메뉴 건너뛰기




Volumn 375, Issue 5, 2008, Pages 1394-1404

α-Synuclein Selectively Binds to Anionic Phospholipids Embedded in Liquid-Disordered Domains

Author keywords

fluorescence microscopy; giant unilamellar vesicles; lipid domains; mutants; synuclein

Indexed keywords

ALPHA SYNUCLEIN; PHOSPHOLIPID DERIVATIVE;

EID: 37549068169     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.051     Document Type: Article
Times cited : (156)

References (53)
  • 1
    • 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. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8 (1988) 2804-2815
    • (1988) J. Neurosci. , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 2
    • 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 Jr. P.T. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35 (1996) 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
  • 3
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., and George J.M. 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
  • 4
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-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. Interaction of human alpha-synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. 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
  • 6
    • 2942555022 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling
    • Jao C.C., Der-Sarkissian A., Chen J., and Langen R. Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc. Natl Acad. Sci. USA 101 (2004) 8331-8336
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8331-8336
    • Jao, C.C.1    Der-Sarkissian, A.2    Chen, J.3    Langen, R.4
  • 7
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer T.S., Bax A., Cole N.B., and Nussbaum R.L. Structure and dynamics of micelle-bound human alpha-synuclein. J. Biol. Chem. 280 (2005) 9595-9603
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 8
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking α-synuclein
    • Cabin D.E., Shimazu K., Murphy D., Cole N.B., Gottschalk W., McIlwain K.L., et al. Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking α-synuclein. J. Neurosci. 22 (2002) 8797-8807
    • (2002) J. Neurosci. , vol.22 , pp. 8797-8807
    • Cabin, D.E.1    Shimazu, K.2    Murphy, D.3    Cole, N.B.4    Gottschalk, W.5    McIlwain, K.L.6
  • 9
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • Cookson M.R. The biochemistry of Parkinson's disease. Annu. Rev. Biochem. 74 (2005) 29-52
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 10
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy D.D., Rueter S.M., Trojanowski J.Q., and Lee V.M. Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J. Neurosci. 20 (2000) 3214-3220
    • (2000) J. Neurosci. , vol.20 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 11
    • 0029127954 scopus 로고
    • Characterization of a novel protein regulated during the critical period for song learning in the zebra finch
    • George J.M., Jin H., Woods W.S., and Clayton D.F. Characterization of a novel protein regulated during the critical period for song learning in the zebra finch. Neuron 15 (1995) 361-372
    • (1995) Neuron , vol.15 , pp. 361-372
    • George, J.M.1    Jin, H.2    Woods, W.S.3    Clayton, D.F.4
  • 12
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
    • Kruger R., Kuhn W., Muller T., Woitalla D., Graeber M., Kosel S., et al. Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nat. Genet. 18 (1998) 106-108
    • (1998) Nat. Genet. , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 13
    • 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. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 276 (1997) 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
  • 15
    • 0642340696 scopus 로고    scopus 로고
    • Alpha-synuclein gene triplication discovered in Parkinson's disease
    • Bradbury J. Alpha-synuclein gene triplication discovered in Parkinson's disease. Lancet Neurol. 2 (2003) 715
    • (2003) Lancet Neurol. , vol.2 , pp. 715
    • Bradbury, J.1
  • 17
    • 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., and 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
  • 18
    • 4344641972 scopus 로고    scopus 로고
    • Interactions among α-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease
    • Rochet J.C., Outeiro T.F., Conway K.A., Ding T.T., Volles M.J., Lashuel H.A., et al. Interactions among α-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease. J. Mol. Neurosci. 23 (2004) 23-33
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 23-33
    • Rochet, J.C.1    Outeiro, T.F.2    Conway, K.A.3    Ding, T.T.4    Volles, M.J.5    Lashuel, H.A.6
  • 20
    • 0037016741 scopus 로고    scopus 로고
    • Membrane-bound alpha-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. Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. J. Biol. Chem. 277 (2002) 671-678
    • (2002) J. Biol. Chem. , vol.277 , pp. 671-678
    • Lee, H.J.1    Choi, C.2    Lee, S.J.3
  • 21
    • 0037930855 scopus 로고    scopus 로고
    • Lipid binding inhibits α-synuclein fibril formation
    • Zhu M., and Fink A.L. Lipid binding inhibits α-synuclein fibril formation. J. Biol. Chem. 278 (2003) 16873-16877
    • (2003) J. Biol. Chem. , vol.278 , pp. 16873-16877
    • Zhu, M.1    Fink, A.L.2
  • 22
    • 0141891097 scopus 로고    scopus 로고
    • The association of α-synuclein with membranes affects bilayer structure, stability, and fibril formation
    • Zhu M., Li J., and Fink A.L. The association of α-synuclein with membranes affects bilayer structure, stability, and fibril formation. J. Biol. Chem. 278 (2003) 40186-40197
    • (2003) J. Biol. Chem. , vol.278 , pp. 40186-40197
    • Zhu, M.1    Li, J.2    Fink, A.L.3
  • 23
    • 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. Vesicle permeabilization by protofibrillar α-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40 (2001) 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.7
  • 24
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
    • Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., and Lansbury P.T. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl Acad. Sci. USA 97 (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.6
  • 25
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-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. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322 (2002) 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, P.T.7
  • 27
    • 33745279409 scopus 로고    scopus 로고
    • A novel mechanism of interaction between α-synuclein and biological membranes
    • Kim Y.S., Laurine E., Woods W., and Lee S.J. A novel mechanism of interaction between α-synuclein and biological membranes. J. Mol. Biol. 360 (2006) 386-397
    • (2006) J. Mol. Biol. , vol.360 , pp. 386-397
    • Kim, Y.S.1    Laurine, E.2    Woods, W.3    Lee, S.J.4
  • 28
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • Eliezer D., Kutluay E., Bussell Jr. R., and 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 Jr., R.3    Browne, G.4
  • 29
    • 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., and 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
  • 30
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • Rhoades E., Ramlall T.F., Webb W.W., and Eliezer D. Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy. Biophys. J. 90 (2006) 4692-4700
    • (2006) Biophys. J. , vol.90 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 31
    • 33646550550 scopus 로고    scopus 로고
    • The role of rafts in fibrillization and aggregation of prions
    • Pinheiro T.J.T. The role of rafts in fibrillization and aggregation of prions. Chem. Phys. Lipids 141 (2006) 66-71
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 66-71
    • Pinheiro, T.J.T.1
  • 33
    • 0033587719 scopus 로고    scopus 로고
    • Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy
    • Korlach J., Schwille P., Webb W.W., and Feigenson G.W. Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy. Proc. Natl Acad. Sci. USA 96 (1999) 8461-8466
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8461-8466
    • Korlach, J.1    Schwille, P.2    Webb, W.W.3    Feigenson, G.W.4
  • 34
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • Veatch S.L. Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol. Biophys. J. 85 (2003) 3074-3083
    • (2003) Biophys. J. , vol.85 , pp. 3074-3083
    • Veatch, S.L.1
  • 35
    • 33645967519 scopus 로고    scopus 로고
    • Correlated fluorescence-atomic force microscopy of membrane domains: structure of fluorescence probes determines lipid localization
    • Shaw J.E., Epand R.F., Epand R.M., Li Z., Bittman R., and Yip C.M. Correlated fluorescence-atomic force microscopy of membrane domains: structure of fluorescence probes determines lipid localization. Biophys. J. 90 (2006) 2170-2178
    • (2006) Biophys. J. , vol.90 , pp. 2170-2178
    • Shaw, J.E.1    Epand, R.F.2    Epand, R.M.3    Li, Z.4    Bittman, R.5    Yip, C.M.6
  • 36
    • 0029970884 scopus 로고    scopus 로고
    • Adsorption of globular proteins on locally planar surfaces, models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria
    • Chatelier R.C., and Minton A.P. Adsorption of globular proteins on locally planar surfaces, models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria. Biophys. J. 71 (1996) 2367-2374
    • (1996) Biophys. J. , vol.71 , pp. 2367-2374
    • Chatelier, R.C.1    Minton, A.P.2
  • 38
    • 0019319535 scopus 로고
    • Bilayers of phosphatidylglycerol. A deuterium and phosphorus nuclear magnetic resonance study of the head-group region
    • Wohlgemuth R., Waespe-Sarcevic N., and Seelig J. Bilayers of phosphatidylglycerol. A deuterium and phosphorus nuclear magnetic resonance study of the head-group region. Biochemistry 19 (1980) 3315-3321
    • (1980) Biochemistry , vol.19 , pp. 3315-3321
    • Wohlgemuth, R.1    Waespe-Sarcevic, N.2    Seelig, J.3
  • 39
    • 2542461043 scopus 로고    scopus 로고
    • Alpha-synuclein has a high affinity for packing defects in a bilayer membrane-a thermodynamics study
    • Nuscher B., Kamp F., Mehnert T., Odoy S., Haass C., Kahle P.J., and Beyer K. Alpha-synuclein has a high affinity for packing defects in a bilayer membrane-a thermodynamics study. J. Biol. Chem. 27 (2004) 21966-21975
    • (2004) J. Biol. Chem. , vol.27 , pp. 21966-21975
    • Nuscher, B.1    Kamp, F.2    Mehnert, T.3    Odoy, S.4    Haass, C.5    Kahle, P.J.6    Beyer, K.7
  • 41
    • 0019884688 scopus 로고
    • Lipids of synaptic vesicles: relevance to the mechanism of membrane fusion
    • Deutsch J.W., and Kelly R.B. Lipids of synaptic vesicles: relevance to the mechanism of membrane fusion. Biochemistry 20 (1981) 378-385
    • (1981) Biochemistry , vol.20 , pp. 378-385
    • Deutsch, J.W.1    Kelly, R.B.2
  • 42
    • 0020743519 scopus 로고
    • Asymmetry of lipid organization in cholinergic synaptic vesicle membranes
    • Michaelson D.M., Barkai G., and Barenholz Y. Asymmetry of lipid organization in cholinergic synaptic vesicle membranes. Biochem. J. 211 (1983) 155-162
    • (1983) Biochem. J. , vol.211 , pp. 155-162
    • Michaelson, D.M.1    Barkai, G.2    Barenholz, Y.3
  • 43
    • 0026521987 scopus 로고
    • Characterization of the P-type and V-type ATPases of cholinergic synaptic vesicles and coupling of nucleotide hydrolysis to acetylcholine transport
    • Hicks B.W., and Parsons S.M. Characterization of the P-type and V-type ATPases of cholinergic synaptic vesicles and coupling of nucleotide hydrolysis to acetylcholine transport. J. Neurochem. 58 (1992) 1211-1220
    • (1992) J. Neurochem. , vol.58 , pp. 1211-1220
    • Hicks, B.W.1    Parsons, S.M.2
  • 44
    • 0029992825 scopus 로고    scopus 로고
    • A subfamily of P-type ATPases with aminophospholipid transporting activity
    • Tang X., Halleck M.S., Schlegel R.A., and Williamson P. A subfamily of P-type ATPases with aminophospholipid transporting activity. Science 272 (1996) 1495-1497
    • (1996) Science , vol.272 , pp. 1495-1497
    • Tang, X.1    Halleck, M.S.2    Schlegel, R.A.3    Williamson, P.4
  • 45
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma P., Varma R., Sarasij R.C., Ira, Gousset K., Krishnamoorthy G., et al. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116 (2004) 577-589
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira4    Gousset, K.5    Krishnamoorthy, G.6
  • 46
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J.S., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.S.6
  • 48
    • 30044450420 scopus 로고    scopus 로고
    • Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants
    • Ulmer T.S., and Bax A. Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants. J. Biol. Chem. 280 (2005) 43179-43187
    • (2005) J. Biol. Chem. , vol.280 , pp. 43179-43187
    • Ulmer, T.S.1    Bax, A.2
  • 49
    • 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. Lipid droplet binding and oligomerization properties of the Parkinson's disease protein α-synuclein. J. Biol. Chem. 277 (2002) 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
  • 50
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • Zhao H.X., Tuominen E.K.J., and Kinnunen P.K.J. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43 (2004) 10302-10307
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.X.1    Tuominen, E.K.J.2    Kinnunen, P.K.J.3
  • 51
    • 33646912812 scopus 로고    scopus 로고
    • Binding of alpha-synuclein affects the lipid packing in bilayers of small vesicles
    • Kamp F., and Beyer K. Binding of alpha-synuclein affects the lipid packing in bilayers of small vesicles. J. Biol. Chem. 281 (2006) 9251-9259
    • (2006) J. Biol. Chem. , vol.281 , pp. 9251-9259
    • Kamp, F.1    Beyer, K.2
  • 52
    • 0001029147 scopus 로고
    • Preparation of giant vesicles by external AC electric fields. Kinetics and applications
    • Angelova M., Soleau S., Meleard P., Faucon J.F., and Bothorel P. Preparation of giant vesicles by external AC electric fields. Kinetics and applications. Prog. Colloid Polym. Sci. 89 (1992) 127-131
    • (1992) Prog. Colloid Polym. Sci. , vol.89 , pp. 127-131
    • Angelova, M.1    Soleau, S.2    Meleard, P.3    Faucon, J.F.4    Bothorel, P.5
  • 53
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of alpha-synuclein fibrils studied by site-directed spin labelling
    • Der-Sarkissian A., Jao C.C., Chen J., and Langen R. Structural organization of alpha-synuclein fibrils studied by site-directed spin labelling. J. Biol. Chem. 278 (2003) 37530-37535
    • (2003) J. Biol. Chem. , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.