메뉴 건너뛰기




Volumn 291, Issue 5, 2016, Pages 2310-2318

α-Synuclein amyloid fibrils with two entwined, asymmetrically associated protofibrils

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON MICROSCOPES; ELECTRON MICROSCOPY; GLYCOPROTEINS; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; METAL IONS; METALS; NEURODEGENERATIVE DISEASES; TRANSMISSION ELECTRON MICROSCOPY;

EID: 84957004495     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.698787     Document Type: Article
Times cited : (45)

References (43)
  • 1
    • 0032568534 scopus 로고    scopus 로고
    • α-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. (1998) α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. U.S.A. 95, 6469-6473
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 3
    • 0031728689 scopus 로고    scopus 로고
    • Synthetic filaments assembled from C-terminally truncated α-synuclein
    • Crowther, R. A., Jakes, R., Spillantini, M. G., and Goedert, M. (1998) Synthetic filaments assembled from C-terminally truncated α-synuclein. FEBS Lett. 436, 309-312
    • (1998) FEBS Lett. , vol.436 , pp. 309-312
    • Crowther, R.A.1    Jakes, R.2    Spillantini, M.G.3    Goedert, M.4
  • 5
    • 0032990543 scopus 로고    scopus 로고
    • Antibodies to α-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease
    • Lippa, C. F., Schmidt, M. L., Lee, V. M., and Trojanowski, J. Q. (1999) Antibodies to α-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease. Ann. Neurol. 45, 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
  • 6
    • 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., and Lansbury, P. T., Jr. (2000) Fibrils formed in vitro from α-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
  • 7
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes, R., Spillantini, M. G., and Goedert, M. (1994) Identification of two distinct synucleins from human brain. FEBS Lett. 345, 27-32
    • (1994) FEBS Lett. , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 8
    • 0028985267 scopus 로고
    • The precursor protein of non-A β component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., de Silva, H. A., Kittel, A., and Saitoh, T. (1995) The precursor protein of non-A β component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 14, 467-475
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.4    Flanagan, L.5    De Silva, H.A.6    Kittel, A.7    Saitoh, T.8
  • 10
    • 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, P. T., Jr. (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35, 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, P.T.5
  • 11
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of syntheticα-synuclein filaments shows amyloidlike cross-α conformation
    • Serpell, L. C., Berriman, J., Jakes, R., Goedert, M., and Crowther, R. A. (2000) Fiber diffraction of syntheticα-synuclein filaments shows amyloidlike cross-α conformation. Proc. Natl. Acad. Sci. U.S.A. 97, 4897-4902
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 13
    • 34548359337 scopus 로고    scopus 로고
    • Investigation of α-synuclein fibril structure by site-directed spin labeling
    • Chen, M., Margittai, M., Chen, J., and Langen, R. (2007) Investigation of α-synuclein fibril structure by site-directed spin labeling. J. Biol. Chem. 282, 24970-24979
    • (2007) J. Biol. Chem. , vol.282 , pp. 24970-24979
    • Chen, M.1    Margittai, M.2    Chen, J.3    Langen, R.4
  • 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., and Langen, R. (2003) Structural organization of α-synuclein fibrils studied by site-directed spin labeling. J. Biol. Chem. 278, 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
    • 84897135636 scopus 로고    scopus 로고
    • Unlike twins: An NMR comparison of two α-synuclein polymorphs featuring different toxicity
    • Gath, J., Bousset, L., Habenstein, B., Melki, R., Böckmann, A., and Meier, B. H. (2014) Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity. PLoS ONE 9, e90659
    • (2014) PLoS ONE , vol.9
    • Gath, J.1    Bousset, L.2    Habenstein, B.3    Melki, R.4    Böckmann, A.5    Meier, B.H.6
  • 16
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
    • Heise, H., Hoyer, W., Becker, S., Andronesi, O. C., Riedel, D., and Baldus, M. (2005) Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. U.S.A. 102, 15871-15876
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 17
    • 0037166267 scopus 로고    scopus 로고
    • Biochemical characterization of the core structure of α-synuclein filaments
    • Miake, H., Mizusawa, H., Iwatsubo, T., and Hasegawa, M. (2002) Biochemical characterization of the core structure of α-synuclein filaments. J. Biol. Chem. 277, 19213-19219
    • (2002) J. Biol. Chem. , vol.277 , pp. 19213-19219
    • Miake, H.1    Mizusawa, H.2    Iwatsubo, T.3    Hasegawa, M.4
  • 18
    • 8544264002 scopus 로고    scopus 로고
    • Impact of the acidic C-terminal region comprising amino acids 109-140 onα-synuclein aggregation in vitro
    • Hoyer, W., Cherny, D., Subramaniam, V., and Jovin, T. M. (2004) Impact of the acidic C-terminal region comprising amino acids 109-140 onα-synuclein aggregation in vitro. Biochemistry 43, 16233-16242
    • (2004) Biochemistry , vol.43 , pp. 16233-16242
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 20
    • 0014098295 scopus 로고
    • High-resolution electron microscopic analysis of the amyloid fibril
    • Shirahama, T., and Cohen, A. S. (1967) High-resolution electron microscopic analysis of the amyloid fibril. J. Cell Biol. 33, 679-708
    • (1967) J. Cell Biol. , vol.33 , pp. 679-708
    • Shirahama, T.1    Cohen, A.S.2
  • 22
    • 0030799122 scopus 로고    scopus 로고
    • Amyloidβ-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) Amyloidβ-protein fibrillogenesis: detection of a protofibrillar intermediate. J. Biol. Chem. 272, 22364-22372
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 23
    • 0035783171 scopus 로고    scopus 로고
    • Bsoft: Image and molecular processing in electron microscopy
    • Heymann, J. B. (2001) Bsoft: image and molecular processing in electron microscopy. J. Struct. Biol. 133, 156-169
    • (2001) J. Struct. Biol. , vol.133 , pp. 156-169
    • Heymann, J.B.1
  • 25
    • 42949133898 scopus 로고    scopus 로고
    • Mass mapping of large globin complexes by scanning transmission electron microscopy
    • Wall, J. S., Simon, M. N., Lin, B. Y., and Vinogradov, S. N. (2008) Mass mapping of large globin complexes by scanning transmission electron microscopy. Methods Enzymol. 436, 487-501
    • (2008) Methods Enzymol. , vol.436 , pp. 487-501
    • Wall, J.S.1    Simon, M.N.2    Lin, B.Y.3    Vinogradov, S.N.4
  • 26
  • 27
    • 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., and Goedert, M. (2000) Characterisation of isolated α-synuclein filaments from substantia nigra of Parkinson's disease brain. Neurosci Lett. 292, 128-130
    • (2000) Neurosci Lett. , vol.292 , pp. 128-130
    • Crowther, R.A.1    Daniel, S.E.2    Goedert, M.3
  • 28
    • 0028297078 scopus 로고
    • Mass and physical dimensions of two distinct populations of paired helical filaments
    • Ksiezak-Reding, H., and Wall, J. S. (1994) Mass and physical dimensions of two distinct populations of paired helical filaments. Neurobiol. Aging 15, 11-19
    • (1994) Neurobiol. Aging , vol.15 , pp. 11-19
    • Ksiezak-Reding, H.1    Wall, J.S.2
  • 29
    • 0028136474 scopus 로고
    • Mass analysis of biological macromolecular complexes by STEM
    • Thomas, D., Schultz, P., Steven, A. C., and Wall, J. S. (1994) Mass analysis of biological macromolecular complexes by STEM. Biol. Cell 80, 181-192
    • (1994) Biol. Cell , vol.80 , pp. 181-192
    • Thomas, D.1    Schultz, P.2    Steven, A.C.3    Wall, J.S.4
  • 30
    • 0035239217 scopus 로고    scopus 로고
    • Structure and mass analysis by scanning transmission electron microscopy
    • Müller, S. A., and Engel, A. (2001) Structure and mass analysis by scanning transmission electron microscopy. Micron 32, 21-31
    • (2001) Micron , vol.32 , pp. 21-31
    • Müller, S.A.1    Engel, A.2
  • 32
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous α-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., and Goedert, M. (1998) Filamentous α-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
  • 34
    • 77956072590 scopus 로고    scopus 로고
    • Metalloproteomics and metal toxicology of α-synuclein
    • Santner, A., and Uversky, V. N. (2010) Metalloproteomics and metal toxicology of α-synuclein. Metallomics 2, 378-392
    • (2010) Metallomics , vol.2 , pp. 378-392
    • Santner, A.1    Uversky, V.N.2
  • 37
    • 36248965693 scopus 로고    scopus 로고
    • Role of different regions of α-synuclein in the assembly of fibrils
    • Qin, Z., Hu, D., Han, S., Hong, D. P., and Fink, A. L. (2007) Role of different regions of α-synuclein in the assembly of fibrils. Biochemistry 46, 13322-13330
    • (2007) Biochemistry , vol.46 , pp. 13322-13330
    • Qin, Z.1    Hu, D.2    Han, S.3    Hong, D.P.4    Fink, A.L.5
  • 38
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: The parallel superpleated β-structure
    • Kajava, A. V., Baxa, U., Wickner, R. B., and Steven, A. C. (2004) A model for Ure2p prion filaments and other amyloids: the parallel superpleated β-structure. Proc. Natl. Acad. Sci. U.S.A. 101, 7885-7890
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7885-7890
    • Kajava, A.V.1    Baxa, U.2    Wickner, R.B.3    Steven, A.C.4
  • 39
    • 84931562363 scopus 로고    scopus 로고
    • A structure-based approach to predict predisposition to amyloidosis
    • Ahmed, A. B., Znassi, N., Château, M. T., and Kajava, A. V. (2015) A structure-based approach to predict predisposition to amyloidosis. Alzheimers Dement. 11, 681-690
    • (2015) Alzheimers Dement. , vol.11 , pp. 681-690
    • Ahmed, A.B.1    Znassi, N.2    Château, M.T.3    Kajava, A.V.4
  • 40
    • 44949250850 scopus 로고    scopus 로고
    • Paired β-sheet structure of an Aβ (1-40) amyloid fibril revealed by electron microscopy
    • Sachse, C., Fändrich, M., and Grigorieff, N. (2008) Paired β-sheet structure of an Aβ (1-40) amyloid fibril revealed by electron microscopy. Proc. Natl. Acad. Sci. U.S.A. 105, 7462-7466
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7462-7466
    • Sachse, C.1    Fändrich, M.2    Grigorieff, N.3
  • 41
    • 79952772833 scopus 로고    scopus 로고
    • Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy
    • Mizuno, N., Baxa, U., and Steven, A. C. (2011) Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy. Proc. Natl. Acad. Sci. U.S.A. 108, 3252-3257
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3252-3257
    • Mizuno, N.1    Baxa, U.2    Steven, A.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.