메뉴 건너뛰기




Volumn , Issue , 2013, Pages

From prion diseases to prion-like propagation mechanisms of neurodegenerative diseases

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

EID: 84886679059     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2013/975832     Document Type: Review
Times cited : (30)

References (68)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S. B., Novel proteinaceous infectious particles cause scrapie. Science 1982 216 4542 136 144 2-s2.0-0020321767 (Pubitemid 12089840)
    • (1982) Science , vol.216 , Issue.4542 , pp. 136-144
    • Prusiner, S.B.1
  • 2
    • 0037010121 scopus 로고    scopus 로고
    • Prion diseases: Pathogenesis and public health concerns
    • DOI 10.1016/S0014-5793(02)03268-4, PII S0014579302032684
    • Dormont D., Prion diseases: pathogenesis and public health concerns. FEBS Letters 2002 529 1 17 21 2-s2.0-0037010121 10.1016/S0014-5793(02)03268-4 (Pubitemid 35283905)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 17-21
    • Dormont, D.1
  • 4
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • DOI 10.1016/S0140-6736(04)16811-6, PII S0140673604168116
    • Peden A. H., Head M. W., Ritchie D. L., Bell P. J. E., Ironside P. J. W., Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. The Lancet 2004 364 9433 527 529 2-s2.0-4043157677 10.1016/S0140- 6736(04)16811-6 (Pubitemid 39070413)
    • (2004) Lancet , vol.364 , Issue.9433 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3    Bell, P.J.E.4    Ironside, P.J.W.5
  • 5
    • 2542501619 scopus 로고    scopus 로고
    • UK patient first to contract vCJD via blood transfusion
    • 2-s2.0-2542501619
    • Sibbald B., UK patient first to contract vCJD via blood transfusion. Canadian Medical Association Journal 2004 170 7 1087 2-s2.0-2542501619
    • (2004) Canadian Medical Association Journal , vol.170 , Issue.7 , pp. 1087
    • Sibbald, B.1
  • 6
    • 33845227845 scopus 로고    scopus 로고
    • Clinical presentation and pre-mortem diagnosis of variant Creutzfeldt-Jakob disease associated with blood transfusion: A case report
    • DOI 10.1016/S0140-6736(06)69835-8, PII S0140673606698358
    • Wroe S. J., Pal S., Siddique D., Hyare H., Macfarlane R., Joiner S., Linehan J. M., Brandner S., Wadsworth J. D., Hewitt P., Collinge J., Clinical presentation and pre-mortem diagnosis of variant Creutzfeldt-Jakob disease associated with blood transfusion: a case report. The Lancet 2006 368 9552 2061 2067 2-s2.0-33845227845 10.1016/S0140-6736(06)69835-8 (Pubitemid 44855106)
    • (2006) Lancet , vol.368 , Issue.9552 , pp. 2061-2067
    • Wroe, S.J.1    Pal, S.2    Siddique, D.3    Hyare, H.4    Macfarlane, R.5    Joiner, S.6    Linehan, J.M.7    Brandner, S.8    Wadsworth, J.D.9    Hewitt, P.10    Collinge, J.11
  • 8
    • 0020481648 scopus 로고
    • Scrapie agent: Prions or virinos?
    • 2-s2.0-0020481648 10.1038/297107a0
    • Kimberlin R. H., Scrapie agent: prions or virinos? Nature 1982 297 5862 107 108 2-s2.0-0020481648 10.1038/297107a0
    • (1982) Nature , vol.297 , Issue.5862 , pp. 107-108
    • Kimberlin, R.H.1
  • 9
    • 0014194776 scopus 로고
    • The possible nature of the transmissible agent of scrapie
    • 2-s2.0-0014194776
    • Pattison I. H., Jones K. M., The possible nature of the transmissible agent of scrapie. Veterinary Record 1967 80 1 2 9 2-s2.0-0014194776
    • (1967) Veterinary Record , vol.80 , Issue.1 , pp. 2-9
    • Pattison, I.H.1    Jones, K.M.2
  • 10
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • 2-s2.0-0014211846 10.1038/214764a0
    • Alper T., Cramp W. A., Haig D. A., Clarke M. C., Does the agent of scrapie replicate without nucleic acid? Nature 1967 214 5090 764 766 2-s2.0-0014211846 10.1038/214764a0
    • (1967) Nature , vol.214 , Issue.5090 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 11
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • 2-s2.0-0014190760 10.1038/2151043a0
    • Griffith J. S., Self-replication and scrapie. Nature 1967 215 5105 1043 1044 2-s2.0-0014190760 10.1038/2151043a0
    • (1967) Nature , vol.215 , Issue.5105 , pp. 1043-1044
    • Griffith, J.S.1
  • 14
    • 0029937271 scopus 로고    scopus 로고
    • NMR structure of the mouse prion protein domain PrP(121-231)
    • DOI 10.1038/382180a0
    • Riek R., Hornemann S., Wider G., Billeter M., Glockshuber R., Wuthrich K., NMR structure of the mouse prion protein domain PrP(121-231). Nature 1996 382 6587 180 182 2-s2.0-0029937271 10.1038/382180a0 (Pubitemid 26242887)
    • (1996) Nature , vol.382 , Issue.6587 , pp. 180-182
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Billeter, M.4    Glockshuber, R.5    Wuthrich, K.6
  • 17
    • 24644448839 scopus 로고    scopus 로고
    • The most infectious prion protein particles
    • DOI 10.1038/nature03989
    • Silveira J. R., Raymond G. J., Hughson A. G., Race R. E., Sim V. L., Hayes S. F., Caughey B., The most infectious prion protein particles. Nature 2005 437 7056 257 261 2-s2.0-24644448839 10.1038/nature03989 (Pubitemid 41294488)
    • (2005) Nature , vol.437 , Issue.7056 , pp. 257-261
    • Silveira, J.R.1    Raymond, G.J.2    Hughson, A.G.3    Race, R.E.4    Sim, V.L.5    Hayes, S.F.6    Caughey, B.7
  • 18
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • DOI 10.1038/35081095
    • Saborio G. P., Permanne B., Soto C., Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001 411 6839 810 813 2-s2.0-0035859102 10.1038/35081095 (Pubitemid 32588105)
    • (2001) Nature , vol.411 , Issue.6839 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 19
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native alpha-helical conformation is under kinetic control
    • 2-s2.0-0035827614 10.1074/jbc.C100180200
    • Baskakov I. V., Legname G., Prusiner S. B., Cohen F. E., Folding of prion protein to its native alpha-helical conformation is under kinetic control. The Journal of Biological Chemistry 2001 276 23 19687 19690 2-s2.0-0035827614 10.1074/jbc.C100180200
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.23 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3    Cohen, F.E.4
  • 20
    • 0037077234 scopus 로고    scopus 로고
    • Pathway complexity of prion protein assembly into amyloid
    • DOI 10.1074/jbc.M111402200
    • Baskakov I. V., Legname G., Baldwin M. A., Prusiner S. B., Cohen F. E., Pathway complexity of prion protein assembly into amyloid. The Journal of Biological Chemistry 2002 277 24 21140 21148 2-s2.0-0037077234 10.1074/jbc.M111402200 (Pubitemid 34952249)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21140-21148
    • Baskakov, I.V.1    Legname, G.2    Baldwin, M.A.3    Prusiner, S.B.4    Cohen, F.E.5
  • 21
    • 12444333644 scopus 로고    scopus 로고
    • Exosomes: A bubble ride for prions?
    • 2-s2.0-12444333644 10.1111/j.1600-0854.2004.00247.x
    • Février B., Vilette D., Laude H., Raposo G., Exosomes: a bubble ride for prions? Traffic 2005 6 1 10 17 2-s2.0-12444333644 10.1111/j.1600-0854. 2004.00247.x
    • (2005) Traffic , vol.6 , Issue.1 , pp. 10-17
    • Février, B.1    Vilette, D.2    Laude, H.3    Raposo, G.4
  • 22
    • 33947709328 scopus 로고    scopus 로고
    • Packaging of prions into exosomes is associated with a novel pathway of PrP processing
    • DOI 10.1002/path.2145
    • Vella L. J., Sharples R. A., Lawson V. A., Masters C. L., Cappai R., Hill A. F., Packaging of prions into exosomes is associated with a novel pathway of PrP processing. Journal of Pathology 2007 211 5 582 590 2-s2.0-33947709328 10.1002/path.2145 (Pubitemid 46502435)
    • (2007) Journal of Pathology , vol.211 , Issue.5 , pp. 582-590
    • Vella, L.J.1    Sharples, R.A.2    Lawson, V.A.3    Masters, C.L.4    Cappai, R.5    Hill, A.F.6
  • 23
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • Caughey B., Lansbury P. T. Jr., Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annual Review of Neuroscience 2003 26 267 298 2-s2.0-0037551741 10.1146/annurev.neuro.26.010302.081142 (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 26
    • 50049085479 scopus 로고    scopus 로고
    • Rodent models for prion diseases
    • ARTICLE 32 2-s2.0-50049085479 10.1051/vetres:2008008
    • Groschup M. H., Buschmann A., Rodent models for prion diseases. Veterinary Research 2008 39 4, article 32 2-s2.0-50049085479 10.1051/vetres:2008008
    • (2008) Veterinary Research , vol.39 , Issue.4
    • Groschup, M.H.1    Buschmann, A.2
  • 27
    • 74749105348 scopus 로고    scopus 로고
    • Prion neurotoxicity: Insights from prion protein mutants
    • 2-s2.0-74749105348
    • Solomon I. H., Schepker J. A., Harris D. A., Prion neurotoxicity: insights from prion protein mutants. Current Issues in Molecular Biology 2010 12 2 51 61 2-s2.0-74749105348
    • (2010) Current Issues in Molecular Biology , vol.12 , Issue.2 , pp. 51-61
    • Solomon, I.H.1    Schepker, J.A.2    Harris, D.A.3
  • 28
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • DOI 10.1016/0092-8674(93)90360-3
    • Bueler H., Aguzzi A., Sailer A., Greiner R.-A., Autenried P., Aguet M., Weissmann C., Mice devoid of PrP are resistant to scrapie. Cell 1993 73 7 1339 1347 2-s2.0-0027319326 10.1016/0092-8674(93)90360-3 (Pubitemid 23201147)
    • (1993) Cell , vol.73 , Issue.7 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3    Greiner, R.-A.4    Autenried, P.5    Aguet, M.6    Weissmann, C.7
  • 30
    • 33846538022 scopus 로고    scopus 로고
    • Targeting Cellular Prion Protein Reverses Early Cognitive Deficits and Neurophysiological Dysfunction in Prion-Infected Mice
    • DOI 10.1016/j.neuron.2007.01.005, PII S0896627307000086
    • Mallucci G. R., White M. D., Farmer M., Dickinson A., Khatun H., Powell A. D., Brandner S., Jefferys J. G. R., Collinge J., Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice. Neuron 2007 53 3 325 335 2-s2.0-33846538022 10.1016/j.neuron.2007.01.005 (Pubitemid 46161264)
    • (2007) Neuron , vol.53 , Issue.3 , pp. 325-335
    • Mallucci, G.R.1    White, M.D.2    Farmer, M.3    Dickinson, A.4    Khatun, H.5    Powell, A.D.6    Brandner, S.7    Jefferys, J.G.R.8    Collinge, J.9
  • 31
    • 0028052363 scopus 로고
    • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins
    • 2-s2.0-0028052363 10.1016/0092-8674(94)90177-5
    • Westaway D., DeArmond S. J., Cayetano-Canlas J., Groth D., Foster D., Yang S.-L., Torchia M., Carlson G. A., Prusiner S. B., Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 1994 76 1 117 129 2-s2.0-0028052363 10.1016/0092-8674(94)90177-5
    • (1994) Cell , vol.76 , Issue.1 , pp. 117-129
    • Westaway, D.1    Dearmond, S.J.2    Cayetano-Canlas, J.3    Groth, D.4    Foster, D.5    Yang, S.-L.6    Torchia, M.7    Carlson, G.A.8    Prusiner, S.B.9
  • 34
    • 0025681138 scopus 로고
    • Spontaneous neurodegeneration in transgenic mice with mutant prion protein
    • Hsiao K. K., Scott M., Foster D., Groth D. F., DeArmond S. J., Prusiner S. B., Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 1990 250 4987 1587 1590 2-s2.0-0025681138 (Pubitemid 120034374)
    • (1990) Science , vol.250 , Issue.4987 , pp. 1587-1590
    • Hsiao, K.K.1    Scott, M.2    Foster, D.3    Groth, D.F.4    Dearmond, S.J.5    Prusiner, S.B.6
  • 35
    • 0029740354 scopus 로고    scopus 로고
    • Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice
    • Telling G. C., Haga T., Torchia M., Tremblay P., DeArmond S. J., Prusiner S. B., Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes and Development 1996 10 14 1736 1750 2-s2.0-0029740354 (Pubitemid 26272380)
    • (1996) Genes and Development , vol.10 , Issue.14 , pp. 1736-1750
    • Telling, G.C.1    Haga, T.2    Torchia, M.3    Tremblay, P.4    DeArmond, S.J.5    Prusiner, S.B.6
  • 36
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • DOI 10.1016/S0896-6273(00)80653-4
    • Chiesa R., Piccardo P., Ghetti B., Harris D. A., Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 1998 21 6 1339 1351 2-s2.0-0032427904 10.1016/S0896-6273(00)80653-4 (Pubitemid 29022536)
    • (1998) Neuron , vol.21 , Issue.6 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 38
    • 81755183039 scopus 로고    scopus 로고
    • Fatal prion disease in a mouse model of genetic E200K Creutzfeldt-Jakob disease
    • 2-s2.0-81755183039 10.1371/journal.ppat.1002350 e1002350
    • Friedman-Levi Y., Meiner Z., Canello T., Frid K., Kovacs G. G., Budka H., Avrahami D., Gabizon R., Fatal prion disease in a mouse model of genetic E200K Creutzfeldt-Jakob disease. PLoS Pathogens 2011 7 11 2-s2.0-81755183039 10.1371/journal.ppat.1002350 e1002350
    • (2011) PLoS Pathogens , vol.7 , Issue.11
    • Friedman-Levi, Y.1    Meiner, Z.2    Canello, T.3    Frid, K.4    Kovacs, G.G.5    Budka, H.6    Avrahami, D.7    Gabizon, R.8
  • 39
    • 68949163542 scopus 로고    scopus 로고
    • Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice
    • 2-s2.0-68949163542 10.1016/j.neuron.2009.07.026
    • Jackson W. S., Borkowski A. W., Faas H., Steele A. D., King O. D., Watson N., Jasanoff A., Lindquist S., Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice. Neuron 2009 63 4 438 450 2-s2.0-68949163542 10.1016/j.neuron.2009.07.026
    • (2009) Neuron , vol.63 , Issue.4 , pp. 438-450
    • Jackson, W.S.1    Borkowski, A.W.2    Faas, H.3    Steele, A.D.4    King, O.D.5    Watson, N.6    Jasanoff, A.7    Lindquist, S.8
  • 40
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer M., Rulicke T., Raeber A., Sailer A., Moser M., Oesch B., Brandner S., Aguzzi A., Weissmann C., Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO Journal 1996 15 6 1255 1264 2-s2.0-0029863648 (Pubitemid 26093461)
    • (1996) EMBO Journal , vol.15 , Issue.6 , pp. 1255-1264
    • Fischer, M.1    Rulicke, T.2    Raeber, A.3    Sailer, A.4    Moser, M.5    Oesch, B.6    Brandner, S.7    Aguzzi, A.8    Weissmann, C.9
  • 42
    • 80855131560 scopus 로고    scopus 로고
    • Variably protease-sensitive prionopathy: A novel disease of the prion protein
    • 2-s2.0-80855131560 10.1007/s12031-011-9543-1
    • Gambetti P., Puoti G., Zou W.-Q., Variably protease-sensitive prionopathy: a novel disease of the prion protein. Journal of Molecular Neuroscience 2011 45 3 422 424 2-s2.0-80855131560 10.1007/s12031-011-9543-1
    • (2011) Journal of Molecular Neuroscience , vol.45 , Issue.3 , pp. 422-424
    • Gambetti, P.1    Puoti, G.2    Zou, W.-Q.3
  • 44
    • 0343683408 scopus 로고    scopus 로고
    • Physical studies of conformational plasticity in a recombinant prion protein
    • DOI 10.1021/bi961965r
    • Zhana H., Stöckel J., Mehlhorn I., Groth D., Baldwin M. A., Prusiner S. B., James T. L., Cohen F. E., Physical studies of conformational plasticity in a recombinant prion protein. Biochemistry 1997 36 12 3543 3553 2-s2.0-0343683408 10.1021/bi961965r (Pubitemid 27143508)
    • (1997) Biochemistry , vol.36 , Issue.12 , pp. 3543-3553
    • Zhana, H.1    Stockel, J.2    Mehlhorn, I.3    Groth, D.4    Baldwin, M.A.5    Prusiner, S.B.6    James, T.L.7    Cohen, F.E.8
  • 47
    • 77449142074 scopus 로고    scopus 로고
    • Recombinant prion protein induces a new transmissible prion disease in wild-type animals
    • 2-s2.0-77449142074 10.1007/s00401-009-0633-x
    • Makarava N., Kovacs G. G., Bocharova O., Savtchenko R., Alexeeva I., Budka H., Rohwer R. G., Baskakov I. V., Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathologica 2010 119 2 177 187 2-s2.0-77449142074 10.1007/s00401-009-0633-x
    • (2010) Acta Neuropathologica , vol.119 , Issue.2 , pp. 177-187
    • Makarava, N.1    Kovacs, G.G.2    Bocharova, O.3    Savtchenko, R.4    Alexeeva, I.5    Budka, H.6    Rohwer, R.G.7    Baskakov, I.V.8
  • 48
    • 84855290517 scopus 로고    scopus 로고
    • Genesis of mammalian prions: From non-infectious amyloid fibrils to a transmissible prion disease
    • 2-s2.0-84855290517 10.1371/journal.ppat.1002419 e1002419
    • Makarava N., Kovacs G. G., Savtchenko R., Alexeeva I., Budka H., Rohwer R. G., Baskakov I. V., Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease. PLoS Pathogens 2011 7 12 2-s2.0-84855290517 10.1371/journal.ppat.1002419 e1002419
    • (2011) PLoS Pathogens , vol.7 , Issue.12
    • Makarava, N.1    Kovacs, G.G.2    Savtchenko, R.3    Alexeeva, I.4    Budka, H.5    Rohwer, R.G.6    Baskakov, I.V.7
  • 50
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • 2-s2.0-77649213673 10.1126/science.1183748
    • Wang F., Wang X., Yuan C.-G., Ma J., Generating a prion with bacterially expressed recombinant prion protein. Science 2010 327 5969 1132 1135 2-s2.0-77649213673 10.1126/science.1183748
    • (2010) Science , vol.327 , Issue.5969 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.-G.3    Ma, J.4
  • 53
    • 0028376473 scopus 로고
    • Induction of β (A4)-amyloid in primates by injection of Alzheimer's disease brain homogenate - Comparison with transmission of spongiform encephalopathy
    • 2-s2.0-0028376473 10.1007/BF02778005
    • Baker H. F., Ridley R. M., Duchen L. W., Crow T. J., Bruton C. J., Induction of β (A4)-amyloid in primates by injection of Alzheimer's disease brain homogenate-comparison with transmission of spongiform encephalopathy. Molecular Neurobiology 1994 8 1 25 39 2-s2.0-0028376473 10.1007/BF02778005
    • (1994) Molecular Neurobiology , vol.8 , Issue.1 , pp. 25-39
    • Baker, H.F.1    Ridley, R.M.2    Duchen, L.W.3    Crow, T.J.4    Bruton, C.J.5
  • 54
    • 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., Walker L. C., Evidence for seeding of β -amyloid by intracerebral infusion of Alzheimer brain extracts in β -amyloid precursor protein-transgenic mice. Journal of Neuroscience 2000 20 10 3606 3611 2-s2.0-0034657130 (Pubitemid 30266223)
    • (2000) Journal of Neuroscience , vol.20 , Issue.10 , 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
  • 55
    • 0036386817 scopus 로고    scopus 로고
    • Modeling Alzheimer's disease and other proteopathies in vivo: Is seeding the key?
    • 2-s2.0-0036386817 10.1007/s00726-001-0113-7
    • Walker L. C., Bian F., Callahan M. J., Lipinski W. J., Durham R. A., LeVine H., Modeling Alzheimer's disease and other proteopathies in vivo: is seeding the key? Amino Acids 2002 23 1-3 87 93 2-s2.0-0036386817 10.1007/s00726-001-0113-7
    • (2002) Amino Acids , vol.23 , Issue.1-3 , pp. 87-93
    • Walker, L.C.1    Bian, F.2    Callahan, M.J.3    Lipinski, W.J.4    Durham, R.A.5    Levine, H.6
  • 58
    • 84870067233 scopus 로고    scopus 로고
    • De novo induction of amyloid- β deposition in vivo
    • 2-s2.0-80053437539 10.1038/mp.2011.120
    • Morales R., Duran-Aniotz C., Castilla J., Estrada L. D., Soto C., De novo induction of amyloid- β deposition in vivo. Molecular Psychiatry 2011 17 12 1347 1353 2-s2.0-80053437539 10.1038/mp.2011.120
    • (2011) Molecular Psychiatry , vol.17 , Issue.12 , pp. 1347-1353
    • Morales, R.1    Duran-Aniotz, C.2    Castilla, J.3    Estrada, L.D.4    Soto, C.5
  • 61
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • DOI 10.1038/nm1747, PII NM1747
    • Kordower J. H., Chu Y., Hauser R. A., Freeman T. B., Olanow C. W., Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nature Medicine 2008 14 5 504 506 2-s2.0-43249114934 10.1038/nm1747 (Pubitemid 351655212)
    • (2008) Nature Medicine , vol.14 , Issue.5 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 63
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice
    • Luk K. C., Kehm V. M., Zhang B., O'Brien P., Trojanowski J. Q., Lee V. M., Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice. The Journal of Experimental Medicine 2012 5 975 986
    • (2012) The Journal of Experimental Medicine , Issue.5 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3    O'Brien, P.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 64
    • 84869109864 scopus 로고    scopus 로고
    • Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk K. C., Kehm V., Carroll J., Zhang B., O'Brien P., Trojanowski J. Q., Lee V. M., Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 2012 338 6109 949 953
    • (2012) Science , vol.338 , Issue.6109 , 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.7
  • 66
    • 68649095434 scopus 로고    scopus 로고
    • Parkinson's disease: The dual hit theory revisited
    • 2-s2.0-68649095434 10.1111/j.1749-6632.2009.04365.x
    • Hawkes C. H., Del Tredici K., Braak H., Parkinson's disease: the dual hit theory revisited. Annals of the New York Academy of Sciences 2009 1170 615 622 2-s2.0-68649095434 10.1111/j.1749-6632.2009.04365.x
    • (2009) Annals of the New York Academy of Sciences , vol.1170 , pp. 615-622
    • Hawkes, C.H.1    Del Tredici, K.2    Braak, H.3
  • 67
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Chan H. Y. E., Warrick J. M., Andriola I., Merry D., Bonini N. M., Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Human Molecular Genetics 2002 11 23 2905 2917 2-s2.0-0036850529 (Pubitemid 35331822)
    • (2002) Human Molecular Genetics , vol.11 , Issue.23 , pp. 2905-2917
    • Chan, H.Y.E.1    Warrick, J.M.2    Andriola, I.3    Merry, D.4    Bonini, N.M.5
  • 68
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • 2-s2.0-59649095699 10.1038/ncb1830
    • Ren P.-H., Lauckner J. E., Kachirskaia I., Heuser J. E., Melki R., Kopito R. R., Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nature Cell Biology 2009 11 2 219 225 2-s2.0-59649095699 10.1038/ncb1830
    • (2009) Nature Cell Biology , vol.11 , Issue.2 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.