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Volumn 23, Issue 1-2, 2004, Pages 23-33

Interactions among α-synuclein, dopamine, and biomembranes: Some clues for understanding neurodegeneration in Parkinson's disease

Author keywords

Dopamine; Fibril; Membrane; Parkinson's disease; Protofibril; Synuclein; Yeast

Indexed keywords

ALPHA SYNUCLEIN; CATECHOLAMINE; DOPAMINE; NERVE PROTEIN; SNCA PROTEIN, HUMAN; SYNUCLEIN;

EID: 4344641972     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1385/jmn:23:1-2:023     Document Type: Review
Times cited : (177)

References (55)
  • 1
    • 0031715398 scopus 로고    scopus 로고
    • NACP/α-synuclein immunoreactivity in fibrillary components of neuronal and oligodendroglial cytoplasmic inclusions in the pontine nuclei in multiple system atrophy
    • Arima K., Ueda K., Sunohara N., Arakawa K., Hirai S., Nakamura M., et al. (1998) NACP/α-synuclein immunoreactivity in fibrillary components of neuronal and oligodendroglial cytoplasmic inclusions in the pontine nuclei in multiple system atrophy. Acta Neuropathol. (Berl.) 96, 439-444.
    • (1998) Acta Neuropathol. (Berl.) , vol.96 , pp. 439-444
    • Arima, K.1    Ueda, K.2    Sunohara, N.3    Arakawa, K.4    Hirai, S.5    Nakamura, M.6
  • 2
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of α-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • Baba M., Nakajo S., Tu P.- H., Tomita T., Nakaya K., Lee V. M.- Y., et al. (1998) Aggregation of α-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am. J. Pathol. 152, 879-884.
    • (1998) Am. J. Pathol. , vol.152 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4    Nakaya, K.5    Lee, V.M.Y.6
  • 4
    • 0038054286 scopus 로고    scopus 로고
    • Astructural and functional role for 11-mer repeats in α-synuclein and other exchangeable lipid binding proteins
    • Bussell R. and Eliezer D. (2003) Astructural and functional role for 11-mer repeats in α-synuclein and other exchangeable lipid binding proteins. J. Mol. Biol. 329, 763-778.
    • (2003) J. Mol. Biol. , vol.329 , pp. 763-778
    • Bussell, R.1    Eliezer, D.2
  • 7
    • 0033215063 scopus 로고    scopus 로고
    • Synucleins in synaptic plasticity and neurodegenerative disorders
    • Clayton D. F. and George J. M. (1999) Synucleins in synaptic plasticity and neurodegenerative disorders. J. Neurosci. Res. 58, 120-129.
    • (1999) J. Neurosci. Res. , vol.58 , pp. 120-129
    • Clayton, D.F.1    George, J.M.2
  • 8
    • 0037155197 scopus 로고    scopus 로고
    • Lipid droplet binding and oligomerization properties of the Parkinson's disease protein α-synuclein
    • Cole N. B., Murphy D. D., Grider T., Rueter S., Brasaemle D., and Nussbaum R. L. (2002) Lipid droplet binding and oligomerization properties of the Parkinson's disease protein α-synuclein. J. Biol. Chem. 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
  • 9
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson 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 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
  • 10
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway K. A., Harper J. D., and Lansbury P. T., Jr. (2000) Fibrils formed in vitro from α-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 Jr., P.T.3
  • 11
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct
    • Conway K. A., Rochet J.-C., Bieganski R. M., and Lansbury P. T., Jr. (2001) Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-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 Jr., P.T.4
  • 12
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W. S., Jonas A., Clayton D. F., and George J. M. (1998) Stabilization of α-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
    • 0036829946 scopus 로고    scopus 로고
    • Neuroprotective and neurorestorative strategies for Parkinson's disease
    • Dawson T. M. and Dawson V. L. (2002) Neuroprotective and neurorestorative strategies for Parkinson's disease. Nat. Neurosci. Suppl. 5, 1058-1061.
    • (2002) Nat. Neurosci. Suppl. , vol.5 , pp. 1058-1061
    • Dawson, T.M.1    Dawson, V.L.2
  • 14
    • 0037072284 scopus 로고    scopus 로고
    • Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • Ding T. T., Lee S.- J., Rochet J.- C , and Lansbury P. T., Jr. (2002) Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry 41, 10209-10217.
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Rochet, J.C.3    Lansbury Jr., P.T.4
  • 15
    • 0040368216 scopus 로고    scopus 로고
    • Prospects for new restorative and neuroprotective treatments in Parkinson's disease
    • Dunnett S. B. and Bjorklund A. (1999) Prospects for new restorative and neuroprotective treatments in Parkinson's disease. Nature (Suppl.)399, A32-A39.
    • (1999) Nature (Suppl.) , vol.399
    • Dunnett, S.B.1    Bjorklund, A.2
  • 16
    • 0032573289 scopus 로고    scopus 로고
    • Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α-synuclein protein implicated in Parkinson's disease
    • El-Agnaf O. M., Jakes R., Curran M. D , and Wallace A. (1998) Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α-synuclein protein implicated in Parkinson's disease. FEBS Lett. 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
  • 17
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • Eliezer D., Kutluay E., Bussell R., Jr., and Browne G. (2001) Conformational properties of α-synuclein in its free and lipid-associated states. J. Mol. Biol. 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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly
    • Giasson B. I., Murray I. V., Trojanowski J. Q., and Lee V. M. (2001) A hydrophobic stretch of 12 amino acid residues in the middle of α-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
  • 21
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human α-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson B. I., Uryu K., Trojanowski J. Q., and Lee V. M.-Y. (1999) Mutant and wild type human α-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 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.-Y.4
  • 22
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β-protein
    • Harper J. D., Lieber C. M., and Lansbury P. T., Jr. (1997a) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β-protein. Chem. Biol. 4, 951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury Jr., P.T.3
  • 23
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper J. D., Wong S. S., Lieber C. M., and Lansbury P. T., Jr. (1997b) Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125.
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 24
    • 0032551656 scopus 로고    scopus 로고
    • Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease
    • Hashimoto M., Hsu L. J., Sisk A., Xia Y., Takeda A., Sundsmo M., and Masliah E. (1998) Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: relevance for Lewy body disease. Brain Res. 799, 301-306.
    • (1998) Brain Res. , vol.799 , pp. 301-306
    • Hashimoto, M.1    Hsu, L.J.2    Sisk, A.3    Xia, Y.4    Takeda, A.5    Sundsmo, M.6    Masliah, E.7
  • 25
    • 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., et al. (1995) The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 14, 467-475.
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.4    Flanagan, L.5    De Silva, H.A.6
  • 26
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes R., Spillantini M. G., and Goedert M. (1994) Identification of two distinct synucleins from human brain. FEBS Lett. 345, 27-32.
    • (1994) FEBS Lett. , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 27
    • 0032500599 scopus 로고    scopus 로고
    • Binding of α-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • Jensen P. H., Nielsen M. S., Jakes R., Dotti C. G., and Goedert M. (1998) Binding of α-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J. Biol. Chem. 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
  • 28
    • 0036307753 scopus 로고    scopus 로고
    • Defective membrane interactions of familial Parkinson's disease mutant A30P α-synuclein
    • Jo E., Fuller N., Rand R. P., St. George-Hyslop P., and Fraser P. E. (2002) Defective membrane interactions of familial Parkinson's disease mutant A30P α-synuclein. J. Mol. Biol. 315, 799-807.
    • (2002) J. Mol. Biol. , vol.315 , pp. 799-807
    • Jo, E.1    Fuller, N.2    Rand, R.P.3    St. George-Hyslop, P.4    Fraser, P.E.5
  • 30
    • 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., et al. (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
  • 31
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
    • Kruger R., Kühn W., Muller T., Woitalla D., Graeber M., Kosel S., et al. (1998) Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nat. Genet. 18, 106-108.
    • (1998) Nat. Genet. , vol.18 , pp. 106-108
    • Kruger, R.1    Kühn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 32
    • 0036415838 scopus 로고    scopus 로고
    • α-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., and Lansbury P. T., Jr. (2002) α-Synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 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
  • 33
    • 0037016741 scopus 로고    scopus 로고
    • Membrane-bound α-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form
    • Lee H.-J., Choi C., and Lee S.-J. (2002) Membrane-bound α-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. J. Biol. Chem. 277, 671-678.
    • (2002) J. Biol. Chem. , vol.277 , pp. 671-678
    • Lee, H.-J.1    Choi, C.2    Lee, S.-J.3
  • 34
    • 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 α-synuclein
    • Li J., Uversky V. N., and Fink A. L. (2001) Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein. Biochemistry 40, 11604-11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 35
    • 0036777533 scopus 로고    scopus 로고
    • Conformational behavior of human α-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T
    • Li J., Uversky V. N., and Fink A. L. (2002) Conformational behavior of human α-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T. Neurotoxicology 23, 553-567.
    • (2002) Neurotoxicology , vol.23 , pp. 553-567
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 36
    • 0037064078 scopus 로고    scopus 로고
    • Effect of mutant α-synuclein on dopamine homeostasis in a new human mesencephalic cell line
    • Lotharius J., Barg S., Wiekop P., Lundberg C., Raymon H. K., and Brundin P. (2002) Effect of mutant α-synuclein on dopamine homeostasis in a new human mesencephalic cell line. J. Biol. Chem. 277, 38884-38894.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38884-38894
    • Lotharius, J.1    Barg, S.2    Wiekop, P.3    Lundberg, C.4    Raymon, H.K.5    Brundin, P.6
  • 37
    • 0023722437 scopus 로고
    • Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • Maroteaux L., Campanelli J. T., and Scheller R. H. (1988) Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8, 2804-2815.
    • (1988) J. Neurosci. , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 38
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in α-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 α-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
  • 39
    • 0033515471 scopus 로고    scopus 로고
    • Both familial Parkinson's disease mutations accelerate α-synuclein aggregation
    • Narhi L., Wood S. J., Steavenson S., Jiang Y., Wu G. M., Anafi D., et al. (1999) Both familial Parkinson's disease mutations accelerate α-synuclein aggregation. J. Biol. Chem. 274, 9843-9846.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9843-9846
    • Narhi, L.1    Wood, S.J.2    Steavenson, S.3    Jiang, Y.4    Wu, G.M.5    Anafi, D.6
  • 40
    • 0036182026 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson's disease
    • Orth M. and Schapira A. H. (2002) Mitochondrial involvement in Parkinson's disease. Neurochem. Int. 40, 533-541.
    • (2002) Neurochem. Int. , vol.40 , pp. 533-541
    • Orth, M.1    Schapira, A.H.2
  • 41
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into α-synuclein biology and pathobiology
    • Outeiro T. F., Lindquist S. (2003) Yeast cells provide insight into α-synuclein biology and pathobiology. Science 302, 1772-1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 42
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human α-synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis
    • Perrin R. J., Woods W. S., Clayton D. F., and George J. M. (2000) Interaction of human α-synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J. Biol. Chem. 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
  • 44
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-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 α-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
  • 45
    • 0036100742 scopus 로고    scopus 로고
    • Environment, mitochondria, and Parkinson's disease
    • Sherer T. B., Betarbet R., and Greenamyre J. T. (2002) Environment, mitochondria, and Parkinson's disease. Neuroscientist 8, 192-197.
    • (2002) Neuroscientist , vol.8 , pp. 192-197
    • Sherer, T.B.1    Betarbet, R.2    Greenamyre, J.T.3
  • 46
    • 0037229425 scopus 로고    scopus 로고
    • Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and α-synuclein aggregation
    • Sherer T. B., Kim J. H., Betarbet R., and Greenamyre J. T. (2003) Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and α-synuclein aggregation. Exp. Neurol. 179, 9-16.
    • (2003) Exp. Neurol. , vol.179 , pp. 9-16
    • Sherer, T.B.1    Kim, J.H.2    Betarbet, R.3    Greenamyre, J.T.4
  • 47
    • 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
  • 49
    • 0035706436 scopus 로고    scopus 로고
    • The cellular pathology of Parkinson's disease
    • Takahashi H. and Wakabayashi K. (2001). The cellular pathology of Parkinson's disease. Neuropathology 21, 315-322.
    • (2001) Neuropathology , vol.21 , pp. 315-322
    • Takahashi, H.1    Wakabayashi, K.2
  • 50
    • 0031474418 scopus 로고    scopus 로고
    • Contribution of somal Lewy bodies to neuronal death
    • Tompkins M. M. and Hill W. D. (1997) Contribution of somal Lewy bodies to neuronal death. Brain Res. 775, 24-29.
    • (1997) Brain Res. , vol.775 , pp. 24-29
    • Tompkins, M.M.1    Hill, W.D.2
  • 51
  • 52
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar α-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., and Lansbury P. T., Jr. (2001) Vesicle permeabilization by protofibrillar α-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 Jr., P.T.7
  • 53
  • 54
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh D. M., Lomakin A., Benedek G. B., Condron M. M., and Teplow D. B. (1997) Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272, 22364-22372.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 55
    • 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., Jr. (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 Jr., P.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.