메뉴 건너뛰기




Volumn 18, Issue , 2016, Pages

Mechanisms of prion-induced neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS REGULATORY PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PRION; TRANSCRIPTION FACTOR; UBIQUITIN;

EID: 84964000628     PISSN: 14623994     EISSN: None     Source Type: Journal    
DOI: 10.1017/erm.2016.8     Document Type: Review
Times cited : (33)

References (248)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 2
    • 84862620376 scopus 로고    scopus 로고
    • Cell biology. A unifying role for prions in neurodegenerative diseases
    • Prusiner S.B. (2012) Cell biology. A unifying role for prions in neurodegenerative diseases. Science 336, 1511-1513
    • (2012) Science , vol.336 , pp. 1511-1513
    • Prusiner, S.B.1
  • 3
    • 84862335459 scopus 로고    scopus 로고
    • Sporadic human prion diseases: Molecular insights and diagnosis
    • Puoti G. et al. (2012) Sporadic human prion diseases: molecular insights and diagnosis. Lancet Neurology 11, 618-628
    • (2012) Lancet Neurology , vol.11 , pp. 618-628
    • Puoti, G.1
  • 4
    • 80054984363 scopus 로고    scopus 로고
    • Sporadic fatal insomnia in a young woman: A diagnostic challenge: Case report
    • Moody K.M. et al. (2011) Sporadic fatal insomnia in a young woman: a diagnostic challenge: case report. BMC Neurology 11, 136
    • (2011) BMC Neurology , vol.11 , pp. 136
    • Moody, K.M.1
  • 5
    • 84922875827 scopus 로고    scopus 로고
    • Transmission characteristics of variably protease-sensitive prionopathy
    • Notari S. et al. (2014) Transmission characteristics of variably protease-sensitive prionopathy. Emerging Infectious Diseases 20, 2006-2014
    • (2014) Emerging Infectious Diseases , vol.20 , pp. 2006-2014
    • Notari, S.1
  • 6
    • 84922931281 scopus 로고    scopus 로고
    • Variably protease-sensitive prionopathy, a unique prion variant with inefficient transmission properties
    • Diack A.B. et al. (2014) Variably protease-sensitive prionopathy, a unique prion variant with inefficient transmission properties. Emerging Infectious Diseases 20, 1969-1979
    • (2014) Emerging Infectious Diseases , vol.20 , pp. 1969-1979
    • Diack, A.B.1
  • 7
    • 46749121818 scopus 로고    scopus 로고
    • A novel human disease with abnormal prion protein sensitive to protease
    • Gambetti P. et al. (2008) A novel human disease with abnormal prion protein sensitive to protease. Annals of Neurology 63, 697-708
    • (2008) Annals of Neurology , vol.63 , pp. 697-708
    • Gambetti, P.1
  • 8
    • 33748743547 scopus 로고    scopus 로고
    • Gerstmann-straussler-scheinker disease. I. Human diseases
    • Liberski P.P. and Budka H. (2004) Gerstmann-Straussler-Scheinker disease. I. Human diseases. Folia Neuropathologica 42 (Suppl B), 120-140
    • (2004) Folia Neuropathologica , vol.42 , pp. 120-140
    • Liberski, P.P.1    Budka, H.2
  • 9
    • 0002554696 scopus 로고
    • Transmissible human spongiform encephalopathy (Infectious cerebral amyloidosis): Creutzfeldt-jakob disease, gerstmann-sträussler-scheinker syndrome and kuru
    • (Calne D.B. ed.), W.B.Saunders, Philadelphia
    • Brown P. (1994) Transmissible human spongiform encephalopathy (Infectious cerebral amyloidosis): Creutzfeldt-Jakob Disease, Gerstmann-Sträussler-Scheinker Syndrome and Kuru. In Neurodegenerative Diseases (Calne D.B. ed.), p. 38. W.B.Saunders, Philadelphia
    • (1994) Neurodegenerative Diseases , pp. 38
    • Brown, P.1
  • 10
    • 0000861256 scopus 로고    scopus 로고
    • Inherited prion diseases
    • (Monograf 38 edn) (Prusiner S. ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Gambetti P. et al. (1999) Inherited prion diseases. In Prion Biology and Diseases (Monograf 38 edn) (Prusiner S. ed.), p. 74. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • (1999) Prion Biology and Diseases , pp. 74
    • Gambetti, P.1
  • 11
    • 85048268509 scopus 로고
    • Genetic prion diseases
    • (Pagon R.A., Adam M., Ardinger H.H., Wallace S.E., Amemiya A., Bean L.J.H., Bird T.D., Fong C.T., Mefford H.C., Smith R.J.H. and Stephens K. eds), University of Washington, Seattle, WA
    • Mastrianni J.A. (1993) Genetic prion diseases. In GeneReviews(R) (Pagon R.A., Adam M.P., Ardinger H.H., Wallace S.E., Amemiya A., Bean L.J.H., Bird T.D., Fong C.T., Mefford H.C., Smith R.J.H. and Stephens K. eds), pp. 1993-2016. University of Washington, Seattle, WA
    • (1993) GeneReviews(R) , pp. 1993-2016
    • Mastrianni, J.A.1
  • 12
    • 0342951746 scopus 로고    scopus 로고
    • A new variant of creutzfeldt-jakob disease in the UK
    • Will R.G. et al. (1996) A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347, 921-925
    • (1996) Lancet , vol.347 , pp. 921-925
    • Will, R.G.1
  • 13
    • 84861220384 scopus 로고    scopus 로고
    • Iatrogenic creutzfeldt-jakob disease, final assessment
    • Brown P. et al. (2012) Iatrogenic Creutzfeldt-Jakob disease, final assessment. Emerging Infectious Diseases 18, 901-907
    • (2012) Emerging Infectious Diseases , vol.18 , pp. 901-907
    • Brown, P.1
  • 15
    • 33745440706 scopus 로고    scopus 로고
    • Kuru in the 21st century – An acquired human prion disease with very long incubation periods
    • Collinge J. et al. (2006) Kuru in the 21st century – an acquired human prion disease with very long incubation periods. Lancet 367, 2068-2074
    • (2006) Lancet , vol.367 , pp. 2068-2074
    • Collinge, J.1
  • 16
    • 0017643758 scopus 로고
    • Unconventional viruses and the origin and disappearance of kuru
    • Gajdusek D.C. (1977) Unconventional viruses and the origin and disappearance of kuru. Science 197, 943-960
    • (1977) Science , vol.197 , pp. 943-960
    • Gajdusek, D.C.1
  • 17
    • 0002685407 scopus 로고
    • Epidemiology and clinical aspects of kuru
    • (Prusiner S.B. and McKinley M. eds), Academic Press, San Diego
    • Alpers M.P. (1987) Epidemiology and clinical aspects of Kuru. In Prions (Prusiner S.B. and McKinley M.P. eds), p. 451-465. Academic Press, San Diego
    • (1987) Prions , pp. 451-465
    • Alpers, M.P.1
  • 18
    • 0025335415 scopus 로고
    • Progressive fatal dementia (Creutzfeldt-jakob disease) in a patient who received homograft tissue for tympanic membrane closure
    • Tange R.A., Troost D. and Limburg M. (1990) Progressive fatal dementia (Creutzfeldt-Jakob disease) in a patient who received homograft tissue for tympanic membrane closure. European Archives of Oto-rhino-laryngology 247, 199-201
    • (1990) European Archives of Oto-Rhino-Laryngology , vol.247 , pp. 199-201
    • Tange, R.A.1    Troost, D.2    Limburg, M.3
  • 19
    • 1142273431 scopus 로고    scopus 로고
    • Possible transmission of variant creutzfeldt-jakob disease by blood transfusion
    • Llewelyn C.A. et al. (2004) Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet 363, 417-421
    • (2004) Lancet , vol.363 , pp. 417-421
    • Llewelyn, C.A.1
  • 20
    • 70349531287 scopus 로고    scopus 로고
    • A retrospective case note review of deceased recipients of vCJD-implicated blood transfusions
    • Gillies M. et al. (2009) A retrospective case note review of deceased recipients of vCJD-implicated blood transfusions. Vox Sanguinis 97, 211-218
    • (2009) Vox Sanguinis , vol.97 , pp. 211-218
    • Gillies, M.1
  • 21
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • Peden A.H. et al. (2004) Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 364, 527-529
    • (2004) Lancet , vol.364 , pp. 527-529
    • Peden, A.H.1
  • 22
    • 33845227845 scopus 로고    scopus 로고
    • Clinical presentation and pre-mortem diagnosis of variant creutzfeldt-jakob disease associated with blood transfusion: A case report
    • Wroe S.J. et al. (2006) Clinical presentation and pre-mortem diagnosis of variant Creutzfeldt-Jakob disease associated with blood transfusion: a case report. Lancet 368, 2061-2067
    • (2006) Lancet , vol.368 , pp. 2061-2067
    • Wroe, S.J.1
  • 23
    • 0041851001 scopus 로고    scopus 로고
    • Familial and sporadic fatal insomnia
    • Montagna P. et al. (2003) Familial and sporadic fatal insomnia. Lancet Neurology 2, 167-176
    • (2003) Lancet Neurology , vol.2 , pp. 167-176
    • Montagna, P.1
  • 24
    • 0030856447 scopus 로고    scopus 로고
    • PrP genetics in sheep and the applications for scrapie and BSE
    • Hunter N. (1997) PrP genetics in sheep and the applications for scrapie and BSE. Trends in Microbiology 5, 331-334
    • (1997) Trends in Microbiology , vol.5 , pp. 331-334
    • Hunter, N.1
  • 27
    • 0025859996 scopus 로고
    • Genetic predisposition to iatrogenic creutzfeldt-jakob disease
    • Collinge J., Palmer M.S. and Dryden A.J. (1991) Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease. Lancet 337, 1441-1442
    • (1991) Lancet , vol.337 , pp. 1441-1442
    • Collinge, J.1    Palmer, M.S.2    Dryden, A.J.3
  • 28
    • 0025820942 scopus 로고
    • Homozygous prion protein genotype predisposes to sporadic creutzfeldt-jakob disease
    • Palmer M.S. et al. (1991) Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 352, 340-342
    • (1991) Nature , vol.352 , pp. 340-342
    • Palmer, M.S.1
  • 29
    • 0027216665 scopus 로고
    • Mutations and polymorphisms in the prion protein gene
    • Palmer M.S. and Collinge J. (1993) Mutations and polymorphisms in the prion protein gene. Human Mutation 2, 168-173
    • (1993) Human Mutation , vol.2 , pp. 168-173
    • Palmer, M.S.1    Collinge, J.2
  • 30
    • 0028928171 scopus 로고
    • Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie
    • Belt P.B. et al. (1995) Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie. Journal of General Virology 76 (Pt 3), 509-517
    • (1995) Journal of General Virology , vol.76 , pp. 509-517
    • Belt, P.B.1
  • 31
    • 0035863452 scopus 로고    scopus 로고
    • Increased susceptibility to kuru of carriers of the PRNP 129 methionine/methionine genotype
    • Lee H.S. et al. (2001) Increased susceptibility to Kuru of carriers of the PRNP 129 methionine/methionine genotype. Journal of Infectious Diseases 183, 192-196
    • (2001) Journal of Infectious Diseases , vol.183 , pp. 192-196
    • Lee, H.S.1
  • 32
    • 78651240044 scopus 로고    scopus 로고
    • Molecular biology and pathology of prion strains in sporadic human prion diseases
    • Gambetti P. et al. (2011) Molecular biology and pathology of prion strains in sporadic human prion diseases. Acta Neuropathologica 121, 79-90
    • (2011) Acta Neuropathologica , vol.121 , pp. 79-90
    • Gambetti, P.1
  • 33
    • 0037677595 scopus 로고    scopus 로고
    • Molecular classification of sporadic creutzfeldt-jakob disease
    • Hill A.F. et al. (2003) Molecular classification of sporadic Creutzfeldt-Jakob disease. Brain 126 (Pt 6), 1333-1346
    • (2003) Brain , vol.126 , pp. 1333-1346
    • Hill, A.F.1
  • 34
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge J. and Clarke A.R. (2007) A general model of prion strains and their pathogenicity. Science 318, 930-936
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 35
    • 0037320066 scopus 로고    scopus 로고
    • PrP polymorphisms tightly control sheep prion replication in cultured cells
    • Sabuncu E. et al. (2003) PrP polymorphisms tightly control sheep prion replication in cultured cells. Journal of Virology 77, 2696-2700
    • (2003) Journal of Virology , vol.77 , pp. 2696-2700
    • Sabuncu, E.1
  • 36
    • 23844476256 scopus 로고    scopus 로고
    • Sheep scrapie susceptibility-linked polymorphisms do not modulate the initial binding of cellular to disease-associated prion protein prior to conversion
    • Rigter A. and Bossers A. (2005) Sheep scrapie susceptibility-linked polymorphisms do not modulate the initial binding of cellular to disease-associated prion protein prior to conversion. Journal of General Virology 86 (Pt 9), 2627-2634
    • (2005) Journal of General Virology , vol.86 , pp. 2627-2634
    • Rigter, A.1    Bossers, A.2
  • 37
    • 79956332419 scopus 로고    scopus 로고
    • Emergence of multiple prion strains from single isolates of ovine scrapie
    • Thackray A.M. et al. (2011) Emergence of multiple prion strains from single isolates of ovine scrapie. Journal of General Virology 92 (Pt 6), 1482-1491
    • (2011) Journal of General Virology , vol.92 , pp. 1482-1491
    • Thackray, A.M.1
  • 38
    • 1642559557 scopus 로고    scopus 로고
    • The same prion strain causes vCJD and BSE
    • 526
    • Hill A.F. et al. (1997) The same prion strain causes vCJD and BSE. Nature 389, 448-450, 526
    • (1997) Nature , vol.389 , pp. 448-450
    • Hill, A.F.1
  • 39
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge J. (2001) Prion diseases of humans and animals: their causes and molecular basis. Annual Review of Neuroscience 24, 519-550
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 519-550
    • Collinge, J.1
  • 40
    • 0022824266 scopus 로고
    • Prions are novel infectious pathogens causing scrapie and creutzfeldt-jakob disease
    • Prusiner S.B. (1986) Prions are novel infectious pathogens causing scrapie and Creutzfeldt-Jakob disease. BioEssays 5, 281-286
    • (1986) BioEssays , vol.5 , pp. 281-286
    • Prusiner, S.B.1
  • 41
    • 80255140360 scopus 로고    scopus 로고
    • Prions on the move
    • Weissmann C. et al. (2011) Prions on the move. EMBO Reports 12, 1109-1117
    • (2011) EMBO Reports , vol.12 , pp. 1109-1117
    • Weissmann, C.1
  • 43
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phos-phatidylinositol glycolipid
    • Stahl N. et al. (1987) Scrapie prion protein contains a phos-phatidylinositol glycolipid. Cell 51, 229-240
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1
  • 44
    • 0031456947 scopus 로고    scopus 로고
    • Structure of the recombinant full-length hamster prion protein PrP(29-231): The n terminus is highly flexible
    • Donne D.G. et al. (1997) Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proceedings of the National Academy of Sciences of the United States of America 94, 13452-13457
    • (1997) Proceedings of The National Academy of Sciences of The United States of America , vol.94 , pp. 13452-13457
    • Donne, D.G.1
  • 45
    • 84883460724 scopus 로고    scopus 로고
    • Roles of endoproteolytic alpha-cleavage and shedding of the prion protein in neurodegeneration
    • Altmeppen H.C. et al. (2013) Roles of endoproteolytic alpha-cleavage and shedding of the prion protein in neurodegeneration. FEBS Journal 280, 4338-4347
    • (2013) FEBS Journal , vol.280 , pp. 4338-4347
    • Altmeppen, H.C.1
  • 46
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Riek R. et al. (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Letters 413, 282-288
    • (1997) FEBS Letters , vol.413 , pp. 282-288
    • Riek, R.1
  • 48
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Bueler H. et al. (1992) Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577-582
    • (1992) Nature , vol.356 , pp. 577-582
    • Bueler, H.1
  • 49
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • Manson J.C. et al. (1994) 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Molecular Neurobiology 8, 121-127
    • (1994) Molecular Neurobiology , vol.8 , pp. 121-127
    • Manson, J.C.1
  • 50
    • 33846172709 scopus 로고    scopus 로고
    • Production of cattle lacking prion protein
    • Richt J.A. et al. (2007) Production of cattle lacking prion protein. Nature Biotechnology 25, 132-138
    • (2007) Nature Biotechnology , vol.25 , pp. 132-138
    • Richt, J.A.1
  • 51
    • 33645535270 scopus 로고    scopus 로고
    • Functional disruption of the prion protein gene in cloned goats
    • Yu G. et al. (2006) Functional disruption of the prion protein gene in cloned goats. Journal of General Virology 87 (Pt 4), 1019-1027
    • (2006) Journal of General Virology , vol.87 , pp. 1019-1027
    • Yu, G.1
  • 52
    • 58449100797 scopus 로고    scopus 로고
    • Generation of goats lacking prion protein
    • Yu G. et al. (2009) Generation of goats lacking prion protein. Molecular Reproduction and Development 76, 3
    • (2009) Molecular Reproduction and Development , vol.76 , pp. 3
    • Yu, G.1
  • 53
    • 84872165752 scopus 로고    scopus 로고
    • Healthy goats naturally devoid of prion protein
    • Benestad S.L. et al. (2012) Healthy goats naturally devoid of prion protein. Veterinary Research 43, 87
    • (2012) Veterinary Research , vol.43 , pp. 87
    • Benestad, S.L.1
  • 54
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • Mallucci G.R. et al. (2002) Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO Journal 21, 202-210
    • (2002) EMBO Journal , vol.21 , pp. 202-210
    • Mallucci, G.R.1
  • 55
    • 15844421385 scopus 로고    scopus 로고
    • Altered circadian activity rhythms and sleep in mice devoid of prion protein
    • Tobler I. et al. (1996) Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 380, 639-642
    • (1996) Nature , vol.380 , pp. 639-642
    • Tobler, I.1
  • 56
    • 34249936265 scopus 로고    scopus 로고
    • The cellular prion protein (PrP(C)): Its physiological function and role in disease
    • Westergard L., Christensen H.M. and Harris D.A. (2007) The cellular prion protein (PrP(C)): its physiological function and role in disease. Biochimica et Biophysica Acta 1772, 629-644
    • (2007) Biochimica Et Biophysica Acta , vol.1772 , pp. 629-644
    • Westergard, L.1    Christensen, H.M.2    Harris, D.A.3
  • 58
    • 34249947609 scopus 로고    scopus 로고
    • Motor behavioral and neuropathological deficits in mice deficient for normal prion protein expression
    • Nazor K.E., Seward T. and Telling G.C. (2007) Motor behavioral and neuropathological deficits in mice deficient for normal prion protein expression. Biochimica et Biophysica Acta 1772, 645-653
    • (2007) Biochimica Et Biophysica Acta , vol.1772 , pp. 645-653
    • Nazor, K.E.1    Seward, T.2    Telling, G.C.3
  • 59
    • 0027997387 scopus 로고
    • Prion protein is necessary for normal synaptic function
    • Collinge J. et al. (1994) Prion protein is necessary for normal synaptic function. Nature 370, 295-297
    • (1994) Nature , vol.370 , pp. 295-297
    • Collinge, J.1
  • 60
    • 0029265461 scopus 로고
    • PrP gene dosage and long term potentiation
    • Manson J.C. et al. (1995) PrP gene dosage and long term potentiation. Neurodegeneration 4, 113-114
    • (1995) Neurodegeneration , vol.4 , pp. 113-114
    • Manson, J.C.1
  • 61
    • 84886870471 scopus 로고    scopus 로고
    • Prion protein and susceptibility to kainate-induced seizures: Genetic pitfalls in the use of PrP knockout mice
    • Striebel J.F., Race B. and Chesebro B. (2013) Prion protein and susceptibility to kainate-induced seizures: genetic pitfalls in the use of PrP knockout mice. Prion 7, 280-285
    • (2013) Prion , vol.7 , pp. 280-285
    • Striebel, J.F.1    Race, B.2    Chesebro, B.3
  • 62
    • 43149121009 scopus 로고    scopus 로고
    • The prion protein knockout mouse: A phenotype under challenge
    • Steele A.D., Lindquist S. and Aguzzi A. (2007) The prion protein knockout mouse: a phenotype under challenge. Prion 1, 83-93
    • (2007) Prion , vol.1 , pp. 83-93
    • Steele, A.D.1    Lindquist, S.2    Aguzzi, A.3
  • 63
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H. et al. (1993) Mice devoid of PrP are resistant to scrapie. Cell 73, 1339-1347
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Bueler, H.1
  • 64
    • 0028343093 scopus 로고
    • No propagation of prions in mice devoid of PrP
    • Sailer A. et al. (1994) No propagation of prions in mice devoid of PrP. Cell 77, 967-968
    • (1994) Cell , vol.77 , pp. 967-968
    • Sailer, A.1
  • 65
    • 0028703452 scopus 로고
    • PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology
    • Manson J.C. et al. (1994) PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 3, 331-340
    • (1994) Neurodegeneration , vol.3 , pp. 331-340
    • Manson, J.C.1
  • 66
    • 0022569404 scopus 로고
    • Scrapie prion proteins are synthesized in neurons
    • Kretzschmar H.A. et al. (1986) Scrapie prion proteins are synthesized in neurons. The American Journal of Pathology 122, 1-5
    • (1986) The American Journal of Pathology , vol.122 , pp. 1-5
    • Kretzschmar, H.A.1
  • 67
    • 0028902465 scopus 로고
    • Developmental expression of the prion protein gene in glial cells
    • Moser M. et al. (1995) Developmental expression of the prion protein gene in glial cells. Neuron 14, 509-517
    • (1995) Neuron , vol.14 , pp. 509-517
    • Moser, M.1
  • 68
    • 0025270288 scopus 로고
    • The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells
    • Brown H.R. et al. (1990) The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells. Acta Neuropathologica 80, 1-6
    • (1990) Acta Neuropathologica , vol.80 , pp. 1-6
    • Brown, H.R.1
  • 69
    • 0029414432 scopus 로고
    • Analysis of PrPc mRNA by in situ hybridization in brain, placenta, uterus and testis of rats
    • Tanji K. et al. (1995) Analysis of PrPc mRNA by in situ hybridization in brain, placenta, uterus and testis of rats. Intervirology 38, 309-315
    • (1995) Intervirology , vol.38 , pp. 309-315
    • Tanji, K.1
  • 70
    • 0034767752 scopus 로고    scopus 로고
    • In situ hybridization analysis of PrP mRNA in human CNS tissues
    • McLennan N.F. et al. (2001) In situ hybridization analysis of PrP mRNA in human CNS tissues. Neuropathology and Applied Neurobiology 27, 373-383
    • (2001) Neuropathology and Applied Neurobiology , vol.27 , pp. 373-383
    • McLennan, N.F.1
  • 71
    • 0026567814 scopus 로고
    • Nearly ubiquitous tissue distribution of the scrapie agent precursor protein
    • Bendheim P.E. et al. (1992) Nearly ubiquitous tissue distribution of the scrapie agent precursor protein. Neurology 42, 149-156
    • (1992) Neurology , vol.42 , pp. 149-156
    • Bendheim, P.E.1
  • 72
    • 0037198401 scopus 로고    scopus 로고
    • A marked disparity between the expression of prion protein and its message by neurones of the CNS
    • Ford M.J. et al. (2002) A marked disparity between the expression of prion protein and its message by neurones of the CNS. Neuroscience 111, 533-551
    • (2002) Neuroscience , vol.111 , pp. 533-551
    • Ford, M.J.1
  • 73
    • 0034899833 scopus 로고    scopus 로고
    • Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum
    • Laine J. et al. (2001) Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum. European Journal of Neuroscience 14, 47-56
    • (2001) European Journal of Neuroscience , vol.14 , pp. 47-56
    • Laine, J.1
  • 74
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • Gorodinsky A. and Harris D.A. (1995) Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. Journal of Cell Biology 129, 19
    • (1995) Journal of Cell Biology , vol.129 , pp. 19
    • Gorodinsky, A.1    Harris, D.A.2
  • 75
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky N. et al. (1997) Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. Journal of Biological Chemistry 272, 6324-6331
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 6324-6331
    • Naslavsky, N.1
  • 77
    • 0034665847 scopus 로고    scopus 로고
    • Signal transduction through prion protein
    • Mouillet-Richard S. et al. (2000) Signal transduction through prion protein. Science 289, 1925-1928
    • (2000) Science , vol.289 , pp. 1925-1928
    • Mouillet-Richard, S.1
  • 78
    • 0345505687 scopus 로고    scopus 로고
    • Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival
    • Chen S. et al. (2003) Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival. Molecular and Cellular Neurosciences 22, 227-233
    • (2003) Molecular and Cellular Neurosciences , vol.22 , pp. 227-233
    • Chen, S.1
  • 79
    • 0034628999 scopus 로고    scopus 로고
    • Cellular prion protein binds laminin and mediates neuritogenesis
    • Graner E. et al. (2000) Cellular prion protein binds laminin and mediates neuritogenesis. Molecular Brain Research 76, 85-92
    • (2000) Molecular Brain Research , vol.76 , pp. 85-92
    • Graner, E.1
  • 80
    • 0042855745 scopus 로고    scopus 로고
    • Cytosolic prion protein in neurons
    • Mironov A. Jr et al. (2003) Cytosolic prion protein in neurons. Journal of Neuroscience 23, 7183-7193
    • (2003) Journal of Neuroscience , vol.23 , pp. 7183-7193
    • Mironov, A.1
  • 81
    • 0029112533 scopus 로고
    • Ultrastructural localization of cellular prion protein (PrPc) in synaptic boutons of normal hamster hippocampus
    • Fournier J.G. et al. (1995) Ultrastructural localization of cellular prion protein (PrPc) in synaptic boutons of normal hamster hippocampus. Comptes Rendus de l’Académie des Sciences – Series III 318, 339-344
    • (1995) Comptes Rendus De L’Académie Des Sciences – Series III , vol.318 , pp. 339-344
    • Fournier, J.G.1
  • 82
    • 0033570367 scopus 로고    scopus 로고
    • Evidence of presynaptic location and function of the prion protein
    • Herms J. et al. (1999) Evidence of presynaptic location and function of the prion protein. Journal of Neuroscience 19, 8866-8875
    • (1999) Journal of Neuroscience , vol.19 , pp. 8866-8875
    • Herms, J.1
  • 83
    • 0034235055 scopus 로고    scopus 로고
    • Synaptic prion protein immuno-reactivity in the rodent cerebellum
    • Haeberle A.M. et al. (2000) Synaptic prion protein immuno-reactivity in the rodent cerebellum. Microscopy Research and Technique 50, 66-75
    • (2000) Microscopy Research and Technique , vol.50 , pp. 66-75
    • Haeberle, A.M.1
  • 84
    • 0034235723 scopus 로고    scopus 로고
    • Immunolocalization of the cellular prion protein in normal brain
    • Moya K.L. et al. (2000) Immunolocalization of the cellular prion protein in normal brain. Microscopy Research and Technique 50, 58-65
    • (2000) Microscopy Research and Technique , vol.50 , pp. 58-65
    • Moya, K.L.1
  • 85
    • 0035977053 scopus 로고    scopus 로고
    • PrPC directly interacts with proteins involved in signaling pathways
    • Spielhaupter C. and Schatzl H.M. (2001) PrPC directly interacts with proteins involved in signaling pathways. Journal of Biological Chemistry 276, 44604-44612
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 44604-44612
    • Spielhaupter, C.1    Schatzl, H.M.2
  • 86
    • 0037031821 scopus 로고    scopus 로고
    • Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein
    • Magalhaes A.C. et al. (2002) Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein. Journal of Biological Chemistry 277, 33311-33318
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 33311-33318
    • Magalhaes, A.C.1
  • 87
    • 84860288578 scopus 로고    scopus 로고
    • Mutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC alpha(2)delta-1 subunit
    • Senatore A. et al. (2012) Mutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC alpha(2)delta-1 Subunit. Neuron 74, 300-313
    • (2012) Neuron , vol.74 , pp. 300-313
    • Senatore, A.1
  • 88
    • 84905671900 scopus 로고    scopus 로고
    • Prion protein facilitates synaptic vesicle release by enhancing release probability
    • Robinson S.W. et al. (2014) Prion protein facilitates synaptic vesicle release by enhancing release probability. Human Molecular Genetics 23, 4581-4596
    • (2014) Human Molecular Genetics , vol.23 , pp. 4581-4596
    • Robinson, S.W.1
  • 89
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma J., Wollmann R. and Lindquist S. (2002) Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298, 1781-1785
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 90
    • 84887879167 scopus 로고    scopus 로고
    • Life cycle of cytosolic prions
    • Hofmann J. and Vorberg I. (2013) Life cycle of cytosolic prions. Prion 7, 369-377
    • (2013) Prion , vol.7 , pp. 369-377
    • Hofmann, J.1    Vorberg, I.2
  • 91
    • 70350065892 scopus 로고    scopus 로고
    • Distribution of the cellular prion protein in the central nervous system of the chicken
    • Atoji Y. and Ishiguro N. (2009) Distribution of the cellular prion protein in the central nervous system of the chicken. Journal of Chemical Neuroanatomy 38, 292-301
    • (2009) Journal of Chemical Neuroanatomy , vol.38 , pp. 292-301
    • Atoji, Y.1    Ishiguro, N.2
  • 92
    • 70349757699 scopus 로고    scopus 로고
    • PrPs: Proteins with a purpose: Lessons from the zebrafish
    • Malaga-Trillo E. and Sempou E. (2009) PrPs: Proteins with a purpose: Lessons from the zebrafish. Prion 3, 129-133
    • (2009) Prion , vol.3 , pp. 129-133
    • Malaga-Trillo, E.1    Sempou, E.2
  • 93
    • 0037301562 scopus 로고    scopus 로고
    • An evolutionary basis for scrapie disease: Identification of a fish prion mRNA
    • Rivera-Milla E., Stuermer C.A. and Malaga-Trillo E. (2003) An evolutionary basis for scrapie disease: identification of a fish prion mRNA. Trends in Genetics 19, 72-75
    • (2003) Trends in Genetics , vol.19 , pp. 72-75
    • Rivera-Milla, E.1    Stuermer, C.A.2    Malaga-Trillo, E.3
  • 94
    • 33644881628 scopus 로고    scopus 로고
    • Disparate evolution of prion protein domains and the distinct origin of doppel- and prion-related loci revealed by fish-to-mammal comparisons
    • Rivera-Milla E. et al. (2006) Disparate evolution of prion protein domains and the distinct origin of Doppel- and prion-related loci revealed by fish-to-mammal comparisons. FASEB Journal 20, 317-319
    • (2006) FASEB Journal , vol.20 , pp. 317-319
    • Rivera-Milla, E.1
  • 95
    • 30944451121 scopus 로고    scopus 로고
    • Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylpho-sphatidylinositol anchor
    • Miesbauer M. et al. (2006) Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylpho-sphatidylinositol anchor. Biochemical and Biophysical Research Communications 341, 218-224
    • (2006) Biochemical and Biophysical Research Communications , vol.341 , pp. 218-224
    • Miesbauer, M.1
  • 96
    • 65949115708 scopus 로고    scopus 로고
    • Regulation of embryonic cell adhesion by the prion protein
    • Malaga-Trillo E. et al. (2009) Regulation of embryonic cell adhesion by the prion protein. PLoS Biology 7, e55
    • (2009) PLoS Biology , vol.7
    • Malaga-Trillo, E.1
  • 98
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endo-cytosis of the prion protein
    • Pauly P.C. and Harris D.A. (1998) Copper stimulates endo-cytosis of the prion protein. Journal of Biological Chemistry 273, 33107-33110
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 99
    • 0037070637 scopus 로고    scopus 로고
    • PrP-dependent cell adhesion in N2a neuroblastoma cells
    • Mange A. et al. (2002) PrP-dependent cell adhesion in N2a neuroblastoma cells. FEBS Letters 514, 159-162
    • (2002) FEBS Letters , vol.514 , pp. 159-162
    • Mange, A.1
  • 100
    • 77649091387 scopus 로고    scopus 로고
    • Axonal prion protein is required for peripheral myelin maintenance
    • Bremer J. et al. (2010) Axonal prion protein is required for peripheral myelin maintenance. Nature Neuroscience 13, 310-318
    • (2010) Nature Neuroscience , vol.13 , pp. 310-318
    • Bremer, J.1
  • 101
    • 0033049539 scopus 로고    scopus 로고
    • A mouse prion protein transgene rescues mice deficient for the prion protein gene from purkinje cell degeneration and demyelination
    • Nishida N. et al. (1999) A mouse prion protein transgene rescues mice deficient for the prion protein gene from Purkinje cell degeneration and demyelination. Laboratory Investigation 79, 689-697
    • (1999) Laboratory Investigation , vol.79 , pp. 689-697
    • Nishida, N.1
  • 102
    • 52049108464 scopus 로고    scopus 로고
    • The involvement of cellular prion protein in the autophagy pathway in neuronal cells
    • Oh J.M. et al. (2008) The involvement of cellular prion protein in the autophagy pathway in neuronal cells. Molecular and Cellular Neurosciences 39, 238-247
    • (2008) Molecular and Cellular Neurosciences , vol.39 , pp. 238-247
    • Oh, J.M.1
  • 103
    • 70349669073 scopus 로고    scopus 로고
    • Evolutionary descent of prion genes from the ZIP family of metal ion transporters
    • Schmitt-Ulms G. et al. (2009) Evolutionary descent of prion genes from the ZIP family of metal ion transporters. PLoS ONE 4, e7208
    • (2009) PLoS ONE , vol.4
    • Schmitt-Ulms, G.1
  • 104
    • 0033571055 scopus 로고    scopus 로고
    • Normal prion protein has an activity like that of superoxide dismutase
    • Brown D.R. et al. (1999) Normal prion protein has an activity like that of superoxide dismutase. Biochemical Journal 344 (Pt 1), 1-5
    • (1999) Biochemical Journal , vol.344 , pp. 1-5
    • Brown, D.R.1
  • 105
    • 0031444294 scopus 로고    scopus 로고
    • The cellular prion protein binds copper in vivo
    • Brown D.R. et al. (1997) The cellular prion protein binds copper in vivo. Nature 390, 684-687
    • (1997) Nature , vol.390 , pp. 684-687
    • Brown, D.R.1
  • 106
    • 29144443530 scopus 로고    scopus 로고
    • Recombinant prion protein does not possess SOD-1 activity
    • Jones S. et al. (2005) Recombinant prion protein does not possess SOD-1 activity. Biochemical Journal 392 (Pt 2), 309-312
    • (2005) Biochemical Journal , vol.392 , pp. 309-312
    • Jones, S.1
  • 107
    • 0141717118 scopus 로고    scopus 로고
    • No superoxide dismutase activity of cellular prion protein in vivo
    • Hutter G., Heppner F.L. and Aguzzi A. (2003) No superoxide dismutase activity of cellular prion protein in vivo. Biological Chemistry 384, 1279-1285
    • (2003) Biological Chemistry , vol.384 , pp. 1279-1285
    • Hutter, G.1    Heppner, F.L.2    Aguzzi, A.3
  • 108
    • 83455213859 scopus 로고    scopus 로고
    • Contribution of individual histidines to prion protein copper binding
    • Davies P. et al. (2011) Contribution of individual histidines to prion protein copper binding. Biochemistry 50, 10781-10791
    • (2011) Biochemistry , vol.50 , pp. 10781-10791
    • Davies, P.1
  • 109
    • 12844250715 scopus 로고    scopus 로고
    • PrP cooperates with STI1 to regulate SOD activity in PrP-deficient neuronal cell line
    • Sakudo A. et al. (2005) PrP cooperates with STI1 to regulate SOD activity in PrP-deficient neuronal cell line. Biochemical and Biophysical Research Communications 328, 14-19
    • (2005) Biochemical and Biophysical Research Communications , vol.328 , pp. 14-19
    • Sakudo, A.1
  • 110
    • 0029932071 scopus 로고    scopus 로고
    • Analysis of interaction sites in homo- and heteromeric complexes containing bcl-2 family members and the cellular prion protein
    • Kurschner C. and Morgan J.I. (1996) Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein. Molecular Brain Research 37, 249-258
    • (1996) Molecular Brain Research , vol.37 , pp. 249-258
    • Kurschner, C.1    Morgan, J.I.2
  • 111
    • 0028911161 scopus 로고
    • The cellular prion protein (PrP) selectively binds to bcl-2 in the yeast two-hybrid system
    • Kurschner C. and Morgan J.I. (1995) The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system. Molecular Brain Research 30, 165-168
    • (1995) Molecular Brain Research , vol.30 , pp. 165-168
    • Kurschner, C.1    Morgan, J.I.2
  • 112
    • 0009782015 scopus 로고    scopus 로고
    • Prions prevent neuronal cell-line death
    • Kuwahara C. et al. (1999) Prions prevent neuronal cell-line death. Nature 400, 225-226
    • (1999) Nature , vol.400 , pp. 225-226
    • Kuwahara, C.1
  • 113
    • 0035914410 scopus 로고    scopus 로고
    • Prion protein protects human neurons against bax-mediated apoptosis
    • Bounhar Y. et al. (2001) Prion protein protects human neurons against Bax-mediated apoptosis. Journal of Biological Chemistry 276, 39145-39149
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 39145-39149
    • Bounhar, Y.1
  • 114
    • 20444454586 scopus 로고    scopus 로고
    • Mammalian prion protein suppresses bax-induced cell death in yeast
    • Li A. and Harris D.A. (2005) Mammalian prion protein suppresses Bax-induced cell death in yeast. Journal of Biological Chemistry 280, 17430-17434
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 17430-17434
    • Li, A.1    Harris, D.A.2
  • 115
    • 11844296730 scopus 로고    scopus 로고
    • Bax deletion prevents neuronal loss but not neurological symptoms in a transgenic model of inherited prion disease
    • Chiesa R. et al. (2005) Bax deletion prevents neuronal loss but not neurological symptoms in a transgenic model of inherited prion disease. Proceedings of the National Academy of Sciences of the United States of America 102, 238-243
    • (2005) Proceedings of The National Academy of Sciences of The United States of America , vol.102 , pp. 238-243
    • Chiesa, R.1
  • 116
    • 33144456321 scopus 로고    scopus 로고
    • Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal
    • Zhang C.C. et al. (2006) Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal. Proceedings of the National Academy of Sciences of the United States of America 103, 2184-2189
    • (2006) Proceedings of The National Academy of Sciences of The United States of America , vol.103 , pp. 2184-2189
    • Zhang, C.C.1
  • 117
    • 50049122656 scopus 로고    scopus 로고
    • Physiological role of the cellular prion protein
    • Zomosa-Signoret V. et al. (2008) Physiological role of the cellular prion protein. Veterinary Research 39, 9
    • (2008) Veterinary Research , vol.39 , pp. 9
    • Zomosa-Signoret, V.1
  • 118
    • 67649304776 scopus 로고    scopus 로고
    • A role of cellular prion protein in programming T-cell cytokine responses in disease
    • Ingram R.J. et al. (2009) A role of cellular prion protein in programming T-cell cytokine responses in disease. FASEB Journal 23, 1672-1684
    • (2009) FASEB Journal , vol.23 , pp. 1672-1684
    • Ingram, R.J.1
  • 119
    • 0038445510 scopus 로고    scopus 로고
    • Expression of normal cellular prion protein (PrP(c)) on t lymphocytes and the effect of copper ion: Analysis by wild-type and prion protein gene-deficient mice
    • Kubosaki A. et al. (2003) Expression of normal cellular prion protein (PrP(c)) on T lymphocytes and the effect of copper ion: Analysis by wild-type and prion protein gene-deficient mice. Biochemical and Biophysical Research Communications 307, 810-813
    • (2003) Biochemical and Biophysical Research Communications , vol.307 , pp. 810-813
    • Kubosaki, A.1
  • 120
    • 33744905327 scopus 로고    scopus 로고
    • Functional implication of cellular prion protein in antigen-driven interactions between t cells and dendritic cells
    • Ballerini C. et al. (2006) Functional implication of cellular prion protein in antigen-driven interactions between T cells and dendritic cells. Journal of Immunology 176, 7254-7262
    • (2006) Journal of Immunology , vol.176 , pp. 7254-7262
    • Ballerini, C.1
  • 121
    • 77951256828 scopus 로고    scopus 로고
    • Beta-amyloid oligomers and cellular prion protein in Alzheimer’s disease
    • Gunther E.C. and Strittmatter S.M. (2010) Beta-amyloid oligomers and cellular prion protein in Alzheimer’s disease. Journal of Molecular Medicine (Berl) 88, 331-338
    • (2010) Journal of Molecular Medicine (Berl) , vol.88 , pp. 331-338
    • Gunther, E.C.1    Strittmatter, S.M.2
  • 122
    • 34547400403 scopus 로고    scopus 로고
    • Cellular prion protein regulates beta-secretase cleavage of the Alzheimer’s amyloid precursor protein
    • Parkin E.T. et al. (2007) Cellular prion protein regulates beta-secretase cleavage of the Alzheimer’s amyloid precursor protein. Proceedings of the National Academy of Sciences of the United States of America 104, 11062-11067
    • (2007) Proceedings of The National Academy of Sciences of The United States of America , vol.104 , pp. 11062-11067
    • Parkin, E.T.1
  • 123
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J. et al. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457, 1128-1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1
  • 124
    • 79956302348 scopus 로고    scopus 로고
    • Alzheimer’s disease brain-derived amyloid-beta-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein
    • Barry A.E. et al. (2011) Alzheimer’s disease brain-derived amyloid-beta-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein. The Journal of Neuroscience 31, 7259-7263
    • (2011) The Journal of Neuroscience , vol.31 , pp. 7259-7263
    • Barry, A.E.1
  • 125
    • 79958249995 scopus 로고    scopus 로고
    • Interaction between prion protein and toxic amyloid [beta] assemblies can be therapeutically targeted at multiple sites
    • Freir D.B. et al. (2011) Interaction between prion protein and toxic amyloid [beta] assemblies can be therapeutically targeted at multiple sites. Nature Communications 2, 336
    • (2011) Nature Communications , vol.2 , pp. 336
    • Freir, D.B.1
  • 126
    • 77951876319 scopus 로고    scopus 로고
    • Memory impairment in transgenic Alzheimer mice requires cellular prion protein
    • Gimbel D.A. et al. (2010) Memory impairment in transgenic Alzheimer mice requires cellular prion protein. Journal of Neuroscience 30, 6367-6374
    • (2010) Journal of Neuroscience , vol.30 , pp. 6367-6374
    • Gimbel, D.A.1
  • 127
    • 84863011560 scopus 로고    scopus 로고
    • Cellular prion protein is essential for oligomeric amyloid-beta-induced neuronal cell death
    • Kudo W. et al. (2012) Cellular prion protein is essential for oligomeric amyloid-beta-induced neuronal cell death. Human Molecular Genetics 21, 1138-1144
    • (2012) Human Molecular Genetics , vol.21 , pp. 1138-1144
    • Kudo, W.1
  • 128
    • 80055071341 scopus 로고    scopus 로고
    • Amyloid-beta-induced synapse damage is mediated via cross-linkage of cellular prion proteins
    • Bate C. and Williams A. (2011) Amyloid-beta-induced synapse damage is mediated via cross-linkage of cellular prion proteins. Journal of Biological Chemistry 286, 37955-37963
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 37955-37963
    • Bate, C.1    Williams, A.2
  • 129
    • 77955617917 scopus 로고    scopus 로고
    • The prion protein as a receptor for amyloid-[beta]
    • Kessels H.W. et al. (2010) The prion protein as a receptor for amyloid-[beta]. Nature 466, E3-E4
    • (2010) Nature , vol.466 , pp. E3-E4
    • Kessels, H.W.1
  • 130
    • 77956165325 scopus 로고    scopus 로고
    • Prion protein and abeta-related synaptic toxicity impairment
    • Calella A.M. et al. (2010) Prion protein and Abeta-related synaptic toxicity impairment. EMBO Molecular Medicine 2, 306-314
    • (2010) EMBO Molecular Medicine , vol.2 , pp. 306-314
    • Calella, A.M.1
  • 132
    • 79960660843 scopus 로고    scopus 로고
    • Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice
    • Cisse M. et al. (2011) Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice. Journal of Neuroscience 31, 10427-10431
    • (2011) Journal of Neuroscience , vol.31 , pp. 10427-10431
    • Cisse, M.1
  • 133
    • 84861814538 scopus 로고    scopus 로고
    • Overexpression of cellular prion protein (PrP(C)) prevents cognitive dysfunction and apoptotic neuronal cell death induced by amyloid-beta (Abeta 1-40) administration in mice
    • Rial D. et al. (2012) Overexpression of cellular prion protein (PrP(C)) prevents cognitive dysfunction and apoptotic neuronal cell death induced by amyloid-beta (Abeta 1-40) administration in mice. Neuroscience 215, 79-89
    • (2012) Neuroscience , vol.215 , pp. 79-89
    • Rial, D.1
  • 134
    • 79956110918 scopus 로고    scopus 로고
    • The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication
    • Resenberger U.K. et al. (2011) The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication. EMBO Journal 30, 2057-2070
    • (2011) EMBO Journal , vol.30 , pp. 2057-2070
    • Resenberger, U.K.1
  • 135
    • 84863116075 scopus 로고    scopus 로고
    • Abeta neurotoxicity depends on interactions between copper ions, prion protein, and N-methyl-D-aspartate receptors
    • You H. et al. (2012) Abeta neurotoxicity depends on interactions between copper ions, prion protein, and N-methyl-D-aspartate receptors. Proceedings of the National Academy of Sciences of the United States of America 109, 1737-1742
    • (2012) Proceedings of The National Academy of Sciences of The United States of America , vol.109 , pp. 1737-1742
    • You, H.1
  • 136
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates fyn to impair neurons
    • Um J.W. et al. (2012) Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nature Neuroscience 15, 1227-1235
    • (2012) Nature Neuroscience , vol.15 , pp. 1227-1235
    • Um, J.W.1
  • 137
    • 40449120471 scopus 로고    scopus 로고
    • Prion diseases: From protein to cell pathology
    • Kovacs G.G. and Budka H. (2008) Prion diseases: from protein to cell pathology. American Journal of Pathology 172, 555-565
    • (2008) American Journal of Pathology , vol.172 , pp. 555-565
    • Kovacs, G.G.1    Budka, H.2
  • 138
    • 58849140480 scopus 로고    scopus 로고
    • Ultrastructural study of florid plaques in variant creutzfeldt-jakob disease: A comparison with amyloid plaques in kuru, sporadic creutzfeldt-jakob disease and gerstmann–Straussler–Scheinker disease
    • Sikorska B. et al. (2009) Ultrastructural study of florid plaques in variant Creutzfeldt-Jakob disease: a comparison with amyloid plaques in kuru, sporadic Creutzfeldt-Jakob disease and Gerstmann–Straussler–Scheinker disease. Neuropathology and Applied Neurobiology 35, 46-59
    • (2009) Neuropathology and Applied Neurobiology , vol.35 , pp. 46-59
    • Sikorska, B.1
  • 139
    • 0027483615 scopus 로고
    • Neurotoxicity of a prion protein fragment
    • Forloni G. et al. (1993) Neurotoxicity of a prion protein fragment. Nature 362, 543-546
    • (1993) Nature , vol.362 , pp. 543-546
    • Forloni, G.1
  • 140
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C. et al. (2003) Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO Journal 22, 5435-5445
    • (2003) EMBO Journal , vol.22 , pp. 5435-5445
    • Hetz, C.1
  • 141
    • 28444470232 scopus 로고    scopus 로고
    • Histopathology and immunohistochemistry of human transmissible spongiform encephalopathies (TSEs)
    • Budka H. (2000) Histopathology and immunohistochemistry of human transmissible spongiform encephalopathies (TSEs). Archives of Virology Supplementum 16, 135-142
    • (2000) Archives of Virology Supplementum , vol.16 , pp. 135-142
    • Budka, H.1
  • 143
    • 33845925066 scopus 로고    scopus 로고
    • Insoluble aggregates and protease-resistant conformers of prion protein in uninfected human brains
    • Yuan J. et al. (2006) Insoluble aggregates and protease-resistant conformers of prion protein in uninfected human brains. Journal of Biological Chemistry 281, 34848-34858
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 34848-34858
    • Yuan, J.1
  • 144
    • 0028608963 scopus 로고
    • Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein
    • Hsiao K.K. et al. (1994) Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proceedings of the National Academy of Sciences of the United States of America 91, 9126-9130
    • (1994) Proceedings of The National Academy of Sciences of The United States of America , vol.91 , pp. 9126-9130
    • Hsiao, K.K.1
  • 145
    • 0029132280 scopus 로고
    • First experimental transmission of fatal familial insomnia
    • Tateishi J. et al. (1995) First experimental transmission of fatal familial insomnia. Nature 376, 434-435
    • (1995) Nature , vol.376 , pp. 434-435
    • Tateishi, J.1
  • 146
    • 0028040838 scopus 로고
    • Prion protein immunocytochemistry: Reliable protocols for the investigation of creutzfeldt-jakob disease
    • Hayward P.A., Bell J.E. and Ironside J.W. (1994) Prion protein immunocytochemistry: reliable protocols for the investigation of Creutzfeldt-Jakob disease. Neuropathology and Applied Neurobiology 20, 375-383
    • (1994) Neuropathology and Applied Neurobiology , vol.20 , pp. 375-383
    • Hayward, P.A.1    Bell, J.E.2    Ironside, J.W.3
  • 147
    • 0029160006 scopus 로고
    • Transmission of fatal familial insomnia to laboratory animals
    • Collinge J. et al. (1995) Transmission of fatal familial insomnia to laboratory animals. Lancet 346, 569-570
    • (1995) Lancet , vol.346 , pp. 569-570
    • Collinge, J.1
  • 148
    • 84904215335 scopus 로고    scopus 로고
    • Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked
    • Sandberg M.K. et al. (2014) Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked. Nature Communications 5, 4347
    • (2014) Nature Communications , vol.5 , pp. 4347
    • Sandberg, M.K.1
  • 149
    • 77950379326 scopus 로고    scopus 로고
    • Fatal transmissible amyloid encephalopathy: A new type of prion disease associated with lack of prion protein membrane anchoring
    • Chesebro B. et al. (2010) Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring. PLoS Pathogens 6, e1000800
    • (2010) PLoS Pathogens , vol.6
    • Chesebro, B.1
  • 150
    • 0028535880 scopus 로고
    • High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene
    • Bueler H. et al. (1994) High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Molecular Medicine 1, 19-30
    • (1994) Molecular Medicine , vol.1 , pp. 19-30
    • Bueler, H.1
  • 151
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • Sandberg M.K. et al. (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
  • 153
    • 0034790796 scopus 로고    scopus 로고
    • Long-term subclinical carrier state precedes scrapie replication and adaptation in a resistant species: Analogies to bovine spongiform encephalopathy and variant creutzfeldt-jakob disease in humans
    • Race R. et al. (2001) Long-term subclinical carrier state precedes scrapie replication and adaptation in a resistant species: analogies to bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease in humans. Journal of Virology 75, 10106-10112
    • (2001) Journal of Virology , vol.75 , pp. 10106-10112
    • Race, R.1
  • 154
    • 0036168776 scopus 로고    scopus 로고
    • Chronic subclinical prion disease induced by low-dose inoculum
    • Thackray A.M. et al. (2002) Chronic subclinical prion disease induced by low-dose inoculum. Journal of Virology 76, 2510-2517
    • (2002) Journal of Virology , vol.76 , pp. 2510-2517
    • Thackray, A.M.1
  • 155
    • 0038082181 scopus 로고    scopus 로고
    • Subclinical prion disease induced by oral inoculation
    • Thackray A.M., Klein M.A. and Bujdoso R. (2003) Subclinical prion disease induced by oral inoculation. Journal of Virology 77, 7991-7998
    • (2003) Journal of Virology , vol.77 , pp. 7991-7998
    • Thackray, A.M.1    Klein, M.A.2    Bujdoso, R.3
  • 156
    • 18744362997 scopus 로고    scopus 로고
    • BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein
    • Asante E.A. et al. (2002) BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein. EMBO Journal 21, 6358-6366
    • (2002) EMBO Journal , vol.21 , pp. 6358-6366
    • Asante, E.A.1
  • 158
    • 0030054010 scopus 로고    scopus 로고
    • Normal host prion protein necessary for scrapie-induced neurotoxicity
    • Brandner S. et al. (1996) Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 379, 339-343
    • (1996) Nature , vol.379 , pp. 339-343
    • Brandner, S.1
  • 159
    • 0032249941 scopus 로고    scopus 로고
    • Use of brain grafts to study the pathogenesis of prion diseases
    • Aguzzi A. et al. (1998) Use of brain grafts to study the pathogenesis of prion diseases. Essays in Biochemistry 33, 133-147
    • (1998) Essays in Biochemistry , vol.33 , pp. 133-147
    • Aguzzi, A.1
  • 160
    • 0242363656 scopus 로고    scopus 로고
    • Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis
    • Mallucci G. et al. (2003) Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 302, 871-874
    • (2003) Science , vol.302 , pp. 871-874
    • Mallucci, G.1
  • 161
    • 12844287619 scopus 로고    scopus 로고
    • An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells
    • Kazlauskaite J. et al. (2005) An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells. Biochemical and Biophysical Research Communications 328, 292-305
    • (2005) Biochemical and Biophysical Research Communications , vol.328 , pp. 292-305
    • Kazlauskaite, J.1
  • 162
    • 11844286389 scopus 로고    scopus 로고
    • Efficient inhibition of prion replication by PrP-Fc(2) suggests that the prion is a PrP(Sc) oligomer
    • Masel J., Genoud N. and Aguzzi A. (2005) Efficient inhibition of prion replication by PrP-Fc(2) suggests that the prion is a PrP(Sc) oligomer. Journal of Molecular Biology 345, 1243-1251
    • (2005) Journal of Molecular Biology , vol.345 , pp. 1243-1251
    • Masel, J.1    Genoud, N.2    Aguzzi, A.3
  • 163
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer’s amyloid beta-peptide
    • Haass C. and Selkoe D.J. (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nature Reviews. Molecular Cell Biology 8, 101-112
    • (2007) Nature Reviews. Molecular Cell Biology , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 165
    • 34548392742 scopus 로고    scopus 로고
    • In vitro and in vivo neurotoxicity of prion protein oligomers
    • Simoneau S. et al. (2007) In vitro and in vivo neurotoxicity of prion protein oligomers. PLoS Pathogens 3, e125
    • (2007) PLoS Pathogens , vol.3
    • Simoneau, S.1
  • 166
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V. et al. (2006) Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. Journal of Biological Chemistry 281, 13828-13836
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 13828-13836
    • Novitskaya, V.1
  • 168
    • 33646126278 scopus 로고    scopus 로고
    • New insights into prion structure and toxicity
    • Harris D.A. and True H.L. (2006) New insights into prion structure and toxicity. Neuron 50, 353-357
    • (2006) Neuron , vol.50 , pp. 353-357
    • Harris, D.A.1    True, H.L.2
  • 169
    • 20344394154 scopus 로고    scopus 로고
    • Anchorless prion protein results in infectious amyloid disease without clinical scrapie
    • Chesebro B. et al. (2005) Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308, 1435-1439
    • (2005) Science , vol.308 , pp. 1435-1439
    • Chesebro, B.1
  • 172
    • 33745910558 scopus 로고    scopus 로고
    • Prion-induced amyloid heart disease with high blood infectivity in transgenic mice
    • Trifilo M.J. et al. (2006) Prion-induced amyloid heart disease with high blood infectivity in transgenic mice. Science 313, 94-97
    • (2006) Science , vol.313 , pp. 94-97
    • Trifilo, M.J.1
  • 173
    • 78951477465 scopus 로고    scopus 로고
    • Crucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infection
    • Klingeborn M. et al. (2011) Crucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infection. Journal of Virology 85, 1484-1494
    • (2011) Journal of Virology , vol.85 , pp. 1484-1494
    • Klingeborn, M.1
  • 174
    • 13344295093 scopus 로고    scopus 로고
    • Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: The phenotype of the stop codon 145 mutation in PRNP
    • Ghetti B. et al. (1996) Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP. Proceedings of the National Academy of Sciences of the United States of America 93, 744-748
    • (1996) Proceedings of The National Academy of Sciences of The United States of America , vol.93 , pp. 744-748
    • Ghetti, B.1
  • 175
    • 67349216125 scopus 로고    scopus 로고
    • Genetics and molecular pathogenesis of sporadic and hereditary cerebral amyloid angiopathies
    • Revesz T. et al. (2009) Genetics and molecular pathogenesis of sporadic and hereditary cerebral amyloid angiopathies. Acta Neuropathologica 118, 115-130
    • (2009) Acta Neuropathologica , vol.118 , pp. 115-130
    • Revesz, T.1
  • 176
    • 77449089995 scopus 로고    scopus 로고
    • Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP
    • Jansen C. et al. (2010) Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP. Acta Neuropathologica 119, 189-197
    • (2010) Acta Neuropathologica , vol.119 , pp. 189-197
    • Jansen, C.1
  • 177
    • 0141514771 scopus 로고    scopus 로고
    • Sporadic and familial CJD: Classification and characterisation
    • Gambetti P. et al. (2003) Sporadic and familial CJD: classification and characterisation. British Medical Bulletin 66, 213-239
    • (2003) British Medical Bulletin , vol.66 , pp. 213-239
    • Gambetti, P.1
  • 178
    • 84908884094 scopus 로고    scopus 로고
    • Proteomics analysis of amyloid and nonamyloid prion disease phenotypes reveals both common and divergent mechanisms of neuropathogenesis
    • Moore R.A. et al. (2014) Proteomics analysis of amyloid and nonamyloid prion disease phenotypes reveals both common and divergent mechanisms of neuropathogenesis. Journal of Proteome Research 13, 4620-4634
    • (2014) Journal of Proteome Research , vol.13 , pp. 4620-4634
    • Moore, R.A.1
  • 179
    • 0141849861 scopus 로고    scopus 로고
    • Neuropathology of prion diseases
    • Budka H. (2003) Neuropathology of prion diseases. British Medical Bulletin 66, 121-130
    • (2003) British Medical Bulletin , vol.66 , pp. 121-130
    • Budka, H.1
  • 180
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky D.J. (2000) Autophagy as a regulated pathway of cellular degradation. Science 290, 1717-1721
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1
  • 182
    • 26444515364 scopus 로고    scopus 로고
    • Autophagy and its possible roles in nervous system diseases, damage and repair
    • Rubinsztein D.C. et al. (2005) Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy 1, 11-22
    • (2005) Autophagy , vol.1 , pp. 11-22
    • Rubinsztein, D.C.1
  • 183
    • 0024328518 scopus 로고
    • Neuronal autophagy in experimental creutzfeldt-jakob’s disease
    • Boellaard J.W., Schlote W. and Tateishi J. (1989) Neuronal autophagy in experimental Creutzfeldt-Jakob’s disease. Acta Neuropathologica 78, 410-418
    • (1989) Acta Neuropathologica , vol.78 , pp. 410-418
    • Boellaard, J.W.1    Schlote, W.2    Tateishi, J.3
  • 184
    • 0036366068 scopus 로고    scopus 로고
    • How do neurons degenerate in prion diseases or transmissible spongiform encephalopathies (TSEs): Neuronal autophagy revisited
    • Liberski P.P., Gajdusek D. and Brown P. (2002) How do neurons degenerate in prion diseases or transmissible spongiform encephalopathies (TSEs): neuronal autophagy revisited. Acta Neurobiologiae Experimentalis 62, 7
    • (2002) Acta Neurobiologiae Experimentalis , vol.62 , pp. 7
    • Liberski, P.P.1    Gajdusek, D.2    Brown, P.3
  • 185
    • 4344656906 scopus 로고    scopus 로고
    • Neuronal cell death in transmissible spongiform encephalopathies (prion diseases) revisited: From apoptosis to autophagy
    • Liberski P.P. et al. (2004) Neuronal cell death in transmissible spongiform encephalopathies (prion diseases) revisited: from apoptosis to autophagy. International Journal of Biochemistry & Cell Biology 36, 2473-2490
    • (2004) International Journal of Biochemistry & Cell Biology , vol.36 , pp. 2473-2490
    • Liberski, P.P.1
  • 186
    • 47949127624 scopus 로고    scopus 로고
    • Trehalose impairs aggregation of PrPSc molecules and protects prion-infected cells against oxidative damage
    • Beranger F. et al. (2008) Trehalose impairs aggregation of PrPSc molecules and protects prion-infected cells against oxidative damage. Biochemical and Biophysical Research Communications 374, 44-48
    • (2008) Biochemical and Biophysical Research Communications , vol.374 , pp. 44-48
    • Beranger, F.1
  • 187
    • 65249103439 scopus 로고    scopus 로고
    • Autophagy induction by trehalose counter-acts cellular prion-infection
    • Aguib Y. et al. (2009) Autophagy induction by trehalose counter-acts cellular prion-infection. Autophagy 5, 9
    • (2009) Autophagy , vol.5 , pp. 9
    • Aguib, Y.1
  • 188
    • 61849102412 scopus 로고    scopus 로고
    • Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy
    • Heiseke A. et al. (2009) Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy. Journal of Neurochemistry 109, 25-34
    • (2009) Journal of Neurochemistry , vol.109 , pp. 25-34
    • Heiseke, A.1
  • 189
    • 4744361580 scopus 로고    scopus 로고
    • The tyrosine kinase inhibitor STI571 induces cellular clearance of PrPSc in prion-infected cells
    • Ertmer A. et al. (2004) The tyrosine kinase inhibitor STI571 induces cellular clearance of PrPSc in prion-infected cells. Journal of Biological Chemistry 279, 41918-41927
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 41918-41927
    • Ertmer, A.1
  • 190
    • 34548633461 scopus 로고    scopus 로고
    • The tyrosine kinase inhibitor imatinib mesylate delays prion neuroinvasion by inhibiting prion propagation in the periphery
    • Yun S.W. et al. (2007) The tyrosine kinase inhibitor imatinib mesylate delays prion neuroinvasion by inhibiting prion propagation in the periphery. Journal of Neurovirology 13, 328-337
    • (2007) Journal of Neurovirology , vol.13 , pp. 328-337
    • Yun, S.W.1
  • 191
    • 84929069363 scopus 로고    scopus 로고
    • + replenishment
    • + replenishment. Brain 138 (Pt 4), 992-1008
    • (2015) Brain , vol.138 , pp. 992-1008
    • Zhou, M.1
  • 192
    • 84865749298 scopus 로고    scopus 로고
    • Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of gerstmann–Straussler–Scheinker disease
    • Cortes C.J. et al. (2012) Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann–Straussler–Scheinker disease. Journal of Neuroscience 32, 12396-12405
    • (2012) Journal of Neuroscience , vol.32 , pp. 12396-12405
    • Cortes, C.J.1
  • 193
    • 0029085515 scopus 로고
    • Neuronal cell death in scrapie-infected mice is due to apoptosis
    • Giese A. et al. (1995) Neuronal cell death in scrapie-infected mice is due to apoptosis. Brain Pathology 5, 213-221
    • (1995) Brain Pathology , vol.5 , pp. 213-221
    • Giese, A.1
  • 194
    • 0028867319 scopus 로고
    • Detection of apoptosis in murine scrapie
    • Lucassen P.J. et al. (1995) Detection of apoptosis in murine scrapie. Neuroscience Letters 198, 185-188
    • (1995) Neuroscience Letters , vol.198 , pp. 185-188
    • Lucassen, P.J.1
  • 195
    • 0031292557 scopus 로고    scopus 로고
    • Programmed cell death (apoptosis) in Alzheimer’s disease and creutzfeldt–Jakob disease
    • Jesionek-Kupnicka D. et al. (1997) Programmed cell death (apoptosis) in Alzheimer’s disease and Creutzfeldt–Jakob disease. Folia Neuropathologica 35, 233-235
    • (1997) Folia Neuropathologica , vol.35 , pp. 233-235
    • Jesionek-Kupnicka, D.1
  • 196
    • 0033769044 scopus 로고    scopus 로고
    • A nonfibrillar form of the fusogenic prion protein fragment [118–135] induces apoptotic cell death in rat cortical neurons
    • Pillot T. et al. (2000) A nonfibrillar form of the fusogenic prion protein fragment [118–135] induces apoptotic cell death in rat cortical neurons. Journal of Neurochemistry 75, 2298-2308
    • (2000) Journal of Neurochemistry , vol.75 , pp. 2298-2308
    • Pillot, T.1
  • 197
    • 0035941307 scopus 로고    scopus 로고
    • Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells
    • O’Donovan C.N., Tobin D. and Cotter T.G. (2001) Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells. Journal of Biological Chemistry 276, 43516-43523
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 43516-43523
    • O’Donovan, C.N.1    Tobin, D.2    Cotter, T.G.3
  • 198
    • 50849114500 scopus 로고    scopus 로고
    • Cytosolic prion protein is the predominant anti-bax prion protein form: Exclusion of transmembrane and secreted prion protein forms in the anti-bax function
    • Lin D.T. et al. (2008) Cytosolic prion protein is the predominant anti-Bax prion protein form: exclusion of transmembrane and secreted prion protein forms in the anti-Bax function. Biochimica et Biophysica Acta 1783, 2001-2012
    • (2008) Biochimica Et Biophysica Acta , vol.1783 , pp. 2001-2012
    • Lin, D.T.1
  • 199
    • 0034625069 scopus 로고    scopus 로고
    • Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation
    • Chiesa R. et al. (2000) Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation. Proceedings of the National Academy of Sciences of the United States of America 97, 5574-5579
    • (2000) Proceedings of The National Academy of Sciences of The United States of America , vol.97 , pp. 5574-5579
    • Chiesa, R.1
  • 200
    • 33747200829 scopus 로고    scopus 로고
    • Bax deletion does not protect neurons from BSE-induced death
    • Coulpier M. et al. (2006) Bax deletion does not protect neurons from BSE-induced death. Neurobiology of Disease 23, 603-611
    • (2006) Neurobiology of Disease , vol.23 , pp. 603-611
    • Coulpier, M.1
  • 201
    • 0036939211 scopus 로고    scopus 로고
    • Abnormal synaptic protein expression and cell death in murine scrapie
    • Siso S. et al. (2002) Abnormal synaptic protein expression and cell death in murine scrapie. Acta Neuropathologica 103, 615-626
    • (2002) Acta Neuropathologica , vol.103 , pp. 615-626
    • Siso, S.1
  • 202
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T. et al. (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403, 98-103
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1
  • 204
    • 51649103992 scopus 로고    scopus 로고
    • Prion pathogenesis is independent of caspase-12
    • Steele A.D. et al. (2007) Prion pathogenesis is independent of caspase-12. Prion 1, 243-247
    • (2007) Prion , vol.1 , pp. 243-247
    • Steele, A.D.1
  • 205
    • 78650994378 scopus 로고    scopus 로고
    • The intricate mechanisms of neurodegeneration in prion diseases
    • Soto C. and Satani N. (2011) The intricate mechanisms of neurodegeneration in prion diseases. Trends in Molecular Medicine 17, 14-24
    • (2011) Trends in Molecular Medicine , vol.17 , pp. 14-24
    • Soto, C.1    Satani, N.2
  • 206
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • Torres M. et al. (2010) Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS ONE 5, e15658
    • (2010) PLoS ONE , vol.5
    • Torres, M.1
  • 207
    • 78449257695 scopus 로고    scopus 로고
    • Calcineurin inhibition at the clinical phase of prion disease reduces neurodegeneration, improves behavioral alterations and increases animal survival
    • Mukherjee A. et al. (2010) Calcineurin inhibition at the clinical phase of prion disease reduces neurodegeneration, improves behavioral alterations and increases animal survival. PLoS Pathogens 6, e1001138
    • (2010) PLoS Pathogens , vol.6
    • Mukherjee, A.1
  • 208
    • 0001552281 scopus 로고    scopus 로고
    • Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions
    • Shmerling D. et al. (1998) Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 93, 203-214
    • (1998) Cell , vol.93 , pp. 203-214
    • Shmerling, D.1
  • 209
    • 33846543360 scopus 로고    scopus 로고
    • Neonatal lethality in transgenic mice expressing prion protein with a deletion of residues 105-125
    • Li A. et al. (2007) Neonatal lethality in transgenic mice expressing prion protein with a deletion of residues 105-125. EMBO Journal 26, 548-558
    • (2007) EMBO Journal , vol.26 , pp. 548-558
    • Li, A.1
  • 210
    • 33846498655 scopus 로고    scopus 로고
    • Lethal recessive myelin toxicity of prion protein lacking its central domain
    • Baumann F. et al. (2007) Lethal recessive myelin toxicity of prion protein lacking its central domain. EMBO Journal 26, 538-547
    • (2007) EMBO Journal , vol.26 , pp. 538-547
    • Baumann, F.1
  • 212
    • 77953206169 scopus 로고    scopus 로고
    • A highly toxic cellular prion protein induces a novel, nonapoptotic form of neuronal death
    • Christensen H.M. et al. (2010) A highly toxic cellular prion protein induces a novel, nonapoptotic form of neuronal death. American Journal of Pathology 176, 2695-2706
    • (2010) American Journal of Pathology , vol.176 , pp. 2695-2706
    • Christensen, H.M.1
  • 213
    • 33750087269 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein
    • Orsi A. et al. (2006) Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein. Journal of Biological Chemistry 281, 30431-30438
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 30431-30438
    • Orsi, A.1
  • 214
    • 51449098355 scopus 로고    scopus 로고
    • Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration
    • Rane N.S. et al. (2008) Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration. Developmental Cell 15, 359-370
    • (2008) Developmental Cell , vol.15 , pp. 359-370
    • Rane, N.S.1
  • 215
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang S.W. et al. (2006) Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127, 999-1013
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1
  • 216
    • 0038159514 scopus 로고    scopus 로고
    • Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation
    • Drisaldi B. et al. (2003) Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. Journal of Biological Chemistry 278, 21732-21743
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 21732-21743
    • Drisaldi, B.1
  • 217
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P. and Ron D. (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 219
    • 38649108109 scopus 로고    scopus 로고
    • Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis
    • Hetz C. et al. (2008) Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. Proceedings of the National Academy of Sciences of the United States of America 105, 757-762
    • (2008) Proceedings of The National Academy of Sciences of The United States of America , vol.105 , pp. 757-762
    • Hetz, C.1
  • 220
    • 81755184374 scopus 로고    scopus 로고
    • The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress
    • Teske B.F. et al. (2011) The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress. Molecular Biology of the Cell 22, 4390-4405
    • (2011) Molecular Biology of The Cell , vol.22 , pp. 4390-4405
    • Teske, B.F.1
  • 221
    • 34250351315 scopus 로고    scopus 로고
    • Perturbation of endoplasmic reticulum homeostasis facilitates prion replication
    • Hetz C., Castilla J. and Soto C. (2007) Perturbation of endoplasmic reticulum homeostasis facilitates prion replication. Journal of Biological Chemistry 282, 12725-12733
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 12725-12733
    • Hetz, C.1    Castilla, J.2    Soto, C.3
  • 222
    • 84861450392 scopus 로고    scopus 로고
    • Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration
    • Moreno J.A. et al. (2012) Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration. Nature 485, 507-511
    • (2012) Nature , vol.485 , pp. 507-511
    • Moreno, J.A.1
  • 223
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A. and Brundin P. (2003) The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40, 427-446
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 224
    • 0037195617 scopus 로고    scopus 로고
    • Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
    • Ma J. and Lindquist S. (2002) Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298, 1785-1788
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 225
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia Y. et al. (2001) Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO Journal 20, 5383-5391
    • (2001) EMBO Journal , vol.20 , pp. 5383-5391
    • Yedidia, Y.1
  • 226
    • 0026452020 scopus 로고
    • Immunoreactivity to ubiquitin-protein conjugates is present early in the disease process in the brains of scrapie-infected mice
    • Lowe J. et al. (1992) Immunoreactivity to ubiquitin-protein conjugates is present early in the disease process in the brains of scrapie-infected mice. Journal of Pathology 168, 169-177
    • (1992) Journal of Pathology , vol.168 , pp. 169-177
    • Lowe, J.1
  • 227
    • 0027194960 scopus 로고
    • Ubiquitin immunocytochemistry in human spongiform encephalopathies
    • Ironside J.W. et al. (1993) Ubiquitin immunocytochemistry in human spongiform encephalopathies. Neuropathology and Applied Neurobiology 19, 134-140
    • (1993) Neuropathology and Applied Neurobiology , vol.19 , pp. 134-140
    • Ironside, J.W.1
  • 228
    • 11144231706 scopus 로고    scopus 로고
    • Subcellular localization of disease-associated prion protein in the human brain
    • Kovacs G.G. et al. (2005) Subcellular localization of disease-associated prion protein in the human brain. American Journal of Pathology 166, 287-294
    • (2005) American Journal of Pathology , vol.166 , pp. 287-294
    • Kovacs, G.G.1
  • 229
    • 1942531594 scopus 로고    scopus 로고
    • Prion protein is ubiquitinated after developing protease resistance in the brains of scrapie-infected mice
    • Kang S.C. et al. (2004) Prion protein is ubiquitinated after developing protease resistance in the brains of scrapie-infected mice. Journal of Pathology 203, 603-608
    • (2004) Journal of Pathology , vol.203 , pp. 603-608
    • Kang, S.C.1
  • 230
    • 33644677579 scopus 로고    scopus 로고
    • Disease-related prion protein forms aggresomes in neuronal cells leading to caspase activation and apoptosis
    • Kristiansen M. et al. (2005) Disease-related prion protein forms aggresomes in neuronal cells leading to caspase activation and apoptosis. Journal of Biological Chemistry 280, 38851-38861
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 38851-38861
    • Kristiansen, M.1
  • 231
    • 34247185404 scopus 로고    scopus 로고
    • Disease-associated prion protein oligomers inhibit the 26S proteasome
    • Kristiansen M. et al. (2007) Disease-associated prion protein oligomers inhibit the 26S proteasome. Molecular Cell 26, 175-188
    • (2007) Molecular Cell , vol.26 , pp. 175-188
    • Kristiansen, M.1
  • 232
    • 0035900447 scopus 로고    scopus 로고
    • Activation of fas and caspase 3 precedes PrP accumulation in 87 V scrapie
    • Jamieson E. et al. (2001) Activation of Fas and caspase 3 precedes PrP accumulation in 87 V scrapie. Neuroreport 12, 3567-3572
    • (2001) Neuroreport , vol.12 , pp. 3567-3572
    • Jamieson, E.1
  • 233
    • 79955781215 scopus 로고    scopus 로고
    • Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction
    • Quaglio E. et al. (2011) Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction. PLoS ONE 6, e19339
    • (2011) PLoS ONE , vol.6
    • Quaglio, E.1
  • 234
    • 61449198575 scopus 로고    scopus 로고
    • HECTD2 is associated with susceptibility to mouse and human prion disease
    • Lloyd S.E. et al. (2009) HECTD2 is associated with susceptibility to mouse and human prion disease. PLoS Genetics 5, e1000383
    • (2009) PLoS Genetics , vol.5
    • Lloyd, S.E.1
  • 235
    • 70349236999 scopus 로고    scopus 로고
    • Prion protein with an insertional mutation accumulates on axonal and dendritic plasmalemma and is associated with distinctive ultrastructural changes
    • Jeffrey M. et al. (2009) Prion protein with an insertional mutation accumulates on axonal and dendritic plasmalemma and is associated with distinctive ultrastructural changes. American Journal of Pathology 175, 1208-1217
    • (2009) American Journal of Pathology , vol.175 , pp. 1208-1217
    • Jeffrey, M.1
  • 236
    • 0038128629 scopus 로고    scopus 로고
    • Molecular distinction between pathogenic and infectious properties of the prion protein
    • Chiesa R. et al. (2003) Molecular distinction between pathogenic and infectious properties of the prion protein. Journal of Virology 77, 7611-7622
    • (2003) Journal of Virology , vol.77 , pp. 7611-7622
    • Chiesa, R.1
  • 237
    • 0029922585 scopus 로고    scopus 로고
    • Strain specific and common pathogenic events in murine models of scrapie and bovine spongiform encephalopathy
    • Lasmezas C.I. et al. (1996) Strain specific and common pathogenic events in murine models of scrapie and bovine spongiform encephalopathy. Journal of General Virology 77 (Pt 7), 1601-1609
    • (1996) Journal of General Virology , vol.77 , pp. 1601-1609
    • Lasmezas, C.I.1
  • 238
    • 33749236787 scopus 로고    scopus 로고
    • A systematic review of prion therapeutics in experimental models
    • Trevitt C.R. and Collinge J. (2006) A systematic review of prion therapeutics in experimental models. Brain 129 (Pt 9), 2241-2265
    • (2006) Brain , vol.129 , pp. 2241-2265
    • Trevitt, C.R.1    Collinge, J.2
  • 239
    • 84885463900 scopus 로고    scopus 로고
    • Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice
    • Moreno J.A. et al. (2013) Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice. Science Translational Medicine 5, 206ra138
    • (2013) Science Translational Medicine , vol.5 , pp. 206ra138
    • Moreno, J.A.1
  • 240
    • 84988811921 scopus 로고    scopus 로고
    • Partial restoration of protein synthesis rates by the small molecule ISRIB prevents neurodegeneration without pancreatic toxicity
    • Halliday M. et al. (2015) Partial restoration of protein synthesis rates by the small molecule ISRIB prevents neurodegeneration without pancreatic toxicity. Cell Death & Disease 6, e1672
    • (2015) Cell Death & Disease , vol.6 , pp. e1672
    • Halliday, M.1
  • 241
  • 242
    • 84873728561 scopus 로고    scopus 로고
    • Immunotherapy in prion disease
    • Roettger Y. et al. (2013) Immunotherapy in prion disease. Nature Reviews Neurology 9, 98-105
    • (2013) Nature Reviews Neurology , vol.9 , pp. 98-105
    • Roettger, Y.1
  • 243
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D. et al. (1999) Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400, 173-177
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1
  • 245
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D. et al. (2001) Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412, 739-743
    • (2001) Nature , vol.412 , pp. 739-743
    • Peretz, D.1
  • 246
    • 0037422133 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit prion replication and delay the development of prion disease
    • White A.R. et al. (2003) Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422, 80-83
    • (2003) Nature , vol.422 , pp. 80-83
    • White, A.R.1
  • 247
    • 21144432949 scopus 로고    scopus 로고
    • Mucosal vaccination delays or prevents prion infection via an oral route
    • Goni F. et al. (2005) Mucosal vaccination delays or prevents prion infection via an oral route. Neuroscience 133, 413-421
    • (2005) Neuroscience , vol.133 , pp. 413-421
    • Goni, F.1
  • 248
    • 84921318133 scopus 로고    scopus 로고
    • Mucosal immunization with an attenuated salmonella vaccine partially protects white-tailed deer from chronic wasting disease
    • Goni F. et al. (2015) Mucosal immunization with an attenuated Salmonella vaccine partially protects white-tailed deer from chronic wasting disease. Vaccine 33, 726-733
    • (2015) Vaccine , vol.33 , pp. 726-733
    • Goni, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.