메뉴 건너뛰기




Volumn 113, Issue 2, 2010, Pages 374-388

A novel, high-efficiency cellular model of fibrillar α-synuclein inclusions and the examination of mutations that inhibit amyloid formation

Author keywords

synuclein; Cellular model; Fibrillization; Inhibitors; Nucleation; Parkinson's disease; Phosphorylation

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; CALCIUM PHOSPHATE; THIOFLAVINE;

EID: 77949706598     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.06592.x     Document Type: Article
Times cited : (69)

References (71)
  • 1
    • 33644954146 scopus 로고    scopus 로고
    • Amino acid sequence motifs and mechanistic features of the membrane translocation of alpha-synuclein
    • Ahn K. J., Paik S. R., Chung K. C. Kim J. (2006) Amino acid sequence motifs and mechanistic features of the membrane translocation of alpha-synuclein. J. Neurochem. 97, 265 279.
    • (2006) J. Neurochem. , vol.97 , pp. 265-279
    • Ahn, K.J.1    Paik, S.R.2    Chung, K.C.3    Kim, J.4
  • 2
    • 33749570292 scopus 로고    scopus 로고
    • Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease
    • Anderson J. P., Walker D. E., Goldstein J. M. et al. (2006) Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J. Biol. Chem. 281, 29739 29752.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29739-29752
    • Anderson, J.P.1    Walker, D.E.2    Goldstein, J.M.3
  • 3
    • 3142724742 scopus 로고    scopus 로고
    • UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease
    • Ardley H. C., Scott G. B., Rose S. A., Tan N. G. Robinson P. A. (2004) UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease. J. Neurochem. 90, 379 391.
    • (2004) J. Neurochem. , vol.90 , pp. 379-391
    • Ardley, H.C.1    Scott, G.B.2    Rose, S.A.3    Tan, N.G.4    Robinson, P.A.5
  • 4
    • 0034602176 scopus 로고    scopus 로고
    • Parkinson's disease-associated alpha-synuclein is more fibrillogenic than β- And γ-synuclein and cannot cross-seed its homologs
    • Biere A. L., Wood S. J., Wypych J. et al. (2000) Parkinson's disease-associated alpha-synuclein is more fibrillogenic than β- and γ-synuclein and cannot cross-seed its homologs. J. Biol. Chem. 275, 34574 34579.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34574-34579
    • Biere, A.L.1    Wood, S.J.2    Wypych, J.3
  • 5
    • 33646228610 scopus 로고    scopus 로고
    • The 11-mer repeats of human alpha-synuclein in vesicle interactions and lipid composition discrimination: A cooperative role
    • Bisaglia M., Schievano E., Caporale A., Peggion E. Mammi S. (2006) The 11-mer repeats of human alpha-synuclein in vesicle interactions and lipid composition discrimination: a cooperative role. Biopolymers 84, 310 316.
    • (2006) Biopolymers , vol.84 , pp. 310-316
    • Bisaglia, M.1    Schievano, E.2    Caporale, A.3    Peggion, E.4    Mammi, S.5
  • 6
    • 5444260407 scopus 로고    scopus 로고
    • Synucleins and their relationship to Parkinson's disease
    • von Bohlen Und H. O. (2004) Synucleins and their relationship to Parkinson's disease. Cell Tissue Res. 318, 163 174.
    • (2004) Cell Tissue Res. , vol.318 , pp. 163-174
    • Von Bohlen Und, H.O.1
  • 7
    • 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. (1998) Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med. 4, 1318 1320.
    • (1998) Nat. Med. , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 8
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway K. A., Harper J. D. Lansbury P. T. (2000) Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39, 2552 2563.
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 11
    • 0042848693 scopus 로고    scopus 로고
    • A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein
    • Du H. N., Tang L., Luo X. Y., Li H. T., Hu J., Zhou J. W. Hu H. Y. (2003) A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein. Biochemistry 42, 8870 8878.
    • (2003) Biochemistry , vol.42 , pp. 8870-8878
    • Du, H.N.1    Tang, L.2    Luo, X.Y.3    Li, H.T.4    Hu, J.5    Zhou, J.W.6    Hu, H.Y.7
  • 12
    • 0033800039 scopus 로고    scopus 로고
    • Immunohistochemical and biochemical studies demonstrate a distinct profile of alpha-synuclein permutations in multiple system atrophy
    • Duda J. E., Giasson B. I., Gur T. L. et al. (2000) Immunohistochemical and biochemical studies demonstrate a distinct profile of alpha-synuclein permutations in multiple system atrophy. J. Neuropathol. Exp. Neurol. 59, 830 841.
    • (2000) J. Neuropathol. Exp. Neurol. , vol.59 , pp. 830-841
    • Duda, J.E.1    Giasson, B.I.2    Gur, T.L.3
  • 13
    • 0036322266 scopus 로고    scopus 로고
    • Novel antibodies to synuclein show abundant striatal pathology in Lewy body diseases
    • Duda J. E., Giasson B. I., Mabon M. E., Lee V. M. Y. Trojanoswki J. Q. (2002) Novel antibodies to synuclein show abundant striatal pathology in Lewy body diseases. Ann. Neurol. 52, 205 210.
    • (2002) Ann. Neurol. , vol.52 , pp. 205-210
    • Duda, J.E.1    Giasson, B.I.2    Mabon, M.E.3    Lee, V.M.Y.4    Trojanoswki, J.Q.5
  • 14
    • 23744443327 scopus 로고    scopus 로고
    • Nosology of Parkinson's disease: Looking for the way out of a quackmire
    • Forman M. S., Lee V. M. Trojanowski J. Q. (2005) Nosology of Parkinson's disease: looking for the way out of a quackmire. Neuron 47, 479 482.
    • (2005) Neuron , vol.47 , pp. 479-482
    • Forman, M.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 15
    • 9144271094 scopus 로고    scopus 로고
    • Methamphetamine produces neuronal inclusions in the nigrostriatal system and in PC12 cells
    • Fornai F., Lenzi P., Gesi M. et al. (2004) Methamphetamine produces neuronal inclusions in the nigrostriatal system and in PC12 cells. J. Neurochem. 88, 114 123.
    • (2004) J. Neurochem. , vol.88 , pp. 114-123
    • Fornai, F.1    Lenzi, P.2    Gesi, M.3
  • 17
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata R., Bebok Z., Sorscher E. J. Sztul E. S. (1999) Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol. 146, 1239 1254.
    • (1999) J. Cell Biol. , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 18
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson B. I., Uryu K., Trojanowski J. Q. Lee V. M. Y. (1999) Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 274, 7619 7622.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7619-7622
    • Giasson, B.I.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 19
    • 0034651575 scopus 로고    scopus 로고
    • A panel of epitope-specific antibodies detects protein domains distributed throughout human alpha-synuclein in Lewy bodies of Parkinson's disease
    • Giasson B. I., Jakes R., Goedert M., Duda J. E., Leight S., Trojanowski J. Q. Lee V. M. Y. (2000) A panel of epitope-specific antibodies detects protein domains distributed throughout human alpha-synuclein in Lewy bodies of Parkinson's disease. J. Neurosci. Res. 59, 528 533.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 528-533
    • Giasson, B.I.1    Jakes, R.2    Goedert, M.3    Duda, J.E.4    Leight, S.5    Trojanowski, J.Q.6    Lee, V.M.Y.7
  • 20
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • Giasson B. I., Murray I. V. J., Trojanowski J. Q. Lee V. M. Y. (2001) A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J. Biol. Chem. 276, 2380 2386.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.J.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 21
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis
    • Glenner G. G. (1980) Amyloid deposits and amyloidosis. N. Engl. J. Med. 302, 1283 1292.
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 22
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert M. (2001) Alpha-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2, 492 501.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 492-501
    • Goedert, M.1
  • 23
  • 26
    • 0032551656 scopus 로고    scopus 로고
    • Human recombinant NACP/alpha-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. (1998) Human recombinant NACP/alpha-synuclein is aggregated and fibrillated in vitro: relevance for Lewy body disease. Brain Res. 799, 301 306.
    • (1998) Brain Res. , vol.799 , pp. 301-306
    • Hashimoto, M.1    Hsu, L.J.2    Sisk, A.3    Xia, Y.4    Takeda, A.5    Sundsmo, M.6    Masliah, E.7
  • 27
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston J. A., Ward C. L. Kopito R. R. (1998) Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143, 1883 1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 28
    • 0036304315 scopus 로고    scopus 로고
    • Hyperphosphorylation and insolubility of alpha-synuclein in transgenic mouse oligodendrocytes
    • Kahle P. J., Neumann M., Ozmen L. et al. (2002) Hyperphosphorylation and insolubility of alpha-synuclein in transgenic mouse oligodendrocytes. EMBO Rep. 3, 583 588.
    • (2002) EMBO Rep. , vol.3 , pp. 583-588
    • Kahle, P.J.1    Neumann, M.2    Ozmen, L.3
  • 29
    • 0024352110 scopus 로고
    • Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk W. E., Pettegrew J. W. Abraham D. J. (1989) Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37, 1273 1281.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 30
    • 39749133508 scopus 로고    scopus 로고
    • Sequence determinants regulating fibrillation of human alpha-synuclein
    • Koo H. J., Lee H. J. Im H. (2008) Sequence determinants regulating fibrillation of human alpha-synuclein. Biochem. Biophys. Res. Commun. 368, 772 778.
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 772-778
    • Koo, H.J.1    Lee, H.J.2    Im, H.3
  • 31
    • 67649213482 scopus 로고    scopus 로고
    • Aggregation-defective alpha-synuclein mutants inhibit the fibrillation of Parkinson's disease-linked alpha-synuclein variants
    • Koo H. J., Choi M. Y. Im H. (2009) Aggregation-defective alpha-synuclein mutants inhibit the fibrillation of Parkinson's disease-linked alpha-synuclein variants. Biochem. Biophys. Res. Commun. 386, 165 169.
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 165-169
    • Koo, H.J.1    Choi, M.Y.2    Im, H.3
  • 32
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower J. H., Chu Y., Hauser R. A., Freeman T. B. Olanow C. W. (2008) Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat. Med. 14, 504 506.
    • (2008) Nat. Med. , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 33
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: New targets for drug discovery
    • Lee V. M. Trojanowski J. Q. (2006) Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: new targets for drug discovery. Neuron 52, 33 38.
    • (2006) Neuron , vol.52 , pp. 33-38
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 34
    • 0037085288 scopus 로고    scopus 로고
    • Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors
    • Lee H. J., Shin S. Y., Choi C., Lee Y. H. Lee S. J. (2002) Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors. J. Biol. Chem. 277, 5411 5417.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5411-5417
    • Lee, H.J.1    Shin, S.Y.2    Choi, C.3    Lee, Y.H.4    Lee, S.J.5
  • 35
    • 1342325420 scopus 로고    scopus 로고
    • Casein kinase II-mediated phosphorylation regulates alpha-synuclein/ synphilin-1 interaction and inclusion body formation
    • Lee G., Tanaka M., Park K., Lee S. S., Kim Y. M., Junn E., Lee S. H. Mouradian M. M. (2004) Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation. J. Biol. Chem. 279, 6834 6839.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6834-6839
    • Lee, G.1    Tanaka, M.2    Park, K.3    Lee, S.S.4    Kim, Y.M.5    Junn, E.6    Lee, S.H.7    Mouradian, M.M.8
  • 36
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of alpha-synuclein and its aggregates
    • Lee H. J., Patel S. Lee S. J. (2005) Intravesicular localization and exocytosis of alpha-synuclein and its aggregates. J. Neurosci. 25, 6016 6024.
    • (2005) J. Neurosci. , vol.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 38
    • 43249110200 scopus 로고    scopus 로고
    • Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation
    • Li J. Y., Englund E., Holton J. L. et al. (2008) Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nat. Med. 14, 501 503.
    • (2008) Nat. Med. , vol.14 , pp. 501-503
    • Li, J.Y.1    Englund, E.2    Holton, J.L.3
  • 44
    • 56449094841 scopus 로고    scopus 로고
    • Autophagy and the ubiquitin-proteasome system: Collaborators in neuroprotection
    • Nedelsky N. B., Todd P. K. Taylor J. P. (2008) Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection. Biochim. Biophys. Acta 1782, 691 699.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 691-699
    • Nedelsky, N.B.1    Todd, P.K.2    Taylor, J.P.3
  • 45
    • 0036855635 scopus 로고    scopus 로고
    • Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies
    • Neumann M., Kahle P. J., Giasson B. I. et al. (2002) Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies. J. Clin. Invest. 110, 1429 1439.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1429-1439
    • Neumann, M.1    Kahle, P.J.2    Giasson, B.I.3
  • 48
    • 48249107510 scopus 로고    scopus 로고
    • Accumulation and clearance of alpha-synuclein aggregates demonstrated by time-lapse imaging
    • Opazo F., Krenz A., Heermann S., Schulz J. B. Falkenburger B. H. (2008) Accumulation and clearance of alpha-synuclein aggregates demonstrated by time-lapse imaging. J. Neurochem. 106, 529 540.
    • (2008) J. Neurochem. , vol.106 , pp. 529-540
    • Opazo, F.1    Krenz, A.2    Heermann, S.3    Schulz, J.B.4    Falkenburger, B.H.5
  • 49
    • 30444457574 scopus 로고    scopus 로고
    • The alpha-synuclein mutation E46K promotes aggregation in cultured cells
    • Pandey N., Schmidt R. E. Galvin J. E. (2006) The alpha-synuclein mutation E46K promotes aggregation in cultured cells. Exp. Neurol. 197, 515 520.
    • (2006) Exp. Neurol. , vol.197 , pp. 515-520
    • Pandey, N.1    Schmidt, R.E.2    Galvin, J.E.3
  • 51
    • 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. George J. M. (2000) Interaction of human alpha-synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J. Biol. Chem. 275, 34393 34398.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 52
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos M. H., Lavedan C., Leroy E. et al. (1997) Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276, 2045 2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3
  • 53
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren P. H., Lauckner J. E., Kachirskaia I., Heuser J. E., Melki R. Kopito R. R. (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 11, 219 225.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 54
    • 0038307156 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies
    • Sampathu D. M., Giasson B. I., Pawlyk A. C., Trojanowski J. Q. Lee V. M. (2003) Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies. Am. J. Pathol. 163, 91 100.
    • (2003) Am. J. Pathol. , vol.163 , pp. 91-100
    • Sampathu, D.M.1    Giasson, B.I.2    Pawlyk, A.C.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 55
    • 1842454976 scopus 로고    scopus 로고
    • Does alpha-synuclein modulate dopaminergic synaptic content and tone at the synapse?
    • Sidhu A., Wersinger C. Vernier P. (2004) Does alpha-synuclein modulate dopaminergic synaptic content and tone at the synapse? FASEB J. 18, 637 647.
    • (2004) FASEB J. , vol.18 , pp. 637-647
    • Sidhu, A.1    Wersinger, C.2    Vernier, P.3
  • 58
    • 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. (1998) Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neurosci. Lett. 251, 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
  • 59
    • 13444251318 scopus 로고    scopus 로고
    • Pro-apoptotic protein glyceraldehyde-3-phosphate dehydrogenase promotes the formation of Lewy body-like inclusions
    • Tsuchiya K., Tajima H., Kuwae T. et al. (2005) Pro-apoptotic protein glyceraldehyde-3-phosphate dehydrogenase promotes the formation of Lewy body-like inclusions. Eur. J. Neurosci. 21, 317 326.
    • (2005) Eur. J. Neurosci. , vol.21 , pp. 317-326
    • Tsuchiya, K.1    Tajima, H.2    Kuwae, T.3
  • 60
    • 0031713491 scopus 로고    scopus 로고
    • Glial cytoplasmic inclusions in white matter oligodendrocytes of multiple system atrophy brains contain insoluble alpha-synuclein
    • Tu P. H., Galvin J. E., Baba M. et al. (1998) Glial cytoplasmic inclusions in white matter oligodendrocytes of multiple system atrophy brains contain insoluble alpha-synuclein. Ann. Neurol. 44, 415 422.
    • (1998) Ann. Neurol. , vol.44 , pp. 415-422
    • Tu, P.H.1    Galvin, J.E.2    Baba, M.3
  • 61
    • 0037181497 scopus 로고    scopus 로고
    • Accelerated alpha-synuclein fibrillation in crowded milieu
    • Uversky V. N., Cooper M., Bower K. S., Li J. Fink A. L. (2002) Accelerated alpha-synuclein fibrillation in crowded milieu. FEBS Lett. 515, 99 103.
    • (2002) FEBS Lett. , vol.515 , pp. 99-103
    • Uversky, V.N.1    Cooper, M.2    Bower, K.S.3    Li, J.4    Fink, A.L.5
  • 62
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter S., Boeddrich A., Lurz R., Scherzinger E., Lueder G., Lehrach H. Wanker E. E. (2001) Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell 12, 1393 1407.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 63
    • 43249108653 scopus 로고    scopus 로고
    • Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein
    • Waxman E. A. Giasson B. I. (2008) Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein. J. Neuropathol. Exp. Neurol. 67, 402 416.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 402-416
    • Waxman, E.A.1    Giasson, B.I.2
  • 64
    • 47749139266 scopus 로고    scopus 로고
    • Characterization of antibodies that selectively detect alpha-synuclein in pathological inclusions
    • Waxman E. A., Duda J. E. Giasson B. I. (2008) Characterization of antibodies that selectively detect alpha-synuclein in pathological inclusions. Acta Neuropathol. 116, 37 46.
    • (2008) Acta Neuropathol. , vol.116 , pp. 37-46
    • Waxman, E.A.1    Duda, J.E.2    Giasson, B.I.3
  • 65
    • 68249153855 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 expression leads to aggresome formation that is not associated with alpha-synuclein inclusions
    • Waxman E. A., Covy J. P., Bukh I., Li X., Dawson T. M. Giasson B. I. (2009a) Leucine-rich repeat kinase 2 expression leads to aggresome formation that is not associated with alpha-synuclein inclusions. J. Neuropathol. Exp. Neurol. 68, 785 796.
    • (2009) J. Neuropathol. Exp. Neurol. , vol.68 , pp. 785-796
    • Waxman, E.A.1    Covy, J.P.2    Bukh, I.3    Li, X.4    Dawson, T.M.5    Giasson, B.I.6
  • 66
    • 70350041314 scopus 로고    scopus 로고
    • Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization
    • Waxman E. A., Mazzulli J. R. Giasson B. I. (2009b) Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization. Biochemistry 48, 9427 9436.
    • (2009) Biochemistry , vol.48 , pp. 9427-9436
    • Waxman, E.A.1    Mazzulli, J.R.2    Giasson, B.I.3
  • 67
    • 0033538541 scopus 로고    scopus 로고
    • Alpha-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. (1999) Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J. Biol. Chem. 274, 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
  • 68
    • 1642381839 scopus 로고    scopus 로고
    • Tyrosine-to-cysteine modification of human alpha-synuclein enhances protein aggregation and cellular toxicity
    • Zhou W. Freed C. R. (2004) Tyrosine-to-cysteine modification of human alpha-synuclein enhances protein aggregation and cellular toxicity. J. Biol. Chem. 279, 10128 10135.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10128-10135
    • Zhou, W.1    Freed, C.R.2
  • 69
    • 71049123175 scopus 로고    scopus 로고
    • Crowded, cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding
    • Zhou Z., Fan J. B., Zhu H. L. et al. (2009) Crowded, cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding. J. Biol. Chem. 284, 30148 30158.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30148-30158
    • Zhou, Z.1    Fan, J.B.2    Zhu, H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.