메뉴 건너뛰기




Volumn 69, Issue , 2014, Pages 76-92

Intracellular processing of disease-associated α-synuclein in the human brain suggests prion-like cell-to-cell spread

Author keywords

Endosome; Ependyma; Gap junction; Internalisation; Lysosome; Mitochondria; Nanotube; Prion like; Spreading; synuclein

Indexed keywords

4D6 ANTIBODY; ALPHA SYNUCLEIN; ANTIBODY; MONOMER; OLIGOMER; UNCLASSIFIED DRUG; SNCA PROTEIN, HUMAN;

EID: 84901985544     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2014.05.020     Document Type: Article
Times cited : (111)

References (86)
  • 5
    • 0029346911 scopus 로고
    • The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain
    • Arnold J.E., Tipler C., Laszlo L., Hope J., Landon M., Mayer R.J. The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J. Pathol. 1995, 176:403-411.
    • (1995) J. Pathol. , vol.176 , pp. 403-411
    • Arnold, J.E.1    Tipler, C.2    Laszlo, L.3    Hope, J.4    Landon, M.5    Mayer, R.J.6
  • 6
    • 77958449984 scopus 로고    scopus 로고
    • Alpha-Synuclein: Membrane interactions and toxicity in Parkinson's disease
    • Auluck P.K., Caraveo G., Lindquist S. alpha-Synuclein: Membrane interactions and toxicity in Parkinson's disease. Annu. Rev. Cell Dev. Biol. 2010, 26:211-233.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 7
    • 0036500554 scopus 로고    scopus 로고
    • Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes
    • Baron G.S., Wehrly K., Dorward D.W., Chesebro B., Caughey B. Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes. EMBO J. 2002, 21:1031-1040.
    • (2002) EMBO J. , vol.21 , pp. 1031-1040
    • Baron, G.S.1    Wehrly, K.2    Dorward, D.W.3    Chesebro, B.4    Caughey, B.5
  • 9
    • 52249123646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits assembly and promotes disassembly of apolipoprotein C-II amyloid fibrils
    • Binger K.J., Griffin M.D., Howlett G.J. Methionine oxidation inhibits assembly and promotes disassembly of apolipoprotein C-II amyloid fibrils. Biochemistry 2008, 47:10208-10217.
    • (2008) Biochemistry , vol.47 , pp. 10208-10217
    • Binger, K.J.1    Griffin, M.D.2    Howlett, G.J.3
  • 10
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt D.R., Taraboulos A., Prusiner S.B. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 1992, 267:16188-16199.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 12
    • 34547727312 scopus 로고    scopus 로고
    • Development of alpha-synuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson's disease
    • Braak H., Sastre M., Del Tredici K. Development of alpha-synuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson's disease. Acta Neuropathol. 2007, 114:231-241.
    • (2007) Acta Neuropathol. , vol.114 , pp. 231-241
    • Braak, H.1    Sastre, M.2    Del Tredici, K.3
  • 13
    • 28244486826 scopus 로고    scopus 로고
    • Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation
    • Breydo L., Bocharova O.V., Makarava N., Salnikov V.V., Anderson M., Baskakov I.V. Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation. Biochemistry 2005, 44:15534-15543.
    • (2005) Biochemistry , vol.44 , pp. 15534-15543
    • Breydo, L.1    Bocharova, O.V.2    Makarava, N.3    Salnikov, V.V.4    Anderson, M.5    Baskakov, I.V.6
  • 15
    • 84861554724 scopus 로고    scopus 로고
    • Alpha-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions
    • Cali T., Ottolini D., Negro A., Brini M. alpha-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions. J. Biol. Chem. 2012, 287:17914-17929.
    • (2012) J. Biol. Chem. , vol.287 , pp. 17914-17929
    • Cali, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 16
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey B., Raymond G.J., Ernst D., Race R.E. N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state. J. Virol. 1991, 65:6597-6603.
    • (1991) J. Virol. , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 17
    • 33646124943 scopus 로고    scopus 로고
    • Abnormal alpha-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease
    • Dalfo E., Martinez A., Muntane G., Ferrer I. Abnormal alpha-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease. Neurosci. Lett. 2006, 400:125-129.
    • (2006) Neurosci. Lett. , vol.400 , pp. 125-129
    • Dalfo, E.1    Martinez, A.2    Muntane, G.3    Ferrer, I.4
  • 18
    • 0029294529 scopus 로고
    • The ependyma: A protective barrier between brain and cerebrospinal fluid
    • Del Bigio M.R. The ependyma: A protective barrier between brain and cerebrospinal fluid. Glia 1995, 14:1-13.
    • (1995) Glia , vol.14 , pp. 1-13
    • Del Bigio, M.R.1
  • 19
    • 77649190846 scopus 로고    scopus 로고
    • Ependymal cells: Biology and pathology
    • Del Bigio M.R. Ependymal cells: Biology and pathology. Acta Neuropathol. 2010, 119:55-73.
    • (2010) Acta Neuropathol. , vol.119 , pp. 55-73
    • Del Bigio, M.R.1
  • 20
    • 77953022918 scopus 로고    scopus 로고
    • Lewy pathology in the submandibular gland of individuals with incidental Lewy body disease and sporadic Parkinson's disease
    • Del Tredici K., Hawkes C.H., Ghebremedhin E., Braak H. Lewy pathology in the submandibular gland of individuals with incidental Lewy body disease and sporadic Parkinson's disease. Acta Neuropathol. 2010, 119:703-713.
    • (2010) Acta Neuropathol. , vol.119 , pp. 703-713
    • Del Tredici, K.1    Hawkes, C.H.2    Ghebremedhin, E.3    Braak, H.4
  • 21
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • Devi L., Raghavendran V., Prabhu B.M., Avadhani N.G., Anandatheerthavarada H.K. Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J. Biol. Chem. 2008, 283:9089-9100.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 23
    • 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., Trojanowski J.Q. Novel antibodies to synuclein show abundant striatal pathology in Lewy body diseases. Ann. Neurol. 2002, 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.4    Trojanowski, J.Q.5
  • 26
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo J.L., Lee V.M. Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat. Med. 2014, 20:130-138.
    • (2014) Nat. Med. , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.2
  • 27
    • 79951499176 scopus 로고    scopus 로고
    • Glia: Initiators and progressors of pathology in Parkinson's disease
    • Halliday G.M., Stevens C.H. Glia: Initiators and progressors of pathology in Parkinson's disease. Mov. Disord. 2011, 26:6-17.
    • (2011) Mov. Disord. , vol.26 , pp. 6-17
    • Halliday, G.M.1    Stevens, C.H.2
  • 29
    • 0032879452 scopus 로고    scopus 로고
    • Role of cytochrome c as a stimulator of alpha-synuclein aggregation in Lewy body disease
    • Hashimoto M., Takeda A., Hsu L.J., Takenouchi T., Masliah E. Role of cytochrome c as a stimulator of alpha-synuclein aggregation in Lewy body disease. J. Biol. Chem. 1999, 274:28849-28852.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28849-28852
    • Hashimoto, M.1    Takeda, A.2    Hsu, L.J.3    Takenouchi, T.4    Masliah, E.5
  • 30
  • 33
    • 0028985267 scopus 로고
    • The precursor protein of non-A beta 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., Saitoh T. The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 1995, 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
  • 34
    • 84890877313 scopus 로고    scopus 로고
    • Modulation of human alpha-synuclein aggregation by a combined effect of calcium and dopamine
    • Jain M.K., Bhat R. Modulation of human alpha-synuclein aggregation by a combined effect of calcium and dopamine. Neurobiol. Dis. 2014, 63:115-128.
    • (2014) Neurobiol. Dis. , vol.63 , pp. 115-128
    • Jain, M.K.1    Bhat, R.2
  • 35
    • 84874962928 scopus 로고    scopus 로고
    • Review: Membrane-associated misfolded protein propagation in natural transmissible spongiform encephalopathies (TSEs), synthetic prion diseases and Alzheimer's disease
    • Jeffrey M. Review: Membrane-associated misfolded protein propagation in natural transmissible spongiform encephalopathies (TSEs), synthetic prion diseases and Alzheimer's disease. Neuropathol. Appl. Neurobiol. 2013, 39:196-216.
    • (2013) Neuropathol. Appl. Neurobiol. , vol.39 , pp. 196-216
    • Jeffrey, M.1
  • 36
    • 84855972240 scopus 로고    scopus 로고
    • Neuropathology of sporadic Parkinson's disease: Evaluation and changes of concepts
    • Jellinger K.A. Neuropathology of sporadic Parkinson's disease: Evaluation and changes of concepts. Mov. Disord. 2012, 27:8-30.
    • (2012) Mov. Disord. , vol.27 , pp. 8-30
    • Jellinger, K.A.1
  • 39
    • 53149130592 scopus 로고    scopus 로고
    • Nigral burden of alpha-synuclein correlates with striatal dopamine deficit
    • Kovacs G.G., Milenkovic I.J., Preusser M., Budka H. Nigral burden of alpha-synuclein correlates with striatal dopamine deficit. Mov. Disord. 2008, 23:1608-1612.
    • (2008) Mov. Disord. , vol.23 , pp. 1608-1612
    • Kovacs, G.G.1    Milenkovic, I.J.2    Preusser, M.3    Budka, H.4
  • 40
    • 77953023964 scopus 로고    scopus 로고
    • Protein coding of neurodegenerative dementias: The neuropathological basis of biomarker diagnostics
    • Kovacs G.G., Botond G., Budka H. Protein coding of neurodegenerative dementias: The neuropathological basis of biomarker diagnostics. Acta Neuropathol. 2010, 119:389-408.
    • (2010) Acta Neuropathol. , vol.119 , pp. 389-408
    • Kovacs, G.G.1    Botond, G.2    Budka, H.3
  • 41
    • 84857612755 scopus 로고    scopus 로고
    • Intraneuronal immunoreactivity for the prion protein distinguishes a subset of E200K genetic from sporadic Creutzfeldt-Jakob disease
    • Kovacs G.G., Molnar K., Keller E., Botond G., Budka H., Laszlo L. Intraneuronal immunoreactivity for the prion protein distinguishes a subset of E200K genetic from sporadic Creutzfeldt-Jakob disease. J. Neuropathol. Exp. Neurol. 2012, 71:223-232.
    • (2012) J. Neuropathol. Exp. Neurol. , vol.71 , pp. 223-232
    • Kovacs, G.G.1    Molnar, K.2    Keller, E.3    Botond, G.4    Budka, H.5    Laszlo, L.6
  • 43
    • 79952796718 scopus 로고    scopus 로고
    • Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways
    • Ladiwala A.R., Dordick J.S., Tessier P.M. Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways. J. Biol. Chem. 2011, 286:3209-3218.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3209-3218
    • Ladiwala, A.R.1    Dordick, J.S.2    Tessier, P.M.3
  • 44
    • 0025098673 scopus 로고
    • Ubiquitinated protein conjugates are specifically enriched in the lysosomal system of fibroblasts
    • Laszlo L., Doherty F.J., Osborn N.U., Mayer R.J. Ubiquitinated protein conjugates are specifically enriched in the lysosomal system of fibroblasts. FEBS Lett. 1990, 261:365-368.
    • (1990) FEBS Lett. , vol.261 , pp. 365-368
    • Laszlo, L.1    Doherty, F.J.2    Osborn, N.U.3    Mayer, R.J.4
  • 45
    • 0025785896 scopus 로고
    • The latent membrane protein-1 in Epstein-Barr virus-transformed lymphoblastoid cells is found with ubiquitin-protein conjugates and heat-shock protein 70 in lysosomes oriented around the microtubule organizing centre
    • Laszlo L., Tuckwell J., Self T., Lowe J., Landon M., Smith S., Hawthorne J.N., Mayer R.J. The latent membrane protein-1 in Epstein-Barr virus-transformed lymphoblastoid cells is found with ubiquitin-protein conjugates and heat-shock protein 70 in lysosomes oriented around the microtubule organizing centre. J. Pathol. 1991, 164:203-214.
    • (1991) J. Pathol. , vol.164 , pp. 203-214
    • Laszlo, L.1    Tuckwell, J.2    Self, T.3    Lowe, J.4    Landon, M.5    Smith, S.6    Hawthorne, J.N.7    Mayer, R.J.8
  • 47
    • 40749094842 scopus 로고    scopus 로고
    • Origins and effects of extracellular alpha-synuclein: Implications in Parkinson's disease
    • Lee S.J. Origins and effects of extracellular alpha-synuclein: Implications in Parkinson's disease. J. Mol. Neurosci. 2008, 34:17-22.
    • (2008) J. Mol. Neurosci. , vol.34 , pp. 17-22
    • Lee, S.J.1
  • 49
    • 84884231134 scopus 로고    scopus 로고
    • Breaking the code of amyloid-oligomers
    • Lesne S.E. Breaking the code of amyloid-oligomers. Int. J. Cell Biol. 2013, 2013:950783.
    • (2013) Int. J. Cell Biol. , vol.2013 , pp. 950783
    • Lesne, S.E.1
  • 53
    • 78449240570 scopus 로고    scopus 로고
    • Polymorphic C-terminal beta-sheet interactions determine the formation of fibril or amyloid beta-derived diffusible ligand-like globulomer for the Alzheimer Abeta42 dodecamer
    • Ma B., Nussinov R. Polymorphic C-terminal beta-sheet interactions determine the formation of fibril or amyloid beta-derived diffusible ligand-like globulomer for the Alzheimer Abeta42 dodecamer. J. Biol. Chem. 2010, 285:37102-37110.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37102-37110
    • Ma, B.1    Nussinov, R.2
  • 55
    • 0029966886 scopus 로고    scopus 로고
    • Catecholaminergic and serotoninergic fibres innervate the ventricular system of the hedgehog CNS
    • Michaloudi H.C., Papadopoulos G.C. Catecholaminergic and serotoninergic fibres innervate the ventricular system of the hedgehog CNS. J. Anat. 1996, 189(Pt 2):273-283.
    • (1996) J. Anat. , vol.189 , Issue.Pt 2 , pp. 273-283
    • Michaloudi, H.C.1    Papadopoulos, G.C.2
  • 57
    • 41549154550 scopus 로고    scopus 로고
    • Phosphorylation of tau and alpha-synuclein in synaptic-enriched fractions of the frontal cortex in Alzheimer's disease, and in Parkinson's disease and related alpha-synucleinopathies
    • Muntane G., Dalfo E., Martinez A., Ferrer I. Phosphorylation of tau and alpha-synuclein in synaptic-enriched fractions of the frontal cortex in Alzheimer's disease, and in Parkinson's disease and related alpha-synucleinopathies. Neuroscience 2008, 152:913-923.
    • (2008) Neuroscience , vol.152 , pp. 913-923
    • Muntane, G.1    Dalfo, E.2    Martinez, A.3    Ferrer, I.4
  • 59
    • 58149379599 scopus 로고    scopus 로고
    • Optical reporters for the conformation of alpha-synuclein reveal a specific interaction with mitochondria
    • Nakamura K., Nemani V.M., Wallender E.K., Kaehlcke K., Ott M., Edwards R.H. Optical reporters for the conformation of alpha-synuclein reveal a specific interaction with mitochondria. J. Neurosci. 2008, 28:12305-12317.
    • (2008) J. Neurosci. , vol.28 , pp. 12305-12317
    • Nakamura, K.1    Nemani, V.M.2    Wallender, E.K.3    Kaehlcke, K.4    Ott, M.5    Edwards, R.H.6
  • 60
    • 67650243261 scopus 로고    scopus 로고
    • Parkin-induced mitophagy in the pathogenesis of Parkinson disease
    • Narendra D., Tanaka A., Suen D.F., Youle R.J. Parkin-induced mitophagy in the pathogenesis of Parkinson disease. Autophagy 2009, 5:706-708.
    • (2009) Autophagy , vol.5 , pp. 706-708
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 62
    • 0030561937 scopus 로고    scopus 로고
    • The supra-ependymal innervation is not responsible for the repression of tight junctions in the rat cerebral ependyma
    • Rodriguez P., Bouchaud C. The supra-ependymal innervation is not responsible for the repression of tight junctions in the rat cerebral ependyma. Neurobiology 1996, 4:185-201.
    • (1996) Neurobiology , vol.4 , pp. 185-201
    • Rodriguez, P.1    Bouchaud, C.2
  • 66
    • 79957606041 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Schapira A.H., Jenner P. Etiology and pathogenesis of Parkinson's disease. Mov. Disord. 2011, 26:1049-1055.
    • (2011) Mov. Disord. , vol.26 , pp. 1049-1055
    • Schapira, A.H.1    Jenner, P.2
  • 68
    • 33846949357 scopus 로고    scopus 로고
    • The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation
    • Siegel S.J., Bieschke J., Powers E.T., Kelly J.W. The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation. Biochemistry 2007, 46:1503-1510.
    • (2007) Biochemistry , vol.46 , pp. 1503-1510
    • Siegel, S.J.1    Bieschke, J.2    Powers, E.T.3    Kelly, J.W.4
  • 69
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen D.F., Norris K.L., Youle R.J. Mitochondrial dynamics and apoptosis. Genes Dev. 2008, 22:1577-1590.
    • (2008) Genes Dev. , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 70
    • 33947605407 scopus 로고    scopus 로고
    • Alpha-synuclein overexpression reduces gap junctional intercellular communication in dopaminergic neuroblastoma cells
    • Sung J.Y., Lee H.J., Jeong E.I., Oh Y., Park J., Kang K.S., Chung K.C. Alpha-synuclein overexpression reduces gap junctional intercellular communication in dopaminergic neuroblastoma cells. Neurosci. Lett. 2007, 416:289-293.
    • (2007) Neurosci. Lett. , vol.416 , pp. 289-293
    • Sung, J.Y.1    Lee, H.J.2    Jeong, E.I.3    Oh, Y.4    Park, J.5    Kang, K.S.6    Chung, K.C.7
  • 72
    • 77950499364 scopus 로고    scopus 로고
    • Parkin-mediated selective mitochondrial autophagy, mitophagy: Parkin purges damaged organelles from the vital mitochondrial network
    • Tanaka A. Parkin-mediated selective mitochondrial autophagy, mitophagy: Parkin purges damaged organelles from the vital mitochondrial network. FEBS Lett. 2010, 584:1386-1392.
    • (2010) FEBS Lett. , vol.584 , pp. 1386-1392
    • Tanaka, A.1
  • 74
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Taraboulos A., Scott M., Semenov A., Avrahami D., Laszlo L., Prusiner S.B. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J. Cell Biol. 1995, 129:121-132.
    • (1995) J. Cell Biol. , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avrahami, D.4    Laszlo, L.5    Prusiner, S.B.6
  • 75
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders
    • Uversky V.N. A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn. 2003, 21:211-234.
    • (2003) J. Biomol. Struct. Dyn. , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 80
    • 33846817163 scopus 로고    scopus 로고
    • Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity
    • Volles M.J., Lansbury P.T. Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity. J. Mol. Biol. 2007, 366:1510-1522.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1510-1522
    • Volles, M.J.1    Lansbury, P.T.2
  • 81
    • 0033973421 scopus 로고    scopus 로고
    • NACP/alpha-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson's disease brains
    • Wakabayashi K., Hayashi S., Yoshimoto M., Kudo H., Takahashi H. NACP/alpha-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson's disease brains. Acta Neuropathol. 2000, 99:14-20.
    • (2000) Acta Neuropathol. , vol.99 , pp. 14-20
    • Wakabayashi, K.1    Hayashi, S.2    Yoshimoto, M.3    Kudo, H.4    Takahashi, H.5
  • 82
    • 77949905345 scopus 로고    scopus 로고
    • Fibrillar oligomers nucleate the oligomerization of monomeric amyloid beta but do not seed fibril formation
    • Wu J.W., Breydo L., Isas J.M., Lee J., Kuznetsov Y.G., Langen R., Glabe C. Fibrillar oligomers nucleate the oligomerization of monomeric amyloid beta but do not seed fibril formation. J. Biol. Chem. 2010, 285:6071-6079.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6071-6079
    • Wu, J.W.1    Breydo, L.2    Isas, J.M.3    Lee, J.4    Kuznetsov, Y.G.5    Langen, R.6    Glabe, C.7
  • 83
    • 84863325404 scopus 로고    scopus 로고
    • Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease
    • Xie W., Chung K.K. Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease. J. Neurochem. 2012, 122:404-414.
    • (2012) J. Neurochem. , vol.122 , pp. 404-414
    • Xie, W.1    Chung, K.K.2
  • 84
    • 0038404977 scopus 로고    scopus 로고
    • Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers
    • Yamin G., Uversky V.N., Fink A.L. Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers. FEBS Lett. 2003, 542:147-152.
    • (2003) FEBS Lett. , vol.542 , pp. 147-152
    • Yamin, G.1    Uversky, V.N.2    Fink, A.L.3
  • 86
    • 74849125564 scopus 로고    scopus 로고
    • Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions
    • Zhou W., Long C., Reaney S.H., Di Monte D.A., Fink A.L., Uversky V.N. Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions. Biochim. Biophys. Acta 2010, 1802:322-330.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 322-330
    • Zhou, W.1    Long, C.2    Reaney, S.H.3    Di Monte, D.A.4    Fink, A.L.5    Uversky, V.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.