajput, A.H.; D'Arcy, C.; Rajput, R. Prevalence of movement disorders in elderly community residents. Neuroepidemiology, 1994, 13, 175-178.
    • (1994) Neuroepidemiology , vol.13 , pp. 175-178
    • Moghal, S.1    Rajput, A.H.2    D'Arcy, C.3    Rajput, R.4
  • 3
    • 0038727936 scopus 로고    scopus 로고
    • Description of Parkinson's disease as a clinical syndrome
    • Fahn, S. Description of Parkinson's disease as a clinical syndrome. Ann. NY. Acad. Sci., 2003, 991, 1-44.
    • (2003) Ann. NY. Acad. Sci , vol.991 , pp. 1-44
    • Fahn, S.1
  • 4
    • 0037208691 scopus 로고    scopus 로고
    • Is the cause of Parkinson's disease environmental or hereditary? Evidence from twin studies
    • Tanner, C.M. Is the cause of Parkinson's disease environmental or hereditary? Evidence from twin studies. Adv. Neurol., 2003, 91, 133-142.
    • (2003) Adv. Neurol , vol.91 , pp. 133-142
    • Tanner, C.M.1
  • 5
    • 33645116252 scopus 로고    scopus 로고
    • Genetics of Parkinson disease: Paradigm shifts and future prospects
    • Farrer, M.J. Genetics of Parkinson disease: paradigm shifts and future prospects. Nat Rev. Genet., 2006, 7, 306-318.
    • (2006) Nat Rev. Genet , vol.7 , pp. 306-318
    • Farrer, M.J.1
  • 8
    • 70349534031 scopus 로고    scopus 로고
    • Lewy, F.H. In Paralysis Agitans. Pathologische Anatomie; Lewandowski M.; Ed.; Handbuch der Neurologie, Springer: Berlin, 1912, pp. 920-933.
    • Lewy, F.H. In Paralysis Agitans. Pathologische Anatomie; Lewandowski M.; Ed.; Handbuch der Neurologie, Springer: Berlin, 1912, pp. 920-933.
  • 9
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • Forno, L.S. Neuropathology of Parkinson's disease. J Neuropathol Exp. Neurol., 1996, 55, 259-272.
    • (1996) J Neuropathol Exp. Neurol , vol.55 , pp. 259-272
    • Forno, L.S.1
  • 10
    • 0000443658 scopus 로고
    • Diffuse intracytoplasmic ganglionic inclusions (Lewy type) associated with progressive dementia and quadriparesis in flexion
    • Okazaki, H.; Lipkin, L.E.; Aronson, S.M. Diffuse intracytoplasmic ganglionic inclusions (Lewy type) associated with progressive dementia and quadriparesis in flexion. J Neuropathol Exp Neurol, 1961, 20, 237-244.
    • (1961) J Neuropathol Exp Neurol , vol.20 , pp. 237-244
    • Okazaki, H.1    Lipkin, L.E.2    Aronson, S.M.3
  • 11
    • 0031762949 scopus 로고    scopus 로고
    • Fatal attractions: Abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia
    • Trojanowski, J.Q.; Goedert, M.; Iwatsubo, T.; Lee, V.M. Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia. Cell Death. Differ., 1998, 5, 832-837.
    • (1998) Cell Death. Differ , vol.5 , pp. 832-837
    • Trojanowski, J.Q.1    Goedert, M.2    Iwatsubo, T.3    Lee, V.M.4
  • 12
    • 0031907128 scopus 로고    scopus 로고
    • Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders
    • Takeda, A.; Mallory, M.; Sundsmo, M.; Honer, W.; Hansen, L.; Masliah, E. Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders. Am. J. Pathol., 1998, 152, 367-372.
    • (1998) Am. J. Pathol , vol.152 , pp. 367-372
    • Takeda, A.1    Mallory, M.2    Sundsmo, M.3    Honer, W.4    Hansen, L.5    Masliah, E.6
  • 13
    • 0034489853 scopus 로고    scopus 로고
    • Alpha-synuclein and Parkinson's disease
    • Lucking, C.B.; Brice, A. Alpha-synuclein and Parkinson's disease. Cell. Mol. Life. Sci., 2000, 57, 1894-1908.
    • (2000) Cell. Mol. Life. Sci , vol.57 , pp. 1894-1908
    • Lucking, C.B.1    Brice, A.2
  • 14
    • 0013785436 scopus 로고
    • Electron microscopic study of the developing neuroblast of the dorsal root ganglion of the rabbit embryo
    • Tennyson, V.M. Electron microscopic study of the developing neuroblast of the dorsal root ganglion of the rabbit embryo. J. Comp. Neurol., 1965, 124, 267-317.
    • (1965) J. Comp. Neurol , vol.124 , pp. 267-317
    • Tennyson, V.M.1
  • 19
    • 0242300619 scopus 로고    scopus 로고
    • Singleton, A.B.; Farrer, M.; Johnson, J.; Singleton, A.; Hague, S.; Kachergus, J.; Hulihan, M.; Peuralinna, T.; Dutra, A.; Nussbaum, R.; Lincoln, S.; Crawley, A.; Hanson, M.; Maraganore, D.; Adler, C.; Cookson, M.R.; Muenter, M.; Baptista, M.; Miller, D.; Blancato, J.; Hardy, J.; Gwinn-Hardy, K. alpha-Synuclein locus triplication causes Parkinson's disease. Science, 2003, 302, 841.
    • Singleton, A.B.; Farrer, M.; Johnson, J.; Singleton, A.; Hague, S.; Kachergus, J.; Hulihan, M.; Peuralinna, T.; Dutra, A.; Nussbaum, R.; Lincoln, S.; Crawley, A.; Hanson, M.; Maraganore, D.; Adler, C.; Cookson, M.R.; Muenter, M.; Baptista, M.; Miller, D.; Blancato, J.; Hardy, J.; Gwinn-Hardy, K. alpha-Synuclein locus triplication causes Parkinson's disease. Science, 2003, 302, 841.
  • 22
    • 0032568534 scopus 로고    scopus 로고
    • Spillantini, M.G.; Crowther, R.A.; Jakes, R.; Hasegawa, M.; Goedert, M. alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. USA, 1998, 95, 6469-6473.
    • Spillantini, M.G.; Crowther, R.A.; Jakes, R.; Hasegawa, M.; Goedert, M. alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. USA, 1998, 95, 6469-6473.
  • 23
    • 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.; Takeda, A.; Sagara, Y.; Sisk, A.; Mucke, L. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science, 2000, 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    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 24
    • 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
  • 25
    • 0038727850 scopus 로고    scopus 로고
    • Parkinson's disease and related alpha-synuclemopathies are brain amyloidoses
    • Trojanowski, J.Q.; Lee, V.M. Parkinson's disease and related alpha-synuclemopathies are brain amyloidoses. Ann. NY Acad. Sci., 2003, 991, 107-110.
    • (2003) Ann. NY Acad. Sci , vol.991 , pp. 107-110
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 26
    • 84940364788 scopus 로고    scopus 로고
    • Alpha-synuclein and the Lewy body disorders
    • Dickson, D.W. Alpha-synuclein and the Lewy body disorders. Curr. Opin Neurol, 2001, 14, 423-432.
    • (2001) Curr. Opin Neurol , vol.14 , pp. 423-432
    • Dickson, D.W.1
  • 27
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert, M. Alpha-synuclein and neurodegenerative diseases. Nat. Rev Neurosci, 2001, 2, 492-501.
    • (2001) Nat. Rev Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 28
    • 0035031135 scopus 로고    scopus 로고
    • Parkinson's disease and other alpha-synucleinopathies
    • Goedert, M. Parkinson's disease and other alpha-synucleinopathies. Clin. Chem. Lab. Med., 2001, 39, 308-312.
    • (2001) Clin. Chem. Lab. Med , vol.39 , pp. 308-312
    • Goedert, M.1
  • 29
    • 0038460184 scopus 로고    scopus 로고
    • Part II: Alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease
    • Dev, K.K.; Hofele, K.; Barbieri, S.; Buchman, V.L.; van der Putten, H. Part II: alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease. Neuropharmacology, 2003, 45, 14-44.
    • (2003) Neuropharmacology , vol.45 , pp. 14-44
    • Dev, K.K.1    Hofele, K.2    Barbieri, S.3    Buchman, V.L.4    van der Putten, H.5
  • 30
    • 0037014618 scopus 로고    scopus 로고
    • Amino acid determinants of alpha-synuclein aggregation: Putting together pieces of the puzzle
    • Uversky, V.N.; Fink, A.L. Amino acid determinants of alpha-synuclein aggregation: putting together pieces of the puzzle. FEBS Lett., 2002, 522, 9-13.
    • (2002) FEBS Lett , vol.522 , pp. 9-13
    • Uversky, V.N.1    Fink, A.L.2
  • 31
    • 55949092886 scopus 로고    scopus 로고
    • Alpha-synuclein misfolding and neurodegenerative diseases
    • Uversky, V.N. Alpha-synuclein misfolding and neurodegenerative diseases. Curr. Protein Pept. Sci., 2008, 9, 507-540.
    • (2008) Curr. Protein Pept. Sci , vol.9 , pp. 507-540
    • Uversky, V.N.1
  • 32
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation
    • Uversky, V.N. Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation. J. Neurochem., 2007, 103, 17-37.
    • (2007) J. Neurochem , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 33
    • 0033614777 scopus 로고    scopus 로고
    • Filamentous nerve cell inclusions in neurodegenerative diseases: Tauopathies and alpha-synupleinopathies
    • Goedert, M. Filamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synupleinopathies. Philos. Trans. R Soc. Land B Biol. Sci., 1999, 354, 1101-1118.
    • (1999) Philos. Trans. R Soc. Land B Biol. Sci , vol.354 , pp. 1101-1118
    • Goedert, M.1
  • 34
    • 0034531475 scopus 로고    scopus 로고
    • The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy
    • Spillantini, M.G.; Goedert, M. The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Ann. NY Acad. Sci., 2000, 920, 16-27.
    • (2000) Ann. NY Acad. Sci , vol.920 , pp. 16-27
    • Spillantini, M.G.1    Goedert, M.2
  • 35
    • 0035109738 scopus 로고    scopus 로고
    • Synuclemopathics: Clinical and pathological implications
    • Galvin, J.E.; Lee, V.M.; Trojanowski, J.Q. Synuclemopathics: clinical and pathological implications. Arch. Neurol., 2001, 58, 186-190.
    • (2001) Arch. Neurol , vol.58 , pp. 186-190
    • Galvin, J.E.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 36
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies
    • Spillantini, M.G.; Crowther, R.A.; Jakes, R.; Cairns, NJ.; Lantos, P.L.; Goedert, M. Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neurosci. Lett., 1998, 251, 205-208.
    • (1998) Neurosci. Lett , vol.251 , pp. 205-208
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Cairns, N.J.4    Lantos, P.L.5    Goedert, M.6
  • 37
    • 0032546895 scopus 로고    scopus 로고
    • Alpha-synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy
    • Wakabayashi, K.; Yoshimoto, M.; Tsuji, S.; Takahashi, H. Alpha-synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy. Neurosci. Lett., 1998, 249, 180-182.
    • (1998) Neurosci. Lett , vol.249 , pp. 180-182
    • Wakabayashi, K.1    Yoshimoto, M.2    Tsuji, S.3    Takahashi, H.4
  • 38
    • 0032529707 scopus 로고    scopus 로고
    • Multiple-system atrophy: A new alpha-synuclein disease?
    • Gai, W.P.; Power, J.H.; Blumbergs, P.C.; Blessing, W.W. Multiple-system atrophy: a new alpha-synuclein disease? Lancet, 1998, 352, 547-548.
    • (1998) Lancet , vol.352 , pp. 547-548
    • Gai, W.P.1    Power, J.H.2    Blumbergs, P.C.3    Blessing, W.W.4
  • 39
    • 0031721278 scopus 로고    scopus 로고
    • Lewy body in neurodegeneration with brain iron accumulation type 1 is immunoreactive for alpha-synuclein
    • Arawaka, S.; Saito, Y.; Murayama, S.; Mori, H. Lewy body in neurodegeneration with brain iron accumulation type 1 is immunoreactive for alpha-synuclein. Neurology, 1998, 51, 887-889.
    • (1998) Neurology , vol.51 , pp. 887-889
    • Arawaka, S.1    Saito, Y.2    Murayama, S.3    Mori, H.4
  • 40
    • 0031566042 scopus 로고    scopus 로고
    • Wakabayashi, K.; Matsumoto, K.; Takayama, K.; Yoshimoto, M.; Takahashi, H. NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease. Neurosci. Lett., 1997, 239, 45-48.
    • Wakabayashi, K.; Matsumoto, K.; Takayama, K.; Yoshimoto, M.; Takahashi, H. NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease. Neurosci. Lett., 1997, 239, 45-48.
  • 42
    • 0018145267 scopus 로고
    • Lewy bodies in cerebral cortex, report of three cases
    • Kosaka, K. Lewy bodies in cerebral cortex, report of three cases. Acta Neuropathol. (Berl.), 1978, 42, 127-134.
    • (1978) Acta Neuropathol. (Berl.) , vol.42 , pp. 127-134
    • Kosaka, K.1
  • 43
    • 0021636665 scopus 로고
    • Diffuse type of Lewy body disease: Progressive dementia with abundant cortical Lewy bodies and senile changes of varying degree - a new disease?
    • Kosaka, K.; Yoshimura, M.; Ikeda, K.; Budka, H. Diffuse type of Lewy body disease: progressive dementia with abundant cortical Lewy bodies and senile changes of varying degree - a new disease? Clin. Neuropathol., 1984, 3, 185-192.
    • (1984) Clin. Neuropathol , vol.3 , pp. 185-192
    • Kosaka, K.1    Yoshimura, M.2    Ikeda, K.3    Budka, H.4
  • 45
    • 33644824239 scopus 로고    scopus 로고
    • Interface between tauopathies and synucleinopathies: A tale of two proteins
    • Galpern, W.R.; Lang, A.E. Interface between tauopathies and synucleinopathies: a tale of two proteins. Ann. Neurol., 2006, 59, 449-458.
    • (2006) Ann. Neurol , vol.59 , pp. 449-458
    • Galpern, W.R.1    Lang, A.E.2
  • 46
    • 0026751822 scopus 로고
    • A population-based investigation of Parkinson's disease with and without dementia. Relationship to age and gender
    • Mayeux, R.; Denaro, J.; Hemenegildo, N.; Marder, K.; Tang, M.X.; Cote, L.J.; Stern, Y. A population-based investigation of Parkinson's disease with and without dementia. Relationship to age and gender. Arch. Neurol., 1992, 49, 492-497.
    • (1992) Arch. Neurol , vol.49 , pp. 492-497
    • Mayeux, R.1    Denaro, J.2    Hemenegildo, N.3    Marder, K.4    Tang, M.X.5    Cote, L.J.6    Stern, Y.7
  • 48
    • 33144489150 scopus 로고    scopus 로고
    • McKeith, I.G.; Dickson, D.W.; Lowe, J.; Emre, M.; O'Brien, J.T.; Feldman, H.; Cummings, J.; Duda, J.E.; Lippa, C.; Perry, E.K.; Aarsland, D.; Arai, H.; Ballard, C.G.; Boeve, B.; Bum, D.J.; Costa, D.; Del Ser, T.; Dubois, B.; Galasko, D.; Gauthier, S.; Goetz, C.G.; Gomez-Tortosa, E.; Halliday, G.; Hansen, L.A.; Hardy, J.; Iwatsubo, T.; Kalaria, R.N.; Kaufer, D.; Kenny, R.A.; Korczyn, A.; Kosaka, K.; Lee, V.M.; Lees, A.; Litvan, I.; Londos, E.; Lopez, O.L.; Minoshima, S.; Mizuno, Y.; Molina, J.A.; Mukaetova-Ladinska, E.B.; Pasquier, F.; Perry, R.H.; Schutz, J.B.; Trojanowski, J.Q.; Yamada, M. Diagnosis and management of dementia with Lewy bodies: third report of the DLB Consortium. Neurology, 2005, 65, 1863-1872.
    • McKeith, I.G.; Dickson, D.W.; Lowe, J.; Emre, M.; O'Brien, J.T.; Feldman, H.; Cummings, J.; Duda, J.E.; Lippa, C.; Perry, E.K.; Aarsland, D.; Arai, H.; Ballard, C.G.; Boeve, B.; Bum, D.J.; Costa, D.; Del Ser, T.; Dubois, B.; Galasko, D.; Gauthier, S.; Goetz, C.G.; Gomez-Tortosa, E.; Halliday, G.; Hansen, L.A.; Hardy, J.; Iwatsubo, T.; Kalaria, R.N.; Kaufer, D.; Kenny, R.A.; Korczyn, A.; Kosaka, K.; Lee, V.M.; Lees, A.; Litvan, I.; Londos, E.; Lopez, O.L.; Minoshima, S.; Mizuno, Y.; Molina, J.A.; Mukaetova-Ladinska, E.B.; Pasquier, F.; Perry, R.H.; Schutz, J.B.; Trojanowski, J.Q.; Yamada, M. Diagnosis and management of dementia with Lewy bodies: third report of the DLB Consortium. Neurology, 2005, 65, 1863-1872.
  • 49
    • 0006164301 scopus 로고    scopus 로고
    • McKeith, I.G.; Galasko, D.; Kosaka, K.; Perry, E.K.; Dickson, D.W.; Hansen, L.A.; Salmon, D.P.; Lowe, J.; Mirra, S.S.; Byme, E.J.; Lennox, G.; Quinn, N.P.; Edwardson, J.A.; Ince, P.G.; Bergeron, C.; Burns, A.; Miller, B.L.; Lovestone, S.; Collerton, D.; Jansen, E.N.; Ballard, C.; de Vos, R.A.; Wilcock, G.K.; Jellinger, K.A.; Perry, R.H. Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop. Neurology, 1996, 47, 1113-1124.
    • McKeith, I.G.; Galasko, D.; Kosaka, K.; Perry, E.K.; Dickson, D.W.; Hansen, L.A.; Salmon, D.P.; Lowe, J.; Mirra, S.S.; Byme, E.J.; Lennox, G.; Quinn, N.P.; Edwardson, J.A.; Ince, P.G.; Bergeron, C.; Burns, A.; Miller, B.L.; Lovestone, S.; Collerton, D.; Jansen, E.N.; Ballard, C.; de Vos, R.A.; Wilcock, G.K.; Jellinger, K.A.; Perry, R.H. Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop. Neurology, 1996, 47, 1113-1124.
  • 51
    • 4043145659 scopus 로고    scopus 로고
    • Dementia in Parkinson's disease: Cause and treatment
    • Emre, M, Dementia in Parkinson's disease: cause and treatment. Curr. Opin. Neurol., 2004, 17, 399-404.
    • (2004) Curr. Opin. Neurol , vol.17 , pp. 399-404
    • Emre, M.1
  • 52
    • 0014491086 scopus 로고
    • Amyotrophic lateral sclerosis-Parkinsonism dementia complex of Guam: Further genetic investigations
    • Plato, C.C.; Cruz, M.T.; Kurland, L.T. Amyotrophic lateral sclerosis-Parkinsonism dementia complex of Guam: further genetic investigations. Am. J. Hum. Genet., 1969, 21, 133-141.
    • (1969) Am. J. Hum. Genet , vol.21 , pp. 133-141
    • Plato, C.C.1    Cruz, M.T.2    Kurland, L.T.3
  • 53
    • 0021676340 scopus 로고
    • Familial occurrence of amyotrophic lateral sclerosis, parkinsonism, and dementia
    • Schmitt, H.P.; Emser, W.; Heimes, C. Familial occurrence of amyotrophic lateral sclerosis, parkinsonism, and dementia. Ann. Neurol., 1984, 16, 642-648.
    • (1984) Ann. Neurol , vol.16 , pp. 642-648
    • Schmitt, H.P.1    Emser, W.2    Heimes, C.3
  • 54
    • 0023181410 scopus 로고
    • Guam amyotropbic lateral sclerosis-parkinsonism-dementia linked to a plant excitant neurotoxin
    • Spencer, P.S.; Nunn, P.B.; Hugon, J.; Ludolph, A.C.; Ross, S.M.; Roy, D.N.; Robertson, R.C. Guam amyotropbic lateral sclerosis-parkinsonism-dementia linked to a plant excitant neurotoxin. Science, 1987, 237, 517-522.
    • (1987) Science , vol.237 , pp. 517-522
    • Spencer, P.S.1    Nunn, P.B.2    Hugon, J.3    Ludolph, A.C.4    Ross, S.M.5    Roy, D.N.6    Robertson, R.C.7
  • 55
    • 0027236685 scopus 로고
    • Guam: Deadly disease dying out
    • Stone, R. Guam: deadly disease dying out. Science, 1993, 261, 424-426.
    • (1993) Science , vol.261 , pp. 424-426
    • Stone, R.1
  • 56
    • 44949193040 scopus 로고    scopus 로고
    • The ALS/PDC syndrome of Guam and the cycad hypothesis
    • Steele, J.C,; McGeer, P.L. The ALS/PDC syndrome of Guam and the cycad hypothesis. Neurology, 2008, 70, 1984-1990.
    • (2008) Neurology , vol.70 , pp. 1984-1990
    • Steele, J.C.1    McGeer, P.L.2
  • 57
    • 0028046648 scopus 로고
    • Familial aggregation of amyotrophic lateral sclerosis, dementia, and Parkinson's disease: Evidence of shared genetic susceptibility
    • Majoor-Krakauer, D.; Ottman, R.; Johnson, W.G.; Rowland, L.P. Familial aggregation of amyotrophic lateral sclerosis, dementia, and Parkinson's disease: evidence of shared genetic susceptibility. Neurology, 1994, 44, 1872-1877.
    • (1994) Neurology , vol.44 , pp. 1872-1877
    • Majoor-Krakauer, D.1    Ottman, R.2    Johnson, W.G.3    Rowland, L.P.4
  • 58
    • 2942656929 scopus 로고    scopus 로고
    • Occurrence of alpha-synuclein pathology in the cerebellum of Guamanian patients with parkinsonism-dementia complex
    • Sebeo, J.; Hof, P.R.; Perl, D.P. Occurrence of alpha-synuclein pathology in the cerebellum of Guamanian patients with parkinsonism-dementia complex. Acta Neuropathol., 2004, 107, 497-503.
    • (2004) Acta Neuropathol , vol.107 , pp. 497-503
    • Sebeo, J.1    Hof, P.R.2    Perl, D.P.3
  • 59
    • 57849084804 scopus 로고
    • The distribution of Lewy bodies in the central and autonomic nervous systems in idiopathic paralysis agitans
    • den Hartog Jager, W.A.; Bethlem, J. The distribution of Lewy bodies in the central and autonomic nervous systems in idiopathic paralysis agitans. J. Neurol. Neurosurg. Psychiatry, 1960, 23, 283-290.
    • (1960) J. Neurol. Neurosurg. Psychiatry , vol.23 , pp. 283-290
    • den Hartog Jager, W.A.1    Bethlem, J.2
  • 60
    • 0018383734 scopus 로고
    • Dementia-Parkinsonism syndrome with numerous Lewy bodies and senile plaques in cerebral cortex
    • Kosaka, K.; Mehraein, P. Dementia-Parkinsonism syndrome with numerous Lewy bodies and senile plaques in cerebral cortex. Arch. Psychiatr. Nervenkr., 1979, 226, 241-250.
    • (1979) Arch. Psychiatr. Nervenkr , vol.226 , pp. 241-250
    • Kosaka, K.1    Mehraein, P.2
  • 61
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
    • McKhann, G.; Drachman, D.; Folstein, M.; Katzman, R.; Price, D.; Stadlan, E.M. Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease. Neurology, 1984, 34, 939-944.
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 62
    • 70349556921 scopus 로고    scopus 로고
    • Clark, C.M.; Ewbank, D.; Lee, V.M.-Y.; Trojanowski, J.Q. In: Molecular Pathology of Alzheimer's Disease: Neuronal Cytoskeletal Abnormalities, Growdon, J.H.; Rossor, M.N. (Eds.), The Dementias. 19 of Blue Books of Practical Neurology, Butterworth-Heinemann: Boston, 1998, pp. 285-304.
    • Clark, C.M.; Ewbank, D.; Lee, V.M.-Y.; Trojanowski, J.Q. In: Molecular Pathology of Alzheimer's Disease: Neuronal Cytoskeletal Abnormalities, Growdon, J.H.; Rossor, M.N. (Eds.), The Dementias. Vol. 19 of Blue Books of Practical Neurology, Butterworth-Heinemann: Boston, 1998, pp. 285-304.
  • 63
    • 0035847186 scopus 로고    scopus 로고
    • Alpha-synuclein-positive structures in cases with sporadic Alzheimer's disease: Morphology and its relationship to tau aggregation
    • Arai, Y.; Yamazaki, M.; Mori, O.; Muramatsu, H.; Asano, G.; Katayama, Y. Alpha-synuclein-positive structures in cases with sporadic Alzheimer's disease: morphology and its relationship to tau aggregation. Brain Res., 2001, 888, 287-296.
    • (2001) Brain Res , vol.888 , pp. 287-296
    • Arai, Y.1    Yamazaki, M.2    Mori, O.3    Muramatsu, H.4    Asano, G.5    Katayama, Y.6
  • 64
    • 0032990543 scopus 로고    scopus 로고
    • Antibodies to alpha-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease
    • Lippa, C.F.; Schmidt, M.L.; Lee, V.M.; Trojanowski, J.Q. Antibodies to alpha-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease. Ann. Neurol., 1999, 45, 353-357.
    • (1999) Ann. Neurol , vol.45 , pp. 353-357
    • Lippa, C.F.1    Schmidt, M.L.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 65
    • 0034653871 scopus 로고    scopus 로고
    • Occurrence of human alpha-synuclein immunoreactive neurons with neurofibrillary tangle formation in the limbic areas of patients with Alzheimer's disease
    • Marui, W.; Iseki, E.; Ueda, K.; Kosaka, K. Occurrence of human alpha-synuclein immunoreactive neurons with neurofibrillary tangle formation in the limbic areas of patients with Alzheimer's disease. J. Neurol. Sci., 2000, 174, 81-84.
    • (2000) J. Neurol. Sci , vol.174 , pp. 81-84
    • Marui, W.1    Iseki, E.2    Ueda, K.3    Kosaka, K.4
  • 66
    • 0002949303 scopus 로고    scopus 로고
    • The Neuropathology and Neurochemistry of Multiple System Atrophy
    • Mathias, C.J, Bannister, R, Eds, Oxford University Press: Oxford
    • Daniel, S. In: The Neuropathology and Neurochemistry of Multiple System Atrophy, Mathias, C.J.; Bannister, R.; Eds.; Autonomic Failure, Oxford University Press: Oxford, 1999, pp. 321-328.
    • (1999) Autonomic Failure , pp. 321-328
    • Daniel, S.1
  • 67
    • 0024843373 scopus 로고
    • Glial cytoplasmic inclusions in the CNS of patients with multiple system atrophy (striatonigral degeneration, olivopontocerebellar atrophy and Shy-Drager syndrome)
    • Papp, M.I.; Kahn, J.E.; Lantos, P.L. Glial cytoplasmic inclusions in the CNS of patients with multiple system atrophy (striatonigral degeneration, olivopontocerebellar atrophy and Shy-Drager syndrome). J. Neurol. Sci., 1989, 94, 79-100.
    • (1989) J. Neurol. Sci , vol.94 , pp. 79-100
    • Papp, M.I.1    Kahn, J.E.2    Lantos, P.L.3
  • 68
    • 33746108503 scopus 로고    scopus 로고
    • Cellular pathology in multiple system atrophy
    • Wakabayashi, K.; Takahashi, H. Cellular pathology in multiple system atrophy. Neuropathology, 2006, 26, 338-345.
    • (2006) Neuropathology , vol.26 , pp. 338-345
    • Wakabayashi, K.1    Takahashi, H.2
  • 71
    • 0027156622 scopus 로고
    • Neuroaxonal dystrophy combined with diffuse Lewy body disease in a young adult
    • Sugiyama, H.; Hainfellner, J.A.; Schmid-Siegel, B.; Budka, H. Neuroaxonal dystrophy combined with diffuse Lewy body disease in a young adult. Clin. Neuropathol., 1993, 12, 147-152.
    • (1993) Clin. Neuropathol , vol.12 , pp. 147-152
    • Sugiyama, H.1    Hainfellner, J.A.2    Schmid-Siegel, B.3    Budka, H.4
  • 72
    • 0026317374 scopus 로고
    • Hallervorden-Spatz syndrome and brain iron metabolism
    • Swaiman, K.F. Hallervorden-Spatz syndrome and brain iron metabolism. Arch. Neurol., 1991, 48, 1285-1293.
    • (1991) Arch. Neurol , vol.48 , pp. 1285-1293
    • Swaiman, K.F.1
  • 75
  • 76
    • 0032719237 scopus 로고    scopus 로고
    • Widespread occurrence of alpha-synuclein/ NACP-immunoreactive neuronal inclusions in juvenile and adult-onset Hallervorden-Spatz disease with Lewy bodies
    • Wakabayashi, K.; Yoshimoto, M.; Fukushima, T.; Koide, R.; Horikawa, Y.; Morita, T.; Takahashi, H. Widespread occurrence of alpha-synuclein/ NACP-immunoreactive neuronal inclusions in juvenile and adult-onset Hallervorden-Spatz disease with Lewy bodies. Neuropathol. Appl. Neurobiol., 1999, 25, 363-368.
    • (1999) Neuropathol. Appl. Neurobiol , vol.25 , pp. 363-368
    • Wakabayashi, K.1    Yoshimoto, M.2    Fukushima, T.3    Koide, R.4    Horikawa, Y.5    Morita, T.6    Takahashi, H.7
  • 77
    • 0033897735 scopus 로고    scopus 로고
    • Neurodegeneration with brain iron accumulation, type 1 is characterized by alpha-, beta-, and gamma-synuclein neuropathology
    • Galvin, J.E.; Giasson, B.; Hurtig, H.I.; Lee, V.M.; Trojanowski, J.Q. Neurodegeneration with brain iron accumulation, type 1 is characterized by alpha-, beta-, and gamma-synuclein neuropathology. Am. J. Pathol., 2000, 157, 361-368.
    • (2000) Am. J. Pathol , vol.157 , pp. 361-368
    • Galvin, J.E.1    Giasson, B.2    Hurtig, H.I.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 78
    • 0033817296 scopus 로고    scopus 로고
    • Alpha-synuclein accumulation in a case of neurodegeneration with brain iron accumulation type 1 (NBIA-1, formerly Hallervorden-Spatz syndrome) with widespread cortical and brainstem-type Lewy bodies
    • Neumann, M.; Adler, S.; Schluter, O.; Kremmer, E.; Benecke, R.; Kretzschmar, H.A. Alpha-synuclein accumulation in a case of neurodegeneration with brain iron accumulation type 1 (NBIA-1, formerly Hallervorden-Spatz syndrome) with widespread cortical and brainstem-type Lewy bodies. Acta Neuropathol. (Berl.), 2000, 100, 568-574.
    • (2000) Acta Neuropathol. (Berl.) , vol.100 , pp. 568-574
    • Neumann, M.1    Adler, S.2    Schluter, O.3    Kremmer, E.4    Benecke, R.5    Kretzschmar, H.A.6
  • 79
    • 0028985267 scopus 로고
    • The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai, A.; Masliah, E.; Yoshimoto, M.; Ge, N.; Flanagan, L.; de Silva, H.A.; 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.4    Flanagan, L.5    de Silva, H.A.6    Kittel, A.7    Saitoh, T.8
  • 80
    • 0035500991 scopus 로고    scopus 로고
    • Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells
    • Payton, J.E.; Perrin, R.J.; Clayton, D.F.; George, J.M. Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells. Brain Res. Mol. Brain Res., 2001, 95, 138-145.
    • (2001) Brain Res. Mol. Brain Res , vol.95 , pp. 138-145
    • Payton, J.E.1    Perrin, R.J.2    Clayton, D.F.3    George, J.M.4
  • 83
    • 0034604583 scopus 로고    scopus 로고
    • Wild-type but not Parkinson's disease-related ala-53 → Thr mutant alpha -synuclein protects neuronal cells from apoptotic stimuli
    • da Costa, C.A.; Ancolio, K.; Checler, F. Wild-type but not Parkinson's disease-related ala-53 → Thr mutant alpha -synuclein protects neuronal cells from apoptotic stimuli. J. Biol. Chem., 2000, 275, 24065-24069.
    • (2000) J. Biol. Chem , vol.275 , pp. 24065-24069
    • da Costa, C.A.1    Ancolio, K.2    Checler, F.3
  • 84
    • 0029904487 scopus 로고    scopus 로고
    • 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.
    • 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.
  • 85
    • 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
  • 86
    • 0037023699 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of alpha-synuclein assembly by beta- and gamma-synucleins
    • Uversky, V.N.; Li, J.; Souillac, P.; Millett, I.S.; Doniach, S.; Jakes, R.; Goedert, M.; Fink, A.L. Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins. J. Biol. Chem., 2002, 277, 11970-11978.
    • (2002) J. Biol. Chem , vol.277 , pp. 11970-11978
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Millett, I.S.4    Doniach, S.5    Jakes, R.6    Goedert, M.7    Fink, A.L.8
  • 87
    • 0034773940 scopus 로고    scopus 로고
    • Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c
    • Morar, A.S.; Olteanu, A.; Young, G.B.; Pielak, G.J. Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c. Protein Sci., 2001, 10, 2195-2199.
    • (2001) Protein Sci , vol.10 , pp. 2195-2199
    • Morar, A.S.1    Olteanu, A.2    Young, G.B.3    Pielak, G.J.4
  • 88
    • 0027955639 scopus 로고    scopus 로고
    • Lattman, E.E. Small angle X-ray scattering studies of protein folding. Curr. Opin. Struct. Biol., 1994, 4, 87-92.
    • Lattman, E.E. Small angle X-ray scattering studies of protein folding. Curr. Opin. Struct. Biol., 1994, 4, 87-92.
  • 89
    • 0030324821 scopus 로고    scopus 로고
    • X-ray solution scattering studies of protein folding
    • Kataoka, M.; Goto, Y. X-ray solution scattering studies of protein folding. Fold. Des., 1996, 1, R107-114.
    • (1996) Fold. Des , vol.1
    • Kataoka, M.1    Goto, Y.2
  • 90
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by small angle X-ray scattering
    • Kataoka, M.; Hagihara, Y.; Mihara, K.; Goto, Y. Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol., 1993, 229, 591-596.
    • (1993) J. Mol. Biol , vol.229 , pp. 591-596
    • Kataoka, M.1    Hagihara, Y.2    Mihara, K.3    Goto, Y.4
  • 91
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka, M.; Nishii, I.; Fujisawa, T.; Ueki, T.; Tokunaga, F.; Goto, Y. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol., 1995, 249, 215-228.
    • (1995) J. Mol. Biol , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 93
    • 0031050429 scopus 로고    scopus 로고
    • Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering
    • Kataoka, M.; Kuwajima, K.; Tokunaga, F.; Goto, Y. Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering. Protein Sci., 1997, 6, 422-430.
    • (1997) Protein Sci , vol.6 , pp. 422-430
    • Kataoka, M.1    Kuwajima, K.2    Tokunaga, F.3    Goto, Y.4
  • 94
    • 0032525256 scopus 로고    scopus 로고
    • Anion-induced folding of Staphylococcal nuclease: Characterization of multiple equilibrium partially folded intermediates
    • Uversky, V.N.; Karnoup, A.S.; Segel, D.J.; Seshadri, S.; Doniach, S.; Fink, A.L. Anion-induced folding of Staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates. J. Mol. Biol., 1998, 278, 879-894.
    • (1998) J. Mol. Biol , vol.278 , pp. 879-894
    • Uversky, V.N.1    Karnoup, A.S.2    Segel, D.J.3    Seshadri, S.4    Doniach, S.5    Fink, A.L.6
  • 95
    • 0031779708 scopus 로고    scopus 로고
    • Chain-like conformation of heat-denatured ribonuclease A and cytochrome c as evidenced by solution X-ray scattering
    • Hagihara, Y.; Hoshino, M.; Hamada, D.; Kataoka, M.; Goto, Y. Chain-like conformation of heat-denatured ribonuclease A and cytochrome c as evidenced by solution X-ray scattering. Fold. Des., 1998, 3, 195-201.
    • (1998) Fold. Des , vol.3 , pp. 195-201
    • Hagihara, Y.1    Hoshino, M.2    Hamada, D.3    Kataoka, M.4    Goto, Y.5
  • 98
    • 0035354585 scopus 로고    scopus 로고
    • Changes in biomolecular conformation seen by small angle X-ray scattering
    • Doniach, S. Changes in biomolecular conformation seen by small angle X-ray scattering. Chem. Rev., 2001, 101, 1763-1778.
    • (2001) Chem. Rev , vol.101 , pp. 1763-1778
    • Doniach, S.1
  • 99
    • 0035824545 scopus 로고    scopus 로고
    • Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein
    • Bussell, R.Jr.; Eliezer, D. Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein. J. Biol. Chem., 2001, 276, 45996-46003.
    • (2001) J. Biol. Chem , vol.276 , pp. 45996-46003
    • Bussell Jr, R.1    Eliezer, D.2
  • 100
    • 12944304172 scopus 로고    scopus 로고
    • Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations
    • Dedmon, M.M.; Lindorff-Larsen, K.; Christodoulou, J.; Vendruscolo, M.; Dobson, C.M. Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. J. Am. Chem. Soc., 2005, 127, 476-477.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 476-477
    • Dedmon, M.M.1    Lindorff-Larsen, K.2    Christodoulou, J.3    Vendruscolo, M.4    Dobson, C.M.5
  • 102
    • 34548184125 scopus 로고    scopus 로고
    • Residual structure, backbone dynamics, and interactions within the symiclein family
    • Sung, Y.H.; Eliezer, D. Residual structure, backbone dynamics, and interactions within the symiclein family. J Mol. Biol., 2007, 372, 689-707.
    • (2007) J Mol. Biol , vol.372 , pp. 689-707
    • Sung, Y.H.1    Eliezer, D.2
  • 103
    • 0034669882 scopus 로고    scopus 로고
    • Uversky, V.N.; Gillespie, J.R.; Fink, A.L. Why are natively unfolded proteins unstructured under physiologic conditions? Proteins, 2000, 41, 415-427.
    • Uversky, V.N.; Gillespie, J.R.; Fink, A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins, 2000, 41, 415-427.
  • 104
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci., 2002, 11, 739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 105
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky, V.N. What does it mean to be natively unfolded? Eur. J. Biochem., 2002, 269, 2-12.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 106
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited: A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go?
    • Uversky, V.N. Protein folding revisited: a polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go? Cell. Mol. Life Sci., 2003, 60, 1852-1871.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 107
    • 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
  • 108
    • 0036777533 scopus 로고    scopus 로고
    • Conformational behavior of human alpha-symiclein is modulated by familial Parkinson's disease point mutations A30P and A53T
    • Li, J.; Uversky, V.N.; Fink, A.L. Conformational behavior of human alpha-symiclein is modulated by familial Parkinson's disease point mutations A30P and A53T. Neurotoxicology, 2002, 23, 553-567.
    • (2002) Neurotoxicology , vol.23 , pp. 553-567
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 109
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway, K.A.; Harper, J.D.; Lansbury, P.T. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med., 1998, 4, 1318-1320.
    • (1998) Nat. Med , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 110
    • 0032573289 scopus 로고    scopus 로고
    • Effects of the mutations Ala3O to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease
    • El-Agnaf, O.M.; Jakes, R.; Curran, M.D.; Wallace, A. Effects of the mutations Ala3O to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease. FEBS Lett., 1998, 440, 67-70.
    • (1998) FEBS Lett , vol.440 , pp. 67-70
    • El-Agnaf, O.M.1    Jakes, R.2    Curran, M.D.3    Wallace, A.4
  • 112
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type, human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson, B.I.; Uryu, K.; Trojanowski, J.Q.; Lee, V.M. Mutant and wild type, human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem., 1999, 274, 7619-7622.
    • (1999) J. Biol. Chem , vol.274 , pp. 7619-7622
    • Giasson, B.I.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 113
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway, K.A.; Harper, J.D.; Lansbury, P.T.; Jr. Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry, 2000, 39, 2552-2563.
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury Jr., P.T.3
  • 115
    • 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
  • 116
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein
    • Li, J.; Uversky, V.N.; Fink, A.L. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry, 2001, 40, 11604-11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 119
    • 24744461907 scopus 로고    scopus 로고
    • Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation
    • Bertoncini, C.W.; Fernandez, C.O.; Griesinger, C.; Jovin, T.M.; Zweckstetter, M. Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation. J. Biol. Chem., 2005, 280, 30649-30652.
    • (2005) J. Biol. Chem , vol.280 , pp. 30649-30652
    • Bertoncini, C.W.1    Fernandez, C.O.2    Griesinger, C.3    Jovin, T.M.4    Zweckstetter, M.5
  • 120
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-Synucleih 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-Synucleih 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
  • 121
    • 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
  • 122
    • 0038054286 scopus 로고    scopus 로고
    • A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins
    • Bussell, R.; Jr.; Eliezer, D. A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins. J. Mol. Biol., 2003, 329, 763-778.
    • (2003) J. Mol. Biol , vol.329 , pp. 763-778
    • Bussell Jr., R.1    Eliezer, D.2
  • 123
    • 0038341134 scopus 로고    scopus 로고
    • A broken alpha -helix in folded alpha -Synuclein
    • Chandra, S.; Chen, X.; Rizo, J.; Jahn, R.; Sudhof, T.C. A broken alpha -helix in folded alpha -Synuclein. J. Biol. Chem., 2003, 278, 15313-15318.
    • (2003) J. Biol. Chem , vol.278 , pp. 15313-15318
    • Chandra, S.1    Chen, X.2    Rizo, J.3    Jahn, R.4    Sudhof, T.C.5
  • 124
    • 15244347219 scopus 로고    scopus 로고
    • Helix periodicity, topology, and dynamics of membrane-associated alpha-synuclein
    • Bussell, R.; Jr.; Ramlall, T.F.; Eliezer, D. Helix periodicity, topology, and dynamics of membrane-associated alpha-synuclein. Protein Sci., 2005, 14, 862-872.
    • (2005) Protein Sci , vol.14 , pp. 862-872
    • Bussell Jr., R.1    Ramlall, T.F.2    Eliezer, D.3
  • 125
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer, T.S.; Bax, A.; Cole, N.B.; Nussbaum, R.L. Structure and dynamics of micelle-bound human alpha-synuclein. J. Biol. Chem., 2005, 280, 9595-9603.
    • (2005) J. Biol. Chem , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 126
    • 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
  • 127
    • 2942555022 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling
    • Jan, 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
    • Jan, C.C.1    Der-Sarkissian, A.2    Chen, J.3    Langen, R.4
  • 128
    • 33746894560 scopus 로고    scopus 로고
    • Inter-helix distances in lysophospholipid micelle-bound alpha-synuclein from pulsed ESR measurements
    • Borbat, P.; Ramlall, T.F.; Freed, J.H.; Eliezer, D. Inter-helix distances in lysophospholipid micelle-bound alpha-synuclein from pulsed ESR measurements. J. Am. Chem. Soc., 2006, 128, 10004-10005.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10004-10005
    • Borbat, P.1    Ramlall, T.F.2    Freed, J.H.3    Eliezer, D.4
  • 129
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound alpha-symiclein 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-symiclein 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
  • 130
    • 84882472237 scopus 로고    scopus 로고
    • In Protein Folding and Aggregation in In Vitro Models of Parkinson's Disease: Structure and Function of Alpha-Synuclein
    • Nash, R, Przedborski, S, Eds, Academic Press: New York
    • Eliezer, D. In Protein Folding and Aggregation in In Vitro Models of Parkinson's Disease: Structure and Function of Alpha-Synuclein, Nash, R.; Przedborski, S.; Eds.; Parkinson's Disease: Pathogenic and Therapeutic Insightsfrom Toxin and Genetic Models, Academic Press: New York, 2008, pp. 575-595.
    • (2008) Parkinson's Disease: Pathogenic and Therapeutic Insightsfrom Toxin and Genetic Models , pp. 575-595
    • Eliezer, D.1
  • 131
    • 0041845349 scopus 로고    scopus 로고
    • Certain metals trigger fibrillation of methionme-oxidized alpha-synuclein
    • Yamin, G.; Glaser, C.B.; Uversky, V.N.; Fink, A.L. Certain metals trigger fibrillation of methionme-oxidized alpha-synuclein. J. Biol, Chem., 2003, 278, 27630-27635.
    • (2003) J. Biol, Chem , vol.278 , pp. 27630-27635
    • Yamin, G.1    Glaser, C.B.2    Uversky, V.N.3    Fink, A.L.4
  • 132
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro
    • Cohlberg, J.A.; Li, J.; Uversky, V.N.; Fink, A.L. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro. Biochemistry, 2002, 41, 1502-1511.
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 133
    • 12844272205 scopus 로고    scopus 로고
    • Methionine oxidation, alpha-synuclein and Parkinson's disease
    • Glaser, C.B.; Yamin, G.; Uversky, V.N.; Fink, A.L. Methionine oxidation, alpha-synuclein and Parkinson's disease, Biochim. Biophys. Acta, 2005, 1703, 157-169.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 157-169
    • Glaser, C.B.1    Yamin, G.2    Uversky, V.N.3    Fink, A.L.4
  • 134
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of alpha-synuclein in organic solvents: Modeling the effects of membianes
    • Munishkina, L.A.; Phelan, C.; Uversky, V.N.; Fink, A.L. Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membianes. Biochemistry, 2003, 42, 2720-2730.
    • (2003) Biochemistry , vol.42 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 135
    • 0035976814 scopus 로고    scopus 로고
    • Trimethylamine-N-oxide-induced folding of alpa-synuclein
    • Uversky, V.N.; Li, J.; Fink, A.L. Trimethylamine-N-oxide-induced folding of alpa-synuclein. FEBS Lett., 2001, 509, 31-35.
    • (2001) FEBS Lett , vol.509 , pp. 31-35
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 136
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations aggregation, and fibrillation of human alpha-synuclein: A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky, V.N.; Li, J.; Fink, A.L. Metal-triggered structural transformations aggregation, and fibrillation of human alpha-synuclein: a possible molecular NK between Parkinson's disease and heavy metal exposure. J. -Biol. Chem., 2001, 276, 44284-44296.
    • (2001) J. -Biol. Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 137
    • 1542533563 scopus 로고    scopus 로고
    • Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation
    • Munishkini, L.A.; Henriques, J.; UVersky, V.N.; Fink, A.L. Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry, 2004, 43, 3289-3300.
    • (2004) Biochemistry , vol.43 , pp. 3289-3300
    • Munishkini, L.A.1    Henriques, J.2    UVersky, V.N.3    Fink, A.L.4
  • 138
    • 0035816404 scopus 로고    scopus 로고
    • Pesticides directly accelerate the rate of alpha-synuclein fibril formation: A possible factor in Parkinson's disease
    • Uversky, V.N.; Li, J.; Fink, A.L. Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease. FEBS Lett., 2001, 500, 105-108.
    • (2001) FEBS Lett , vol.500 , pp. 105-108
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 139
    • 0036777847 scopus 로고    scopus 로고
    • Synergistic effects of pesticides and metals on the fibrillation of alpha-synuclein: Implications for Parkinson's disease
    • Uversky, V.N.; Li, J.; Bower, K.; Fink, A.L. Synergistic effects of pesticides and metals on the fibrillation of alpha-synuclein: implications for Parkinson's disease. Neurotoxicology, 2002, 23, 527-536.
    • (2002) Neurotoxicology , vol.23 , pp. 527-536
    • Uversky, V.N.1    Li, J.2    Bower, K.3    Fink, A.L.4
  • 140
    • 0037127197 scopus 로고    scopus 로고
    • The herbicide paraquat causes upregulation and aggregation of alpha-synuclein in mice: Paraquat and alpha-synuclein
    • Manning-Bog, A.B.; McCormack, A.L.; Li, J.; Uversky, V.N.; Fink, A.L.; Di Monte, D.A. The herbicide paraquat causes upregulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein. J. Biol. Chem., 2002, 277, 1641-1644.
    • (2002) J. Biol. Chem , vol.277 , pp. 1641-1644
    • Manning-Bog, A.B.1    McCormack, A.L.2    Li, J.3    Uversky, V.N.4    Fink, A.L.5    Di Monte, D.A.6
  • 141
    • 0037378356 scopus 로고    scopus 로고
    • Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro
    • Goers, J.; Uversky, V.N.; Fink, A.L. Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro. Protein Sci, 2003, 12, 702-707.
    • (2003) Protein Sci , vol.12 , pp. 702-707
    • Goers, J.1    Uversky, V.N.2    Fink, A.L.3
  • 142
    • 0035941305 scopus 로고    scopus 로고
    • Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations
    • Uversky, V.N.; Lee, H.J.; Li, J.; Fink, A.L.; Lee, S.J. Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations. J. Biol. Chem., 2001, 276, 43495-43498.
    • (2001) J. Biol. Chem , vol.276 , pp. 43495-43498
    • Uversky, V.N.1    Lee, H.J.2    Li, J.3    Fink, A.L.4    Lee, S.J.5
  • 143
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alpha - synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • Souza, J.M.; Giasson, B.I.; Chen, Q.; Lee, V.M.; Ischiropoulos, H. Dityrosine cross-linking promotes formation of stable alpha - synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem., 2000, 275, 18344-18349.
    • (2000) J. Biol. Chem , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 144
    • 0038404977 scopus 로고    scopus 로고
    • Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers
    • Yamin, G.; Uversky, V.N.; Fink, A.L. Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers. FEBS Lett., 2003, 542, 147-152.
    • (2003) FEBS Lett , vol.542 , pp. 147-152
    • Yamin, G.1    Uversky, V.N.2    Fink, A.L.3
  • 145
    • 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
  • 146
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders
    • Uversky, V.N. A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn., 2003, 21, 211-234.
    • (2003) J. Biomol. Struct. Dyn , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 147
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of alpha-synuclein
    • Fink, A.L. The aggregation and fibrillation of alpha-synuclein. Acc. Chem. Res., 2006, 39, 628-634.
    • (2006) Acc. Chem. Res , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 148
    • 6344228684 scopus 로고    scopus 로고
    • Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein
    • Choi, W.; Zibaee, S.; Jakes, R.; Serpell, L.C.; Davletov, B.; Crowther, R.A.; Goedert, M. Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein. FEBS Lett., 2004, 576, 363-368.
    • (2004) FEBS Lett , vol.576 , pp. 363-368
    • Choi, W.1    Zibaee, S.2    Jakes, R.3    Serpell, L.C.4    Davletov, B.5    Crowther, R.A.6    Goedert, M.7
  • 149
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • Zimmerman, S.B.; Trach, S.O. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J. Mol. Biol., 1991, 222, 599-620.
    • (1991) J. Mol. Biol , vol.222 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2
  • 150
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton, A.P. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem., 2001, 276, 10577-10580.
    • (2001) J. Biol. Chem , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 151
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton, A.P. Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol., 2000, 10, 34-39.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 152
    • 0037181497 scopus 로고    scopus 로고
    • Accelerated alpha-synuclein fibrillation in crowded milieu
    • Uversky, V.N.; Cooper, E.M.; Bower, K.S.; Li, J.; Fink, A.L. Accelerated alpha-synuclein fibrillation in crowded milieu. FEBS Lett., 2002, 515, 99-103.
    • (2002) FEBS Lett , vol.515 , pp. 99-103
    • Uversky, V.N.1    Cooper, E.M.2    Bower, K.S.3    Li, J.4    Fink, A.L.5
  • 153
    • 0037177250 scopus 로고    scopus 로고
    • Molecular crowding accelerates fibrillization of alpha-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease?
    • Shtilerman, M.D.; Ding, T.T.; Lansbury, P.T.; Jr. Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry, 2002, 41, 3855-3860.
    • (2002) Biochemistry , vol.41 , pp. 3855-3860
    • Shtilerman, M.D.1    Ding, T.T.2    Lansbury Jr., P.T.3
  • 154
    • 4544252011 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
    • Munishkina, L.A.; Cooper, E.M.; Uversky, V.N.; Fink, A.L. The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit., 2004, 17, 456-464.
    • (2004) J. Mol. Recognit , vol.17 , pp. 456-464
    • Munishkina, L.A.1    Cooper, E.M.2    Uversky, V.N.3    Fink, A.L.4
  • 155
    • 54249116911 scopus 로고    scopus 로고
    • Concerted action of metals and macromolecular crowding on the fibrillation of alpha-synuclein
    • Munishkina, L.A.; Fink, A.L.; Uversky, V.N. Concerted action of metals and macromolecular crowding on the fibrillation of alpha-synuclein. Protein Pept. Lett., 2008, 15, 1079-1085.
    • (2008) Protein Pept. Lett , vol.15 , pp. 1079-1085
    • Munishkina, L.A.1    Fink, A.L.2    Uversky, V.N.3
  • 156
    • 50149096820 scopus 로고    scopus 로고
    • Guiding protein aggregation with macromolecular crowding
    • Munishkina, L.A.; Ahmad, A.; Fink, A.L.; Uversky, V.N. Guiding protein aggregation with macromolecular crowding. Biochemistry, 2008, 47, 8993-9006.
    • (2008) Biochemistry , vol.47 , pp. 8993-9006
    • Munishkina, L.A.1    Ahmad, A.2    Fink, A.L.3    Uversky, V.N.4
  • 157
    • 0033865052 scopus 로고    scopus 로고
    • Review: Amyloidogenesis-unquestioned answers and unanswered questions
    • Kisilevsky, R. Review: amyloidogenesis-unquestioned answers and unanswered questions. J. Struct. Biol., 2000, 130, 99-108.
    • (2000) J. Struct. Biol , vol.130 , pp. 99-108
    • Kisilevsky, R.1
  • 158
    • 0033863798 scopus 로고    scopus 로고
    • Review: Modulating factors in amyloid-beta fibril formation
    • McLaurin, J.; Yang, D.; Yip, C.M.; Fraser, P.E. Review: modulating factors in amyloid-beta fibril formation. J. Struct. Biol., 2000, 130, 259-270.
    • (2000) J. Struct. Biol , vol.130 , pp. 259-270
    • McLaurin, J.1    Yang, D.2    Yip, C.M.3    Fraser, P.E.4
  • 159
    • 0028813382 scopus 로고
    • Agrin is a heparan sulfate proteoglycan
    • Tsen, G.; Halfter, W.; Kroger, S.; Cole, G.J. Agrin is a heparan sulfate proteoglycan. J. Biol. Chem., 1995, 270, 3392-3399.
    • (1995) J. Biol. Chem , vol.270 , pp. 3392-3399
    • Tsen, G.1    Halfter, W.2    Kroger, S.3    Cole, G.J.4
  • 160
    • 0030902790 scopus 로고    scopus 로고
    • Distribution and substrate properties of agrin, a heparan sulfate proteoglycan of developing axonal pathways
    • Halfter, W.; Schurer, B.; Yip, J.; Yip, L.; Tsen, G.; Lee, J.A.; Cole, G.J. Distribution and substrate properties of agrin, a heparan sulfate proteoglycan of developing axonal pathways. J. Comp. Neurol., 1997, 383, 1-17.
    • (1997) J. Comp. Neurol , vol.383 , pp. 1-17
    • Halfter, W.1    Schurer, B.2    Yip, J.3    Yip, L.4    Tsen, G.5    Lee, J.A.6    Cole, G.J.7
  • 161
    • 0031023262 scopus 로고    scopus 로고
    • Expression of agrin in the developing and adult rat brain
    • Cohen, N.A.; Kaufmann, W.E.; Worley, P.F.; Rupp, F. Expression of agrin in the developing and adult rat brain. Neuroscience, 1997, 76, 581-596.
    • (1997) Neuroscience , vol.76 , pp. 581-596
    • Cohen, N.A.1    Kaufmann, W.E.2    Worley, P.F.3    Rupp, F.4
  • 164
    • 0024546234 scopus 로고
    • The role of environmental toxins in the etiology of Parkinson's disease
    • Tanner, C.M. The role of environmental toxins in the etiology of Parkinson's disease. Trends Neurosci., 1989, 12, 49-54.
    • (1989) Trends Neurosci , vol.12 , pp. 49-54
    • Tanner, C.M.1
  • 166
    • 0042521076 scopus 로고    scopus 로고
    • The environment and Parkinson's disease: Is the nigrostriatal system preferentially targeted by neurotoxins?
    • Di Monte, D.A. The environment and Parkinson's disease: is the nigrostriatal system preferentially targeted by neurotoxins? Lancet Neurol., 2003, 2, 531-538.
    • (2003) Lancet Neurol , vol.2 , pp. 531-538
    • Di Monte, D.A.1
  • 167
  • 169
    • 0012678765 scopus 로고    scopus 로고
    • The role of environmental agents in Parkinson's disease
    • Di Monte, D.A. The role of environmental agents in Parkinson's disease. Clin. Neurosci. Res., 2001, 1, 419-426.
    • (2001) Clin. Neurosci. Res , vol.1 , pp. 419-426
    • Di Monte, D.A.1
  • 170
    • 5444255433 scopus 로고    scopus 로고
    • Neurotoxicant-induced animal models of Parkinson's disease: Understanding the role of rotenone, maneb and paraquat in neurodegeneration
    • Uversky, V.N. Neurotoxicant-induced animal models of Parkinson's disease: understanding the role of rotenone, maneb and paraquat in neurodegeneration. Cell. Tissue Res., 2004, 318, 225-241.
    • (2004) Cell. Tissue Res , vol.318 , pp. 225-241
    • Uversky, V.N.1
  • 172
    • 0033153770 scopus 로고    scopus 로고
    • Aluminum-containing antacids as a cause of idiopathic Parkinson's disease
    • Altschuler, E. Aluminum-containing antacids as a cause of idiopathic Parkinson's disease. Med. Hypotheses, 1999, 53, 22-23.
    • (1999) Med. Hypotheses , vol.53 , pp. 22-23
    • Altschuler, E.1
  • 175
    • 0027508966 scopus 로고
    • Parkinson's disease mortality and the industrial use of heavy metals in Michigan
    • Rybicki, B.A.; Johnson, C.C.; Uman, J.; Gorell, J.M. Parkinson's disease mortality and the industrial use of heavy metals in Michigan. Mov. Disord., 1993, 8, 87-92.
    • (1993) Mov. Disord , vol.8 , pp. 87-92
    • Rybicki, B.A.1    Johnson, C.C.2    Uman, J.3    Gorell, J.M.4
  • 176
    • 0026034279 scopus 로고    scopus 로고
    • Hirsch, E.C.; Brandel, J.P.; Galle, P.; Javoy-Agid, F.; Agid, Y. Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: an X-ray microanalysis. J. Neurochem., 1991, 56, 446-451.
    • Hirsch, E.C.; Brandel, J.P.; Galle, P.; Javoy-Agid, F.; Agid, Y. Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: an X-ray microanalysis. J. Neurochem., 1991, 56, 446-451.
  • 178
    • 0025821265 scopus 로고
    • Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia
    • Dexter, D.T.; Carayon, A.; Javoy-Agid, F.; Agid, Y.; Wells, F.R.; Daniel, S.E.; Lees, A.J.; Jenner, P.; Marsden, C.D. Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia. Brain, 1991, 114 (Pt 4), 1953-1975.
    • (1991) Brain , vol.114 , Issue.PART 4 , pp. 1953-1975
    • Dexter, D.T.1    Carayon, A.2    Javoy-Agid, F.3    Agid, Y.4    Wells, F.R.5    Daniel, S.E.6    Lees, A.J.7    Jenner, P.8    Marsden, C.D.9
  • 179
    • 33644847016 scopus 로고    scopus 로고
    • NMR mapping of copper binding sites in alpha-synuclein
    • Sung, Y.H.; Rospigliosi, C.; Eliezer, D. NMR mapping of copper binding sites in alpha-synuclein. Biochim. Biophys. Acta, 2006, 1764, 5-12.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 5-12
    • Sung, Y.H.1    Rospigliosi, C.2    Eliezer, D.3
  • 180
    • 0030012558 scopus 로고    scopus 로고
    • Possible environmental, occupational, and other etiologic factors for Parkinson's disease: A case-control study in Germany
    • Seidler, A.; Hellenbrand, W.; Robra, B.P.; Vieregge, P.; Nischan, P.; Joerg, J.; Oertel, W.H.; Ulm, G.; Schneider, E. Possible environmental, occupational, and other etiologic factors for Parkinson's disease: a case-control study in Germany. Neurology, 1996, 46, 1275-1284.
    • (1996) Neurology , vol.46 , pp. 1275-1284
    • Seidler, A.1    Hellenbrand, W.2    Robra, B.P.3    Vieregge, P.4    Nischan, P.5    Joerg, J.6    Oertel, W.H.7    Ulm, G.8    Schneider, E.9
  • 181
    • 0033436303 scopus 로고    scopus 로고
    • Parkinsonism from methanol poisoning: Benefit from treatment with anti-Parkinson drugs
    • Davis, L.E.; Adair, J.C. Parkinsonism from methanol poisoning: benefit from treatment with anti-Parkinson drugs. Mov. Disord., 1999, 14, 520-522.
    • (1999) Mov. Disord , vol.14 , pp. 520-522
    • Davis, L.E.1    Adair, J.C.2
  • 182
    • 0032895184 scopus 로고    scopus 로고
    • Parkinsonism, pyramidal signs, polyneuropathy, and cognitive decline after long-term occupational solvent exposure
    • Hageman, G.; van der Hoek, J.; van Hout, M.; van der Laan, G.; Steur, E.J.; de Bruin, W.; Herholz, K. Parkinsonism, pyramidal signs, polyneuropathy, and cognitive decline after long-term occupational solvent exposure. J. Neurol., 1999, 246, 198-206.
    • (1999) J. Neurol , vol.246 , pp. 198-206
    • Hageman, G.1    van der Hoek, J.2    van Hout, M.3    van der Laan, G.4    Steur, E.J.5    de Bruin, W.6    Herholz, K.7
  • 185
    • 0032733691 scopus 로고    scopus 로고
    • The role of oxidative stress in Alzheimer disease
    • Markesbery, W.R. The role of oxidative stress in Alzheimer disease. Arch. Neurol., 1999, 56, 1449-1452.
    • (1999) Arch. Neurol , vol.56 , pp. 1449-1452
    • Markesbery, W.R.1
  • 186
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • Markesbery, W.R.; Carney, J.M. Oxidative alterations in Alzheimer's disease. Brain Pathol., 1999, 9, 133-146.
    • (1999) Brain Pathol , vol.9 , pp. 133-146
    • Markesbery, W.R.1    Carney, J.M.2
  • 188
    • 0031842223 scopus 로고    scopus 로고
    • Oxidative damage to proteins, lipids, and DNA in cortical brain regions from patients with dementia with Lewy bodies
    • Lyras, L.; Perry, R.H.; Perry, E.K.; Ince, P.G.; Jenner, A.; Jenner, P.; Halliwell, B. Oxidative damage to proteins, lipids, and DNA in cortical brain regions from patients with dementia with Lewy bodies. J Neurochem, 1998, 71, 302-312.
    • (1998) J Neurochem , vol.71 , pp. 302-312
    • Lyras, L.1    Perry, R.H.2    Perry, E.K.3    Ince, P.G.4    Jenner, A.5    Jenner, P.6    Halliwell, B.7
  • 189
    • 0032949602 scopus 로고    scopus 로고
    • Oxidative stress and motor neurone disease
    • Cookson, M.R.; Shaw, P.J. Oxidative stress and motor neurone disease. Brain Pathol., 1999, 9, 165-186.
    • (1999) Brain Pathol , vol.9 , pp. 165-186
    • Cookson, M.R.1    Shaw, P.J.2
  • 190
    • 0032903802 scopus 로고    scopus 로고
    • Oxidative stress in Huntington's disease
    • Browne, S.E.; Ferrante, R.J.; Beal, M.F. Oxidative stress in Huntington's disease. Brain Pathol., 1999, 9, 147-163.
    • (1999) Brain Pathol , vol.9 , pp. 147-163
    • Browne, S.E.1    Ferrante, R.J.2    Beal, M.F.3
  • 191
    • 0032246425 scopus 로고    scopus 로고
    • Advanced oxidation protein products: Oxidative stress markers and mediators of inflammation in uremia
    • Witko-Sarsat, V.; Khoa, T.N.; Jungers, P.; Drueke, T.; Descamps-Latscha, B. Advanced oxidation protein products: oxidative stress markers and mediators of inflammation in uremia. Adv. Nephrol Necker. Hosp., 1998, 28, 321-341.
    • (1998) Adv. Nephrol Necker. Hosp , vol.28 , pp. 321-341
    • Witko-Sarsat, V.1    Khoa, T.N.2    Jungers, P.3    Drueke, T.4    Descamps-Latscha, B.5
  • 193
    • 0032582822 scopus 로고    scopus 로고
    • The hydroxyl radical in lens nuclear cataractogenesis
    • Fu, S.; Dean, R.; Southan, M.; Truscott, R. The hydroxyl radical in lens nuclear cataractogenesis. J. Biol. Chem., 1998, 273, 28603-28609.
    • (1998) J. Biol. Chem , vol.273 , pp. 28603-28609
    • Fu, S.1    Dean, R.2    Southan, M.3    Truscott, R.4
  • 194
    • 0025314685 scopus 로고
    • Role of oxygen free radicals in carcinogenesis and brain ischemia
    • Floyd, R.A. Role of oxygen free radicals in carcinogenesis and brain ischemia. FASEB J., 1990, 4, 2587-2597.
    • (1990) FASEB J , vol.4 , pp. 2587-2597
    • Floyd, R.A.1
  • 197
    • 0031992238 scopus 로고    scopus 로고
    • Markers of protein oxidation by hydroxyl radical and reactive nitrogen species in tissues of aging rats
    • Leeuwenburgh, C.; Hansen, P.; Shaish, A.; Holloszy, J.O.; Heinecke, J.W. Markers of protein oxidation by hydroxyl radical and reactive nitrogen species in tissues of aging rats. Am. J. Physiol., 1998, 274, R453-461.
    • (1998) Am. J. Physiol , vol.274
    • Leeuwenburgh, C.1    Hansen, P.2    Shaish, A.3    Holloszy, J.O.4    Heinecke, J.W.5
  • 198
    • 0037165646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro
    • Uversky, V.N.; Yamin, G.; Souillac, P.O.; Goers, J.; Glaser, C.B.; Fink, A.L. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS Lett, 2002, 517, 239-244.
    • (2002) FEBS Lett , vol.517 , pp. 239-244
    • Uversky, V.N.1    Yamin, G.2    Souillac, P.O.3    Goers, J.4    Glaser, C.B.5    Fink, A.L.6
  • 199
    • 9144274018 scopus 로고    scopus 로고
    • Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein
    • Hokenson, M.J.; Uversky, V.N.; Goers, J.; Yamin, G.; Munishkina, L.A.; Fink, A.L. Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein. Biochemistry, 2004, 43, 4621-4633.
    • (2004) Biochemistry , vol.43 , pp. 4621-4633
    • Hokenson, M.J.1    Uversky, V.N.2    Goers, J.3    Yamin, G.4    Munishkina, L.A.5    Fink, A.L.6
  • 200
    • 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
  • 201
    • 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
  • 203
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • Mucke, L.; Masliah, E.; Yu, G.Q.; Mallory, M.; Rockenstein, E.M.; Tatsuno, G.; Hu, K.; Kholodenko, D.; Johnson-Wood, K.; McConlogue, L. High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J Neurosci., 2000, 20, 4050-4058.
    • (2000) J Neurosci , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3    Mallory, M.4    Rockenstein, E.M.5    Tatsuno, G.6    Hu, K.7    Kholodenko, D.8    Johnson-Wood, K.9    McConlogue, L.10
  • 204
    • 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
  • 205
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel, H.A.; Hartley, D.; Petre, B.M.; Walz, T.; Lansbury, P.T.; Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature, 2002, 418, 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 206
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B.; Lansbury, P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci., 2003, 26, 267-298.
    • (2003) Annu. Rev. Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 207
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • Walsh, D.M.; Selkoe, D.J. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett., 2004, 11, 213-228.
    • (2004) Protein Pept. Lett , vol.11 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 208
    • 33751510212 scopus 로고    scopus 로고
    • Amyloid ion channels: A porous argument or a thin excuse?
    • Eliezer, D. Amyloid ion channels: a porous argument or a thin excuse? J. Gen. Physiol., 2006, 128, 631-633.
    • (2006) J. Gen. Physiol , vol.128 , pp. 631-633
    • Eliezer, D.1
  • 209
    • 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
  • 210
    • 15544374153 scopus 로고    scopus 로고
    • Biological significance and clinical relevance of nitric oxide-mediated protein modifications
    • Ischiropoulos, H. Biological significance and clinical relevance of nitric oxide-mediated protein modifications. Free Radic. Res., 2003, 37, 15.
    • (2003) Free Radic. Res , vol.37 , pp. 15
    • Ischiropoulos, H.1
  • 211
    • 0038731081 scopus 로고    scopus 로고
    • Biological selectivity and functional aspects of protein tyrosine nitration
    • Ischiropoulos, H. Biological selectivity and functional aspects of protein tyrosine nitration. Biochem. Biophys. Res. Commun., 2003, 305, 776-783.
    • (2003) Biochem. Biophys. Res. Commun , vol.305 , pp. 776-783
    • Ischiropoulos, H.1
  • 212
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos, H. Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch. Biochem. Biophys., 1998, 356, 1-11.
    • (1998) Arch. Biochem. Biophys , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 215
    • 34247130917 scopus 로고    scopus 로고
    • Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation
    • Qin, Z.; Hu, D.; Han, S.; Reaney, S.H.; Di Monte, D.A.; Fink, A.L. Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation. J. Biol. Chem., 2007, 282, 5862-5870.
    • (2007) J. Biol. Chem , vol.282 , pp. 5862-5870
    • Qin, Z.1    Hu, D.2    Han, S.3    Reaney, S.H.4    Di Monte, D.A.5    Fink, A.L.6
  • 216
    • 0035950270 scopus 로고    scopus 로고
    • Hashimoto, M.; Rockenstein, E.; Mante, M.; Mallory, M.; Masliah, E. beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor. Neuron, 2001, 32, 213-223.
    • Hashimoto, M.; Rockenstein, E.; Mante, M.; Mallory, M.; Masliah, E. beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor. Neuron, 2001, 32, 213-223.
  • 217
    • 31344464179 scopus 로고    scopus 로고
    • The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein
    • Zhou, W.; Zhu, M.; Wilson, M.A.; Petsko, G.A.; Fink, A.L. The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein. J. Mol. Biol., 2006, 356, 1036-1048.
    • (2006) J. Mol. Biol , vol.356 , pp. 1036-1048
    • Zhou, W.1    Zhu, M.2    Wilson, M.A.3    Petsko, G.A.4    Fink, A.L.5
  • 218
    • 13944267769 scopus 로고    scopus 로고
    • DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation
    • Shendelman, S.; Jonason, A.; Martinat, C.; Leete, T.; Abeliovich, A. DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol., 2004, 2, e362.
    • (2004) PLoS Biol , vol.2
    • Shendelman, S.1    Jonason, A.2    Martinat, C.3    Leete, T.4    Abeliovich, A.5
  • 219
    • 0023722437 scopus 로고    scopus 로고
    • Maroteaux, L.; Campanelli, J.T.; Scheller, R.H. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci., 1988, 8, 2804-2815.
    • Maroteaux, L.; Campanelli, J.T.; Scheller, R.H. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci., 1988, 8, 2804-2815.
  • 220
    • 0032500599 scopus 로고    scopus 로고
    • Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • Jensen, P.H.; Nielsen, M.S.; Jakes, R.; Dotti, C.G.; Goedert, M. Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J. Biol. Chem., 1998, 273, 26292-26294.
    • (1998) J. Biol. Chem , vol.273 , pp. 26292-26294
    • Jensen, P.H.1    Nielsen, M.S.2    Jakes, R.3    Dotti, C.G.4    Goedert, M.5
  • 221
    • 0032492689 scopus 로고    scopus 로고
    • Regulation of phospholipase D2: Selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins
    • Jenco, J.M.; Rawlingson, A.; Daniels, B.; Morris, A.J. Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins. Biochemistry, 1998, 37, 4901-4909.
    • (1998) Biochemistry , vol.37 , pp. 4901-4909
    • Jenco, J.M.1    Rawlingson, A.2    Daniels, B.3    Morris, A.J.4
  • 222
    • 0033215063 scopus 로고    scopus 로고
    • Synucleins in synaptic plasticity and neurodegenerative disorders
    • Clayton, D.F.; George, J.M. Synucleins in synaptic plasticity and neurodegenerative disorders. J. Neurosci. Res., 1999, 58, 120-129.
    • (1999) J. Neurosci. Res , vol.58 , pp. 120-129
    • Clayton, D.F.1    George, J.M.2
  • 223
    • 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
  • 224
    • 0037155197 scopus 로고    scopus 로고
    • Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein
    • Cole, N.B.; Murphy, D.D.; Grider, T.; Rueter, S.; Brasaemle, D.; Nussbaum, R.L. Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein. J. Biol. Chem., 2002, 277, 6344-6352.
    • (2002) J. Biol. Chem , vol.277 , pp. 6344-6352
    • Cole, N.B.1    Murphy, D.D.2    Grider, T.3    Rueter, S.4    Brasaemle, D.5    Nussbaum, R.L.6
  • 225
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • Rhoades, E.; Ramlall, T.F.; Webb, W.W.; Eliezer, D. Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy. Biophys. J., 2006, 90, 4692-4700.
    • (2006) Biophys. J , vol.90 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 226
    • 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
  • 227
    • 0036150971 scopus 로고    scopus 로고
    • The synucleins
    • REVIEWS 3002
    • George, J.M. The synucleins. Genome. Biol., 2002, 3, REVIEWS 3002.
    • (2002) Genome. Biol , vol.3
    • George, J.M.1
  • 228
    • 0037930855 scopus 로고    scopus 로고
    • Lipid binding inhibits alpha-synuclein fibril formation
    • Zhu, M.; Fink, A.L. Lipid binding inhibits alpha-synuclein fibril formation. J. Biol. Chem., 2003, 278, 16873-16877.
    • (2003) J. Biol. Chem , vol.278 , pp. 16873-16877
    • Zhu, M.1    Fink, A.L.2
  • 229
    • 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
  • 230
    • 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. 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., 2003, 85, 1468-1479.
    • (2003) J Neurochem , vol.85 , pp. 1468-1479
    • Hashimoto, M.1    Takenouchi, T.2    Rockenstein, E.3    Masliah, E.4
  • 231
    • 33846798329 scopus 로고    scopus 로고
    • Climbing the scaffolds of Parkinson's disease pathogenesis
    • Spencer, B.; Crews, L.; Masliah, E. Climbing the scaffolds of Parkinson's disease pathogenesis. Neuron, 2007, 53, 469-470.
    • (2007) Neuron , vol.53 , pp. 469-470
    • Spencer, B.1    Crews, L.2    Masliah, E.3
  • 232
    • 35848961655 scopus 로고    scopus 로고
    • Lipid rafts, protein scaffolds, and neurologic disease
    • Benarroch, E.E. Lipid rafts, protein scaffolds, and neurologic disease. Neurology, 2007, 69, 1635-1639.
    • (2007) Neurology , vol.69 , pp. 1635-1639
    • Benarroch, E.E.1
  • 233
    • 33847022701 scopus 로고    scopus 로고
    • GMI specifically interacts with alpha-synuclein and inhibits fibrillation
    • Martinez, Z.; Zhu, M.; Han, S.; Fink, A.L. GMI specifically interacts with alpha-synuclein and inhibits fibrillation. Biochemistry, 2007, 46, 1868-1877.
    • (2007) Biochemistry , vol.46 , pp. 1868-1877
    • Martinez, Z.1    Zhu, M.2    Han, S.3    Fink, A.L.4
  • 234
    • 0037713491 scopus 로고    scopus 로고
    • Convergent pathobiologic model of Parkinson's disease
    • Maguire-Zeiss, K.A.; Federoff, H.J. Convergent pathobiologic model of Parkinson's disease. Ann. NY Acad. Sci., 2003, 991, 152-166.
    • (2003) Ann. NY Acad. Sci , vol.991 , pp. 152-166
    • Maguire-Zeiss, K.A.1    Federoff, H.J.2
  • 235
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: Implications for Parkinson's and Alzheimer's disease
    • Li, J.; Zhu, M.; Manning-Bog, A.B.; Di Monte, D.A.; Fink, A.L. Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. FASEB J., 2004, 18, 962-964.
    • (2004) FASEB J , vol.18 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di Monte, D.A.4    Fink, A.L.5
  • 236
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway, K.A.; Rochet, J.C.; Bieganski, R.M.; Lansbury, P.T.; Jr. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science, 2001, 294, 1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 237
    • 0026793767 scopus 로고
    • Neumfibrillary tangles and senile plaques in brain of elderly leprosy patients
    • Namba, Y.; Kawatsu, K.; Izumi, S.; Ueki, A.; Ikeda, K. Neumfibrillary tangles and senile plaques in brain of elderly leprosy patients. Lancet, 1992, 340, 978.
    • (1992) Lancet , vol.340 , pp. 978
    • Namba, Y.1    Kawatsu, K.2    Izumi, S.3    Ueki, A.4    Ikeda, K.5
  • 238
    • 0028173384 scopus 로고
    • Decreased beta-amyloid and increased abnormal Tau deposition in the brain of aged patients with leprosy
    • Chui, D.H.; Tabira, T.; Izumi, S.; Koya, G.; Ogata, J. Decreased beta-amyloid and increased abnormal Tau deposition in the brain of aged patients with leprosy. Am. J. Pathol., 1994, 145, 771-775.
    • (1994) Am. J. Pathol , vol.145 , pp. 771-775
    • Chui, D.H.1    Tabira, T.2    Izumi, S.3    Koya, G.4    Ogata, J.5
  • 239
    • 0026777109 scopus 로고
    • Prevalence of dementia amongst elderly japanese with leprosy - apparent effect of chronic drug-therapy
    • Mcgeer, P.L.; Harada, N.; Kimura, H.; Mcgeer, E.G.; Schulzer, M. Prevalence of dementia amongst elderly japanese with leprosy - apparent effect of chronic drug-therapy. Dementia, 1992, 3, 146-149.
    • (1992) Dementia , vol.3 , pp. 146-149
    • Mcgeer, P.L.1    Harada, N.2    Kimura, H.3    Mcgeer, E.G.4    Schulzer, M.5
  • 240
    • 0029863551 scopus 로고    scopus 로고
    • Inhibition of amyloid beta protein aggregation and neurritoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger
    • Tomiyama, T.; Shoji, A.; Kataoka, K.; Suwa, Y.; Asano, S.; Kaneko, H.; Endo, N. Inhibition of amyloid beta protein aggregation and neurritoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger. J. Biol. Chem., 1996, 271, 6839-6844.
    • (1996) J. Biol. Chem , vol.271 , pp. 6839-6844
    • Tomiyama, T.1    Shoji, A.2    Kataoka, K.3    Suwa, Y.4    Asano, S.5    Kaneko, H.6    Endo, N.7
  • 241
    • 0030905125 scopus 로고    scopus 로고
    • Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction
    • Tomiyama, T.; Kaneko, H.; Kataoka, K.; Asano, S.; Endo, N. Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction. Biochem. J., 1997, 322 (Pt 3), 859-865.
    • (1997) Biochem. J , vol.322 , Issue.PART 3 , pp. 859-865
    • Tomiyama, T.1    Kaneko, H.2    Kataoka, K.3    Asano, S.4    Endo, N.5
  • 243
    • 8844224948 scopus 로고    scopus 로고
    • Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils
    • Li, J.; Zhu, M.; Rajamani, S.; Uversky, V.N.; Fink, A.L. Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils. Chem. Biol., 2004, 11, 1513-1521.
    • (2004) Chem. Biol , vol.11 , pp. 1513-1521
    • Li, J.1    Zhu, M.2    Rajamani, S.3    Uversky, V.N.4    Fink, A.L.5
  • 244
    • 0035221973 scopus 로고    scopus 로고
    • Anti-HIV activity of medicinal herbs: Usage and potential development
    • Wu, J.A.; Attele, A.S.; Zhang, L.; Yuan, C.S. Anti-HIV activity of medicinal herbs: usage and potential development. Am. J. Chin. Med., 2001, 29, 69-81.
    • (2001) Am. J. Chin. Med , vol.29 , pp. 69-81
    • Wu, J.A.1    Attele, A.S.2    Zhang, L.3    Yuan, C.S.4
  • 245
    • 0035212167 scopus 로고    scopus 로고
    • Baicalin is a major component of PC-SPES which inhibits the proliferation of human cancer cells via apoptosis and cell cycle arrest
    • Ikezoe, T.; Chen, S.S.; Heber, D.; Taguchi, H.; Koeffler, H.P. Baicalin is a major component of PC-SPES which inhibits the proliferation of human cancer cells via apoptosis and cell cycle arrest. Prostate, 2001, 49, 285-292.
    • (2001) Prostate , vol.49 , pp. 285-292
    • Ikezoe, T.1    Chen, S.S.2    Heber, D.3    Taguchi, H.4    Koeffler, H.P.5
  • 246
    • 0034950875 scopus 로고    scopus 로고
    • Protective effects of flavonoids in the roots of Scutellaria baicalensis Georgi against hydrogen peroxide-induced oxidative stress in HS-SY5Y cells
    • Gao, Z.; Huang, K.; Xu, H. Protective effects of flavonoids in the roots of Scutellaria baicalensis Georgi against hydrogen peroxide-induced oxidative stress in HS-SY5Y cells. Pharmacol. Res., 2001, 43, 173-178.
    • (2001) Pharmacol. Res , vol.43 , pp. 173-178
    • Gao, Z.1    Huang, K.2    Xu, H.3
  • 247
    • 0033794615 scopus 로고    scopus 로고
    • Antioxidant and free radical scavenging effects of baicalein, baicalin and wogonhi
    • Shieh, D.E.; Liu, L.T.; Lin, C.C. Antioxidant and free radical scavenging effects of baicalein, baicalin and wogonhi. Anticancer Res., 2000, 20, 2861-2865.
    • (2000) Anticancer Res , vol.20 , pp. 2861-2865
    • Shieh, D.E.1    Liu, L.T.2    Lin, C.C.3
  • 248
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils
    • Zhu, M.; Rajamani, S.; Kaylor, J.; Han, S.; Zhou, F.; Fink, A.L. The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils. J. Biol. Chem., 2004, 279, 26846-26857.
    • (2004) J. Biol. Chem , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 249
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein
    • Hong, D.P.; Fink, A.L.; Uversky, V.N. Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein. J. Mol. Biol., 2008, 383, 214-223.
    • (2008) J. Mol. Biol , vol.383 , pp. 214-223
    • Hong, D.P.1    Fink, A.L.2    Uversky, V.N.3
  • 250
    • 0036714747 scopus 로고    scopus 로고
    • A meta-analysis of coffee drinking, cigarette smoking, and the risk of Parkinson's disease
    • Hernan, M.A.; Takkouche, B.; Caamano-Isorna, F.; Gestal-Otero, J.J. A meta-analysis of coffee drinking, cigarette smoking, and the risk of Parkinson's disease. Ann. Neurol., 2002, 52, 276-284.
    • (2002) Ann. Neurol , vol.52 , pp. 276-284
    • Hernan, M.A.1    Takkouche, B.2    Caamano-Isorna, F.3    Gestal-Otero, J.J.4
  • 252
    • 0033842094 scopus 로고    scopus 로고
    • Smoking and Parkinson's and Alzheimer's disease: Review of the epidemiological studies
    • Fratiglioni, L.; Wang, H.X. Smoking and Parkinson's and Alzheimer's disease: review of the epidemiological studies. Behav. Brain Res, 2000, 113, 117-120.
    • (2000) Behav. Brain Res , vol.113 , pp. 117-120
    • Fratiglioni, L.1    Wang, H.X.2
  • 253
    • 4344698859 scopus 로고    scopus 로고
    • Smoking, nicotine and Parkinson's disease
    • Quik, M. Smoking, nicotine and Parkinson's disease. Trends Neurosci., 2004, 27, 561-568.
    • (2004) Trends Neurosci , vol.27 , pp. 561-568
    • Quik, M.1
  • 254
    • 58149199681 scopus 로고    scopus 로고
    • Smoking and Parkinson's disease: Does nicotine affect alpha-synuclein fibrillation?
    • Hong, D.P.; Fink, A.L.; Uversky, V.N. Smoking and Parkinson's disease: does nicotine affect alpha-synuclein fibrillation? Biochim. Biophys. Acta, 2009, 1794, 282-290.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 282-290
    • Hong, D.P.1    Fink, A.L.2    Uversky, V.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.