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Volumn 322, Issue 5, 2002, Pages 1089-1102

α-synuclein, especially the parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils

Author keywords

Parkinson's disease; Protofibrils; Scanning transmission electron microscopy; Transmission electron microscopy; synuclein

Indexed keywords

ALPHA SYNUCLEIN;

EID: 0036415838     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00735-0     Document Type: Article
Times cited : (725)

References (47)
  • 2
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • Forno, L. S. (1996). Neuropathology of Parkinson's disease. J. Neuropathol. Expt. Neurol. 55, 259-272.
    • (1996) J. Neuropathol. Expt. Neurol. , vol.55 , pp. 259-272
    • Forno, L.S.1
  • 3
    • 0040368216 scopus 로고    scopus 로고
    • Prospects for new restorative and neuroprotective treatments in Parkinson's disease
    • Dunnett, S. B. & Bjorklund, A. (1999). Prospects for new restorative and neuroprotective treatments in Parkinson's disease. Nature, 399, A32-A39.
    • (1999) Nature , vol.399
    • Dunnett, S.B.1    Bjorklund, A.2
  • 4
    • 0032568534 scopus 로고    scopus 로고
    • Alpha-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. & Goedert, M. (1998). alpha-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
  • 5
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A. et al. (1997). Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science, 276, 2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5    Dutra, A.6
  • 6
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger, R., Kuhn, W., Muller, T., Woitalla, D., Graeber, M., Kosel, S. et al. (1998). Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nature Genet. 18, 106-108.
    • (1998) Nature Genet. , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 7
    • 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. et al. (2000). Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science, 287, 1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6
  • 8
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany, M. B. & 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
  • 9
    • 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. (1998). Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nature Med. 4, 1318-1320.
    • (1998) Nature Med. , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 11
    • 0034609561 scopus 로고    scopus 로고
    • Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein
    • Rochet, J. C., Conway, K. A. & Lansbury, P. T., Jr (2000). Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein. Biochemistry, 39, 10619-10626.
    • (2000) Biochemistry , vol.39 , pp. 10619-10626
    • Rochet, J.C.1    Conway, K.A.2    Lansbury P.T., Jr.3
  • 12
    • 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. (2001). Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry, 40, 11604-11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 13
    • 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 (2000). Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl Acad. Sci. USA, 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 P.T., Jr.6
  • 14
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg, M. S. & Lansbury, P. T., Jr (2000). Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nature Cell Biol. 2, E115-E119.
    • (2000) Nature Cell Biol. , vol.2
    • Goldberg, M.S.1    Lansbury P.T., Jr.2
  • 15
    • 0031013141 scopus 로고    scopus 로고
    • Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons
    • Tompkins, M. M., Basgall, E. J., Zamrini, E. & Hill, W. D. (1997). Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons. Am. J. Pathol. 150, 119-131.
    • (1997) Am. J. Pathol. , vol.150 , pp. 119-131
    • Tompkins, M.M.1    Basgall, E.J.2    Zamrini, E.3    Hill, W.D.4
  • 16
    • 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 (2000). Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry, 39, 2552-2563.
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury P.T., Jr.3
  • 17
    • 0037072284 scopus 로고    scopus 로고
    • Annular a-synuclein protofibrils are produced by spherical protofibrils incubated in solution or bound to membrane surfaces
    • Ding, T. M., Lee, S-J., Rochet, C. J. & Lansbury, P. T., Jr (2002). Annular a-synuclein protofibrils are produced by spherical protofibrils incubated in solution or bound to membrane surfaces. Biochemistry, 41, 10209-10217.
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.M.1    Lee, S.-J.2    Rochet, C.J.3    Lansbury P.T., Jr.4
  • 18
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • Giasson, B. I., Murray, I. V., Trojanowski, J. Q. & Lee, V. M. (2001). A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J. Biol. Chem. 276, 2380-2386.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 19
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • Volles, M. J., Lee, S. J., Rochet, J. C., Shtilerman, M. D., Ding, T. T., Kessler, J. C. & Lansbury, P. T., Jr (2001). Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry, 40, 7812-7819.
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.J.2    Rochet, J.C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury P.T., Jr.7
  • 20
    • 0030735356 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages
    • Valeva, A., Palmer, M. & Bhakdi, S. (1997). Staphylococcal alpha-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry, 36, 13298-13304.
    • (1997) Biochemistry , vol.36 , pp. 13298-13304
    • Valeva, A.1    Palmer, M.2    Bhakdi, S.3
  • 21
    • 0035822706 scopus 로고    scopus 로고
    • B-Barrel pore-forming toxins: Intriguing dimorphic proteins
    • Heuck, A. P., Tweten, R. K. & Johnson, A. E. (2001). B-Barrel pore-forming toxins: intriguing dimorphic proteins. Biochemistry, 40, 9065-9073.
    • (2001) Biochemistry , vol.40 , pp. 9065-9073
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 22
    • 0033636662 scopus 로고    scopus 로고
    • Mechanism of membrane insertion of a multimeric beta-barrel protein. Perfringolysin O creates a pore using ordered and coupled conformational changes
    • Heuck, A. P., Hotze, E. M., Tweten, R. K. & Johnson, A. E. (2000). Mechanism of membrane insertion of a multimeric beta-barrel protein. Perfringolysin O creates a pore using ordered and coupled conformational changes. Mol. Cell, 6, 1233-1242.
    • (2000) Mol. Cell , vol.6 , pp. 1233-1242
    • Heuck, A.P.1    Hotze, E.M.2    Tweten, R.K.3    Johnson, A.E.4
  • 23
    • 0034869444 scopus 로고    scopus 로고
    • Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family
    • Menestrina, G., Serra, M. D. & Prevost, G. (2001). Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family. Toxicon, 39, 1661-1672.
    • (2001) Toxicon , vol.39 , pp. 1661-1672
    • Menestrina, G.1    Serra, M.D.2    Prevost, G.3
  • 24
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's beta(1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik, S. B., Inouye, H., Szumowski, K. E. & Kirschner, D. A. (1998). Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils. Biophys. J. 74, 537-545.
    • (1998) Biophys. J. , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.E.3    Kirschner, D.A.4
  • 25
    • 0033790878 scopus 로고    scopus 로고
    • Molecular structure of a fibrillar Alzheimer's A beta fragment
    • Serpell, L. C., Blake, C. C. & Fraser, P. E. (2000). Molecular structure of a fibrillar Alzheimer's A beta fragment. Biochemistry, 39, 13269-13275.
    • (2000) Biochemistry , vol.39 , pp. 13269-13275
    • Serpell, L.C.1    Blake, C.C.2    Fraser, P.E.3
  • 27
    • 0034869176 scopus 로고    scopus 로고
    • Protofibrils, the unifying toxic molecule of neurodegenerative disorders?
    • Haass, C. & Steiner, H. (2001). Protofibrils, the unifying toxic molecule of neurodegenerative disorders? Nature Neurosci. 4, 859-860.
    • (2001) Nature Neurosci , vol.4 , pp. 859-860
    • Haass, C.1    Steiner, H.2
  • 28
    • 0035967889 scopus 로고    scopus 로고
    • Non-fibrillar oligomeric species of the amyloid ABri peptide, implicated in familial British dementia, are more potent at inducing apoptotic cell death than protofibrils or mature fibrils
    • El-Agnaf, O. M., Nagala, S., Patel, B. P. & Austen, B. M. (2001). Non-fibrillar oligomeric species of the amyloid ABri peptide, implicated in familial British dementia, are more potent at inducing apoptotic cell death than protofibrils or mature fibrils. J. Mol. Biol. 310, 157-168.
    • (2001) J. Mol. Biol. , vol.310 , pp. 157-168
    • El-Agnaf, O.M.1    Nagala, S.2    Patel, B.P.3    Austen, B.M.4
  • 29
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar α-synuclein: Comparison of wild-type with parkinson's disease linked mutants and insights in the mechanism
    • Volles, M. J. & Lansbury, P. T., Jr. (2002). Vesicle permeabilization by protofibrillar α-synuclein: comparison of wild-type with parkinson's disease linked mutants and insights in the mechanism. Biochemistry, 41, 4595-4602.
    • (2002) Biochemistry , vol.41 , pp. 4595-4602
    • Volles, M.J.1    Lansbury P.T., Jr.2
  • 30
    • 0030043134 scopus 로고    scopus 로고
    • Aerolysin - The ins and outs of a model channel-forming toxin
    • Parker, M. W., van der Goot, F. G. & Buckley, J. T. (1996). Aerolysin - the ins and outs of a model channel-forming toxin. Mol. Microbiol. 19, 205-212.
    • (1996) Mol. Microbiol. , vol.19 , pp. 205-212
    • Parker, M.W.1    Van der Goot, F.G.2    Buckley, J.T.3
  • 31
    • 0034319190 scopus 로고    scopus 로고
    • Molecular mechanism of neurodegeneration induced by Alzheimer's beta-amyloid protein: Channel formation and disruption of calcium homeostasis
    • Kawahara, M. & Kuroda, Y. (2000). Molecular mechanism of neurodegeneration induced by Alzheimer's beta-amyloid protein: channel formation and disruption of calcium homeostasis. Brain Res. Bull. 53, 389-397.
    • (2000) Brain Res. Bull. , vol.53 , pp. 389-397
    • Kawahara, M.1    Kuroda, Y.2
  • 32
    • 0034994097 scopus 로고    scopus 로고
    • Pore formation by beta-2-microglobulin: A mechanism for the pathogenesis of dialysis associated amyloidosis
    • Hirakura, Y. & Kagan, B. L. (2001). Pore formation by beta-2-microglobulin: a mechanism for the pathogenesis of dialysis associated amyloidosis. Amyloid, 8, 94-100.
    • (2001) Amyloid , vol.8 , pp. 94-100
    • Hirakura, Y.1    Kagan, B.L.2
  • 33
    • 0034856924 scopus 로고    scopus 로고
    • Diversity of amyloid beta protein fragment [1-40]-formed channels
    • Kourie, J. I., Henry, C. L. & Farrelly, P. (2001). Diversity of amyloid beta protein fragment [1-40]-formed channels. Cell. Mol. Neurobiol. 21, 255-284.
    • (2001) Cell. Mol. Neurobiol. , vol.21 , pp. 255-284
    • Kourie, J.I.1    Henry, C.L.2    Farrelly, P.3
  • 34
    • 0033769044 scopus 로고    scopus 로고
    • A nonfibrillar form of the fusogenic prion protein fragment [118-135] induces apoptotic cell death in rat cortical neurons
    • Pillot, T., Drouet, B., Pincon-Ramond, M., Vandekerckhove, J., Rosseneu, M. & Chambaz, J. (2000). A nonfibrillar form of the fusogenic prion protein fragment [118-135] induces apoptotic cell death in rat cortical neurons. J. Neurochem. 75, 2298-2308.
    • (2000) J. Neurochem. , vol.75 , pp. 2298-2308
    • Pillot, T.1    Drouet, B.2    Pincon-Ramond, M.3    Vandekerckhove, J.4    Rosseneu, M.5    Chambaz, J.6
  • 35
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin, H., Bhatia, R. & Lal, R. (2001). Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J. 15, 2433-2444.
    • (2001) FASEB J. , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 36
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • Mirzabekov, T. A., Lin, M. C. & Kagan, B. L. (1996). Pore formation by the cytotoxic islet amyloid peptide amylin. J. Biol. Chem. 271, 1988-1992.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 37
    • 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 (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., Jr.4
  • 39
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M. & Leith, A. (1996). SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 40
    • 0002682751 scopus 로고
    • Measuring sedimentation, diffusion, and molecular weights of small molecules by direct fitting of sedimentation velocity concentration profiles
    • Shuster, T. M. & Laue, T. M., eds, Springer-Verlag, Heidelberg
    • Philo, S. J. (1994). Measuring sedimentation, diffusion, and molecular weights of small molecules by direct fitting of sedimentation velocity concentration profiles. In Modern Analytical Ultracentrifugation (Shuster, T. M. & Laue, T. M., eds), pp. 156-170, Springer-Verlag, Heidelberg.
    • (1994) Modern Analytical Ultracentrifugation , pp. 156-170
    • Philo, S.J.1
  • 41
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low-molecular-weight solutes
    • Philo, J. S. (1997). An improved function for fitting sedimentation velocity data for low-molecular-weight solutes. Biophys. J. 72, 435-444.
    • (1997) Biophys. J. , vol.72 , pp. 435-444
    • Philo, J.S.1
  • 42
    • 0028672523 scopus 로고
    • Boundary analysis in sedimentation velocity experiments
    • Stafford, W. F., III (1994). Boundary analysis in sedimentation velocity experiments. Methods Enzymol. 240, 478-501.
    • (1994) Methods Enzymol. , vol.240 , pp. 478-501
    • Stafford W.F. III1
  • 43
    • 0032558978 scopus 로고    scopus 로고
    • Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation
    • Lashuel, H. A., Lai, Z. & Kelly, J. W. (1998). Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry, 37, 17851-17864.
    • (1998) Biochemistry , vol.37 , pp. 17851-17864
    • Lashuel, H.A.1    Lai, Z.2    Kelly, J.W.3
  • 44
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • Hinz, H.-J., ed., Springer, New York
    • Durchschlag, H. (1986). Specific volumes of biological macromolecules and some other molecules of biological interest. In Thermodynamic Data for Biochemistry and Biotechnology (Hinz, H.-J., ed.), pp. 45, Springer, New York.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45
    • Durchschlag, H.1
  • 45
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S. J. (1986). Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157, 169.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169
    • Perkins, S.J.1
  • 46
    • 0035231630 scopus 로고    scopus 로고
    • Scanning transmission electron microscopy of DNA-protein complexes
    • Wall, J. S. & Simon, M. N. (2001). Scanning transmission electron microscopy of DNA-protein complexes. Methods Mol. Biol. 148, 589-601.
    • (2001) Methods Mol. Biol. , vol.148 , pp. 589-601
    • Wall, J.S.1    Simon, M.N.2


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