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Volumn 340, Issue 1, 2004, Pages 127-139

Rapid self-assembly of α-synuclein observed by in situ atomic force microscopy

Author keywords

AFM, atomic force microscopy; amyloid fibril; atomic force microscopy; A , Alzheimer's amyloid peptide; EPR, electron paramagnetic resonance; ESI MS, electrospray ionization mass spectrometry; soluble oligomer; synuclein; sheet

Indexed keywords

ALPHA SYNUCLEIN; MUTANT PROTEIN; POLYAMINE; SPERMIDINE; SPERMINE;

EID: 2942592408     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.051     Document Type: Article
Times cited : (158)

References (60)
  • 1
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert M. Alpha-synuclein and neurodegenerative diseases. Nature Rev. Neurosci. 2:2001;492-501
    • (2001) Nature Rev. Neurosci. , vol.2 , pp. 492-501
    • Goedert, M.1
  • 2
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease?
    • Goldberg M.S., Lansbury P.T. Jr. Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease? Nature Cell. Biol. 2:2000;E115-E119
    • (2000) Nature Cell. Biol. , vol.2
    • Goldberg, M.S.1    Lansbury Jr., P.T.2
  • 3
    • 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
  • 4
    • 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. Nature Genet. 18:1998;106-108
    • (1998) Nature Genet. , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 6
    • 0035838284 scopus 로고    scopus 로고
    • Multiple ligand interaction of α-synuclein produced various forms of protein aggregates in the presence of Aβ25-35, copper, and eosin
    • Kim Y.S., Lee D., Lee E.K., Sung J.Y., Chung K.C., Kim J., Paik S.R. Multiple ligand interaction of α-synuclein produced various forms of protein aggregates in the presence of Aβ25-35, copper, and eosin. Brain Res. 908:2001;93-98
    • (2001) Brain Res. , vol.908 , pp. 93-98
    • Kim, Y.S.1    Lee, D.2    Lee, E.K.3    Sung, J.Y.4    Chung, K.C.5    Kim, J.6    Paik, S.R.7
  • 7
    • 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., 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.6
  • 9
    • 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., Lansbury P.T. Jr. 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
  • 10
    • 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., Masliah E. Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: relevance for Lewy body disease. Brain Res. 799:1998;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
  • 11
    • 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., Lee V.M. Mutant and wild type human α-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 274:1999;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.4
  • 12
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation
    • Serpell L.C., Berriman J., Jakes R., Goedert M., Crowther R.A. Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation. Proc. Natl Acad. Sci. USA. 97:2000;4897-4902
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 13
    • 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., Lansbury P.T. Jr. Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry. 39:2000;2552-2563
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury Jr., P.T.3
  • 14
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of α-synuclein fibrils studied by site-directed spin labeling
    • Der-Sarkissian A., Jao C.C., Chen J., Langen R. Structural organization of α-synuclein fibrils studied by site-directed spin labeling. 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
  • 15
    • 0037166267 scopus 로고    scopus 로고
    • Biochemical characterization of the core structure of α-synuclein filaments
    • Miake H., Mizusawa H., Iwatsubo T., Hasegawa M. Biochemical characterization of the core structure of α-synuclein filaments. J. Biol. Chem. 277:2002;19213-19219
    • (2002) J. Biol. Chem. , vol.277 , pp. 19213-19219
    • Miake, H.1    Mizusawa, H.2    Iwatsubo, T.3    Hasegawa, M.4
  • 16
    • 0031728689 scopus 로고    scopus 로고
    • Synthetic filaments assembled from C-terminally truncated α-synuclein
    • Crowther R.A., Jakes R., Spillantini M.G., Goedert M. Synthetic filaments assembled from C-terminally truncated α-synuclein. FEBS Letters. 436:1998;309-312
    • (1998) FEBS Letters , vol.436 , pp. 309-312
    • Crowther, R.A.1    Jakes, R.2    Spillantini, M.G.3    Goedert, M.4
  • 18
    • 0033564726 scopus 로고    scopus 로고
    • Copper(II)-induced self-oligomerization of α-synuclein
    • Paik S.R., Shin H.J., Lee J.H., Chang C.S., Kim J. Copper(II)-induced self-oligomerization of α-synuclein. Biochem. J. 340:1999;821-828
    • (1999) Biochem. J. , vol.340 , pp. 821-828
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3    Chang, C.S.4    Kim, J.5
  • 20
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure
    • Uversky V.N., Li J., Fink A.L. Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 276:2001;44284-44296
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 24
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in α-synuclein fibril formation
    • Uversky V.N., Li J., Fink A.L. Evidence for a partially folded intermediate in α-synuclein fibril formation. J. Biol. Chem. 276:2001;10737-10744
    • (2001) J. Biol. Chem. , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 25
    • 0031787871 scopus 로고    scopus 로고
    • Jr accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson's disease
    • Conway K.A., Harper J.D., Lansbury P.T. Jr. Jr accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson's disease. Nature Med. 4:1998;1318-1320
    • (1998) Nature Med. , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury Jr., P.T.3
  • 26
    • 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. Both familial Parkinson's disease mutations accelerate α-synuclein aggregation. J. Biol. Chem. 274:1999;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
  • 27
    • 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., Lansbury P.T. Jr. 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 Jr., P.T.6
  • 28
    • 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., Fink A.L. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein. Biochemistry. 40:2001;11604-11613
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 29
    • 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., Lansbury P.T. Jr. Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry. 41:2002;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
  • 30
    • 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., Lansbury P.T. Jr. α-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 Jr., P.T.7
  • 31
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature. 426:2003;884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 33
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation
    • Kowalewski T., Holtzman D.M. In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: new insights into mechanism of β-sheet formation. Proc. Natl Acad. Sci. USA. 96:1999;3688-3693
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 36
    • 0034613450 scopus 로고    scopus 로고
    • Characterisation of isolated α-synuclein filaments from substantia nigra of Parkinson's disease brain
    • Crowther R.A., Daniel S.E., Goedert M. Characterisation of isolated α-synuclein filaments from substantia nigra of Parkinson's disease brain. Neurosci. Letters. 292:2000;128-130
    • (2000) Neurosci. Letters , vol.292 , pp. 128-130
    • Crowther, R.A.1    Daniel, S.E.2    Goedert, M.3
  • 37
    • 0033538541 scopus 로고    scopus 로고
    • α-Synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease
    • Wood S.J., Wypych J., Steavenson S., Louis J.C., Citron M., Biere A.L. α-Synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J. Biol. Chem. 274:1999;19509-19512
    • (1999) J. Biol. Chem. , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6
  • 38
    • 0036233931 scopus 로고    scopus 로고
    • Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
    • DePace A.H., Weissman J.S. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nature Struct. Biol. 9:2002;389-396
    • (2002) Nature Struct. Biol. , vol.9 , pp. 389-396
    • Depace, A.H.1    Weissman, J.S.2
  • 40
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., George J.M. Stabilization of α-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
  • 41
    • 0034708767 scopus 로고    scopus 로고
    • Membrane association and protein conformation of α-synuclein in intact neurons. Effect of Parkinson's disease-linked mutations
    • McLean P.J., Kawamata H., Ribich S., Hyman B.T. Membrane association and protein conformation of α-synuclein in intact neurons. Effect of Parkinson's disease-linked mutations. J. Biol. Chem. 275:2000;8812-8816
    • (2000) J. Biol. Chem. , vol.275 , pp. 8812-8816
    • McLean, P.J.1    Kawamata, H.2    Ribich, S.3    Hyman, B.T.4
  • 43
    • 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., Lee S.J. Membrane-bound α-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
  • 44
    • 0035928748 scopus 로고    scopus 로고
    • Membrane binding and self-association of α-synucleins
    • Narayanan V., Scarlata S. Membrane binding and self-association of α-synucleins. Biochemistry. 40:2001;9927-9934
    • (2001) Biochemistry , vol.40 , pp. 9927-9934
    • Narayanan, V.1    Scarlata, S.2
  • 45
    • 0037930855 scopus 로고    scopus 로고
    • Lipid binding inhibits α-synuclein fibril formation
    • Zhu M., 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
  • 46
    • 0345306656 scopus 로고    scopus 로고
    • Rapid anionic micelle-mediated α-synuclein fibrillization in vitro
    • Necula M., Chirita C.N., Kuret J. Rapid anionic micelle-mediated α-synuclein fibrillization in vitro. J. Biol. Chem. 278:2003;46674-46680
    • (2003) J. Biol. Chem. , vol.278 , pp. 46674-46680
    • Necula, M.1    Chirita, C.N.2    Kuret, J.3
  • 47
    • 0036531566 scopus 로고    scopus 로고
    • Structural relationship between epitaxially grown para-sexiphenyl and mica (0 0 1) substrates
    • Plank H., Resel R., Andreev A., Sariciftci N.S., Sitter H. Structural relationship between epitaxially grown para-sexiphenyl and mica (0 0 1) substrates. J. Cryst. Growth. 237-239:2002;2076-2081
    • (2002) J. Cryst. Growth , vol.237-239 , pp. 2076-2081
    • Plank, H.1    Resel, R.2    Andreev, A.3    Sariciftci, N.S.4    Sitter, H.5
  • 48
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec C.P., MacPhee C.E., Bajaj V.S., McMahon M.T., Dobson C.M., Griffin R.G. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc. Natl Acad. Sci. USA. 101:2004;711-716
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 711-716
    • Jaroniec, C.P.1    MacPhee, C.E.2    Bajaj, V.S.3    McMahon, M.T.4    Dobson, C.M.5    Griffin, R.G.6
  • 49
    • 0037063510 scopus 로고    scopus 로고
    • Substrate-facilitated assembly of elastin-like peptides: Studies by variable-temperature in situ atomic force microscopy
    • Yang G., Woodhouse K.A., Yip C.M. Substrate-facilitated assembly of elastin-like peptides: studies by variable-temperature in situ atomic force microscopy. J. Am. Chem. Soc. 124:2002;10648-10649
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10648-10649
    • Yang, G.1    Woodhouse, K.A.2    Yip, C.M.3
  • 50
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro
    • Cohlberg J.A., Li J., Uversky V.N., Fink A.L. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro. Biochemistry. 41:2002;1502-1511
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 51
    • 0141483558 scopus 로고    scopus 로고
    • Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV
    • Hong Y., Legge R.L., Zhang S., Chen P. Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV. Biomacromolecules. 4:2003;1433-1442
    • (2003) Biomacromolecules , vol.4 , pp. 1433-1442
    • Hong, Y.1    Legge, R.L.2    Zhang, S.3    Chen, P.4
  • 52
    • 0037243355 scopus 로고    scopus 로고
    • Self-assembly of template-directed J-aggregates of porphyrin
    • Koti A.S.R., Periasamy N. Self-assembly of template-directed J-aggregates of porphyrin. Chem. Mater. 15:2003;369-371
    • (2003) Chem. Mater. , vol.15 , pp. 369-371
    • Koti, A.S.R.1    Periasamy, N.2
  • 53
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., et al. Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc. Natl Acad. Sci. USA. 95:1998;6448-6453
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 55
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of Aβ amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • Harper J.D., Wong S.S., Lieber C.M., Lansbury P.T. Jr. Assembly of Aβ amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry. 38:1999;8972-8980
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 56
    • 0037039394 scopus 로고    scopus 로고
    • Structure determination of micelle-like intermediates in amyloid β-protein fibril assembly by using small angle neutron scattering
    • Yong W., Lomakin A., Kirkitadze M.D., Teplow D.B., Chen S.H., Benedek G.B. Structure determination of micelle-like intermediates in amyloid β-protein fibril assembly by using small angle neutron scattering. Proc. Natl Acad. Sci. USA. 99:2002;150-154
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 150-154
    • Yong, W.1    Lomakin, A.2    Kirkitadze, M.D.3    Teplow, D.B.4    Chen, S.H.5    Benedek, G.B.6
  • 57
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J., Serpell L., et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science. 289:2000;1317-1321
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 58
    • 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., Lansbury P.T. Jr. 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 Jr., P.T.7
  • 59
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by Thioflavin T fluorescence
    • Ban T., Hamada D., Hasegawa K., Naiki H., Goto Y. Direct observation of amyloid fibril growth monitored by Thioflavin T fluorescence. J. Biol. Chem. 278:2003;16462-16465
    • (2003) J. Biol. Chem. , vol.278 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5


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