메뉴 건너뛰기




Volumn 452, Issue 1, 2013, Pages 1-17

The cell biology of prion-like spread of protein aggregates: Mechanisms and implication in neurodegeneration

Author keywords

A synuclein; Amyloid ; Cell to cell transfer; Huntingtin; Prion like; Tau

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; CASPASE 3; HUNTINGTIN; PRION PROTEIN; TAU PROTEIN;

EID: 84876945450     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121898     Document Type: Review
Times cited : (116)

References (215)
  • 2
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron x-ray diffraction
    • Sunde, M., Serpell, L. C., Bartlam, M., Fraser, P. E., Pepys, M. B. and Blake, C. C. (1997) Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273, 729-739
    • (1997) J. Mol. Biol , Issue.273 , pp. 729-739
    • Sunde, M.1    Serpell, L.C.2    Bartlam, M.3    Fraser, P.E.4    Pepys, M.B.5    Blake, C.C.6
  • 3
    • 70349705441 scopus 로고    scopus 로고
    • Prions: Protein aggregation and infectious diseases
    • Aguzzi, A. and Calella, A. M. (2009) Prions: protein aggregation and infectious diseases. Physiol. Rev. 89, 1105-1152
    • (2009) Physiol. Rev , Issue.89 , pp. 1105-1152
    • Aguzzi, A.1    Calella, A.M.2
  • 5
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi, A. and Rajendran, L. (2009) The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64, 783-790
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 6
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin, P., Melki, R. and Kopito, R. (2010) Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell Biol. 11, 301-307
    • (2010) Nat. Rev. Mol. Cell Biol , Issue.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 9
    • 33745018376 scopus 로고    scopus 로고
    • The genetics of neurodegenerative diseases
    • Hardy, J. and Orr, H. (2006) The genetics of neurodegenerative diseases. J. Neurochem. 97, 1690-1699
    • (2006) J. Neurochem , vol.97 , pp. 1690-1699
    • Hardy, J.1    Orr, H.2
  • 11
    • 79959623739 scopus 로고    scopus 로고
    • The role of lipid rafts in prion protein biology
    • Lewis, V. and Hooper, N. M. (2011) The role of lipid rafts in prion protein biology. Front. Biosci. 16, 151-168
    • (2011) Front. Biosci , Issue.16 , pp. 151-168
    • Lewis, V.1    Hooper, N.M.2
  • 15
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in alzheimer disease and other neurodegenerative disorders
    • Jucker, M. and Walker, L. C. (2011) Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann. Neurol. 70, 532-540
    • (2011) Ann. Neurol , Issue.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 16
    • 80053563923 scopus 로고    scopus 로고
    • Misfolded protein aggregates: Mechanisms, structures and potential for disease transmission
    • Moreno-Gonzalez, I. and Soto, C. (2011) Misfolded protein aggregates: mechanisms, structures and potential for disease transmission. Semin. Cell Dev. Biol. 22, 482-487
    • (2011) Semin. Cell Dev. Biol , Issue.22 , pp. 482-487
    • Moreno-Gonzalez, I.1    Soto, C.2
  • 17
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost, B. and Diamond, M. I. (2010) Prion-like mechanisms in neurodegenerative diseases. Nat. Rev. Neurosci. 11, 155-159
    • (2010) Nat. Rev. Neurosci , Issue.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 18
    • 70349581486 scopus 로고    scopus 로고
    • The expanding realm of prion phenomena in neurodegenerative disease
    • Frost, B. and Diamond, M. I. (2009) The expanding realm of prion phenomena in neurodegenerative disease. Prion 3, 74-77
    • (2009) Prion , vol.3 , pp. 74-77
    • Frost, B.1    Diamond, M.I.2
  • 19
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in alzheimer's β-Amyloid fibrils
    • Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P. and Tycko, R. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's β-Amyloid fibrils. Science 307, 262-265
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 20
    • 63649160214 scopus 로고    scopus 로고
    • Conformational diversity of wild-type tau fibrils specified by templated conformation change
    • Frost, B., Ollesch, J., Wille, H. and Diamond, M. I. (2009) Conformational diversity of wild-type Tau fibrils specified by templated conformation change. J. Biol. Chem. 284, 3546-3551
    • (2009) J. Biol. Chem , Issue.284 , pp. 3546-3551
    • Frost, B.1    Ollesch, J.2    Wille, H.3    Diamond, M.I.4
  • 21
    • 0026595846 scopus 로고
    • Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert, M., Spillantini, M. G., Cairns, N. J. and Crowther, R. A. (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8, 159-168
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 22
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida, Y., Kurosawa, M., Nukina, N., Ito, K., Oda, T. and Tanaka, M. (2009) Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc. Natl. Acad. Sci. U.S.A. 106, 9679-9684
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 23
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: Blurring the divide between transmissibility and infectivity
    • Cushman, M., Johnson, B. S., King, O. D., Gitler, A. D. and Shorter, J. (2010) Prion-like disorders: blurring the divide between transmissibility and infectivity. J. Cell Sci. 123, 1191-1201
    • (2010) J. Cell Sci , Issue.123 , pp. 1191-1201
    • Cushman, M.1    Johnson, B.S.2    King, O.D.3    Gitler, A.D.4    Shorter, J.5
  • 24
    • 74249089262 scopus 로고    scopus 로고
    • Prion-like propagation of cytosolic protein aggregates: Insights from cell culture models
    • Krammer, C., Scȟatzl, H. M. and Vorberg, I. (2009) Prion-like propagation of cytosolic protein aggregates: insights from cell culture models. Prion 3, 206-212
    • (2009) Prion , vol.3 , pp. 206-212
    • Krammer, C.1    Scȟatzl, H.M.2    Vorberg, I.3
  • 25
    • 84860686110 scopus 로고    scopus 로고
    • Can parkinson's disease pathology be propagated from one neuron to anotheř
    • Dunning, C. J. R., Reyes, J. F., Steiner, J. A. and Brundin, P. (2011) Can Parkinson's disease pathology be propagated from one neuron to anotheř Prog. Neurobiol. 97, 205-219
    • (2011) Prog. Neurobiol , Issue.97 , pp. 205-219
    • Dunning, C.J.R.1    Reyes, J.F.2    Steiner, J.A.3    Brundin, P.4
  • 26
    • 84863694542 scopus 로고    scopus 로고
    • Is tau ready for admission to the prion club?
    • Hall, G. F. and Patuto, B. A. (2012) Is tau ready for admission to the prion club? Prion 6, 223-233
    • (2012) Prion , vol.6 , pp. 223-233
    • Hall, G.F.1    Patuto, B.A.2
  • 28
    • 0025863618 scopus 로고
    • Neuropathological stageing of alzheimer-related changes
    • Braak, H. and Braak, E. (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82, 239-259
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 29
    • 84858017006 scopus 로고    scopus 로고
    • Intercellular (mis)communication in neurodegenerative disease
    • Garden, G. A. and La Spada, A. R. (2012) Intercellular (mis)communication in neurodegenerative disease. Neuron 73, 886-901
    • (2012) Neuron , vol.73 , pp. 886-901
    • Garden, G.A.1    La Spada, A.R.2
  • 30
    • 79960167259 scopus 로고    scopus 로고
    • Selective neuronal vulnerability in neurodegenerative diseases: From stressor thresholds to degeneration
    • Saxena, S. and Caroni, P. (2011) Selective neuronal vulnerability in neurodegenerative diseases: from stressor thresholds to degeneration. Neuron 71, 35-48
    • (2011) Neuron , vol.71 , pp. 35-48
    • Saxena, S.1    Caroni, P.2
  • 31
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Protein misfolding revisited
    • Williams, A. J. and Paulson, H. L. (2008) Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci. 31, 521-528
    • (2008) Trends Neurosci , Issue.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 32
    • 79959923467 scopus 로고    scopus 로고
    • Protein aggregate spreading in neurodegenerative diseases: Problems and perspectives
    • Lee, S.-J., Lim, H.-S., Masliah, E. and Lee, H.-J. (2011) Protein aggregate spreading in neurodegenerative diseases: problems and perspectives. Neurosci. Res. 70, 339-348
    • (2011) Neurosci. Res , Issue.70 , pp. 339-348
    • Lee, S.-J.1    Lim, H.-S.2    Masliah, E.3    Lee, H.-J.4
  • 33
    • 35949004474 scopus 로고    scopus 로고
    • Parkinson's disease: A dual-hit hypothesis. Neuropathol
    • Hawkes, C. H., Del Tredici, K. and Braak, H. (2007) Parkinson's disease: a dual-hit hypothesis. Neuropathol. Appl. Neurobiol. 33, 599-614
    • (2007) Appl. Neurobiol , vol.33 , pp. 599-614
    • Hawkes, C.H.1    Del Tredici, K.2    Braak, H.3
  • 34
    • 68649095434 scopus 로고    scopus 로고
    • Parkinson's disease: The dual hit theory revisited
    • Hawkes, C. H., Del Tredici, K. and Braak, H. (2009) Parkinson's disease: the dual hit theory revisited. Ann. N.Y. Acad. Sci. 1170, 615-622
    • (2009) Ann. N.Y. Acad. Sci , vol.1170 , pp. 615-622
    • Hawkes, C.H.1    Del Tredici, K.2    Braak, H.3
  • 35
    • 0034531475 scopus 로고    scopus 로고
    • The α-synucleinopathies: Parkinson's disease, dementia with lewy bodies, and multiple system atrophy
    • Spillantini, M. G. and Goedert, M. (2000) The α-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Ann. N.Y. Acad. Sci. 920, 16-27
    • (2000) Ann. N.Y. Acad. Sci , vol.920 , pp. 16-27
    • Spillantini, M.G.1    Goedert, M.2
  • 36
    • 41849133159 scopus 로고    scopus 로고
    • Cerebral cortex and the clinical expression of huntington's disease: Complexity and heterogeneity
    • Rosas, H. D., Salat, D. H., Lee, S. Y., Zaleta, A. K., Pappu, V., Fischl, B., Greve, D., Hevelone, N. and Hersch, S. M. (2008) Cerebral cortex and the clinical expression of Huntington's disease: complexity and heterogeneity. Brain 131, 1057-1068
    • (2008) Brain , vol.131 , pp. 1057-1068
    • Rosas, H.D.1    Salat, D.H.2    Lee, S.Y.3    Zaleta, A.K.4    Pappu, V.5    Fischl, B.6    Greve, D.7    Hevelone, N.8    Hersch, S.M.9
  • 38
    • 2942625910 scopus 로고    scopus 로고
    • Differential loss of striatal projection systems in huntington's disease: A quantitative immunohistochemical study
    • Deng, Y. P., Albin, R. L., Penney, J. B., Young, A. B., Anderson, K. D. and Reiner, A. (2004) Differential loss of striatal projection systems in Huntington's disease: a quantitative immunohistochemical study. J. Chem. Neuroanat. 27, 143-164
    • (2004) J. Chem. Neuroanat , vol.27 , pp. 143-164
    • Deng, Y.P.1    Albin, R.L.2    Penney, J.B.3    Young, A.B.4    Anderson, K.D.5    Reiner, A.6
  • 40
    • 33846551867 scopus 로고    scopus 로고
    • The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies
    • Beekes, M. and McBride, P. A. (2007) The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies. FEBS J. 274, 588-605
    • (2007) FEBS J , vol.274 , pp. 588-605
    • Beekes, M.1    McBride, P.A.2
  • 44
    • 33645833848 scopus 로고    scopus 로고
    • Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for parkinson's disease
    • El-Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Curran, M. D., Gibson, M. J., Court, J. A., Schlossmacher, M. G. and Allsop, D. (2006) Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB J. 20, 419-425
    • (2006) FASEB J , vol.20 , pp. 419-425
    • El-Agnaf, O.M.A.1    Salem, S.A.2    Paleologou, K.E.3    Curran, M.D.4    Gibson, M.J.5    Court, J.A.6    Schlossmacher, M.G.7    Allsop, D.8
  • 47
    • 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. and 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.4    Olanow, C.W.5
  • 48
    • 61449216234 scopus 로고    scopus 로고
    • Transplanted dopaminergic neurons develop pd pathologic changes: A second case report
    • Kordower, J. H., Chu, Y., Hauser, R. A., Olanow, C. W. and Freeman, T. B. (2008) Transplanted dopaminergic neurons develop PD pathologic changes: a second case report. Mov. Disord. 23, 2303-2306
    • (2008) Mov. Disord , vol.23 , pp. 2303-2306
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Olanow, C.W.4    Freeman, T.B.5
  • 50
    • 77949820437 scopus 로고    scopus 로고
    • Characterization of lewy body pathology in 12- and 16-year-old intrastriatal mesencephalic grafts surviving in a patient with parkinson's disease
    • Li, J.-Y., Englund, E., Widner, H., Rehncrona, S., Bǰorklund, A., Lindvall, O. and Brundin, P. (2010) Characterization of Lewy body pathology in 12- and 16-year-old intrastriatal mesencephalic grafts surviving in a patient with Parkinson's disease. Mov. Disord. 25, 1091-1096
    • (2010) Mov. Disord , Issue.25 , pp. 1091-1096
    • Li, J.-Y.1    Englund, E.2    Widner, H.3    Rehncrona, S.4    Bǰorklund, A.5    Lindvall, O.6    Brundin, P.7
  • 51
  • 52
    • 52449117926 scopus 로고    scopus 로고
    • Research in motion: The enigma of parkinson's disease pathology spread
    • Brundin, P., Li, J.-Y., Holton, J. L., Lindvall, O. and Revesz, T. (2008) Research in motion: the enigma of Parkinson's disease pathology spread. Nat. Rev. Neurosci. 9, 741-745
    • (2008) Nat. Rev. Neurosci , vol.9 , pp. 741-745
    • Brundin, P.1    Li, J.-Y.2    Holton, J.L.3    Lindvall, O.4    Revesz, T.5
  • 56
    • 77950571596 scopus 로고    scopus 로고
    • Direct transfer of α-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies
    • Lee, H.-J., Suk, J.-E., Patrick, C., Bae, E.-J., Cho, J.-H., Rho, S., Hwang, D., Masliah, E. and Lee, S.-J. (2010) Direct transfer of α-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies. J. Biol. Chem. 285, 9262-9272
    • (2010) J. Biol. Chem , Issue.285 , pp. 9262-9272
    • Lee, H.-J.1    Suk, J.-E.2    Patrick, C.3    Bae, E.-J.4    Cho, J.-H.5    Rho, S.6    Hwang, D.7    Masliah, E.8    Lee, S.-J.9
  • 58
    • 77949706598 scopus 로고    scopus 로고
    • A novel, high-efficiency cellular model of fibrillar α-synuclein inclusions and the examination of mutations that inhibit amyloid formation
    • Waxman, E. A. and Giasson, B. I. (2010) A novel, high-efficiency cellular model of fibrillar α-synuclein inclusions and the examination of mutations that inhibit amyloid formation. J. Neurochem. 113, 374-388
    • (2010) J. Neurochem , Issue.113 , pp. 374-388
    • Waxman, E.A.1    Giasson, B.I.2
  • 59
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology
    • Danzer, K. M., Krebs, S. K., Wolff, M., Birk, G. and Hengerer, B. (2009) Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology. J. Neurochem. 111, 192-203
    • (2009) J. Neurochem , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 60
    • 78049376559 scopus 로고    scopus 로고
    • Seeded aggregation and toxicity of α-synuclein and tau: Cellular models of neurodegenerative diseases
    • Nonaka, T., Watanabe, S. T., Iwatsubo, T. and Hasegawa, M. (2010) Seeded aggregation and toxicity of α-synuclein and tau: cellular models of neurodegenerative diseases. J. Biol. Chem. 285, 34885-34898
    • (2010) J. Biol. Chem , Issue.285 , pp. 34885-34898
    • Nonaka, T.1    Watanabe, S.T.2    Iwatsubo, T.3    Hasegawa, M.4
  • 62
    • 84864915936 scopus 로고    scopus 로고
    • Suppression of dynamin gtpase decreases α-synuclein uptake by neuronal and oligodendroglial cells: A potent therapeutic target for synucleinopathy
    • Konno, M., Hasegawa, T., Baba, T., Miura, E., Sugeno, N., Kikuchi, A., Fiesel, F. C., Sasaki, T., Aoki, M., Itoyama, Y. et al. (2012) Suppression of dynamin GTPase decreases α-synuclein uptake by neuronal and oligodendroglial cells: a potent therapeutic target for synucleinopathy. Mol. Neurodegener. 7, 38
    • (2012) Mol. Neurodegener , Issue.7 , pp. 38
    • Konno, M.1    Hasegawa, T.2    Baba, T.3    Miura, E.4    Sugeno, N.5    Kikuchi, A.6    Fiesel, F.C.7    Sasaki, T.8    Aoki, M.9    Itoyama, Y.10
  • 63
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice
    • Luk, K. C., Kehm, V. M., Zhang, B., O'Brien, P., Trojanowski, J. Q. and Lee, V. M.-Y. (2012) Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. J. Exp. Med. 209, 975-986
    • (2012) J. Exp. Med , Issue.209 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3    O'Brien, P.4    Trojanowski, J.5    Lee, V.6
  • 65
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates parkinson-like neurodegeneration in nontransgenic mice
    • Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O'Brien, P., Trojanowski, J. Q. and Lee, V. M.-Y. (2012) Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338, 949-953
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6    Lee, V.M.-Y.7
  • 68
    • 84864378643 scopus 로고    scopus 로고
    • What is the pathological significance of tau oligomers?
    • Cowan, C. M., Quraishe, S. and Mudher, A. (2012) What is the pathological significance of tau oligomers? Biochem. Soc. Trans. 40, 693-697
    • (2012) Biochem. Soc. Trans , Issue.40 , pp. 693-697
    • Cowan, C.M.1    Quraishe, S.2    Mudher, A.3
  • 72
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost, B., Jacks, R. L. and Diamond, M. I. (2009) Propagation of tau misfolding from the outside to the inside of a cell. J. Biol. Chem. 284, 12845-12852
    • (2009) J. Biol. Chem , Issue.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 73
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal tau by pathological tau conformers drives pathogenesis of alzheimer-like tangles
    • Guo, J. L. and Lee, V. M.-Y. (2011) Seeding of normal tau by pathological tau conformers drives pathogenesis of Alzheimer-like tangles. J. Biol. Chem. 286, 15317-15331
    • (2011) J. Biol. Chem , Issue.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.-Y.2
  • 74
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-β in alzheimer's disease
    • LaFerla, F. M., Green, K. N. and Oddo, S. (2007) Intracellular amyloid-β in Alzheimer's disease. Nat. Rev. Neurosci. 8, 499-509
    • (2007) Nat. Rev. Neurosci , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 75
    • 77953019895 scopus 로고    scopus 로고
    • Intraneuronal β-Amyloid accumulation and synapse pathology in alzheimer's disease
    • Gouras, G. K., Tampellini, D., Takahashi, R. H. and Capetillo-Zarate, E. (2010) Intraneuronal β-Amyloid accumulation and synapse pathology in Alzheimer's disease. Acta Neuropathol. 119, 523-541
    • (2010) Acta Neuropathol , vol.119 , pp. 523-541
    • Gouras, G.K.1    Tampellini, D.2    Takahashi, R.H.3    Capetillo-Zarate, E.4
  • 77
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 78
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of β-Amyloid by intracerebral infusion of alzheimer brain extracts in β-Amyloid precursor protein-transgenic mice
    • Kane, M. D., Lipinski, W. J., Callahan, M. J., Bian, F., Durham, R. A., Schwarz, R. D., Roher, A. E. and Walker, L. C. (2000) Evidence for seeding of β-Amyloid by intracerebral infusion of Alzheimer brain extracts in β-Amyloid precursor protein-transgenic mice. J. Neurosci. 20, 3606-3611
    • (2000) J. Neurosci , Issue.20 , pp. 3606-3611
    • Kane, M.D.1    Lipinski, W.J.2    Callahan, M.J.3    Bian, F.4    Durham, R.A.5    Schwarz, R.D.6    Roher, A.E.7    Walker, L.C.8
  • 84
    • 79952619322 scopus 로고    scopus 로고
    • Tunneling-nanotube development in astrocytes depends on p53 activation
    • Wang, Y., Cui, J., Sun, X. and Zhang, Y. (2011) Tunneling-nanotube development in astrocytes depends on p53 activation. Cell Death Differ. 18, 732-742
    • (2011) Cell Death Differ , Issue.18 , pp. 732-742
    • Wang, Y.1    Cui, J.2    Sun, X.3    Zhang, Y.4
  • 85
    • 84862868531 scopus 로고    scopus 로고
    • Spreading of neurodegenerative pathology via neuron-to-neuron transmission of β-Amyloid
    • Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J. and Hallbeck, M. (2012) Spreading of neurodegenerative pathology via neuron-to-neuron transmission of β-Amyloid. J. Neurosci. 32, 8767-8777
    • (2012) J. Neurosci , Issue.32 , pp. 8767-8777
    • Nath, S.1    Agholme, L.2    Kurudenkandy, F.R.3    Granseth, B.4    Marcusson, J.5    Hallbeck, M.6
  • 87
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P. and Aronin, N. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 88
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang, W., Dunlap, J. R., Andrews, R. B. and Wetzel, R. (2002) Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum. Mol. Genet. 11, 2905-2917
    • (2002) Hum. Mol. Genet , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 89
    • 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. and 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
  • 90
    • 84866322000 scopus 로고    scopus 로고
    • Visualization of cell-to-cell transmission of mutant huntingtin oligomers
    • Herrera, F., Tenreiro, S., Miller-Fleming, L. and Outeiro, T. F. (2011) Visualization of cell-to-cell transmission of mutant huntingtin oligomers. PLoS Curr. 3, RRN1210
    • (2011) PLoS Curr , vol.3
    • Herrera, F.1    Tenreiro, S.2    Miller-Fleming, L.3    Outeiro, T.F.4
  • 91
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou, F., Finkbeiner, S., Devys, D. and Greenberg, M. E. (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55-66
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 92
    • 57049184027 scopus 로고    scopus 로고
    • Phosphorylation of mutant huntingtin at s421 restores anterograde and retrograde transport in neurons
    • Zala, D., Colin, E., Rangone, H., Liot, G., Humbert, S. and Saudou, F. (2008) Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons. Hum. Mol. Genet. 17, 3837-3846
    • (2008) Hum. Mol. Genet , vol.17 , pp. 3837-3846
    • Zala, D.1    Colin, E.2    Rangone, H.3    Liot, G.4    Humbert, S.5    Saudou, F.6
  • 94
    • 77957329900 scopus 로고    scopus 로고
    • Pathways of unconventional protein secretion
    • Nickel, W. (2010) Pathways of unconventional protein secretion. Curr. Opin. Biotechnol. 21, 621-626
    • (2010) Curr. Opin. Biotechnol , Issue.21 , pp. 621-626
    • Nickel, W.1
  • 95
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W. and Rabouille, C. (2009) Mechanisms of regulated unconventional protein secretion. Nat. Rev. Mol. Cell Biol. 10, 148-155
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 96
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of α-synuclein and its aggregates
    • Lee, H.-J., Patel, S. and Lee, S.-J. (2005) Intravesicular localization and exocytosis of α-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
  • 97
    • 77951885732 scopus 로고    scopus 로고
    • Non-classical exocytosis of α-synuclein is sensitive to folding states and promoted under stress conditions
    • Jang, A., Lee, H.-J., Suk, J.-E., Jung, J.-W., Kim, K.-P. and Lee, S.-J. (2010) Non-classical exocytosis of α-synuclein is sensitive to folding states and promoted under stress conditions. J. Neurochem. 113, 1263-1274
    • (2010) J. Neurochem , Issue.113 , pp. 1263-1274
    • Jang, A.1    Lee, H.-J.2    Suk, J.-E.3    Jung, J.-W.4    Kim K.-P Lee, S.-J.5
  • 98
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W. S., Jonas, A., Clayton, D. F. and George, J. M. (1998) Stabilization of α-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273, 9443-9449
    • (1998) J. Biol. Chem , Issue.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 100
    • 33847022701 scopus 로고    scopus 로고
    • Gm1 specifically interacts with α-synuclein and inhibits fibrillation
    • Martinez, Z., Zhu, M., Han, S. and Fink, A. L. (2007) GM1 specifically interacts with α-synuclein and inhibits fibrillation. Biochemistry 46, 1868-1877
    • (2007) Biochemistry , vol.46 , pp. 1868-1877
    • Martinez, Z.1    Zhu, M.2    Han, S.3    Fink, A.L.4
  • 101
    • 84855444970 scopus 로고    scopus 로고
    • Biophysics of α-synuclein membrane interactions
    • Pfefferkorn, C. M., Jiang, Z. and Lee, J. C. (2012) Biophysics of α-synuclein membrane interactions. Biochim. Biophys. Acta 1818, 162-171
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 162-171
    • Pfefferkorn, C.M.1    Jiang, Z.2    Lee, J.C.3
  • 102
    • 33644954146 scopus 로고    scopus 로고
    • Amino acid sequence motifs and mechanistic features of the membrane translocation of α-synuclein
    • Ahn, K. J., Paik, S. R., Chung, K. C. and Kim, J. (2006) Amino acid sequence motifs and mechanistic features of the membrane translocation of α-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
  • 103
    • 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. and Lansbury, Jr., P. T. (2001) Vesicle permeabilization by protofibrillar α-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40, 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
  • 104
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar α-synuclein is sensitive to parkinson's disease-linked mutations and occurs by a pore-like mechanism
    • Volles, M. J. and Lansbury, Jr., P. T. (2002) Vesicle permeabilization by protofibrillar α-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. Biochemistry 41, 4595-4602
    • (2002) Biochemistry , vol.41 , pp. 4595-4602
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 105
    • 0030950504 scopus 로고    scopus 로고
    • Occurrence of two types of secretory vesicles in the human neuroblastoma sh-sy5y
    • Goodall, A. R., Danks, K., Walker, J. H., Ball, S. G. and Vaughan, P. F. (1997) Occurrence of two types of secretory vesicles in the human neuroblastoma SH-SY5Y. J. Neurochem. 68, 1542-1552
    • (1997) J. Neurochem , vol.68 , pp. 1542-1552
    • Goodall, A.R.1    Danks, K.2    Walker, J.H.3    Ball, S.G.4    Vaughan, P.F.5
  • 112
    • 0034051803 scopus 로고    scopus 로고
    • Cysteine-string protein: The chaperone at the synapse
    • Chamberlain, L. H. and Burgoyne, R. D. (2000) Cysteine-string protein: the chaperone at the synapse. J. Neurochem. 74, 1781-1789
    • (2000) J. Neurochem , Issue.74 , pp. 1781-1789
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 113
    • 0032080204 scopus 로고    scopus 로고
    • Attenuated influx of calcium ions at nerve endings of csp and shibire mutant drosophila
    • Umbach, J. A., Saitoe, M., Kidokoro, Y. and Gundersen, C. B. (1998) Attenuated influx of calcium ions at nerve endings of csp and shibire mutant Drosophila . J. Neurosci. 18, 3233-3240
    • (1998) J. Neurosci , vol.18 , pp. 3233-3240
    • Umbach, J.A.1    Saitoe, M.2    Kidokoro, Y.3    Gundersen, C.B.4
  • 114
    • 0031916186 scopus 로고    scopus 로고
    • Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in drosophila but not for vesicle recycling
    • Ranjan, R., Bronk, P. and Zinsmaier, K. E. (1998) Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling. J. Neurosci. 18, 956-964
    • (1998) J. Neurosci , vol.18 , pp. 956-964
    • Ranjan, R.1    Bronk, P.2    Zinsmaier, K.E.3
  • 115
    • 0034663177 scopus 로고    scopus 로고
    • Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis in drosophila
    • Dawson-Scully, K., Bronk, P., Atwood, H. L. and Zinsmaier, K. E. (2000) Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis in Drosophila. J. Neurosci. 20, 6039-6047
    • (2000) J. Neurosci , vol.20 , pp. 6039-6047
    • Dawson-Scully, K.1    Bronk, P.2    Atwood, H.L.3    Zinsmaier, K.E.4
  • 116
    • 0032561426 scopus 로고    scopus 로고
    • Cysteine-string proteins regulate exocytosis of insulin independent from transmembrane ion fluxes
    • Zhang, H., Kelley, W. L., Chamberlain, L. H., Burgoyne, R. D., Wollheim, C. B. and Lang, J. (1998) Cysteine-string proteins regulate exocytosis of insulin independent from transmembrane ion fluxes. FEBS Lett. 437, 267-272
    • (1998) FEBS Lett , vol.437 , pp. 267-272
    • Zhang, H.1    Kelley, W.L.2    Chamberlain, L.H.3    Burgoyne, R.D.4    Wollheim, C.B.5    Lang, J.6
  • 118
    • 0034652087 scopus 로고    scopus 로고
    • Comparison of cysteine string protein (csp) and mutant α-snap overexpression reveals a role for csp in late steps of membrane fusion in dense-core granule exocytosis in adrenal chromaffin cells
    • Graham, M. E. and Burgoyne, R. D. (2000) Comparison of cysteine string protein (Csp) and mutant α-SNAP overexpression reveals a role for csp in late steps of membrane fusion in dense-core granule exocytosis in adrenal chromaffin cells. J. Neurosci. 20, 1281-1289
    • (2000) J. Neurosci , Issue.20 , pp. 1281-1289
    • Graham, M.E.1    Burgoyne, R.D.2
  • 119
    • 0032531986 scopus 로고    scopus 로고
    • The cysteine-string domain of the secretory vesicle cysteine-string protein is required for membrane targeting
    • Chamberlain, L. H. and Burgoyne, R. D. (1998) The cysteine-string domain of the secretory vesicle cysteine-string protein is required for membrane targeting. Biochem. J. 335, 205-209
    • (1998) Biochem. J , Issue.335 , pp. 205-209
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 120
    • 84860501370 scopus 로고    scopus 로고
    • Beyond α-synuclein transfer: Pathology propagation in parkinson's disease
    • Hansen, C. and Li, J.-Y. (2012) Beyond α-synuclein transfer: pathology propagation in Parkinson's disease. Trends Mol. Med. 18, 248-255
    • (2012) Trends Mol. Med , Issue.18 , pp. 248-255
    • Hansen, C.1    Li, J.-Y.2
  • 121
    • 44749090147 scopus 로고    scopus 로고
    • Clearance and deposition of extracellular α-synuclein aggregates in microglia
    • Lee, H.-J., Suk, J.-E., Bae, E.-J. and Lee, S.-J. (2008) Clearance and deposition of extracellular α-synuclein aggregates in microglia. Biochem. Biophys. Res. Commun. 372, 423-428
    • (2008) Biochem. Biophys. Res. Commun , vol.372 , pp. 423-428
    • Lee, H.-J.1    Suk, J.-E.2    Bae E.-J Lee, S.-J.3
  • 123
    • 0035920226 scopus 로고    scopus 로고
    • Induction of neuronal cell death by rab5a-dependent endocytosis of α-synuclein
    • Sung, J. Y., Kim, J., Paik, S. R., Park, J. H., Ahn, Y. S. and Chung, K. C. (2001) Induction of neuronal cell death by Rab5A-dependent endocytosis of α-synuclein. J. Biol. Chem. 276, 27441-27448
    • (2001) J. Biol. Chem , Issue.276 , pp. 27441-27448
    • Sung, J.Y.1    Kim, J.2    Paik, S.R.3    Park, J.H.4    Ahn, Y.S.5    Chung, K.C.6
  • 125
    • 67949093139 scopus 로고    scopus 로고
    • On the fate of early endosomes
    • Spang, A. (2009) On the fate of early endosomes. Biol. Chem. 390, 753-759
    • (2009) Biol. Chem , vol.390 , pp. 753-759
    • Spang, A.1
  • 127
    • 79952109595 scopus 로고    scopus 로고
    • How can mammalian rab small gtpases be comprehensively analyzed? Development of new tools to comprehensively analyze mammalian rabs in membrane traffic
    • Fukuda, M. (2010) How can mammalian Rab small GTPases be comprehensively analyzed? Development of new tools to comprehensively analyze mammalian Rabs in membrane traffic. Histol. Histopathol. 25, 1473-1480
    • (2010) Histol. Histopathol , Issue.25 , pp. 1473-1480
    • Fukuda, M.1
  • 128
    • 78651105303 scopus 로고    scopus 로고
    • Spatial restriction of receptor tyrosine kinase activity through a polarized endocytic cycle controls border cell migration
    • Assaker, G., Ramel, D., Wculek, S. K., Gonźalez-Gait́an, M. and Emery, G. (2010) Spatial restriction of receptor tyrosine kinase activity through a polarized endocytic cycle controls border cell migration. Proc. Natl. Acad. Sci. U.S.A. 107, 22558-22563
    • (2010) Proc. Natl. Acad. Sci. U.S.A , Issue.107 , pp. 22558-22563
    • Assaker, G.1    Ramel, D.2    Wculek, S.K.3    Gonźalez-Gait́an, M.4    Emery, G.5
  • 130
    • 34948870903 scopus 로고    scopus 로고
    • Identification of proteins involved in microglial endocytosis of α-synuclein
    • Liu, J., Zhou, Y., Wang, Y., Fong, H., Murray, T. M. and Zhang, J. (2007) Identification of proteins involved in microglial endocytosis of α-synuclein. J. Proteome Res. 6, 3614-3627
    • (2007) J. Proteome Res , vol.6 , pp. 3614-3627
    • Liu, J.1    Zhou, Y.2    Wang, Y.3    Fong, H.4    Murray, T.M.5    Zhang, J.6
  • 131
    • 0036701910 scopus 로고    scopus 로고
    • Dynamin and endocytosis
    • Sever, S. (2002) Dynamin and endocytosis. Curr. Opin. Cell Biol. 14, 463-467
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 463-467
    • Sever, S.1
  • 133
    • 48849085276 scopus 로고    scopus 로고
    • Some selective serotonin reuptake inhibitors inhibit dynamin i guanosine triphosphatase (gtpase)
    • Otomo, M., Takahashi, K., Miyoshi, H., Osada, K., Nakashima, H. and Yamaguchi, N. (2008) Some selective serotonin reuptake inhibitors inhibit dynamin I guanosine triphosphatase (GTPase). Biol. Pharm. Bull. 31, 1489-1495
    • (2008) Biol. Pharm. Bull , vol.31 , pp. 1489-1495
    • Otomo, M.1    Takahashi, K.2    Miyoshi, H.3    Osada, K.4    Nakashima, H.5    Yamaguchi, N.6
  • 135
    • 0029780757 scopus 로고    scopus 로고
    • Dynamin and β-Arrestin reveal distinct mechanisms for g protein-coupled receptor internalization
    • Zhang, J., Ferguson, S. S., Barak, L. S., Ḿenard, L. and Caron, M. G. (1996) Dynamin and β-Arrestin reveal distinct mechanisms for G protein-coupled receptor internalization. J. Biol. Chem. 271, 18302-18305
    • (1996) J. Biol. Chem , vol.271 , pp. 18302-18305
    • Zhang, J.1    Ferguson, S.S.2    Barak, L.S.3    Ḿenard, L.4    Caron, M.G.5
  • 137
    • 0036441135 scopus 로고    scopus 로고
    • Membrane traffic exploited by protein toxins
    • Sandvig, K. and Van Deurs, B. (2002) Membrane traffic exploited by protein toxins. Annu. Rev. Cell Dev. Biol. 18, 1-24
    • (2002) Annu. Rev. Cell Dev. Biol , vol.18 , pp. 1-24
    • Sandvig, K.1    Van Deurs, B.2
  • 139
    • 80555155665 scopus 로고    scopus 로고
    • The role of alpha-synuclein in neurotransmission and synaptic plasticity
    • Cheng, F., Vivacqua, G. and Yu, S. (2011) The role of alpha-synuclein in neurotransmission and synaptic plasticity. J. Chem. Neuroanat. 42, 242-248
    • (2011) J. Chem. Neuroanat , Issue.42 , pp. 242-248
    • Cheng, F.1    Vivacqua, G.2    Yu, S.3
  • 140
    • 84872744821 scopus 로고    scopus 로고
    • Monomeric synucleins generate membrane curvature
    • Westphal, C. H. and Chandra, S. S. (2012) Monomeric synucleins generate membrane curvature. J. Biol. Chem. 288, 1829-1840
    • (2012) J. Biol. Chem , vol.288 , pp. 1829-1840
    • Westphal, C.H.1    Chandra, S.S.2
  • 141
    • 84876891740 scopus 로고    scopus 로고
    • α-Synuclein oligomers: An amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions
    • Stǒckl, M. T., Zijlstra, N. and Subramaniam, V. (2012) α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions. Mol. Neurobiol. 47, 613-621
    • (2012) Mol. Neurobiol , Issue.47 , pp. 613-621
    • Stǒckl, M.T.1    Zijlstra, N.2    Subramaniam, V.3
  • 143
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in parkinson's disease: Relationship to α-synuclein inclusions
    • Chu, Y., Dodiya, H., Aebischer, P., Olanow, C. W. and Kordower, J. H. (2009) Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to α-synuclein inclusions. Neurobiol. Dis. 35, 385-398
    • (2009) Neurobiol. Dis , vol.35 , pp. 385-398
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 147
    • 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
  • 148
    • 84859577559 scopus 로고    scopus 로고
    • α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer
    • Fauvet, B., Mbefo, M. K., Fares, M.-B., Desobry, C., Michael, S., Ardah, M. T., Tsika, E., Coune, P., Prudent, M., Lion, N. et al. (2012) α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer. J. Biol. Chem. 287, 15345-15364
    • (2012) J. Biol. Chem , Issue.287 , pp. 15345-15364
    • Fauvet, B.1    Mbefo, M.K.2    Fares, M.-B.3    Desobry, C.4    Michael, S.5    Ardah, M.T.6    Tsika, E.7    Coune, P.8    Prudent, M.9    Lion, N.10
  • 149
    • 67449123312 scopus 로고    scopus 로고
    • On the mechanism of internalization of α-synuclein into microglia: Roles of ganglioside gm1 and lipid raft
    • Park, J.-Y., Kim, K. S., Lee, S.-B., Ryu, J.-S., Chung, K. C., Choo, Y.-K., Jou, I., Kim, J. and Park, S. M. (2009) On the mechanism of internalization of α-synuclein into microglia: roles of ganglioside GM1 and lipid raft. J. Neurochem. 110, 400-411
    • (2009) J. Neurochem , Issue.110 , pp. 400-411
    • Park, J.-Y.1    Kim, K.S.2    Lee, S.-B.3    Ryu, J.-S.4    Chung, K.C.5    Choo, Y.-K.6    Jou, I.7    Kim, J.8    Park, S.M.9
  • 150
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D. and Simons, K. (2010) Lipid rafts as a membrane-organizing principle. Science 327, 46-50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 151
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: New tools and insights
    • Simons, K. and Gerl, M. J. (2010) Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 11, 688-699
    • (2010) Nat. Rev. Mol. Cell Biol , Issue.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 152
    • 33751199883 scopus 로고    scopus 로고
    • Exosomes: From biogenesis and secretion to biological function
    • Keller, S., Sanderson, M. P., Stoeck, A. and Altevogt, P. (2006) Exosomes: from biogenesis and secretion to biological function. Immunol. Lett. 107, 102-108
    • (2006) Immunol. Lett , vol.107 , pp. 102-108
    • Keller, S.1    Sanderson, M.P.2    Stoeck, A.3    Altevogt, P.4
  • 153
    • 0036676445 scopus 로고    scopus 로고
    • Exosomes: Composition, biogenesis and function
    • Th́ery, C., Zitvogel, L. and Amigorena, S. (2002) Exosomes: composition, biogenesis and function. Nat. Rev. Immunol. 2, 569-579
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 569-579
    • Th́ery, C.1    Zitvogel, L.2    Amigorena, S.3
  • 154
    • 84865191058 scopus 로고    scopus 로고
    • Is the amyloid hypothesis of alzheimer's disease therapeutically relevant?
    • Teich, A. F. and Arancio, O. (2012) Is the amyloid hypothesis of Alzheimer's disease therapeutically relevant? Biochem. J. 446, 165-177
    • (2012) Biochem. J , Issue.446 , pp. 165-177
    • Teich, A.F.1    Arancio, O.2
  • 159
    • 43249087541 scopus 로고    scopus 로고
    • Inhibition of γ secretase causes increased secretion of amyloid precursor protein c-terminal fragments in association with exosomes
    • Sharples, R. A., Vella, L. J., Nisbet, R. M., Naylor, R., Perez, K., Barnham, K. J., Masters, C. L. and Hill, A. F. (2008) Inhibition of γ -secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes. FASEB J. 22, 1469-1478
    • (2008) FASEB J , vol.22 , pp. 1469-1478
    • Sharples, R.A.1    Vella, L.J.2    Nisbet, R.M.3    Naylor, R.4    Perez, K.5    Barnham, K.J.6    Masters, C.L.7    Hill, A.F.8
  • 160
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-Associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early alzheimer disease
    • Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y. et al. (2012) Exosome-Associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J. Biol. Chem. 287, 3842-3849
    • (2012) J. Biol. Chem , Issue.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Saman, S.6    Jackson, B.7    McKee, A.C.8    Alvarez, V.E.9    Lee, N.C.Y.10
  • 161
    • 84655176335 scopus 로고    scopus 로고
    • Proteostasis of tau. Tau overexpression results in its secretion via membrane vesicles
    • Siḿon, D., Garćia-Garćia, E., Royo, F., Falćon-Ṕerez, J. M. and Avila, J. (2012) Proteostasis of tau. Tau overexpression results in its secretion via membrane vesicles. FEBS Lett. 586, 47-54
    • (2012) FEBS Lett , Issue.586 , pp. 47-54
    • Siḿon, D.1    Garćia-Garćia, E.2    Royo, F.3    Falćon-Ṕerez, J.M.4    Avila, J.5
  • 163
    • 84864935106 scopus 로고    scopus 로고
    • Constitutive secretion of tau protein by an unconventional mechanism
    • Chai, X., Dage, J. L. and Citron, M. (2012) Constitutive secretion of tau protein by an unconventional mechanism. Neurobiol. Dis. 48, 356-366
    • (2012) Neurobiol. Dis , Issue.48 , pp. 356-366
    • Chai, X.1    Dage, J.L.2    Citron, M.3
  • 164
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert, M., Clavaguera, F. and Tolnay, M. (2010) The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci. 33, 317-325
    • (2010) Trends Neurosci , Issue.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 165
  • 166
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-β peptide
    • Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V. and Lee, J.-M. (2009) Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-β peptide. Proc. Natl. Acad. Sci. U.S.A. 106, 20324-20329
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.-M.6
  • 167
    • 84863306256 scopus 로고    scopus 로고
    • Differences in the cellular uptake and intracellular itineraries of amyloid β proteins 40 and 42: Ramifications for the alzheimer's drug discovery
    • doi:10.1021/mp200530q
    • Omtri, R. S., Davidson, M. W., Arumugam, B., Poduslo, J. F. and Kandimalla, K. K. (2012) Differences in the cellular uptake and intracellular itineraries of amyloid β proteins 40 and 42: ramifications for the Alzheimer's drug discovery. Mol. Pharm., doi:10.1021/mp200530q
    • (2012) Mol. Pharm.
    • Omtri, R.S.1    Davidson, M.W.2    Arumugam, B.3    Poduslo, J.F.4    Kandimalla, K.K.5
  • 168
    • 39849107466 scopus 로고    scopus 로고
    • Retinoic acid- and phorbol ester-induced neuronal differentiation down-regulates caveolin expression in gnrh neurons
    • D'Orlando, C., Guzzi, F., Gravati, M., Biella, G., Toselli, M., Meneveri, R., Barisani, D. and Parenti, M. (2008) Retinoic acid- and phorbol ester-induced neuronal differentiation down-regulates caveolin expression in GnRH neurons. J. Neurochem. 104, 1577-1587
    • (2008) J. Neurochem , Issue.104 , pp. 1577-1587
    • D'Orlando, C.1    Guzzi, F.2    Gravati, M.3    Biella, G.4    Toselli, M.5    Meneveri, R.6    Barisani, D.7    Parenti, M.8
  • 169
    • 78149464299 scopus 로고    scopus 로고
    • Caveolin regulation of neuronal intracellular signaling
    • Stern, C. M. and Mermelstein, P. G. (2010) Caveolin regulation of neuronal intracellular signaling. Cell. Mol. Life Sci. 67, 3785-3795
    • (2010) Cell. Mol. Life Sci , Issue.67 , pp. 3785-3795
    • Stern, C.M.1    Mermelstein, P.G.2
  • 170
    • 33846680684 scopus 로고    scopus 로고
    • Do caveolins regulate cells by actions outside of caveolae?
    • Head, B. P. and Insel, P. A. (2007) Do caveolins regulate cells by actions outside of caveolae? Trends Cell Biol. 17, 51-57
    • (2007) Trends Cell Biol , vol.17 , pp. 51-57
    • Head, B.P.1    Insel, P.A.2
  • 171
    • 0031030053 scopus 로고    scopus 로고
    • Preferential adsorption, internalization and resistance to degradation of the major isoform of the alzheimer's amyloid peptide, aβ1-42, in differentiated pc12 cells
    • Burdick, D., Kosmoski, J., Knauer, M. F. and Glabe, C. G. (1997) Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ1-42, in differentiated PC12 cells. Brain Res. 746, 275-284
    • (1997) Brain Res , vol.746 , pp. 275-284
    • Burdick, D.1    Kosmoski, J.2    Knauer, M.F.3    Glabe, C.G.4
  • 172
    • 0032712028 scopus 로고    scopus 로고
    • Differential accumulation of soluble amyloid β 1-40 and 1-42 in human monocytic and neuroblastoma cell lines. Implications for cerebral amyloidogenesis
    • Morelli, L., Prat, M. I. and Castano, E. M. (1999) Differential accumulation of soluble amyloid β 1-40 and 1-42 in human monocytic and neuroblastoma cell lines. Implications for cerebral amyloidogenesis. Cell Tissue Res. 298, 225-232
    • (1999) Cell Tissue Res , vol.298 , pp. 225-232
    • Morelli, L.1    Prat, M.I.2    Castano, E.M.3
  • 173
    • 84935851672 scopus 로고    scopus 로고
    • Mechanism of neuronal versus endothelial cell uptake of alzheimer's disease amyloid β protein
    • Kandimalla, K. K., Scott, O. G., Fulzele, S., Davidson, M. W. and Poduslo, J. F. (2009) Mechanism of neuronal versus endothelial cell uptake of Alzheimer's disease amyloid β protein. PLoS ONE 4, e4627
    • (2009) PLoS ONE , vol.4
    • Kandimalla, K.K.1    Scott, O.G.2    Fulzele, S.3    Davidson, M.W.4    Poduslo, J.F.5
  • 174
    • 52049104649 scopus 로고    scopus 로고
    • α7 Nicotinic acetylcholine receptor expression by vascular smooth muscle cells facilitates the deposition of Aβ peptides and promotes cerebrovascular amyloid angiopathy
    • Clifford, P. M., Siu, G., Kosciuk, M., Levin, E. C., Venkataraman, V., D'Andrea, M. R. and Nagele, R. G. (2008) α7 Nicotinic acetylcholine receptor expression by vascular smooth muscle cells facilitates the deposition of Aβ peptides and promotes cerebrovascular amyloid angiopathy. Brain Res. 1234, 158-171
    • (2008) Brain Res , vol.1234 , pp. 158-171
    • Clifford, P.M.1    Siu, G.2    Kosciuk, M.3    Levin, E.C.4    Venkataraman, V.5    D'Andrea, M.R.6    Nagele, R.G.7
  • 175
    • 79951567728 scopus 로고    scopus 로고
    • Functional interactions of fibrillar and oligomeric amyloid-β with α7 nicotinic receptors in alzheimer's disease
    • Lilja, A. M., Porras, O., Storelli, E., Nordberg, A. and Marutle, A. (2011) Functional interactions of fibrillar and oligomeric amyloid-β with α7 nicotinic receptors in Alzheimer's disease. J. Alzheimer's Dis. 23, 335-347
    • (2011) J. Alzheimer's Dis , Issue.23 , pp. 335-347
    • Lilja, A.M.1    Porras, O.2    Storelli, E.3    Nordberg, A.4    Marutle, A.5
  • 176
    • 84872441075 scopus 로고    scopus 로고
    • Modulation of α7 nicotinic acetylcholine receptor and fibrillar amyloid-β interactions in alzheimer's disease brain
    • Ni, R., Marutle, A. and Nordberg, A. (2012) Modulation of α7 nicotinic acetylcholine receptor and fibrillar amyloid-β interactions in Alzheimer's disease brain. J. Alzheimer's Dis. 33, 841-851
    • (2012) J. Alzheimer's Dis , Issue.33 , pp. 841-851
    • Ni, R.1    Marutle, A.2    Nordberg, A.3
  • 177
    • 0037135272 scopus 로고    scopus 로고
    • Uptake and pathogenic effects of amyloidβ peptide 1-42 are enhanced by integrin antagonists and blocked by nmda receptor antagonists
    • Bi, X., Gall, C. M., Zhou, J. and Lynch, G. (2002) Uptake and pathogenic effects of amyloidβ peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists. Neuroscience 112, 827-840
    • (2002) Neuroscience , vol.112 , pp. 827-840
    • Bi, X.1    Gall, C.M.2    Zhou, J.3    Lynch, G.4
  • 178
    • 77955604553 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 1 (lrp1) mediates neuronal aβ42 uptake and lysosomal trafficking
    • Fuentealba, R. A., Liu, Q., Zhang, J., Kanekiyo, T., Hu, X., Lee, J.-M., LaDu, M. J. and Bu, G. (2010) Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal Aβ42 uptake and lysosomal trafficking. PLoS ONE 5, e11884
    • (2010) PLoS ONE , vol.5
    • Fuentealba, R.A.1    Liu, Q.2    Zhang, J.3    Kanekiyo, T.4    Hu, X.5    Lee, J.-M.6    LaDu, M.J.7    Bu, G.8
  • 179
    • 0030793522 scopus 로고    scopus 로고
    • Neuronal cell death in alzheimer's disease correlates with apoe uptake and intracellular aβ stabilization
    • LaFerla, F. M., Troncoso, J. C., Strickland, D. K., Kawas, C. H. and Jay, G. (1997) Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Aβ stabilization. J. Clin. Invest. 100, 310-320
    • (1997) J. Clin. Invest , vol.100 , pp. 310-320
    • LaFerla, F.M.1    Troncoso, J.C.2    Strickland, D.K.3    Kawas, C.H.4    Jay, G.5
  • 180
    • 33846021307 scopus 로고    scopus 로고
    • Apolipoprotein e and low density lipoprotein receptor-related protein facilitate intraneuronal aβ42 accumulation in amyloid model mice
    • Zerbinatti, C. V., Wahrle, S. E., Kim, H., Cam, J. A., Bales, K., Paul, S. M., Holtzman, D. M. and Bu, G. (2006) Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Aβ42 accumulation in amyloid model mice. J. Biol. Chem. 281, 36180-36186
    • (2006) J. Biol. Chem , vol.281 , pp. 36180-36186
    • Zerbinatti, C.V.1    Wahrle, S.E.2    Kim, H.3    Cam, J.A.4    Bales, K.5    Paul, S.M.6    Holtzman, D.M.7    Bu, G.8
  • 181
    • 84869508475 scopus 로고    scopus 로고
    • Sortilin is required for toxic action of aβ oligomers (aβos): Extracellular aβos trigger apoptosis, and intraneuronal aβos impair degradation pathways
    • Takamura, A., Sato, Y., Watabe, D., Okamoto, Y., Nakata, T., Kawarabayashi, T., Oddo, S., Laferla, F. M., Shoji, M. and Matsubara, E. (2012) Sortilin is required for toxic action of Aβ oligomers (AβOs): extracellular AβOs trigger apoptosis, and intraneuronal AβOs impair degradation pathways. Life Sci. 91, 1177-1186
    • (2012) Life Sci , Issue.91 , pp. 1177-1186
    • Takamura, A.1    Sato, Y.2    Watabe, D.3    Okamoto, Y.4    Nakata, T.5    Kawarabayashi, T.6    Oddo, S.7    Laferla, F.M.8    Shoji, M.9    Matsubara, E.10
  • 182
    • 80053589341 scopus 로고    scopus 로고
    • Membrane and surface interactions of alzheimer's aβ peptide: Insights into the mechanism of cytotoxicity
    • Williams, T. L. and Serpell, L. C. (2011) Membrane and surface interactions of Alzheimer's Aβ peptide: insights into the mechanism of cytotoxicity. FEBS J. 278, 3905-3917
    • (2011) FEBS J , Issue.278 , pp. 3905-3917
    • Williams, T.L.1    Serpell, L.C.2
  • 183
    • 84866563494 scopus 로고    scopus 로고
    • Alzheimer aβ peptide interactions with lipid membranes: Fibrils, oligomers and polymorphic amyloid channels
    • Tofoleanu, F. and Buchete, N.-V. (2012) Alzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels. Prion 6, 339-345
    • (2012) Prion , vol.6 , pp. 339-345
    • Tofoleanu, F.1    Buchete, N.-V.2
  • 184
    • 84862868531 scopus 로고    scopus 로고
    • Spreading of neurodegenerative pathology via neuron-to-neuron transmission of β-Amyloid
    • Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J. and Hallbeck, M. (2012) Spreading of neurodegenerative pathology via neuron-to-neuron transmission of β-Amyloid. J. Neurosci. 32, 8767-8777
    • (2012) J. Neurosci , Issue.32 , pp. 8767-8777
    • Nath, S.1    Agholme, L.2    Kurudenkandy, F.R.3    Granseth, B.4    Marcusson, J.5    Hallbeck, M.6
  • 185
    • 1142286348 scopus 로고    scopus 로고
    • Nanotubular highways for intercellular organelle transport
    • Rustom, A., Saffrich, R., Markovic, I., Walther, P. and Gerdes, H.-H. (2004) Nanotubular highways for intercellular organelle transport. Science 303, 1007-1010
    • (2004) Science , vol.303 , pp. 1007-1010
    • Rustom, A.1    Saffrich, R.2    Markovic, I.3    Walther, P.4    Gerdes, H.-H.5
  • 186
    • 84861361400 scopus 로고    scopus 로고
    • Wiring through tunneling nanotubes: From electrical signals to organelle transfer
    • Abounit, S. and Zurzolo, C. (2012) Wiring through tunneling nanotubes: from electrical signals to organelle transfer. J. Cell. Sci. 125, 1089-1098
    • (2012) J. Cell. Sci , Issue.125 , pp. 1089-1098
    • Abounit, S.1    Zurzolo, C.2
  • 187
    • 84866327994 scopus 로고    scopus 로고
    • Multifaceted roles of tunneling nanotubes in intercellular communication
    • Marzo, L., Gousset, K. and Zurzolo, C. (2012) Multifaceted roles of tunneling nanotubes in intercellular communication. Front. Physiol. 3, 72
    • (2012) Front. Physiol , Issue.3 , pp. 72
    • Marzo, L.1    Gousset, K.2    Zurzolo, C.3
  • 190
    • 84865522898 scopus 로고    scopus 로고
    • Fibrillar structure and charge determine the interaction of polyglutamine protein aggregates with the cell surface
    • Trevino, R. S., Lauckner, J. E., Sourigues, Y., Pearce, M. M., Bousset, L., Melki, R. and Kopito, R. R. (2012) Fibrillar structure and charge determine the interaction of polyglutamine protein aggregates with the cell surface. J. Biol. Chem. 287, 29722-29728
    • (2012) J. Biol. Chem , Issue.287 , pp. 29722-29728
    • Trevino, R.S.1    Lauckner, J.E.2    Sourigues, Y.3    Pearce, M.M.4    Bousset, L.5    Melki, R.6    Kopito, R.R.7
  • 191
    • 70349373396 scopus 로고    scopus 로고
    • Visualization of molecular interactions using bimolecular fluorescence complementation analysis: Characteristics of protein fragment complementation
    • Kerppola, T. K. (2009) Visualization of molecular interactions using bimolecular fluorescence complementation analysis: characteristics of protein fragment complementation. Chem. Soc. Rev. 38, 2876-2886
    • (2009) Chem. Soc. Rev , vol.38 , pp. 2876-2886
    • Kerppola, T.K.1
  • 195
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B. and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298
    • (2003) Annu. Rev. Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 196
    • 33344463679 scopus 로고    scopus 로고
    • Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
    • Glabe, C. G. (2006) Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol. Aging 27, 570-575
    • (2006) Neurobiol. Aging , vol.27 , pp. 570-575
    • Glabe, C.G.1
  • 197
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers: A decade of discovery
    • Walsh, D. M. and Selkoe, D. J. (2007) Aβ oligomers: a decade of discovery. J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 198
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I. and Glabe, C. G. (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 280, 17294-17300
    • (2005) J. Biol. Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 204
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • Sandberg, M. K., Al-Doujaily, H., Sharps, B., Clarke, A. R. and Collinge, J. (2011) Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 470, 540-542
    • (2011) Nature , vol.470 , pp. 540-542
    • Sandberg, M.K.1    Al-Doujaily, H.2    Sharps, B.3    Clarke, A.R.4    Collinge, J.5
  • 205
    • 33947407685 scopus 로고    scopus 로고
    • Cytosolic prion protein toxicity is independent of cellular prion protein expression and prion propagation
    • Norstrom, E. M., Ciaccio, M. F., Rassbach, B., Wollmann, R. and Mastrianni, J. A. (2007) Cytosolic prion protein toxicity is independent of cellular prion protein expression and prion propagation. J. Virol. 81, 2831-2837
    • (2007) J. Virol , vol.81 , pp. 2831-2837
    • Norstrom, E.M.1    Ciaccio, M.F.2    Rassbach, B.3    Wollmann, R.4    Mastrianni, J.A.5
  • 208
    • 84867295592 scopus 로고    scopus 로고
    • Molecular machines governing exocytosis of synaptic vesicles
    • Jahn, R. and Fasshauer, D. (2012) Molecular machines governing exocytosis of synaptic vesicles. Nature 490, 201-207
    • (2012) Nature , vol.490 , pp. 201-207
    • Jahn, R.1    Fasshauer, D.2
  • 209
    • 46349098379 scopus 로고    scopus 로고
    • A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2
    • Temmerman, K., Ebert, A. D., Muller, H.-M., Sinning, I., Tews, I. and Nickel, W. (2008) A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2. Traffic 9, 1204-1217
    • (2008) Traffic , vol.9 , pp. 1204-1217
    • Temmerman, K.1    Ebert, A.D.2    Muller, H.-M.3    Sinning, I.4    Tews, I.5    Nickel, W.6
  • 210
    • 84864295258 scopus 로고    scopus 로고
    • Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation
    • Deretic, V., Jiang, S. and Dupont, N. (2012) Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation. Trends Cell Biol. 22, 397-406
    • (2012) Trends Cell Biol , Issue.22 , pp. 397-406
    • Deretic, V.1    Jiang, S.2    Dupont, N.3
  • 212
    • 69249106881 scopus 로고    scopus 로고
    • Pathways and mechanisms of endocytic recycling
    • Grant, B. D. and Donaldson, J. G. (2009) Pathways and mechanisms of endocytic recycling. Nat. Rev. Mol. Cell Biol. 10, 597-608
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 597-608
    • Grant, B.D.1    Donaldson, J.G.2
  • 213
    • 70350322116 scopus 로고    scopus 로고
    • Endocytosis of glycosylphosphatidylinositol-Anchored proteins
    • Lakhan, S. E., Sabharanjak, S. and De, A. (2009) Endocytosis of glycosylphosphatidylinositol-Anchored proteins. J. Biomed. Sci. 16, 93
    • (2009) J. Biomed. Sci , vol.16 , pp. 93
    • Lakhan, S.E.1    Sabharanjak, S.2    De, A.3
  • 214
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final escrt
    • Babst, M. (2005) A protein's final ESCRT. Traffic 6, 2-9
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 215
    • 78049255782 scopus 로고    scopus 로고
    • Animal cells connected by nanotubes can be electrically coupled through interposed gap-junction channels
    • Wang, X., Veruki, M. L., Bukoreshtliev, N. V., Hartveit, E. and Gerdes, H.-H. (2010) Animal cells connected by nanotubes can be electrically coupled through interposed gap-junction channels. Proc. Natl. Acad. Sci. U.S.A. 107, 17194-17199
    • (2010) Proc. Natl. Acad. Sci. U.S.A , Issue.107 , pp. 17194-17199
    • Wang, X.1    Veruki, M.L.2    Bukoreshtliev, N.V.3    Hartveit, E.4    Gerdes, H.-H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.