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Volumn 24, Issue 1, 2003, Pages 91-105

Mutations in the lipid-binding domain of α-synuclein confer overlapping, yet distinct, functional properties in the regulation of dopamine transporter activity

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMINO ACID; COMPLEMENTARY DNA; DOPAMINE RECEPTOR; DOPAMINE TRANSPORTER; LIPID; MUTANT PROTEIN;

EID: 0141726844     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1044-7431(03)00124-6     Document Type: Article
Times cited : (48)

References (64)
  • 2
    • 0034993599 scopus 로고    scopus 로고
    • Molecular pathways involved in the neurotoxicity of 6-OHDA, dopamine and MPTP: Contribution to the apoptotic theory in Parkinson's disease
    • Blum D., Torch S., Lambeng N., Nissou M., Benabid A.L., Sadoul R. Molecular pathways involved in the neurotoxicity of 6-OHDA, dopamine and MPTP: contribution to the apoptotic theory in Parkinson's disease. Prog. Neurobiol. 65:2001;135-172.
    • (2001) Prog. Neurobiol , vol.65 , pp. 135-172
    • Blum, D.1    Torch, S.2    Lambeng, N.3    Nissou, M.4    Benabid, A.L.5    Sadoul, R.6
  • 3
    • 0031900214 scopus 로고    scopus 로고
    • Absence of mutations in the coding region of the alpha-synuclein gene in pathologically proven Parkinson's disease
    • Chan P., Jiang X., Forno L.S., DiMonte D.A., Tanner C.M., Langston J.W. Absence of mutations in the coding region of the alpha-synuclein gene in pathologically proven Parkinson's disease. Neurology. 50:1998;1136-1137.
    • (1998) Neurology , vol.50 , pp. 1136-1137
    • Chan, P.1    Jiang, X.2    Forno, L.S.3    DiMonte, D.A.4    Tanner, C.M.5    Langston, J.W.6
  • 5
    • 0032102455 scopus 로고    scopus 로고
    • The synucleins: A family of proteins involved in synaptic function, plasticity, neurodegeneration and disease
    • Clayton D.F., George J.M. The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease. Trends Neurosci. 21:1998;249-254.
    • (1998) Trends Neurosci , vol.21 , pp. 249-254
    • Clayton, D.F.1    George, J.M.2
  • 6
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway K.A., Harper J.D., Lansbury P.T. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med. 4:1998;1318-1320.
    • (1998) Nat. Med , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 7
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., Lansbury P.T. Jr. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. USA. 97:2000;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
  • 8
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway K.A., Rochet J.C., Bieganski R.M., Lansbury P.T. Jr. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science. 294:2001;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
  • 9
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273:1998;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
  • 10
    • 0028089896 scopus 로고
    • Expression of inducible nitric oxide synthase causes delayed neurotoxicity in primary mixed neuronal-glial cortical cultures
    • Dawson V.L., Brahmbhatt H.P., Mong J.A., Dawson T.M. Expression of inducible nitric oxide synthase causes delayed neurotoxicity in primary mixed neuronal-glial cortical cultures. Neuropharmacology. 33:1994;1425-1430.
    • (1994) Neuropharmacology , vol.33 , pp. 1425-1430
    • Dawson, V.L.1    Brahmbhatt, H.P.2    Mong, J.A.3    Dawson, T.M.4
  • 11
    • 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., Wallace A. 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. 440:1998;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
  • 12
    • 0033850190 scopus 로고    scopus 로고
    • Review: Formation and properties of amyloid-like fibrils derived from alpha-synuclein and related proteins
    • El-Agnaf O.M., Irvine G.B. Review: formation and properties of amyloid-like fibrils derived from alpha-synuclein and related proteins. J. Struct. Biol. 130:2000;300-309.
    • (2000) J. Struct. Biol , vol.130 , pp. 300-309
    • El-Agnaf, O.M.1    Irvine, G.B.2
  • 13
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • Eliezer D., Kutluay E., Bussell R. Jr., Browne G. Conformational properties of alpha-synuclein in its free and lipid-associated states. J. Mol. Biol. 307:2001;1061-1073.
    • (2001) J. Mol. Biol , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell R., Jr.3    Browne, G.4
  • 14
    • 0032529707 scopus 로고    scopus 로고
    • Multiple-system atrophy: A new alpha-synuclein disease?
    • Gai W.P., Power J.H.T., Blumberg P.C., Blessing W.W. Multiple-system atrophy: a new alpha-synuclein disease? Lancet. 352:1998;547-548.
    • (1998) Lancet , vol.352 , pp. 547-548
    • Gai, W.P.1    Power, J.H.T.2    Blumberg, P.C.3    Blessing, W.W.4
  • 15
    • 0037118259 scopus 로고    scopus 로고
    • Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein
    • Giasson B.I., Duda J.E., Quinn S.M., Zhang B., Trojanowski J.Q., Lee V.M. Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein. Neuron. 34:2002;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.6
  • 16
    • 0031789960 scopus 로고    scopus 로고
    • Lewy body diseases and multiple system atrophy as alpha-synucleinopathies
    • Goedert M., Spillantini M.G. Lewy body diseases and multiple system atrophy as alpha-synucleinopathies. Mol. Psychiatry. 3:1998;462-465.
    • (1998) Mol. Psychiatry , vol.3 , pp. 462-465
    • Goedert, M.1    Spillantini, M.G.2
  • 17
    • 0032191105 scopus 로고    scopus 로고
    • Filamentous nerve cell inclusions in neurodegenerative diseases
    • Goedert M., Spillantini M.G., Davies S.W. Filamentous nerve cell inclusions in neurodegenerative diseases. Curr. Opin. Neurobiol. 8:1998;619-632.
    • (1998) Curr. Opin. Neurobiol , vol.8 , pp. 619-632
    • Goedert, M.1    Spillantini, M.G.2    Davies, S.W.3
  • 18
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar α-synuclein aggregates and precedes the formation of fibrillar inclusion
    • Gosavi N., Lee H.J., Lee J.S., Patel S., Lee S.J. Golgi fragmentation occurs in the cells with prefibrillar α-synuclein aggregates and precedes the formation of fibrillar inclusion. J. Biol. Chem. 277:2002;48984-48992.
    • (2002) J. Biol. Chem , vol.277 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 19
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M., Hsu L.J., Xia Y., Takeda A., Sisk A., Sundsmo M., Masliah E. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. NeuroReport. 10:1999;717-721.
    • (1999) NeuroReport , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6    Masliah, E.7
  • 20
    • 0031944830 scopus 로고    scopus 로고
    • Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity
    • Irizarry M.C., Growdon W., Gomez-Isla T., Newell K., George J.M., Clayton D.F., Hyman B.T. Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity. J. Neuropathol. Exp. Neurol. 57:1998;334-337.
    • (1998) J. Neuropathol. Exp. Neurol , vol.57 , pp. 334-337
    • Irizarry, M.C.1    Growdon, W.2    Gomez-Isla, T.3    Newell, K.4    George, J.M.5    Clayton, D.F.6    Hyman, B.T.7
  • 21
    • 0034889140 scopus 로고    scopus 로고
    • Postnatal expression of alpha-synuclein protein in rodent substantia nigra and striatum
    • Jakowec M.W., Donaldson D.M., Barba J., Petzinger G.M. Postnatal expression of alpha-synuclein protein in rodent substantia nigra and striatum. Dev. Neurosci. 23:2001;91-99.
    • (2001) Dev. Neurosci , vol.23 , pp. 91-99
    • Jakowec, M.W.1    Donaldson, D.M.2    Barba, J.3    Petzinger, G.M.4
  • 22
    • 0032500599 scopus 로고    scopus 로고
    • Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • Jensen P.H., Nielsen M.S., Jakes R., Dotti C.G., Goedert M. Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J. Biol. Chem. 273:1998;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
  • 23
    • 0036307753 scopus 로고    scopus 로고
    • Defective membrane interactions of familial Parkinson's disease mutant A30P alpha-synuclein
    • Jo E., Fuller N., Rand R.P., St. George-Hyslop P., Fraser P.E. Defective membrane interactions of familial Parkinson's disease mutant A30P alpha-synuclein. J. Mol. Biol. 315:2002;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
  • 25
    • 0037040491 scopus 로고    scopus 로고
    • Human alpha-synuclein over-expression increases intracellular reactive oxygen species levels and susceptibility to dopamine
    • Junn E., Mouradian M.M. Human alpha-synuclein over-expression increases intracellular reactive oxygen species levels and susceptibility to dopamine. Neurosci. Lett. 320:2002;146-150.
    • (2002) Neurosci. Lett , vol.320 , pp. 146-150
    • Junn, E.1    Mouradian, M.M.2
  • 26
    • 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., Meyer E.M. Dopaminergic cell loss induced by human A30P alpha-synuclein gene transfer to the rat substantia nigra. Hum. Gene Ther. 13:2002;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
  • 28
    • 0035066885 scopus 로고    scopus 로고
    • Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
    • 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.
    • (2001) FASEB J , vol.15 , pp. 916-926
    • Lee, F.J.1    Liu, F.2    Pristupa, Z.B.3    Niznik, H.B.4
  • 29
    • 0037073747 scopus 로고    scopus 로고
    • Characterization of cytoplasmic alpha-synuclein aggregates: Fibril formation is tightly linked to the inclusion-forming process in cells
    • Lee H.J., Lee S.J. Characterization of cytoplasmic alpha-synuclein aggregates: fibril formation is tightly linked to the inclusion-forming process in cells. J. Biol. Chem. 277:2002;48976-48983.
    • (2002) J. Biol. Chem , vol.277 , pp. 48976-48983
    • Lee, H.J.1    Lee, S.J.2
  • 30
    • 0035109909 scopus 로고    scopus 로고
    • Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult
    • Lee M.H., Hyun D.H., Halliwell B., Jenner P. Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult. J. Neurochem. 76:2001;998-1009.
    • (2001) J. Neurochem , vol.76 , pp. 998-1009
    • Lee, M.H.1    Hyun, D.H.2    Halliwell, B.3    Jenner, P.4
  • 31
    • 0037173006 scopus 로고    scopus 로고
    • Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr 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., Price D.L. Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice. Proc. Natl. Acad. Sci. USA. 99:2002;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
  • 32
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein
    • Li J., Uversky V.N., Fink A.L. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry. 40:2001;11604-11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 33
    • 0037067993 scopus 로고    scopus 로고
    • Differential localization of alpha, beta- and gamma-synucleins in the rat CNS
    • Li J.Y., Henning Jensen P., Dahlstrom A. Differential localization of alpha, beta- and gamma-synucleins in the rat CNS. Neuroscience. 113:2002;463-478.
    • (2002) Neuroscience , vol.113 , pp. 463-478
    • Li, J.Y.1    Henning Jensen, P.2    Dahlstrom, A.3
  • 34
    • 0032990543 scopus 로고    scopus 로고
    • Antibodies to alpha-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease
    • Lippa C.F., Schmidt M.L., Lee V.M., Trojanowski J.Q. Antibodies to alpha-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease. Ann. Neurol. 45:1999;353-357.
    • (1999) Ann. Neurol , vol.45 , pp. 353-357
    • Lippa, C.F.1    Schmidt, M.L.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 35
    • 0036679197 scopus 로고    scopus 로고
    • Alpha-synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease
    • Lo Bianco C.L., Ridet J.L., Schneider B.L., Deglon N., Aebischer P. Alpha-synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease. Proc. Natl. Acad. Sci. USA. 99:2002;10813-10818.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10813-10818
    • Lo Bianco, C.L.1    Ridet, J.L.2    Schneider, B.L.3    Deglon, N.4    Aebischer, P.5
  • 37
    • 0037154184 scopus 로고    scopus 로고
    • Recent advances in the genetics and pathogenesis of Parkinson disease
    • Mouradian M.M. Recent advances in the genetics and pathogenesis of Parkinson disease. Neurology. 58:2002;179-185.
    • (2002) Neurology , vol.58 , pp. 179-185
    • Mouradian, M.M.1
  • 39
    • 0031753789 scopus 로고    scopus 로고
    • - neurotransmitter transporters
    • - neurotransmitter transporters. J. Neurochem. 71:1998;1785-1803.
    • (1998) J. Neurochem , vol.71 , pp. 1785-1803
    • Nelson, N.1
  • 40
  • 42
    • 0034602271 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., George J.M. Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J. Biol. Chem. 275:2000;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
    • 0034752954 scopus 로고    scopus 로고
    • Intracellular retention of the two isoforms of the D(2) dopamine receptor promotes endoplasmic reticulum disruption
    • Prou D., Gu W.J., Le Crom S., Vincent J.D., Salamero J., Vernier P. Intracellular retention of the two isoforms of the D(2) dopamine receptor promotes endoplasmic reticulum disruption. J. Cell Sci. 114:2001;3517-3527.
    • (2001) J. Cell Sci. , vol.114 , pp. 3517-3527
    • Prou, D.1    Gu, W.J.2    Le Crom, S.3    Vincent, J.D.4    Salamero, J.5    Vernier, P.6
  • 45
    • 0036605566 scopus 로고    scopus 로고
    • Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters
    • Rockenstein E., Mallory M., Hashimoto M., Song D., Shults C.W., Lang I., Masliah E. Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters. J. Neurosci. Res. 68:2002;568-578.
    • (2002) J. Neurosci. Res , vol.68 , pp. 568-578
    • Rockenstein, E.1    Mallory, M.2    Hashimoto, M.3    Song, D.4    Shults, C.W.5    Lang, I.6    Masliah, E.7
  • 46
    • 0031746740 scopus 로고    scopus 로고
    • Multiple coupling of human D5 dopamine receptors to guanine nucleotide binding proteins Gs and Gz
    • Sidhu A., Kimura K., Uh M., White B.H., Patel S. Multiple coupling of human D5 dopamine receptors to guanine nucleotide binding proteins Gs and Gz. J. Neurochem. 70:1998;2459-2467.
    • (1998) J. Neurochem , vol.70 , pp. 2459-2467
    • Sidhu, A.1    Kimura, K.2    Uh, M.3    White, B.H.4    Patel, S.5
  • 47
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers: Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • Souza J.M., Giasson B.I., Chen Q., Lee V.M., Ischiropoulos H. Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers: implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 275:2000;18344-18349.
    • (2000) J. Biol. Chem , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 48
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies
    • Spillantini M.G., Crowther R.A., Jakes R., Cairns N.J., Lantos P.L., Goedert M. Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neurosci. Lett. 251:1998;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
  • 49
    • 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. Alpha-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. USA. 95:1998;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
  • 50
    • 0034531475 scopus 로고    scopus 로고
    • The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy
    • Spillantini M.G., Goedert M. The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Ann. N.Y. Acad. Sci. 920:2000;16-27.
    • (2000) Ann. N.Y. Acad. Sci , vol.920 , pp. 16-27
    • Spillantini, M.G.1    Goedert, M.2
  • 53
    • 0031762949 scopus 로고    scopus 로고
    • Fatal attractions: Abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia
    • Trojanowski J.Q., Goedert M., Iwatsubo T., Lee V.M. Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia. Cell Death Differ. 5:1998;832-837.
    • (1998) Cell Death Differ , vol.5 , pp. 832-837
    • Trojanowski, J.Q.1    Goedert, M.2    Iwatsubo, T.3    Lee, V.M.4
  • 54
    • 0031910093 scopus 로고    scopus 로고
    • Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: Implications for the pathogenesis of Parkinson disease and Lewy body dementia
    • Trojanowski J.Q., Lee V.M.Y. Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: implications for the pathogenesis of Parkinson disease and Lewy body dementia. Arch. Neurol. 55:1998;151-152.
    • (1998) Arch. Neurol , vol.55 , pp. 151-152
    • Trojanowski, J.Q.1    Lee, V.M.Y.2
  • 57
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism
    • Volles M.J., Lansbury P.T. Jr. Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. Biochemistry. 41:2002;4595-4602.
    • (2002) Biochemistry , vol.41 , pp. 4595-4602
    • Volles, M.J.1    Lansbury P.T., Jr.2
  • 60
    • 0037448010 scopus 로고    scopus 로고
    • 2 in a human neuroblastoma derived cell line transfected with α-synuclein and its familial Parkinson's disease-linked mutants
    • 2 in a human neuroblastoma derived cell line transfected with α-synuclein and its familial Parkinson's disease-linked mutants. Neurosci. Lett. 342, 124-128.
    • (2003) Neurosci. Lett. , vol.342 , pp. 124-128
    • Wersinger, C.1    Sidhu, A.2
  • 61
    • 0037451858 scopus 로고    scopus 로고
    • Attenuation of dopamine transporter activity by alpha-synuclein
    • Wersinger, C., Sidhu, A., 2003b. Attenuation of dopamine transporter activity by alpha-synuclein. Neurosci. Lett. 340, 189-192.
    • (2003) Neurosci. Lett. , vol.340 , pp. 189-192
    • Wersinger, C.1    Sidhu, A.2
  • 62
    • 0034595728 scopus 로고    scopus 로고
    • Overexpression of human alpha-synuclein causes dopamine neuron death in rat primary culture and immortalized mesencephalon-derived cells
    • Zhou W., Hurlbert M.S., Schaack J., Prasad K.N., Freed C.R. Overexpression of human alpha-synuclein causes dopamine neuron death in rat primary culture and immortalized mesencephalon-derived cells. Brain Res. 866:2000;33-43.
    • (2000) Brain Res , vol.866 , pp. 33-43
    • Zhou, W.1    Hurlbert, M.S.2    Schaack, J.3    Prasad, K.N.4    Freed, C.R.5
  • 63
    • 0036468957 scopus 로고    scopus 로고
    • Overexpression of human alpha-synuclein causes dopamine neuron death in primary human mesencephalic culture
    • Zhou W., Schaack J., Zawada W.M., Freed C.R. Overexpression of human alpha-synuclein causes dopamine neuron death in primary human mesencephalic culture. Brain Res. 926:2002;42-50.
    • (2002) Brain Res , vol.926 , pp. 42-50
    • Zhou, W.1    Schaack, J.2    Zawada, W.M.3    Freed, C.R.4
  • 64
    • 0037930855 scopus 로고    scopus 로고
    • Lipid binding inhibits alpha-synuclein fibril formation
    • Zhu, M., Fink, A.L., 2003. Lipid binding inhibits alpha-synuclein fibril formation. J. Biol. Chem. 278, 16873-16877.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16873-16877
    • Zhu, M.1    Fink, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.