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New animal models for Parkinson's disease
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Dawson T.M. New animal models for Parkinson's disease. Cell. 101:2000;115-118.
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Dawson, T.M.1
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Pramipexole vs levodopa as initial treatment for Parkinson disease: A randomized controlled trial
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Parkinson Study Group . Pramipexole vs levodopa as initial treatment for Parkinson disease: a randomized controlled trial. J Am Med Assoc. 284:2000;1931-1938.
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Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
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Polymeropoulos M.H., Lavedan C., Leroy E., Ide S.E., Dehejia A., Dutra A., Pike B., Root H., Rubenstein J., Boyer R., et al. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science. 276:1997;2045-2047.
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Polymeropoulos, M.H.1
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Dehejia, A.5
Dutra, A.6
Pike, B.7
Root, H.8
Rubenstein, J.9
Boyer, R.10
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4
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0035526288
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Clinical features of parkinsonian patients with the alpha-synuclein (G209A) mutation
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Bostantjopoulou S., Katsarou Z., Papadimitriou A., Veletza V., Hatzigeorgiou G., Lees A. Clinical features of parkinsonian patients with the alpha-synuclein (G209A) mutation. Mov Disord. 16:2001;1007-1013.
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Bostantjopoulou, S.1
Katsarou, Z.2
Papadimitriou, A.3
Veletza, V.4
Hatzigeorgiou, G.5
Lees, A.6
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5
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0035031258
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Clinical phenotype in patients with alpha-synuclein Parkinson's disease living in Greece in comparison with patients with sporadic Parkinson's disease
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Papapetropoulos S., Paschalis C., Athanassiadou A., Papadimitriou A., Ellul J., Polymeropoulos M.H., Papapetropoulos T. Clinical phenotype in patients with alpha-synuclein Parkinson's disease living in Greece in comparison with patients with sporadic Parkinson's disease. J Neurol Neurosurg Psychiatry. 70:2001;662-665.
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Papapetropoulos, S.1
Paschalis, C.2
Athanassiadou, A.3
Papadimitriou, A.4
Ellul, J.5
Polymeropoulos, M.H.6
Papapetropoulos, T.7
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6
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0035097503
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Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr alpha-synuclein mutation
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Description of clinical and neuropathological features highly atypical of PD in an Australian family with the A53T mutation of the α-synuclein gene.
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Spira P.J., Sharpe D.M., Halliday G., Cavanagh J., Nicholson G.A. Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr alpha-synuclein mutation. Ann Neurol. 49:2001;313-319. Description of clinical and neuropathological features highly atypical of PD in an Australian family with the A53T mutation of the α-synuclein gene.
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Ann Neurol
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Spira, P.J.1
Sharpe, D.M.2
Halliday, G.3
Cavanagh, J.4
Nicholson, G.A.5
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7
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0031990490
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Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
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Kruger R., Kuhn W., Muller T., Woitalla D., Graeber M., Kosel S., Przuntek H., Epplen J.T., Schols L., Riess O. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat Genet. 18:1998;106-108.
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Kruger, R.1
Kuhn, W.2
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Woitalla, D.4
Graeber, M.5
Kosel, S.6
Przuntek, H.7
Epplen, J.T.8
Schols, L.9
Riess, O.10
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8
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18544406092
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Parkinson's disease is not associated with the combined alpha-synuclein/apolipoprotein E susceptibility genotype
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Khan N., Graham E., Dixon P., Morris C., Mander A., Clayton D., Vaughan J., Quinn N., Lees A., Daniel S., et al. Parkinson's disease is not associated with the combined alpha-synuclein/apolipoprotein E susceptibility genotype. Ann Neurol. 49:2001;665-668.
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Ann Neurol
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Khan, N.1
Graham, E.2
Dixon, P.3
Morris, C.4
Mander, A.5
Clayton, D.6
Vaughan, J.7
Quinn, N.8
Lees, A.9
Daniel, S.10
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9
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0035831303
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Genetic studies in Parkinson's disease with an alpha-synuclein/NACP gene polymorphism in Japan
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Izumi Y., Morino H., Oda M., Maruyama H., Udaka F., Kameyama M., Nakamura S., Kawakami H. Genetic studies in Parkinson's disease with an alpha-synuclein/NACP gene polymorphism in Japan. Neurosci Lett. 300:2001;125-127.
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Neurosci Lett
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Izumi, Y.1
Morino, H.2
Oda, M.3
Maruyama, H.4
Udaka, F.5
Kameyama, M.6
Nakamura, S.7
Kawakami, H.8
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10
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0035880458
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Alpha-Synuclein gene haplotypes are associated with Parkinson's disease
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Farrer M., Maraganore D.M., Lockhart P., Singleton A., Lesnick T.G., de Andrade M., West A., de Silva R., Hardy J., Hernandez D. alpha-Synuclein gene haplotypes are associated with Parkinson's disease. Hum Mol Genet. 10:2001;1847-1851.
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(2001)
Hum Mol Genet
, vol.10
, pp. 1847-1851
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Farrer, M.1
Maraganore, D.M.2
Lockhart, P.3
Singleton, A.4
Lesnick, T.G.5
De Andrade, M.6
West, A.7
De Silva, R.8
Hardy, J.9
Hernandez, D.10
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11
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0034681163
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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
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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. 97:2000;571-576.
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Proc Natl Acad Sci USA
, vol.97
, pp. 571-576
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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
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12
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0035941305
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Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations
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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. 276:2001;43495-43498.
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(2001)
J Biol Chem
, vol.276
, pp. 43495-43498
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Uversky, V.N.1
Lee, H.J.2
Li, J.3
Fink, A.L.4
Lee, S.J.5
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13
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0035815664
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Evidence for a partially folded intermediate in alpha-synuclein fibril formation
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Uversky V.N., Li J., Fink A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J Biol Chem. 276:2001;10737-10744.
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(2001)
J Biol Chem
, vol.276
, pp. 10737-10744
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Uversky, V.N.1
Li, J.2
Fink, A.L.3
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14
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0035815115
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Conformational properties of alpha-synuclein in its free and lipid-associated states
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Using NMR, Eliezer et al. find that free monomeric wild-type α-synuclein exists in a mostly unfolded state in solution but shows a region with a preference for helical conformations that may be important for the known propensity of α-synuclein to aggregate into fibrils.
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Eliezer D., Kutluay E., Bussell R. Jr, Browne G. Conformational properties of alpha-synuclein in its free and lipid-associated states. J Mol Biol. 307:2001;1061-1073. Using NMR, Eliezer et al. find that free monomeric wild-type α-synuclein exists in a mostly unfolded state in solution but shows a region with a preference for helical conformations that may be important for the known propensity of α-synuclein to aggregate into fibrils.
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(2001)
J Mol Biol
, vol.307
, pp. 1061-1073
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Eliezer, D.1
Kutluay, E.2
Bussell R., Jr.3
Browne, G.4
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15
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0035800097
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Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
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One of us (PL) has demonstrated that protofibrils are rich in β-sheet structure and bind membrane surfaces much more avidly than either monomer or fibril. Furthermore, protofibrils permeabilize synthetic vesicles and lead to destruction of vesicular membranes, as demonstrated by atomic force microscopy.
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Volles M.J., Lee S.J., Rochet J.C., Shtilerman M.D., Ding T.T., Kessler J.C., Lansbury P.T. Jr. Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry. 40:2001;7812-7819. One of us (PL) has demonstrated that protofibrils are rich in β-sheet structure and bind membrane surfaces much more avidly than either monomer or fibril. Furthermore, protofibrils permeabilize synthetic vesicles and lead to destruction of vesicular membranes, as demonstrated by atomic force microscopy.
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(2001)
Biochemistry
, vol.40
, pp. 7812-7819
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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
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16
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0035951869
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A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
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Giasson B.I., Murray I.V., Trojanowski J.Q., Lee V.M. A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J Biol Chem. 276:2001;2380-2386.
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(2001)
J Biol Chem
, vol.276
, pp. 2380-2386
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Giasson, B.I.1
Murray, I.V.2
Trojanowski, J.Q.3
Lee, V.M.4
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17
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0035941201
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Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
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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. 276:2001;44284-44296.
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(2001)
J Biol Chem
, vol.276
, pp. 44284-44296
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Uversky, V.N.1
Li, J.2
Fink, A.L.3
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18
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0035816404
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Pesticides directly accelerate the rate of alpha-synuclein fibril formation: A possible factor in Parkinson's disease
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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. 500:2001;105-108.
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(2001)
FEBS Lett
, vol.500
, pp. 105-108
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Uversky, V.N.1
Li, J.2
Fink, A.L.3
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19
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0035979233
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Alpha-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins
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This paper provides data to support the idea that α-synuclein is a fatty acid binding protein, and is associated with membrane compartments in cells. This possible function is consistent with the localization of α-synuclein to plasma membranes, which is disrupted by the A30P mutation.
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Sharon R., Goldberg M.S., Bar-Josef I., Betensky R.A., Shen J., Selkoe D.J. alpha-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins. Proc Natl Acad Sci USA. 98:2001;9110-9115. This paper provides data to support the idea that α-synuclein is a fatty acid binding protein, and is associated with membrane compartments in cells. This possible function is consistent with the localization of α-synuclein to plasma membranes, which is disrupted by the A30P mutation.
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(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 9110-9115
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Sharon, R.1
Goldberg, M.S.2
Bar-Josef, I.3
Betensky, R.A.4
Shen, J.5
Selkoe, D.J.6
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20
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0035066885
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Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
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Lee F.J., Liu F., Pristupa Z.B., Niznik H.B. Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB J. 15:2001;916-926.
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(2001)
FASEB J
, vol.15
, pp. 916-926
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Lee, F.J.1
Liu, F.2
Pristupa, Z.B.3
Niznik, H.B.4
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21
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0037155197
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Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein
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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. 277:2002;6344-6352.
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(2002)
J Biol Chem
, vol.277
, pp. 6344-6352
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Cole, N.B.1
Murphy, D.D.2
Grider, T.3
Rueter, S.4
Brasaemle, D.5
Nussbaum, R.L.6
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22
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0035928748
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Membrane binding and self-association of alpha-synucleins
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Narayanan V., Scarlata S. Membrane binding and self-association of alpha-synucleins. Biochemistry. 40:2001;9927-9934.
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(2001)
Biochemistry
, vol.40
, pp. 9927-9934
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Narayanan, V.1
Scarlata, S.2
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23
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0035834655
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Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins
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Perrin R.J., Woods W.S., Clayton D.F., George J.M. Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J Biol Chem. 276:2001;41958-41962.
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(2001)
J Biol Chem
, vol.276
, pp. 41958-41962
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Perrin, R.J.1
Woods, W.S.2
Clayton, D.F.3
George, J.M.4
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24
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0035854437
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Ubiquitination of a new form of alpha-synuclein by parkin from human brain: Implications for Parkinson's disease
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Shimura et al. identify a protein complex in normal human brain that includes parkin as the E3 ubiquitin ligase (UbcH7) as its associated E2 ubiquitin conjugating enzyme, in addition to a new 22kD glycosylated form of α-synuclein (alphaSp22) as its substrate. They report that, in contrast to normal parkin, mutant parkin associated with autosomal recessive PD fails to bind alphaSp22. Furthermore, in an in vitro ubiquitination assay, alphaSp22 is reported to be modified by normal but not the mutant parkin into a high molecular weight poly-ubiquitinated species. They further report that alphaSp22 accumulates in a non-ubiquitinated form in the parkin-deficient PD brains. The authors conclude that alphaSp22 is a substrate for parkin's ubiquitin ligase activity in normal human brain and that loss of parkin function causes pathological alphaSp22 accumulation.
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Shimura H., Schlossmacher M.G., Hattori N., Frosch M.P., Trockenbacher A., Schneider R., Mizuno Y., Kosik K.S., Selkoe D.J. Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science. 293:2001;263-269. Shimura et al. identify a protein complex in normal human brain that includes parkin as the E3 ubiquitin ligase (UbcH7) as its associated E2 ubiquitin conjugating enzyme, in addition to a new 22kD glycosylated form of α-synuclein (alphaSp22) as its substrate. They report that, in contrast to normal parkin, mutant parkin associated with autosomal recessive PD fails to bind alphaSp22. Furthermore, in an in vitro ubiquitination assay, alphaSp22 is reported to be modified by normal but not the mutant parkin into a high molecular weight poly-ubiquitinated species. They further report that alphaSp22 accumulates in a non-ubiquitinated form in the parkin-deficient PD brains. The authors conclude that alphaSp22 is a substrate for parkin's ubiquitin ligase activity in normal human brain and that loss of parkin function causes pathological alphaSp22 accumulation.
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(2001)
Science
, vol.293
, pp. 263-269
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Shimura, H.1
Schlossmacher, M.G.2
Hattori, N.3
Frosch, M.P.4
Trockenbacher, A.5
Schneider, R.6
Mizuno, Y.7
Kosik, K.S.8
Selkoe, D.J.9
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25
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0035860682
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Tetrahydrobiopterin scavenges superoxide in dopaminergic neurons
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Nakamura K., Bindokas V.P., Kowlessur D., Elas M., Milstien S., Marks J.D., Halpern H.J., Kang U.J. Tetrahydrobiopterin scavenges superoxide in dopaminergic neurons. J Biol Chem. 276:2001;34402-34407.
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(2001)
J Biol Chem
, vol.276
, pp. 34402-34407
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Nakamura, K.1
Bindokas, V.P.2
Kowlessur, D.3
Elas, M.4
Milstien, S.5
Marks, J.D.6
Halpern, H.J.7
Kang, U.J.8
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26
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0035830913
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Alpha-synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases
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Ellis C.E., Schwartzberg P.L., Grider T.L., Fink D.W., Nussbaum R.L. alpha-synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases. J Biol Chem. 276:2001;3879-3884.
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(2001)
J Biol Chem
, vol.276
, pp. 3879-3884
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Ellis, C.E.1
Schwartzberg, P.L.2
Grider, T.L.3
Fink, D.W.4
Nussbaum, R.L.5
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27
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0035144650
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Oxidative post-translational modifications of alpha-synuclein in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease
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Przedborski S., Chen Q., Vila M., Giasson B.I., Djaldatti R., Vukosavic S., Souza J.M., Jackson-Lewis V.V., Lee V.M., Ischiropoulos H. Oxidative post-translational modifications of alpha-synuclein in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease. J Neurochem. 76:2001;637-640.
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(2001)
J Neurochem
, vol.76
, pp. 637-640
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Przedborski, S.1
Chen, Q.2
Vila, M.3
Giasson, B.I.4
Djaldatti, R.5
Vukosavic, S.6
Souza, J.M.7
Jackson-Lewis, V.V.8
Lee, V.M.9
Ischiropoulos, H.10
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28
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0035834360
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Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
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One of us (PL) has shown that an in vitro incubation of α-synuclein with dopamine and structurally related catecholamines, results in a covalently modified protein adduct (DA-α-synuclein); furthermore, the DA-α-synuclein adduct was shown to selectively inhibit protofibril → fibril conversion, resulting in accumulation of the α-synuclein protofibril, a presumably neurotoxic species. This finding suggests that cytosolic dopamine under oxidative stress conditions leads to accumulation of a toxic protofibrillar intermediate(s), and provides an explanation for the dopaminergic selectivity of α-synuclein associated neurotoxicity in PD.
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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. 294:2001;1346-1349. One of us (PL) has shown that an in vitro incubation of α-synuclein with dopamine and structurally related catecholamines, results in a covalently modified protein adduct (DA-α-synuclein); furthermore, the DA-α-synuclein adduct was shown to selectively inhibit protofibril → fibril conversion, resulting in accumulation of the α-synuclein protofibril, a presumably neurotoxic species. This finding suggests that cytosolic dopamine under oxidative stress conditions leads to accumulation of a toxic protofibrillar intermediate(s), and provides an explanation for the dopaminergic selectivity of α-synuclein associated neurotoxicity in PD.
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(2001)
Science
, vol.294
, pp. 1346-1349
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Conway, K.A.1
Rochet, J.C.2
Bieganski, R.M.3
Lansbury P.T., Jr.4
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29
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0035964758
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Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease
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Rockenstein E., Hansen L.A., Mallory M., Trojanowski J.Q., Galasko D., Masliah E. Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease. Brain Res. 914:2001;48-56.
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(2001)
Brain Res
, vol.914
, pp. 48-56
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Rockenstein, E.1
Hansen, L.A.2
Mallory, M.3
Trojanowski, J.Q.4
Galasko, D.5
Masliah, E.6
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30
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0035950270
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Beta-Synuclein inhibits alpha-synuclein aggregation: A possible role as an anti-parkinsonian factor
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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. 32:2001;213-223.
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(2001)
Neuron
, vol.32
, pp. 213-223
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Hashimoto, M.1
Rockenstein, E.2
Mante, M.3
Mallory, M.4
Masliah, E.5
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31
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0035500991
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Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells
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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. 95:2001;138-145.
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(2001)
Brain Res Mol Brain Res
, vol.95
, pp. 138-145
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Payton, J.E.1
Perrin, R.J.2
Clayton, D.F.3
George, J.M.4
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32
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0034996655
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Interaction of alpha-synuclein and synphilin-1: Effect of Parkinson's disease-associated mutations
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Kawamata H., McLean P.J., Sharma N., Hyman B.T. Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations. J Neurochem. 77:2001;929-934.
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(2001)
J Neurochem
, vol.77
, pp. 929-934
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Kawamata, H.1
McLean, P.J.2
Sharma, N.3
Hyman, B.T.4
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33
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0035066885
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Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
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Lee F.J., Liu F., Pristupa Z.B., Niznik H.B. Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB J. 15:2001;916-926.
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(2001)
FASEB J
, vol.15
, pp. 916-926
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Lee, F.J.1
Liu, F.2
Pristupa, Z.B.3
Niznik, H.B.4
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34
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0035132189
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No evidence of association between a dopamine transporter gene polymorphism (1215A/G) and Parkinson's disease
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Kimura M., Matsushita S., Arai H., Takeda A., Higuchi S. No evidence of association between a dopamine transporter gene polymorphism (1215A/G) and Parkinson's disease. Ann Neurol. 49:2001;276-277.
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(2001)
Ann Neurol
, vol.49
, pp. 276-277
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Kimura, M.1
Matsushita, S.2
Arai, H.3
Takeda, A.4
Higuchi, S.5
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35
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0035029340
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Genetic analysis of synphilin-1 in familial Parkinson's disease
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Farrer M., Destee A., Levecque C., Singleton A., Engelender S., Becquet E., Mouroux V., Richard F., Defebvre L., Crook R., et al. Genetic analysis of synphilin-1 in familial Parkinson's disease. Neurobiol Dis. 8:2001;317-323.
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(2001)
Neurobiol Dis
, vol.8
, pp. 317-323
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Farrer, M.1
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Park7, a novel locus for autosomal recessive early-onset parkinsonism, on chromosome 1p36
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This study of an isolate from the south-west of the Netherlands enabled the gene for a new form of autosomal recessive early-onset parkinsonism to be mapped to chromosome 1p36.
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van Duijn C.M., Dekker M.C., Bonifati V., Galjaard R.J., Houwing-Duistermaat J.J., Snijders P.J., Testers L., Breedveld G.J., Horstink M., Sandkuijl L.A., et al. Park7, a novel locus for autosomal recessive early-onset parkinsonism, on chromosome 1p36. Am J Hum Genet. 69:2001;629-634. This study of an isolate from the south-west of the Netherlands enabled the gene for a new form of autosomal recessive early-onset parkinsonism to be mapped to chromosome 1p36.
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Localization of autosomal recessive early-onset parkinsonism to chromosome 1p36 (PARK7) in an independent dataset
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A new locus for Parkinson's disease (PARK8) maps to chromosome 12p11.2-q13.1
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The study of a large Japanese family with autosomal-dominant parkinsonism permitting the mapping of PARK8 to chromosome 12p11.2-q13.1. Patients present with dopa-responsive parkinsonism, caused by pure nigral degeneration without Lewy bodies.
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Genome-wide scan for Parkinson's disease: The GenePD Study
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DeStefano A.L., Golbe L.I., Mark M.H., Lazzarini A.M., Maher N.E., Saint-Hilaire M., Feldman R.G., Guttman M., Watts R.L., Suchowersky O., et al. Genome-wide scan for Parkinson's disease: the GenePD Study. Neurology. 57:2001;1124-1126.
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Familial atypical progressive supranuclear palsy associated with homozigosity for the delN296 mutation in the tau gene
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The tau A0 allele in Parkinson's disease
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Golbe L.I., Lazzarini A.M., Spychala J.R., Johnson W.G., Stenroos E.S., Mark M.H., Sage J.I. The tau A0 allele in Parkinson's disease. Mov Disord. 16:2001;442-447.
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A susceptibility gene to late-onset idiopathic Parkinson's disease successfully mapped [Abstract 123]
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