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Volumn 288, Issue 9, 2013, Pages 6371-6385

In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells

Author keywords

[No Author keywords available]

Indexed keywords

CELL LYSIS; CYTOPATHOLOGY; ERYTHROID CELLS; IN-VIVO; INTACT CELLS; ISO-ELECTRIC POINTS; LIPID VESICLES; LIVING CELL; NEUROBLASTOMA CELLS; PARKINSON DISEASE; PARTIAL RECOVERY; PROTEIN CONCENTRATIONS; SCHNEIDER; SIMILAR PATTERN; SYNUCLEIN; TETRAMERS;

EID: 84874769548     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.403311     Document Type: Article
Times cited : (204)

References (36)
  • 1
    • 80052398365 scopus 로고    scopus 로고
    • α-synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels, T., Choi, J. G., and Selkoe, D. J. (2011) α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477, 107-110
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 5
    • 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 Jr., P.T.5
  • 7
    • 84860172516 scopus 로고    scopus 로고
    • N-terminal acetylation is critical for forming α-helical oligomer of α-synuclein
    • Trexler, A. J., and Rhoades, E. (2012) N-terminal acetylation is critical for forming α-helical oligomer of α-synuclein. Protein Sci. 21, 601-605
    • (2012) Protein Sci. , vol.21 , pp. 601-605
    • Trexler, A.J.1    Rhoades, E.2
  • 8
    • 84872744821 scopus 로고    scopus 로고
    • Monomeric synucleins generate membrane curvature
    • Westphal, C. H., and Chandra, S. S. (2013) Monomeric synucleins generate membrane curvature. J. Biol. Chem. 288, 1829-1840
    • (2013) J. Biol. Chem. , vol.288 , pp. 1829-1840
    • Westphal, C.H.1    Chandra, S.S.2
  • 10
    • 7244229744 scopus 로고    scopus 로고
    • Dimerization of Parkinson's disease-causing DJ-1 and formation of high molecular weight complexes in human brain
    • Baulac, S., LaVoie, M. J., Strahle, J., Schlossmacher, M. G., and Xia, W. (2004) Dimerization of Parkinson's disease-causing DJ-1 and formation of high molecular weight complexes in human brain. Mol Cell Neurosci. 27, 236-246
    • (2004) Mol Cell Neurosci. , vol.27 , pp. 236-246
    • Baulac, S.1    Lavoie, M.J.2    Strahle, J.3    Schlossmacher, M.G.4    Xia, W.5
  • 11
    • 80051855646 scopus 로고    scopus 로고
    • Improved immunodetection of endogenous α-synuclein
    • Lee, B. R., and Kamitani, T. (2011) Improved immunodetection of endogenous α-synuclein. PLoS One 6, e23939
    • (2011) PLoS One , vol.6
    • Lee, B.R.1    Kamitani, T.2
  • 15
    • 0020321974 scopus 로고
    • HEL cells. A new human erythroleukemia cell line with spontaneous and induced globin expression
    • Martin, P., and Papayannopoulou, T. (1982) HEL cells. A new human erythroleukemia cell line with spontaneous and induced globin expression. Science 216, 1233-1235
    • (1982) Science , vol.216 , pp. 1233-1235
    • Martin, P.1    Papayannopoulou, T.2
  • 16
    • 33750117120 scopus 로고    scopus 로고
    • Detection of novel intracellular α-synuclein oligomeric species by fluorescence lifetime imaging
    • Klucken, J., Outeiro, T. F., Nguyen, P., McLean, P. J., and Hyman, B. T. (2006) Detection of novel intracellular α-synuclein oligomeric species by fluorescence lifetime imaging. FASEB J.. 20, 2050-2057
    • (2006) FASEB J. , vol.20 , pp. 2050-2057
    • Klucken, J.1    Outeiro, T.F.2    Nguyen, P.3    McLean, P.J.4    Hyman, B.T.5
  • 17
    • 0042130551 scopus 로고    scopus 로고
    • The 1.1 Å resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease
    • Wilson, M. A., Collins, J. L., Hod, Y., Ringe, D., and Petsko, G. A.. (2003) The 1.1 Å resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 100, 9256-9261
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9256-9261
    • Wilson, M.A.1    Collins, J.L.2    Hod, Y.3    Ringe, D.4    Petsko, G.A.5
  • 18
    • 0042232039 scopus 로고    scopus 로고
    • Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease
    • Tao, X., and Tong, L. (2003) Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease. J. Biol. Chem. 278, 31372-31379
    • (2003) J. Biol. Chem. , vol.278 , pp. 31372-31379
    • Tao, X.1    Tong, L.2
  • 20
    • 0142058187 scopus 로고    scopus 로고
    • Epitope mapping and specificity of the anti-α-synuclein monoclonal antibody Syn-1 in mouse brain and cultured cell lines
    • Perrin, R. J., Payton, J. E., Barnett, D. H., Wraight, C. L., Woods, W. S., Ye, L., and George J. M. (2003) Epitope mapping and specificity of the anti-α-synuclein monoclonal antibody Syn-1 in mouse brain and cultured cell lines. Neurosci. Lett. 349, 133-135
    • (2003) Neurosci. Lett. , vol.349 , pp. 133-135
    • Perrin, R.J.1    Payton, J.E.2    Barnett, D.H.3    Wraight, C.L.4    Woods, W.S.5    Ye, L.6    George, J.M.7
  • 21
    • 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. (1995) Characterization of a novel protein regulated during the critical period for song learning in the zebra finch. Neuron. 15, 361-372
    • (1995) Neuron. , vol.15 , pp. 361-372
    • George, J.M.1    Jin, H.2    Woods, W.S.3    Clayton, D.F.4
  • 22
    • 0029820770 scopus 로고    scopus 로고
    • Characterization of the precursor protein of the non-Aβ component of senile plaques (NACP) in the human central nervous system
    • Irizarry, M. C., Kim, T. W., McNamara, M., Tanzi, R. E., George, J. M., Clayton, D. F., and Hyman, B. T. (1996) Characterization of the precursor protein of the non-Aβ component of senile plaques (NACP) in the human central nervous system. J Neuropathol. Exp. Neurol. 55, 889-895
    • (1996) J Neuropathol. Exp. Neurol. , vol.55 , pp. 889-895
    • Irizarry, M.C.1    Kim, T.W.2    McNamara, M.3    Tanzi, R.E.4    George, J.M.5    Clayton, D.F.6    Hyman, B.T.7
  • 26
    • 0035500991 scopus 로고    scopus 로고
    • Proteinprotein interactions of α-synuclein in brain homogenates and transfected cells
    • Payton, J. E., Perrin, R. J., Clayton, D. F., and George, J. M. (2001) Proteinprotein interactions of α-synuclein in brain homogenates and transfected cells. Brain Res. Mol. Brain Res. 95, 138-145
    • (2001) Brain Res. Mol. Brain Res. , vol.95 , pp. 138-145
    • Payton, J.E.1    Perrin, R.J.2    Clayton, D.F.3    George, J.M.4
  • 28
    • 0021097241 scopus 로고
    • Hydrodynamic properties of porin isolated from outer membranes of rat liver mitochondria
    • Lindén, M., and Gellerfors, P. (1983) Hydrodynamic properties of porin isolated from outer membranes of rat liver mitochondria. Biochim. Biophys. Acta 736, 125-129
    • (1983) Biochim. Biophys. Acta , vol.736 , pp. 125-129
    • Lindén, M.1    Gellerfors, P.2
  • 29
    • 0032875663 scopus 로고    scopus 로고
    • Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids
    • Dolder, M., Zeth, K., Tittmann, P., Gross, H., Welte, W., and Wallimann, T. (1999) Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids. J. Struct. Biol. 127, 64-71
    • (1999) J. Struct. Biol. , vol.127 , pp. 64-71
    • Dolder, M.1    Zeth, K.2    Tittmann, P.3    Gross, H.4    Welte, W.5    Wallimann, T.6
  • 30
    • 0002815512 scopus 로고
    • D-Glyceraldehyde-3-phosphate dehydrogenase. Three-dimensional structure and evolutionary significance
    • Buehner, M., Ford, G. C., Moras, D., Olsen, K. W., and Rossman, M. G. (1973) D-Glyceraldehyde-3-phosphate dehydrogenase. Three-dimensional structure and evolutionary significance. Proc. Natl. Acad. Sci. U.S.A. 70, 3052-3054
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 3052-3054
    • Buehner, M.1    Ford, G.C.2    Moras, D.3    Olsen, K.W.4    Rossman, M.G.5
  • 31
    • 77957798188 scopus 로고    scopus 로고
    • A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division
    • Chang, C. R., Manlandro, C. M., Arnoult, D., Stadler, J., Posey, A. E., Hill, R. B., and Blackstone, C. (2010) A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division. J. Biol. Chem. 285, 32494-324503
    • (2010) J. Biol. Chem. , vol.285 , pp. 32494-324503
    • Chang, C.R.1    Manlandro, C.M.2    Arnoult, D.3    Stadler, J.4    Posey, A.E.5    Hill, R.B.6    Blackstone, C.7
  • 33
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and α-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. (2000) Synucleins are developmentally expressed, and α-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J Neurosci. 20, 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
  • 34
    • 0037023699 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate. Inhibition of α-synuclein assembly by β- And γ-synucleins
    • Uversky, V. N., Li, J., Souillac, P., Millett, I. S., Doniach, S., Jakes, R., Goedert, M., and Fink A. L. (2002) Biophysical properties of the synucleins and their propensities to fibrillate. Inhibition of α-synuclein assembly by β- and γ-synucleins. J. Biol. Chem. 277, 11970-11978
    • (2002) J. Biol. Chem. , vol.277 , pp. 11970-11978
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Millett, I.S.4    Doniach, S.5    Jakes, R.6    Goedert, M.7    Fink, A.L.8
  • 35
    • 0035950270 scopus 로고    scopus 로고
    • β-synuclein inhibits α-synuclein aggregation. A possible role as an anti-parkinsonian factor
    • Hashimoto, M., Rockenstein, E., Mante, M., Mallory, M., and Masliah, E. (2001) β-Synuclein inhibits α-synuclein aggregation. A possible role as an anti-parkinsonian factor. Neuron. 32, 213-223
    • (2001) Neuron. , vol.32 , pp. 213-223
    • Hashimoto, M.1    Rockenstein, E.2    Mante, M.3    Mallory, M.4    Masliah, E.5
  • 36
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly
    • Giasson, B. I., Murray, I. V., Trojanowski, J. Q., and Lee, V. M. (2001) A hydrophobic stretch of 12 amino acid residues in the middle of α-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.2    Trojanowski, J.Q.3    Lee, V.M.4


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