메뉴 건너뛰기




Volumn 64, Issue 17, 2007, Pages 2194-2201

Physiological and pathological properties of α-synuclein

Author keywords

Synuclein; synucleinopathies; Lewy body; Neurodegeneration; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN;

EID: 34548318990     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-7217-5     Document Type: Review
Times cited : (109)

References (82)
  • 1
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • Forno, L. S. (1996) Neuropathology of Parkinson's disease. J. Neuropathol. Exp. Neurol. 55, 259-272.
    • (1996) J. Neuropathol. Exp. Neurol , vol.55 , pp. 259-272
    • Forno, L.S.1
  • 2
    • 26444544353 scopus 로고    scopus 로고
    • α-Synuclein dysfunction in Lewy body diseases
    • Tofaris, G. K. and Spillantini, M. G. (2005) α-Synuclein dysfunction in Lewy body diseases. Mov. Disorders 20, S37-S44.
    • (2005) Mov. Disorders , vol.20
    • Tofaris, G.K.1    Spillantini, M.G.2
  • 3
    • 0034704386 scopus 로고    scopus 로고
    • Pure autonomic failure in association with human α-synucleinopathy
    • Arai, K., Kato, N., Kashiwado, K. and Hattori, T. (2000) Pure autonomic failure in association with human α-synucleinopathy. Neurosci. Lett. 296, 171-173.
    • (2000) Neurosci. Lett , vol.296 , pp. 171-173
    • Arai, K.1    Kato, N.2    Kashiwado, K.3    Hattori, T.4
  • 4
    • 0031721278 scopus 로고    scopus 로고
    • Lewy body in neurodegeneration with brain iron accumulation type 1 is immunoreactive for α-synuclein
    • Arawaka, S., Saito, Y., Murayama, S. and Mori, H. (1998) Lewy body in neurodegeneration with brain iron accumulation type 1 is immunoreactive for α-synuclein. Neurology 51, 887-889.
    • (1998) Neurology , vol.51 , pp. 887-889
    • Arawaka, S.1    Saito, Y.2    Murayama, S.3    Mori, H.4
  • 5
    • 0032719237 scopus 로고    scopus 로고
    • Widespread occurrence of α-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. and Takahashi, H. (1999) Widespread occurrence of α-synuclein/NACP- immunoreactive neuronal inclusions in juvenile and adult-onset Hallervorden-Spatz disease with Lewy bodies. Neuropathol. Appl. Neurobiol. 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    Takahashi, H.6
  • 6
    • 0033936784 scopus 로고    scopus 로고
    • α-Synuclein inclusions in amygdala in the brains of patients with the Parkinsonism-Dementia complex of Guam
    • Yamazaki, M., Arai, Y., Baba, M., Iwatsubo, T., Mori, O., Katayama, Y. and Oyanagi, K. (2000) α-Synuclein inclusions in amygdala in the brains of patients with the Parkinsonism-Dementia complex of Guam. J. Neuropathol. Exp. Neurol. 59, 585-591.
    • (2000) J. Neuropathol. Exp. Neurol , vol.59 , pp. 585-591
    • Yamazaki, M.1    Arai, Y.2    Baba, M.3    Iwatsubo, T.4    Mori, O.5    Katayama, Y.6    Oyanagi, K.7
  • 7
    • 0032990543 scopus 로고    scopus 로고
    • Antibodies to α-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimers disease
    • Lippa, C. F., Schmidt, M. L., Lee, V. M.-Y. and Trojanowski, J. Q. (1999) Antibodies to α-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimers disease. Ann. Neurol. 45, 353-357.
    • (1999) Ann. Neurol , vol.45 , pp. 353-357
    • Lippa, C.F.1    Schmidt, M.L.2    Lee, V.M.-Y.3    Trojanowski, J.Q.4
  • 8
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies
    • Spillantini, M. G., Crowther, R. A., Jakes, R., Cairns, N. J., Lantos, P. L. and Goedert, M. (1998) Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neurosci. Lett. 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
  • 9
    • 33846989334 scopus 로고    scopus 로고
    • Adult-onset neurodegeneration with brain iron accumulation and cortical α-synuclein and tau pathology: A distinct clinico-pathological entity
    • Tofaris, G. K, Revesz, T., Jacques, T., Papacostas, S. and Chataway, J. (2007) Adult-onset neurodegeneration with brain iron accumulation and cortical α-synuclein and tau pathology: a distinct clinico-pathological entity. Arch. Neurol. 64, 280-282.
    • (2007) Arch. Neurol , vol.64 , pp. 280-282
    • Tofaris, G.K.1    Revesz, T.2    Jacques, T.3    Papacostas, S.4    Chataway, J.5
  • 11
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning is natively unfolded
    • Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A. and Lansbury, P. T (1996) NACP, a protein implicated in Alzheimer's disease and learning is natively unfolded. Biochemistry 35, 13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, P.T.5
  • 12
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W. S., Jonas, A., Clayton, D. F. and George, J. M. (1998) Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 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
  • 13
    • 0032492689 scopus 로고    scopus 로고
    • Regulation of phospholipase D2: Selective inhibition of mammalian phospholipase D isoenzymes by α- and β-synucleins
    • Jenco, J. M., Rawlingson, A., Daniels, B. and Morris, A. J. (1998) Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by α- and β-synucleins. Biochemistry 37, 4901-4909.
    • (1998) Biochemistry , vol.37 , pp. 4901-4909
    • Jenco, J.M.1    Rawlingson, A.2    Daniels, B.3    Morris, A.J.4
  • 15
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed and α-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy, D. D., Rueter, S. M., Trojanowski, J. Q. and Lee, V. M.-Y. (2000) Synucleins are developmentally expressed and α-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J. Neurosci. 20, 3214-3220.
    • (2000) J. Neurosci , vol.20 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 16
    • 0029127954 scopus 로고
    • Characterization of a novel protein regulated during the critical period for song learning in the zebra finch
    • George, J. M., Jin, H., Woods, W. S. and Clayton, D. F. (1995) Characterization of a novel protein regulated during the critical period for song learning in the zebra finch. Neuron 15, 361-372.
    • (1995) Neuron , vol.15 , pp. 361-372
    • George, J.M.1    Jin, H.2    Woods, W.S.3    Clayton, D.F.4
  • 17
    • 27544507306 scopus 로고    scopus 로고
    • alpha-Synuclein cooperates with CSPalpha in preventing neurodegeneration
    • Chandra, S., Gallardo, G., Fernandez-Chacon, R., Schluter, O. M. and Sudhof, T. C. (2005) alpha-Synuclein cooperates with CSPalpha in preventing neurodegeneration. Cell 123, 383-396.
    • (2005) Cell , vol.123 , pp. 383-396
    • Chandra, S.1    Gallardo, G.2    Fernandez-Chacon, R.3    Schluter, O.M.4    Sudhof, T.C.5
  • 18
    • 0038460184 scopus 로고    scopus 로고
    • Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease
    • Dev, K. K., Hofele, K., Barbieri, S., Buchman, V. L. and van der Putten, H. (2003) Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease. Neuropharmacolology 45, 14-44.
    • (2003) Neuropharmacolology , vol.45 , pp. 14-44
    • Dev, K.K.1    Hofele, K.2    Barbieri, S.3    Buchman, V.L.4    van der Putten, H.5
  • 21
    • 0035976959 scopus 로고    scopus 로고
    • α-Synuclein affects the MAP kinase pathway and accelerates cell death
    • Iwata, A., Maruyama, M., Kanazawa, I. and Nukina, N. (2001) α-Synuclein affects the MAP kinase pathway and accelerates cell death. J. Biol. Chem. 276, 45320-45329.
    • (2001) J. Biol. Chem , vol.276 , pp. 45320-45329
    • Iwata, A.1    Maruyama, M.2    Kanazawa, I.3    Nukina, N.4
  • 22
    • 0034604583 scopus 로고    scopus 로고
    • Wild-type but not Parkinson's disease-related Ala-53-Thr mutant α-synuclein protects neuronal cells from apoptotic stimuli
    • Alves da Costa, C., Ancolio, K. and Checler, F. (2000) Wild-type but not Parkinson's disease-related Ala-53-Thr mutant α-synuclein protects neuronal cells from apoptotic stimuli. J. Biol. Chem. 275, 24065-24069.
    • (2000) J. Biol. Chem , vol.275 , pp. 24065-24069
    • Alves da Costa, C.1    Ancolio, K.2    Checler, F.3
  • 23
    • 0035109909 scopus 로고    scopus 로고
    • Effect of the over-expression of wild-type or mutant alpha-synuclein on cell susceptibility to insult
    • Lee, M., Hyun, D., Halliwell, B. and Jenner, P. (2001) Effect of the over-expression of wild-type or mutant alpha-synuclein on cell susceptibility to insult. J. Neurochem. 76, 998-1009
    • (2001) J. Neurochem , vol.76 , pp. 998-1009
    • Lee, M.1    Hyun, D.2    Halliwell, B.3    Jenner, P.4
  • 24
    • 0037192865 scopus 로고    scopus 로고
    • α-Synuclein protects against oxidative stress via inactivation of the c-Jun N-terminal kinase stress signalling pathway in neuronal cells
    • Hashimoto, M., Hsu, L. J., Rockenstein, E., Takenouchi, T., Mallory, M. and Masliah, E. (2002) α-Synuclein protects against oxidative stress via inactivation of the c-Jun N-terminal kinase stress signalling pathway in neuronal cells. J. Biol. Chem. 277, 11465-11472.
    • (2002) J. Biol. Chem , vol.277 , pp. 11465-11472
    • Hashimoto, M.1    Hsu, L.J.2    Rockenstein, E.3    Takenouchi, T.4    Mallory, M.5    Masliah, E.6
  • 25
    • 34548341065 scopus 로고    scopus 로고
    • The effect of truncated human α-synuclein (1-120) on dopaminergic cells in a transgenic mouse model of Parkinson's disease
    • in press
    • Michell, A. W., Tofaris, G. K., Gossage, H., Tyers, P., Spillantini, M. G. and Barker, R. A. (2007) The effect of truncated human α-synuclein (1-120) on dopaminergic cells in a transgenic mouse model of Parkinson's disease. Cell Transplant., in press.
    • (2007) Cell Transplant
    • Michell, A.W.1    Tofaris, G.K.2    Gossage, H.3    Tyers, P.4    Spillantini, M.G.5    Barker, R.A.6
  • 28
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G protein-coupled receptor kinases
    • Pronin, A. N., Morris, A. J., Surguchov, A. and Benovic, J. L. (2000) Synucleins are a novel class of substrates for G protein-coupled receptor kinases. J. Biol. Chem. 275, 26515-26522.
    • (2000) J. Biol. Chem , vol.275 , pp. 26515-26522
    • Pronin, A.N.1    Morris, A.J.2    Surguchov, A.3    Benovic, J.L.4
  • 29
    • 0036484302 scopus 로고    scopus 로고
    • Multiple phosphorylation of α-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation
    • Negro, A., Brunati, A. M., Donella-Deana, A. Massimino, M. L. and Pinna, L. A. (2002) Multiple phosphorylation of α-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation. FASEB J. 16, 210-212.
    • (2002) FASEB J , vol.16 , pp. 210-212
    • Negro, A.1    Brunati, A.M.2    Donella-Deana, A.3    Massimino, M.L.4    Pinna, L.A.5
  • 31
    • 0032568534 scopus 로고    scopus 로고
    • α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies
    • Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M. and Goedert, M. (1998) α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. USA 95, 6469-6473.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 36
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross beta conformation
    • Serpell, L. C., Berriman, J., Jakes, R., Goedert, M. and Crowther, R. A. (2000) Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross beta conformation. Proc. Natl. Acad. Sci. USA 97, 4897-4902.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 37
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A., Lee S.-L., Rochet, J. C., Ding, T. T., Williamson, R. E. and Lansbury, P. T. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc Natl Acad Sci USA 97, 571-576.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.-L.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 38
    • 6344228684 scopus 로고    scopus 로고
    • Mutation E46K increases phospholipids binding and assembly into filaments of human alpha-synuclein
    • Choi, W., Zibanee, S., Jakes, R., Serpell, L. C., Davletov, B., Crowther, R. A. and Goedert, M. (2004) Mutation E46K increases phospholipids binding and assembly into filaments of human alpha-synuclein. FEBS Lett. 576, 363-368.
    • (2004) FEBS Lett , vol.576 , pp. 363-368
    • Choi, W.1    Zibanee, S.2    Jakes, R.3    Serpell, L.C.4    Davletov, B.5    Crowther, R.A.6    Goedert, M.7
  • 43
    • 0037118259 scopus 로고    scopus 로고
    • Neuronal α-synucleinopathy with severe movement disorder in mice expressing A53T human a-synuclein
    • Giasson, B. I., Duda, J. E., Quinn, S. M., Zhang, B., Trojanowski, J. Q. and Lee, V. M.-Y. (2002) Neuronal α-synucleinopathy with severe movement disorder in mice expressing A53T human a-synuclein. Neuron 34, 521-533.
    • (2002) Neuron , vol.34 , pp. 521-533
    • Giasson, B.I.1    Duda, J.E.2    Quinn, S.M.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 44
    • 0037173006 scopus 로고    scopus 로고
    • Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala53Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice
    • Lee, M. K., Stirling, W., Xu, Y., Xu, X., Qui, D., Mandir, A. S., Dawson, T. M., Copeland, N. G., Jenkins, N. A. and Price, D. L. (2002) Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala53Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice. Proc. Natl. Acad. Sci. USA 99, 8968-8973.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8968-8973
    • Lee, M.K.1    Stirling, W.2    Xu, Y.3    Xu, X.4    Qui, D.5    Mandir, A.S.6    Dawson, T.M.7    Copeland, N.G.8    Jenkins, N.A.9    Price, D.L.10
  • 45
    • 0036855635 scopus 로고    scopus 로고
    • Neumann, M., Kahle, P. J., Giasson, B. I., Ozmen, L., Borroni, E., Spooren, W., Muller, V., Odoy, S., Fujiwara, H., Hasegawa, M. et al. C. (2002) Misfolded proteinase K-resistant hyperphosphorylated α-synuclein in aged transgenic mice with locomotor deterioration and in human α- synucleinopathies. J. Clin. Invest. 110, 1429-1439.
    • Neumann, M., Kahle, P. J., Giasson, B. I., Ozmen, L., Borroni, E., Spooren, W., Muller, V., Odoy, S., Fujiwara, H., Hasegawa, M. et al. C. (2002) Misfolded proteinase K-resistant hyperphosphorylated α-synuclein in aged transgenic mice with locomotor deterioration and in human α- synucleinopathies. J. Clin. Invest. 110, 1429-1439.
  • 47
    • 0036550101 scopus 로고    scopus 로고
    • Parkinson-like neurodegeneration induced by targeted overexpression of α-synuclein in the nigrostriatal system
    • Kirik, D., Rosenblad, C., Burger, C., Lundberg, C., Johansen, T. E., Muzyczka, N., Mandel, R. J. and Bjorklund, A. (2002) Parkinson-like neurodegeneration induced by targeted overexpression of α-synuclein in the nigrostriatal system. J. Neurosci. 22, 2780-2791.
    • (2002) J. Neurosci , vol.22 , pp. 2780-2791
    • Kirik, D.1    Rosenblad, C.2    Burger, C.3    Lundberg, C.4    Johansen, T.E.5    Muzyczka, N.6    Mandel, R.J.7    Bjorklund, A.8
  • 48
    • 0036202813 scopus 로고    scopus 로고
    • Dopaminergic cell loss induced by human A30P alpha-synuclein gene transfer to the rat substantia nigra
    • Klein, R. L., King, M. A., Hamby, M. E. and Meyer, E. M. (2002) Dopaminergic cell loss induced by human A30P alpha-synuclein gene transfer to the rat substantia nigra. (2002) Hum. Gene Ther. 13, 605-612.
    • (2002) Hum. Gene Ther , vol.13 , pp. 605-612
    • Klein, R.L.1    King, M.A.2    Hamby, M.E.3    Meyer, E.M.4
  • 49
    • 0036679197 scopus 로고    scopus 로고
    • α-Synucleinopathy and selective dopaminergic neurone loss in a rat lentiviral-based model of Parkinson's disease
    • Lo Bianco, C., Ridet, J.-L., Schneider, B. L., Deglon, N. and Aebischer, P. (2002) α-Synucleinopathy and selective dopaminergic neurone loss in a rat lentiviral-based model of Parkinson's disease. Proc. Natl. Acad. Sci. USA 99, 10813-10818.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10813-10818
    • Lo Bianco, C.1    Ridet, J.-L.2    Schneider, B.L.3    Deglon, N.4    Aebischer, P.5
  • 50
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany, M. B. and Bender, W. W. (2000)A Drosophila model of Parkinson's disease. Nature 404, 394-398.
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 51
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson's disease
    • Conway, K. A., Harper, J. D. and Lansbury, P. T. (1998) Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson's disease. Nat. Med. 4, 1318-1320.
    • (1998) Nat. Med , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 52
    • 0034663039 scopus 로고    scopus 로고
    • The A53T α-synuclein mutation increases iron-dependent aggregation and toxicity
    • Ostrerova-Golts, N., Petrucelli, L., Hardy, J., Lee, J. M., Farer, M. and Wolozin, B. (2000) The A53T α-synuclein mutation increases iron-dependent aggregation and toxicity. J. Neurosci. 20, 6048-6054.
    • (2000) J. Neurosci , vol.20 , pp. 6048-6054
    • Ostrerova-Golts, N.1    Petrucelli, L.2    Hardy, J.3    Lee, J.M.4    Farer, M.5    Wolozin, B.6
  • 55
    • 9144229591 scopus 로고    scopus 로고
    • Functional consequences of alpha-synuclein tyrosine nitration: Diminished binding to lipid vesicles and increased fibril formation
    • Hodara, R., Norris, E. H., Giasson, B. I., Mishizen-Eberz, A. J., Lynch, D. R., Lee, V. M. and Ischiropoulos, H. (2004) Functional consequences of alpha-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation. J. Biol. Chem. 279, 47746-47753.
    • (2004) J. Biol. Chem , vol.279 , pp. 47746-47753
    • Hodara, R.1    Norris, E.H.2    Giasson, B.I.3    Mishizen-Eberz, A.J.4    Lynch, D.R.5    Lee, V.M.6    Ischiropoulos, H.7
  • 57
    • 0031728689 scopus 로고    scopus 로고
    • Synthetic filaments assembled from C-terminally truncated α-synuclein
    • Crowther, R. A., Jakes, R., Spillantini, M. G. and Goedert, M. (1998) Synthetic filaments assembled from C-terminally truncated α-synuclein. FEBS Lett. 436, 309-312.
    • (1998) FEBS Lett , vol.436 , pp. 309-312
    • Crowther, R.A.1    Jakes, R.2    Spillantini, M.G.3    Goedert, M.4
  • 59
    • 0242666359 scopus 로고    scopus 로고
    • Ubiquitination of α-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function
    • Tofaris, G. K., Razzaq, A., Ghetti, B., Lilley, K. S. and Spillantini, M. G. (2003) Ubiquitination of α-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function. J. Biol. Chem. 278, 44405-44411.
    • (2003) J. Biol. Chem , vol.278 , pp. 44405-44411
    • Tofaris, G.K.1    Razzaq, A.2    Ghetti, B.3    Lilley, K.S.4    Spillantini, M.G.5
  • 61
    • 0032879452 scopus 로고    scopus 로고
    • Role of cytochrome c as a stimulator of alpha-synuclein aggregation in Lewy body disease
    • Hashimoto, M., Takeda, A., Hsu, L. J., Takenouchi, T. and Masliah, E. (1999) Role of cytochrome c as a stimulator of alpha-synuclein aggregation in Lewy body disease. J. Biol. Chem. 274, 28849-2885.
    • (1999) J. Biol. Chem , vol.274 , pp. 28849-22885
    • Hashimoto, M.1    Takeda, A.2    Hsu, L.J.3    Takenouchi, T.4    Masliah, E.5
  • 64
    • 0037378356 scopus 로고    scopus 로고
    • Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro
    • Goers, J., Uversky, V. N. and Fink, A. L. (2003) Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro. Protein Sci. 12, 702-707.
    • (2003) Protein Sci , vol.12 , pp. 702-707
    • Goers, J.1    Uversky, V.N.2    Fink, A.L.3
  • 65
    • 20444401187 scopus 로고    scopus 로고
    • Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations
    • Norris, E. H., Giasson, B. I., Hodara, R., Xu, S., Trojanowski, J. Q., Ischiropoulos H and Lee, V. M. (2005) Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations. J. Biol. Chem. 280, 21212-2129.
    • (2005) J. Biol. Chem , vol.280 , pp. 21212-22129
    • Norris, E.H.1    Giasson, B.I.2    Hodara, R.3    Xu, S.4    Trojanowski, J.Q.5    Ischiropoulos, H.6    Lee, V.M.7
  • 66
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N. F., Sampat, R. M. and Kopito, R. R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 67
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman, P., Wetzel, R., Tanaka, M., Nukina, N. and Goldberg, A. L. (2004) Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol. Cell 14, 95-104.
    • (2004) Mol. Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 69
    • 0035976835 scopus 로고    scopus 로고
    • α-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris, G. K., Layfield, R. and Spillantini, M. G. (2001) α-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 509, 22-26.
    • (2001) FEBS Lett , vol.509 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 70
  • 71
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of α-synuclein toxicity in a Drosophila Model for Parkinson's disease
    • Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M. and Bonini, N. M. (2002) Chaperone suppression of α-synuclein toxicity in a Drosophila Model for Parkinson's disease. Science 295, 865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.E.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 72
    • 21244499845 scopus 로고    scopus 로고
    • The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways
    • Shin, Y., Klucken, J., Patterson, C., Hyman, B. T. and McLean, P. J. (2005) The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways., J. Biol. Chem. 280, 23727-23734.
    • (2005) J. Biol. Chem , vol.280 , pp. 23727-23734
    • Shin, Y.1    Klucken, J.2    Patterson, C.3    Hyman, B.T.4    McLean, P.J.5
  • 73
    • 0035834655 scopus 로고    scopus 로고
    • Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins
    • Perrin, R. J., Woods, W. S., Clayton, D. F. and George, J. M. (2001) Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J. Biol. Chem. 276, 41958-41962.
    • (2001) J. Biol. Chem , vol.276 , pp. 41958-41962
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 74
    • 0037456578 scopus 로고    scopus 로고
    • The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease
    • Sharon, R., Bar-Joseph, I., Frosch, M. P., Walsh, D. M., Hamilton, J. A. and Selkoe, D. J. (2003) The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron 37, 583-595.
    • (2003) Neuron , vol.37 , pp. 583-595
    • Sharon, R.1    Bar-Joseph, I.2    Frosch, M.P.3    Walsh, D.M.4    Hamilton, J.A.5    Selkoe, D.J.6
  • 76
    • 0141891097 scopus 로고    scopus 로고
    • The association of alpha-synuclein with membranes affects bilayer structure, stability and fibril formation
    • Zhu, M., Li, J. and Fink, A. L. (2003) The association of alpha-synuclein with membranes affects bilayer structure, stability and fibril formation. J. Biol. Chem. 278, 40186-40197.
    • (2003) J. Biol. Chem , vol.278 , pp. 40186-40197
    • Zhu, M.1    Li, J.2    Fink, A.L.3
  • 78
    • 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. and Lansbury, P. T. (2001) Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294, 1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury, P.T.4
  • 79
    • 33749170166 scopus 로고    scopus 로고
    • Cytosolic catechols inhibit alpha-synuclein aggregation and facilitate the formation of intracellular soluble oligomeric intermediates
    • Mazzulli, J. R., Mishizen, A. J., Giasson, B. I., Lynch, D. R., Thomas, S. A., Nakashima, A., Nagatsu, T., Ota, A. and Ischiropoulos, H. (2006) Cytosolic catechols inhibit alpha-synuclein aggregation and facilitate the formation of intracellular soluble oligomeric intermediates. J. Neurosci. 26, 10068-10078.
    • (2006) J. Neurosci , vol.26 , pp. 10068-10078
    • Mazzulli, J.R.1    Mishizen, A.J.2    Giasson, B.I.3    Lynch, D.R.4    Thomas, S.A.5    Nakashima, A.6    Nagatsu, T.7    Ota, A.8    Ischiropoulos, H.9
  • 80
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson's disease
    • Xu, J., Kao, S.-Y., Lee, F. J. S., Song, W., Jin, L.-W. and Yanker, B. A. (2002) Dopamine-dependent neurotoxicity of α-synuclein: a mechanism for selective neurodegeneration in Parkinson's disease. Nat. Med. 8, 600-606.
    • (2002) Nat. Med , vol.8 , pp. 600-606
    • Xu, J.1    Kao, S.-Y.2    Lee, F.J.S.3    Song, W.4    Jin, L.-W.5    Yanker, B.A.6
  • 81
    • 0036468957 scopus 로고    scopus 로고
    • Overexpression of human α-synuclein causes dopamine neurone death in primary human mesencephalic culture
    • Zhou, W., Schaak, J., Zawada, W. M. and Freed, C. R. (2002) Overexpression of human α-synuclein causes dopamine neurone death in primary human mesencephalic culture. Brain Res. 926, 42-50.
    • (2002) Brain Res , vol.926 , pp. 42-50
    • Zhou, W.1    Schaak, J.2    Zawada, W.M.3    Freed, C.R.4
  • 82
    • 30044439773 scopus 로고    scopus 로고
    • Interaction with phospholipids modulates alpha-synuclein nitration and lipi-protein adduct formation
    • Trostchansky, A., Lind, S., Hodara, R., Oe, T., Blair, I. A., Ischiropoulos, H., Rubbo, H. and Souza, J. M. (2006) Interaction with phospholipids modulates alpha-synuclein nitration and lipi-protein adduct formation. Biochem. J. 393, 343-349.
    • (2006) Biochem. J , vol.393 , pp. 343-349
    • Trostchansky, A.1    Lind, S.2    Hodara, R.3    Oe, T.4    Blair, I.A.5    Ischiropoulos, H.6    Rubbo, H.7    Souza, J.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.