메뉴 건너뛰기




Volumn 1, Issue , 2013, Pages

Prions

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84974678558     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (452)
  • 1
    • 77952956256 scopus 로고    scopus 로고
    • Cellular factors implicated in prion replication
    • Abid K, Morales R, Soto C. Cellular factors implicated in prion replication. FEBS Lett 2010;584:2409-2414.
    • (2010) FEBS Lett , vol.584 , pp. 2409-2414
    • Abid, K.1    Morales, R.2    Soto, C.3
  • 2
    • 77954238207 scopus 로고    scopus 로고
    • Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3
    • Adrover M, Pauwels K, Prigent S, et al. Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3. J Biol Chem 2010;285:21004-21012.
    • (2010) J Biol Chem , vol.285 , pp. 21004-21012
    • Adrover, M.1    Pauwels, K.2    Prigent, S.3
  • 3
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper T, Cramp WA, Haig DA, et al. Does the agent of scrapie replicate without nucleic acid? Nature 1967;214:764-766.
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3
  • 4
    • 53749099166 scopus 로고    scopus 로고
    • A history of kuru
    • Alpers MP. A history of kuru. P N G Med J 2007;50:10-19.
    • (2007) P N G Med J , vol.50 , pp. 10-19
    • Alpers, M.P.1
  • 5
    • 0002168901 scopus 로고
    • Kuru: implications of its transmissibility for the interpretation of its changing epidemiological pattern
    • Bailey OT, Smith DE, eds, Baltimore: Williams and Wilkins Company
    • Alpers MP. Kuru: implications of its transmissibility for the interpretation of its changing epidemiological pattern. In: Bailey OT, Smith DE, eds. The Central Nervous System: Some Experimental Models of Neurological Diseases. Baltimore: Williams and Wilkins Company; 1968:234-251.
    • (1968) The Central Nervous System: Some Experimental Models of Neurological Diseases , pp. 234-251
    • Alpers, M.P.1
  • 6
    • 0008390602 scopus 로고
    • Creutzfeldt-Jakob disease among Libyan Jews in Israel
    • Alter M, Kahana E. Creutzfeldt-Jakob disease among Libyan Jews in Israel. Science 1976;192:428.
    • (1976) Science , vol.192 , pp. 428
    • Alter, M.1    Kahana, E.2
  • 7
    • 9544238083 scopus 로고    scopus 로고
    • Transmission dynamics and epidemiology of BSE in British cattle
    • Anderson RM, Donnelly CA, Ferguson NM, et al. Transmission dynamics and epidemiology of BSE in British cattle. Nature 1996;382:779-788.
    • (1996) Nature , vol.382 , pp. 779-788
    • Anderson, R.M.1    Donnelly, C.A.2    Ferguson, N.M.3
  • 8
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 1973;181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 9
    • 77957939093 scopus 로고    scopus 로고
    • Are synucleinopathies prion-like disorders?
    • Angot E, Steiner JA, Hansen C, et al. Are synucleinopathies prion-like disorders? Lancet Neurol 2010;9:1128-1138.
    • (2010) Lancet Neurol , vol.9 , pp. 1128-1138
    • Angot, E.1    Steiner, J.A.2    Hansen, C.3
  • 10
    • 62449203220 scopus 로고    scopus 로고
    • Crystal structure of human prion protein bound to a therapeutic antibody
    • Antonyuk SV, Trevitt CR, Strange RW, et al. Crystal structure of human prion protein bound to a therapeutic antibody. Proc Natl Acad Sci U S A 2009;106:2554-2558.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2554-2558
    • Antonyuk, S.V.1    Trevitt, C.R.2    Strange, R.W.3
  • 11
    • 77956941468 scopus 로고    scopus 로고
    • Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease
    • Apostol MI, Sawaya MR, Cascio D, et al. Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem 2010;285:29671-29675.
    • (2010) J Biol Chem , vol.285 , pp. 29671-29675
    • Apostol, M.I.1    Sawaya, M.R.2    Cascio, D.3
  • 12
    • 79953183597 scopus 로고    scopus 로고
    • Atomic structures suggest determinants of transmission barriers in mammalian prion disease
    • Apostol MI, Wiltzius JJ, Sawaya MR, et al. Atomic structures suggest determinants of transmission barriers in mammalian prion disease. Biochemistry 2011;50:2456-2463.
    • (2011) Biochemistry , vol.50 , pp. 2456-2463
    • Apostol, M.I.1    Wiltzius, J.J.2    Sawaya, M.R.3
  • 13
    • 0034649237 scopus 로고    scopus 로고
    • Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy
    • Aronoff-Spencer E, Burns CS, Avdievich NI, et al. Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochemistry 2000;39:13760-13771.
    • (2000) Biochemistry , vol.39 , pp. 13760-13771
    • Aronoff-Spencer, E.1    Burns, C.S.2    Avdievich, N.I.3
  • 14
    • 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 EA, Linehan JM, Desbruslais M, et al. BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein. EMBO J 2002;21:6358-6366.
    • (2002) EMBO J , vol.21 , pp. 6358-6366
    • Asante, E.A.1    Linehan, J.M.2    Desbruslais, M.3
  • 15
    • 79953286302 scopus 로고    scopus 로고
    • The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease
    • Ayers JI, Schutt CR, Shikiya RA, et al. The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease. PLoS Pathog 2011;7:e1001317.
    • (2011) PLoS Pathog , vol.7 , pp. e1001317
    • Ayers, J.I.1    Schutt, C.R.2    Shikiya, R.A.3
  • 16
    • 0027919287 scopus 로고
    • Experimental transmission of BSE and scrapie to the common marmoset
    • Baker HF, Ridley RM, Wells GAH. Experimental transmission of BSE and scrapie to the common marmoset. Vet Rec 1993;132:403-406.
    • (1993) Vet Rec , vol.132 , pp. 403-406
    • Baker, H.F.1    Ridley, R.M.2    Wells, G.A.H.3
  • 17
    • 0038447100 scopus 로고    scopus 로고
    • Evaluation of quinacrine treatment for prion diseases
    • Barret A, Tagliavini F, Forloni G, et al. Evaluation of quinacrine treatment for prion diseases. J Virol 2003;77:8462-8469.
    • (2003) J Virol , vol.77 , pp. 8462-8469
    • Barret, A.1    Tagliavini, F.2    Forloni, G.3
  • 18
    • 67249123069 scopus 로고    scopus 로고
    • De novo generation of infectious prions in vitro produces a new disease phenotype
    • Barria MA, Mukherjee A, Gonzalez-Romero D, et al. De novo generation of infectious prions in vitro produces a new disease phenotype. PLoS Pathog 2009;5:e1000421.
    • (2009) PLoS Pathog , vol.5 , pp. e1000421
    • Barria, M.A.1    Mukherjee, A.2    Gonzalez-Romero, D.3
  • 19
    • 80052398365 scopus 로고    scopus 로고
    • α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels T, Choi JG, Selkoe DJ. α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 2011;477:107-110.
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 20
    • 0023888782 scopus 로고
    • Scrapie prion liposomes and rods exhibit target sizes of 55,000 Da
    • Bellinger-Kawahara CG, Kempner E, Groth DF, et al. Scrapie prion liposomes and rods exhibit target sizes of 55,000 Da. Virology 1988;164:537-541.
    • (1988) Virology , vol.164 , pp. 537-541
    • Bellinger-Kawahara, C.G.1    Kempner, E.2    Groth, D.F.3
  • 21
    • 0037813125 scopus 로고    scopus 로고
    • Improved conformation-dependent immunoassay: suitability for human prion detection with enhanced sensitivity
    • Bellon A, Seyfert-Brandt W, Lang W, et al. Improved conformation-dependent immunoassay: suitability for human prion detection with enhanced sensitivity. J Gen Virol 2003;84:1921-1925.
    • (2003) J Gen Virol , vol.84 , pp. 1921-1925
    • Bellon, A.1    Seyfert-Brandt, W.2    Lang, W.3
  • 22
    • 44649141265 scopus 로고    scopus 로고
    • The key-role of tyrosine 155 in the mechanism of prion transconformation as highlighted by a study of sheep mutant peptides
    • Bertho G, Bouvier G, Hoa GH, et al. The key-role of tyrosine 155 in the mechanism of prion transconformation as highlighted by a study of sheep mutant peptides. Peptides 2008;29:1073-1084.
    • (2008) Peptides , vol.29 , pp. 1073-1084
    • Bertho, G.1    Bouvier, G.2    Hoa, G.H.3
  • 23
    • 0028997297 scopus 로고
    • Non-genetic propagation of strain-specific properties of scrapie prion protein
    • Bessen RA, Kocisko DA, Raymond GJ, et al. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 1995;375:698-700.
    • (1995) Nature , vol.375 , pp. 698-700
    • Bessen, R.A.1    Kocisko, D.A.2    Raymond, G.J.3
  • 24
    • 0026583834 scopus 로고
    • Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent
    • Bessen RA, Marsh RF. Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 1992;66:2096-2101.
    • (1992) J Virol , vol.66 , pp. 2096-2101
    • Bessen, R.A.1    Marsh, R.F.2
  • 25
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen RA, Marsh RF. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 1994;68:7859-7868.
    • (1994) J Virol , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 26
    • 0026558780 scopus 로고
    • Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters
    • Bessen RA, Marsh RF. Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters. J Gen Virol 1992;73:329-334.
    • (1992) J Gen Virol , vol.73 , pp. 329-334
    • Bessen, R.A.1    Marsh, R.F.2
  • 27
    • 84860389727 scopus 로고    scopus 로고
    • Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation
    • Biljan I, Ilc G, Giachin G, et al. Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation. J Mol Biol 2011;412:660-673.
    • (2011) J Mol Biol , vol.412 , pp. 660-673
    • Biljan, I.1    Ilc, G.2    Giachin, G.3
  • 28
    • 9744245200 scopus 로고    scopus 로고
    • NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein
    • Biverstahl H, Andersson A, Graslund A, et al. NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein. Biochemistry 2004;43:14940-14947.
    • (2004) Biochemistry , vol.43 , pp. 14940-14947
    • Biverstahl, H.1    Andersson, A.2    Graslund, A.3
  • 29
    • 0025304678 scopus 로고
    • Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells
    • Borchelt DR, Scott M, Taraboulos A, et al. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J Cell Biol 1990;110:743-752.
    • (1990) J Cell Biol , vol.110 , pp. 743-752
    • Borchelt, D.R.1    Scott, M.2    Taraboulos, A.3
  • 31
    • 0035156642 scopus 로고    scopus 로고
    • Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
    • Bousset L, Belrhali H, Janin J, et al. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 2001;9:39-46.
    • (2001) Structure , vol.9 , pp. 39-46
    • Bousset, L.1    Belrhali, H.2    Janin, J.3
  • 32
    • 0035856522 scopus 로고    scopus 로고
    • Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds
    • Bousset L, Belrhali H, Melki R, et al. Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Biochemistry 2001;40:13564-13573.
    • (2001) Biochemistry , vol.40 , pp. 13564-13573
    • Bousset, L.1    Belrhali, H.2    Melki, R.3
  • 33
    • 3843142665 scopus 로고    scopus 로고
    • The neurodegeneration sequence in prion diseases: Evidence from functional, morphological and ultrastructural studies of the GABAergic system
    • Bouzamondo-Bernstein E, Hopkins SD, Spilman P, et al. The neurodegeneration sequence in prion diseases: Evidence from functional, morphological and ultrastructural studies of the GABAergic system. J Neuropathol Exp Neurol 2004;63:882-899.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 882-899
    • Bouzamondo-Bernstein, E.1    Hopkins, S.D.2    Spilman, P.3
  • 34
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimer-related changes
    • Braak H, Braak E. Neuropathological staging of Alzheimer-related changes. Acta Neuropathol (Berl) 1991;82:239-259.
    • (1991) Acta Neuropathol (Berl) , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 35
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • Braak H, Braak E. Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol Aging 1995;16:271-284.
    • (1995) Neurobiol Aging , vol.16 , pp. 271-284
    • Braak, H.1    Braak, E.2
  • 36
    • 43649106356 scopus 로고    scopus 로고
    • Invited Article: Nervous system pathology in sporadic Parkinson disease
    • Braak H, Del Tredici K. Invited Article: Nervous system pathology in sporadic Parkinson disease. Neurology 2008;70:1916-1925.
    • (2008) Neurology , vol.70 , pp. 1916-1925
    • Braak, H.1    Del Tredici, K.2
  • 37
    • 0030054010 scopus 로고    scopus 로고
    • Normal host prion protein necessary for scrapie-induced neurotoxicity
    • Brandner S, Isenmann S, Raeber A, et al. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 1996;379:339-343.
    • (1996) Nature , vol.379 , pp. 339-343
    • Brandner, S.1    Isenmann, S.2    Raeber, A.3
  • 38
    • 0021909302 scopus 로고
    • Neurofibrillary tangles of Alzheimer's disease: an immunohistochemical study
    • Brion JP, Couck AM, Passareiro E, et al. Neurofibrillary tangles of Alzheimer's disease: an immunohistochemical study. J Submicrosc Cytol 1985;17:89-96.
    • (1985) J Submicrosc Cytol , vol.17 , pp. 89-96
    • Brion, J.P.1    Couck, A.M.2    Passareiro, E.3
  • 39
    • 23844471279 scopus 로고    scopus 로고
    • Blood infectivity, processing and screening tests in transmissible spongiform encephalopathy
    • Brown P. Blood infectivity, processing and screening tests in transmissible spongiform encephalopathy. Vox Sang 2005;89:63-70.
    • (2005) Vox Sang , vol.89 , pp. 63-70
    • Brown, P.1
  • 40
    • 8644260825 scopus 로고    scopus 로고
    • Transmission of prions from mule deer and elk with chronic wasting disease to transgenic mice expressing cervid PrP
    • Browning SR, Mason GL, Seward T, et al. Transmission of prions from mule deer and elk with chronic wasting disease to transgenic mice expressing cervid PrP. J Virol 2004;78:13345-13350.
    • (2004) J Virol , vol.78 , pp. 13345-13350
    • Browning, S.R.1    Mason, G.L.2    Seward, T.3
  • 41
    • 0023205075 scopus 로고
    • Biological evidence that the scrapie agent has an independent genome
    • Bruce ME, Dickinson AG. Biological evidence that the scrapie agent has an independent genome. J Gen Virol 1987;68:79-89.
    • (1987) J Gen Virol , vol.68 , pp. 79-89
    • Bruce, M.E.1    Dickinson, A.G.2
  • 42
    • 0021846543 scopus 로고
    • Genetic control of amyloid plaque production and incubation period in scrapie-infected mice
    • Bruce ME, Dickinson AG. Genetic control of amyloid plaque production and incubation period in scrapie-infected mice. J Neuropathol Exp Neurol 1985;44:285-294.
    • (1985) J Neuropathol Exp Neurol , vol.44 , pp. 285-294
    • Bruce, M.E.1    Dickinson, A.G.2
  • 43
    • 0030775632 scopus 로고    scopus 로고
    • Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent
    • Bruce ME, Will RG, Ironside JW, et al. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature 1997;389:498-501.
    • (1997) Nature , vol.389 , pp. 498-501
    • Bruce, M.E.1    Will, R.G.2    Ironside, J.W.3
  • 44
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 2010;11:301-307.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 45
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Büeler H, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993;73:1339-1347.
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Büeler, H.1    Aguzzi, A.2    Sailer, A.3
  • 46
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Büeler H, Fisher M, Lang Y, et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992;356:577-582.
    • (1992) Nature , vol.356 , pp. 577-582
    • Büeler, H.1    Fisher, M.2    Lang, Y.3
  • 47
    • 0028535880 scopus 로고
    • High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene
    • Büeler H, Raeber A, Sailer A, et al. High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Mol Med 1994;1:19-30.
    • (1994) Mol Med , vol.1 , pp. 19-30
    • Büeler, H.1    Raeber, A.2    Sailer, A.3
  • 48
    • 18344369706 scopus 로고    scopus 로고
    • Molecular features of the copper binding sites in the octarepeat domain of the prion protein
    • Burns CS, Aronoff-Spencer E, Dunham CM, et al. Molecular features of the copper binding sites in the octarepeat domain of the prion protein. Biochemistry 2002;41:3991-4001.
    • (2002) Biochemistry , vol.41 , pp. 3991-4001
    • Burns, C.S.1    Aronoff-Spencer, E.2    Dunham, C.M.3
  • 49
    • 28444450920 scopus 로고    scopus 로고
    • Detection of cattle-derived BSE prions using transgenic mice overexpressing bovine PrPC
    • Buschmann A, Pfaff E, Reifenberg K, et al. Detection of cattle-derived BSE prions using transgenic mice overexpressing bovine PrPC. Arch Virol Suppl 2000;16:75-86.
    • (2000) Arch Virol Suppl , vol.16 , pp. 75-86
    • Buschmann, A.1    Pfaff, E.2    Reifenberg, K.3
  • 50
    • 0034682489 scopus 로고    scopus 로고
    • NMR structures of three single-residue variants of the human prion protein
    • Calzolai L, Lysek DA, Güntert P, et al. NMR structures of three single-residue variants of the human prion protein. Proc Natl Acad Sci U S A 2000;97:8340-8345.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8340-8345
    • Calzolai, L.1    Lysek, D.A.2    Güntert, P.3
  • 51
    • 14144253010 scopus 로고    scopus 로고
    • Prion protein NMR structures of chickens, turtles, and frogs
    • Calzolai L, Lysek DA, Perez DR, et al. Prion protein NMR structures of chickens, turtles, and frogs. Proc Natl Acad Sci U S A 2005;102:651-655.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 651-655
    • Calzolai, L.1    Lysek, D.A.2    Perez, D.R.3
  • 52
    • 0041315527 scopus 로고    scopus 로고
    • Influence of pH on NMR structure and stability of the human prion protein globular domain
    • Calzolai L, Zahn R. Influence of pH on NMR structure and stability of the human prion protein globular domain. J Biol Chem 2003;278:35592-35596.
    • (2003) J Biol Chem , vol.278 , pp. 35592-35596
    • Calzolai, L.1    Zahn, R.2
  • 53
    • 0028276015 scopus 로고
    • Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice
    • Carlson GA, Ebeling C, Yang S-L, et al. Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice. Proc Natl Acad Sci U S A 1994;91:5690-5694.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 5690-5694
    • Carlson, G.A.1    Ebeling, C.2    Yang, S.-L.3
  • 54
    • 0022530549 scopus 로고
    • Linkage of prion protein and scrapie incubation time genes
    • Carlson GA, Kingsbury DT, Goodman PA, et al. Linkage of prion protein and scrapie incubation time genes. Cell 1986;46:503-511.
    • (1986) Cell , vol.46 , pp. 503-511
    • Carlson, G.A.1    Kingsbury, D.T.2    Goodman, P.A.3
  • 55
    • 50249157526 scopus 로고    scopus 로고
    • Crossing the species barrier by PrPSc replication in vitro generates unique infectious prions
    • Castilla J, Gonzalez-Romero D, Saa P, et al. Crossing the species barrier by PrPSc replication in vitro generates unique infectious prions. Cell 2008;134:757-768.
    • (2008) Cell , vol.134 , pp. 757-768
    • Castilla, J.1    Gonzalez-Romero, D.2    Saa, P.3
  • 56
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J, Saa P, Hetz C, et al. In vitro generation of infectious scrapie prions. Cell 2005;121:195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3
  • 57
    • 0015367453 scopus 로고
    • Amyloid-inducing factor and immunological unresponsiveness
    • Cathcart ES, Rodgers OG, Cohen AS. Amyloid-inducing factor and immunological unresponsiveness. Ann Rheum Dis 1972;31:303-307.
    • (1972) Ann Rheum Dis , vol.31 , pp. 303-307
    • Cathcart, E.S.1    Rodgers, O.G.2    Cohen, A.S.3
  • 58
    • 0029583794 scopus 로고
    • Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state
    • Caughey B, Kocisko DA, Raymond GJ, et al. Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem Biol 1995;2:807-817.
    • (1995) Chem Biol , vol.2 , pp. 807-817
    • Caughey, B.1    Kocisko, D.A.2    Raymond, G.J.3
  • 59
    • 0026638150 scopus 로고
    • Potent inhibition of scrapie-associated PrP accumulation by Congo red
    • Caughey B, Race RE. Potent inhibition of scrapie-associated PrP accumulation by Congo red. J Neurochem 1992;59:768-771.
    • (1992) J Neurochem , vol.59 , pp. 768-771
    • Caughey, B.1    Race, R.E.2
  • 60
    • 0024545093 scopus 로고
    • Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells
    • Caughey B, Race RE, Ernst D, et al. Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells. J Virol 1989;63:175-181.
    • (1989) J Virol , vol.63 , pp. 175-181
    • Caughey, B.1    Race, R.E.2    Ernst, D.3
  • 61
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-and phospholipase-sensitive
    • Caughey B, Raymond GJ. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-and phospholipase-sensitive. J Biol Chem 1991;266:18217-18223.
    • (1991) J Biol Chem , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 62
    • 0030944992 scopus 로고    scopus 로고
    • Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies
    • Caughey B, Raymond GJ, Kocisko DA, et al. Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies. J Virol 1997;71:4107-4110.
    • (1997) J Virol , vol.71 , pp. 4107-4110
    • Caughey, B.1    Raymond, G.J.2    Kocisko, D.A.3
  • 63
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey BW, Dong A, Bhat KS, et al. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 1991;30:7672-7680.
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3
  • 64
    • 0030576389 scopus 로고    scopus 로고
    • Surveillance for Creutzfeldt-Jakob Disease-United States
    • Centers for Disease Control. Surveillance for Creutzfeldt-Jakob Disease-United States. MMWR Morb Mortal Wkly Rep 1996;45:665-668.
    • (1996) MMWR Morb Mortal Wkly Rep , vol.45 , pp. 665-668
  • 65
    • 0028145428 scopus 로고
    • The risk of developing Creutzfeldt-Jakob disease in subjects with the PRNP gene codon 200 point mutation
    • Chapman J, Ben-Israel J, Goldhammer Y, et al. The risk of developing Creutzfeldt-Jakob disease in subjects with the PRNP gene codon 200 point mutation. Neurology 1994;44:1683-1686.
    • (1994) Neurology , vol.44 , pp. 1683-1686
    • Chapman, J.1    Ben-Israel, J.2    Goldhammer, Y.3
  • 66
    • 0345505687 scopus 로고    scopus 로고
    • Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival
    • Chen S, Mange A, Dong L, et al. Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival. Mol Cell Neurosci 2003;22:227-233.
    • (2003) Mol Cell Neurosci , vol.22 , pp. 227-233
    • Chen, S.1    Mange, A.2    Dong, L.3
  • 67
    • 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, Race B, Meade-White K, et al. Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring. PLoS Pathog 2010;6:e1000800.
    • (2010) PLoS Pathog , vol.6 , pp. e1000800
    • Chesebro, B.1    Race, B.2    Meade-White, K.3
  • 68
    • 0021884354 scopus 로고
    • Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain
    • Chesebro B, Race R, Wehrly K, et al. Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain. Nature 1985;315:331-333.
    • (1985) Nature , vol.315 , pp. 331-333
    • Chesebro, B.1    Race, R.2    Wehrly, K.3
  • 69
    • 20344394154 scopus 로고    scopus 로고
    • Anchorless prion protein results in infectious amyloid disease without clinical scrapie
    • Chesebro B, Trifilo M, Race R, et al. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 2005;308:1435-1439.
    • (2005) Science , vol.308 , pp. 1435-1439
    • Chesebro, B.1    Trifilo, M.2    Race, R.3
  • 70
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien P, Weissman JS, DePace AH. Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 2004;73:617-656.
    • (2004) Annu Rev Biochem , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 71
    • 0038128629 scopus 로고    scopus 로고
    • Molecular distinction between pathogenic and infectious properties of the prion protein
    • Chiesa R, Piccardo P, Quaglio E, et al. Molecular distinction between pathogenic and infectious properties of the prion protein. J Virol 2003;77:7611-7622.
    • (2003) J Virol , vol.77 , pp. 7611-7622
    • Chiesa, R.1    Piccardo, P.2    Quaglio, E.3
  • 72
    • 67349152665 scopus 로고    scopus 로고
    • Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects
    • Christen B, Hornemann S, Damberger FF, et al. Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects. J Mol Biol 2009;389:833-845.
    • (2009) J Mol Biol , vol.389 , pp. 833-845
    • Christen, B.1    Hornemann, S.2    Damberger, F.F.3
  • 73
    • 52949137870 scopus 로고    scopus 로고
    • NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171
    • Christen B, Perez DR, Hornemann S, et al. NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171. J Mol Biol 2008;383:306-312.
    • (2008) J Mol Biol , vol.383 , pp. 306-312
    • Christen, B.1    Perez, D.R.2    Hornemann, S.3
  • 74
    • 80052821738 scopus 로고    scopus 로고
    • Styryl-based and tricyclic compounds as potential anti-prion agents
    • Chung E, Prelli F, Dealler S, et al. Styryl-based and tricyclic compounds as potential anti-prion agents. PLoS One 2011;6:e24844.
    • (2011) PLoS One , vol.6 , pp. e24844
    • Chung, E.1    Prelli, F.2    Dealler, S.3
  • 75
    • 67650077008 scopus 로고    scopus 로고
    • Transmission and spreading of tauopathy in transgenic mouse brain
    • Clavaguera F, Bolmont T, Crowther RA, et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat Cell Biol 2009;11:909-913.
    • (2009) Nat Cell Biol , vol.11 , pp. 909-913
    • Clavaguera, F.1    Bolmont, T.2    Crowther, R.A.3
  • 76
    • 0029161777 scopus 로고
    • Different allelic effects of the codons 136 and 171 of the prion protein gene in sheep with natural scrapie
    • Clousard C, Beaudry P, Elsen JM, et al. Different allelic effects of the codons 136 and 171 of the prion protein gene in sheep with natural scrapie. J Gen Virol 1995;76:2097-2101.
    • (1995) J Gen Virol , vol.76 , pp. 2097-2101
    • Clousard, C.1    Beaudry, P.2    Elsen, J.M.3
  • 77
    • 73949160065 scopus 로고    scopus 로고
    • Design and construction of diverse mammalian prion strains
    • Colby DW, Giles K, Legname G, et al. Design and construction of diverse mammalian prion strains. Proc Natl Acad Sci U S A 2009;106:20417-20422.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20417-20422
    • Colby, D.W.1    Giles, K.2    Legname, G.3
  • 79
    • 77649214076 scopus 로고    scopus 로고
    • Protease-sensitive synthetic prions
    • Colby DW, Wain R, Baskakov IV, et al. Protease-sensitive synthetic prions. PLoS Pathog 2010;6:e1000736.
    • (2010) PLoS Pathog , vol.6 , pp. e1000736
    • Colby, D.W.1    Wain, R.2    Baskakov, I.V.3
  • 80
    • 62149105940 scopus 로고    scopus 로고
    • Safety and efficacy of quinacrine in human prion disease (PRION-1 study): a patient-preference trial
    • Collinge J, Gorham M, Hudson F, et al. Safety and efficacy of quinacrine in human prion disease (PRION-1 study): a patient-preference trial. Lancet Neurol 2009;8:334-344.
    • (2009) Lancet Neurol , vol.8 , pp. 334-344
    • Collinge, J.1    Gorham, M.2    Hudson, F.3
  • 81
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of "new variant" CJD
    • Collinge J, Sidle KCL, Meads J, et al. Molecular analysis of prion strain variation and the aetiology of "new variant" CJD. Nature 1996;383:685-690.
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.L.2    Meads, J.3
  • 82
    • 0036791880 scopus 로고    scopus 로고
    • Quinacrine does not prolong survival in a murine Creutzfeldt-Jakob disease model
    • Collins SJ, Lewis V, Brazier M, et al. Quinacrine does not prolong survival in a murine Creutzfeldt-Jakob disease model. Ann Neurol 2002;52:503-506.
    • (2002) Ann Neurol , vol.52 , pp. 503-506
    • Collins, S.J.1    Lewis, V.2    Brazier, M.3
  • 84
    • 0345923010 scopus 로고
    • Posttraumatic dementia
    • Corsellis JAN. Posttraumatic dementia. Aging 1978;7:125-133.
    • (1978) Aging , vol.7 , pp. 125-133
    • Corsellis, J.A.N.1
  • 85
    • 0014208039 scopus 로고
    • Aromatic amino acids and modification of parkinsonism
    • Cotzias GC, Van Woert MH, Schiffer LM. Aromatic amino acids and modification of parkinsonism. N Engl J Med 1967;276:374-379.
    • (1967) N Engl J Med , vol.276 , pp. 374-379
    • Cotzias, G.C.1    Van Woert, M.H.2    Schiffer, L.M.3
  • 86
    • 0025302625 scopus 로고
    • Geographical distribution of cases of Creutzfeldt-Jakob disease in England and Wales 1970-84
    • Cousens SN, Harries-Jones R, Knight R, et al. Geographical distribution of cases of Creutzfeldt-Jakob disease in England and Wales 1970-84. J Neurol Neurosurg Psychiatry 1990;53:459-465.
    • (1990) J Neurol Neurosurg Psychiatry , vol.53 , pp. 459-465
    • Cousens, S.N.1    Harries-Jones, R.2    Knight, R.3
  • 87
    • 20244371991 scopus 로고    scopus 로고
    • Mice devoid of prion protein have cognitive deficits that are rescued by reconstitution of PrP in neurons
    • Criado JR, Sanchez-Alavez M, Conti B, et al. Mice devoid of prion protein have cognitive deficits that are rescued by reconstitution of PrP in neurons. Neurobiol Dis 2005;19:255-265.
    • (2005) Neurobiol Dis , vol.19 , pp. 255-265
    • Criado, J.R.1    Sanchez-Alavez, M.2    Conti, B.3
  • 88
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: blurring the divide between transmissibility and infectivity
    • Cushman M, Johnson BS, King OD, et al. Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 2010;123:1191-1201.
    • (2010) J Cell Sci , vol.123 , pp. 1191-1201
    • Cushman, M.1    Johnson, B.S.2    King, O.D.3
  • 89
    • 0030896803 scopus 로고    scopus 로고
    • Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells
    • Daude N, Lehmann S, Harris DA. Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J Biol Chem 1997;272:11604-11612.
    • (1997) J Biol Chem , vol.272 , pp. 11604-11612
    • Daude, N.1    Lehmann, S.2    Harris, D.A.3
  • 90
    • 10844250483 scopus 로고    scopus 로고
    • Neuropathology of prion diseases
    • Prusiner SB, ed, 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • DeArmond SJ, Ironside JW, Bouzamondo-Bernstein E, et al. Neuropathology of prion diseases. In: Prusiner SB, ed. Prion Biology and Diseases. 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; 2004:777-856.
    • (2004) Prion Biology and Diseases , pp. 777-856
    • DeArmond, S.J.1    Ironside, J.W.2    Bouzamondo-Bernstein, E.3
  • 92
    • 0021879270 scopus 로고
    • Identification of prion amyloid filaments in scrapie-infected brain
    • DeArmond SJ, McKinley MP, Barry RA, et al. Identification of prion amyloid filaments in scrapie-infected brain. Cell 1985;41:221-235.
    • (1985) Cell , vol.41 , pp. 221-235
    • DeArmond, S.J.1    McKinley, M.P.2    Barry, R.A.3
  • 93
    • 34547491652 scopus 로고    scopus 로고
    • Formation of native prions from minimal components in vitro
    • Deleault NR, Harris BT, Rees JR, et al. Formation of native prions from minimal components in vitro. Proc Natl Acad Sci U S A 2007;104:9741-9746.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9741-9746
    • Deleault, N.R.1    Harris, B.T.2    Rees, J.R.3
  • 94
    • 77951923337 scopus 로고    scopus 로고
    • Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro
    • Deleault NR, Kascsak R, Geoghegan JC, et al. Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro. Biochemistry 2010;49:3928-3934.
    • (2010) Biochemistry , vol.49 , pp. 3928-3934
    • Deleault, N.R.1    Kascsak, R.2    Geoghegan, J.C.3
  • 95
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein
    • Desplats P, Lee HJ, Bae EJ, et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci U S A 2009;106:13010-13015.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.J.3
  • 96
    • 77955598977 scopus 로고    scopus 로고
    • Generation of prions in vitro and the protein-only hypothesis
    • Diaz-Espinoza R, Soto C. Generation of prions in vitro and the protein-only hypothesis. Prion 2010;4:1-7.
    • (2010) Prion , vol.4 , pp. 1-7
    • Diaz-Espinoza, R.1    Soto, C.2
  • 97
    • 0015518449 scopus 로고
    • Competition between different scrapie agents in mice
    • Dickinson AG, Fraser H, Meikle VMH, et al. Competition between different scrapie agents in mice. Nat New Biol 1972;237:244-245.
    • (1972) Nat New Biol , vol.237 , pp. 244-245
    • Dickinson, A.G.1    Fraser, H.2    Meikle, V.M.H.3
  • 98
    • 0014305661 scopus 로고
    • Identification of a gene which controls the incubation period of some strains of scrapie agent in mice
    • Dickinson AG, Meikle VMH, Fraser H. Identification of a gene which controls the incubation period of some strains of scrapie agent in mice. J Comp Pathol 1968;78:293-299.
    • (1968) J Comp Pathol , vol.78 , pp. 293-299
    • Dickinson, A.G.1    Meikle, V.M.H.2    Fraser, H.3
  • 99
    • 0013815614 scopus 로고
    • An analysis of natural scrapie in Suffolk sheep
    • Dickinson AG, Young GB, Stamp JT, et al. An analysis of natural scrapie in Suffolk sheep. Heredity 1965;20:485-503.
    • (1965) Heredity , vol.20 , pp. 485-503
    • Dickinson, A.G.1    Young, G.B.2    Stamp, J.T.3
  • 101
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation
    • Doh-ura K, Iwaki T, Caughey B. Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation. J Virol 2000;74:4894-4897.
    • (2000) J Virol , vol.74 , pp. 4894-4897
    • Doh-ura, K.1    Iwaki, T.2    Caughey, B.3
  • 102
    • 0031456947 scopus 로고    scopus 로고
    • Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible
    • Donne DG, Viles JH, Groth D, et al. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc Natl Acad Sci U S A 1997;94:13452-13457.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13452-13457
    • Donne, D.G.1    Viles, J.H.2    Groth, D.3
  • 103
    • 79551681376 scopus 로고    scopus 로고
    • Detection of prion infection in variant Creutzfeldt-Jakob disease: a blood-based assay
    • Edgeworth JA, Farmer M, Sicilia A, et al. Detection of prion infection in variant Creutzfeldt-Jakob disease: a blood-based assay. Lancet 2011;377:487-493.
    • (2011) Lancet , vol.377 , pp. 487-493
    • Edgeworth, J.A.1    Farmer, M.2    Sicilia, A.3
  • 104
    • 3142683624 scopus 로고    scopus 로고
    • Insight into the PrPC->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants
    • Eghiaian F, Grosclaude J, Lesceu S, et al. Insight into the PrPC->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants. Proc Natl Acad Sci U S A 2004;101:10254-10259.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10254-10259
    • Eghiaian, F.1    Grosclaude, J.2    Lesceu, S.3
  • 105
    • 0035979274 scopus 로고    scopus 로고
    • Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody
    • Enari M, Flechsig E, Weissmann C. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc Natl Acad Sci U S A 2001;98:9295-9299.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9295-9299
    • Enari, M.1    Flechsig, E.2    Weissmann, C.3
  • 106
    • 0024434503 scopus 로고
    • Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein
    • Endo T, Groth D, Prusiner SB, et al. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 1989;28:8380-8388.
    • (1989) Biochemistry , vol.28 , pp. 8380-8388
    • Endo, T.1    Groth, D.2    Prusiner, S.B.3
  • 107
    • 17044361848 scopus 로고    scopus 로고
    • Variation in concentration of prion protein in the peripheral blood of patients with variant and sporadic Creutzfeldt-Jakob disease detected by dissociation enhanced lanthanide fluoroimmunoassay and flow cytometry
    • Fagge T, Barclay GR, Macgregor I, et al. Variation in concentration of prion protein in the peripheral blood of patients with variant and sporadic Creutzfeldt-Jakob disease detected by dissociation enhanced lanthanide fluoroimmunoassay and flow cytometry. Transfusion 2005;45:504-513.
    • (2005) Transfusion , vol.45 , pp. 504-513
    • Fagge, T.1    Barclay, G.R.2    Macgregor, I.3
  • 108
    • 4043153397 scopus 로고    scopus 로고
    • Novel methods for disinfection of prion-contaminated medical devices
    • Fichet G, Comoy E, Duval C, et al. Novel methods for disinfection of prion-contaminated medical devices. Lancet 2004;364:521-526.
    • (2004) Lancet , vol.364 , pp. 521-526
    • Fichet, G.1    Comoy, E.2    Duval, C.3
  • 109
    • 0028287867 scopus 로고
    • Detecting prion protein gene mutations by denaturing gradient gel electrophoresis
    • Fink JK, Peacock ML, Warren JT, et al. Detecting prion protein gene mutations by denaturing gradient gel electrophoresis. Hum Mutat 1994;4:42-50.
    • (1994) Hum Mutat , vol.4 , pp. 42-50
    • Fink, J.K.1    Peacock, M.L.2    Warren, J.T.3
  • 110
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer M, Rülicke T, Raeber A, et al. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J 1996;15:1255-1264.
    • (1996) EMBO J , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rülicke, T.2    Raeber, A.3
  • 111
    • 5644262484 scopus 로고
    • The temperature of cavitation
    • Flint EB, Suslick KS. The temperature of cavitation. Science 1991;253:1397-1399.
    • (1991) Science , vol.253 , pp. 1397-1399
    • Flint, E.B.1    Suslick, K.S.2
  • 112
    • 0027483615 scopus 로고
    • Neurotoxicity of a prion protein fragment
    • Forloni G, Angeretti N, Chiesa R, et al. Neurotoxicity of a prion protein fragment. Nature 1993;362:543-546.
    • (1993) Nature , vol.362 , pp. 543-546
    • Forloni, G.1    Angeretti, N.2    Chiesa, R.3
  • 113
    • 0035149502 scopus 로고    scopus 로고
    • Partial dissociation of PrPSc deposition and vacuolation in the brains of scrapie and BSE experimentally affected goats
    • Foster J, Goldmann W, Parnham D, et al. Partial dissociation of PrPSc deposition and vacuolation in the brains of scrapie and BSE experimentally affected goats. J Gen Virol 2001;82:267-273.
    • (2001) J Gen Virol , vol.82 , pp. 267-273
    • Foster, J.1    Goldmann, W.2    Parnham, D.3
  • 114
    • 0026801020 scopus 로고
    • Transmission of bovine spongiform encephalopathy and scrapie to mice
    • Fraser H, Bruce ME, Chree A, et al. Transmission of bovine spongiform encephalopathy and scrapie to mice. J Gen Virol 1992;73:1891-1897.
    • (1992) J Gen Virol , vol.73 , pp. 1891-1897
    • Fraser, H.1    Bruce, M.E.2    Chree, A.3
  • 115
    • 0015550206 scopus 로고
    • Scrapie in mice. Agent-strain differences in the distribution and intensity of grey matter vacuolation
    • Fraser H, Dickinson AG. Scrapie in mice. Agent-strain differences in the distribution and intensity of grey matter vacuolation. J Comp Pathol 1973;83:29-40.
    • (1973) J Comp Pathol , vol.83 , pp. 29-40
    • Fraser, H.1    Dickinson, A.G.2
  • 116
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 2009;284:12845-12852.
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 117
    • 65549100291 scopus 로고    scopus 로고
    • Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases
    • Furukawa Y, Kaneko K, Matsumoto G, et al. Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases. J Neurosci 2009;29:5153-5162.
    • (2009) J Neurosci , vol.29 , pp. 5153-5162
    • Furukawa, Y.1    Kaneko, K.2    Matsumoto, G.3
  • 118
    • 0003279877 scopus 로고
    • Immunoaffinity purification and neutralization of scrapie prion infectivity
    • Gabizon R, McKinley MP, Groth D, et al. Immunoaffinity purification and neutralization of scrapie prion infectivity. Proc Natl Acad Sci U S A 1988;85:6617-6621.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 6617-6621
    • Gabizon, R.1    McKinley, M.P.2    Groth, D.3
  • 119
    • 0027373649 scopus 로고
    • Mutation and polymorphism of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease (CJD)
    • Gabizon R, Rosenmann H, Meiner Z, et al. Mutation and polymorphism of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease (CJD). Am J Hum Genet 1993;53:828-835.
    • (1993) Am J Hum Genet , vol.53 , pp. 828-835
    • Gabizon, R.1    Rosenmann, H.2    Meiner, Z.3
  • 120
    • 0017643758 scopus 로고
    • Unconventional viruses and the origin and disappearance of kuru
    • Gajdusek DC. Unconventional viruses and the origin and disappearance of kuru. Science 1977;197:943-960.
    • (1977) Science , vol.197 , pp. 943-960
    • Gajdusek, D.C.1
  • 121
    • 46749121818 scopus 로고    scopus 로고
    • A novel human disease with abnormal prion protein sensitive to protease
    • Gambetti P, Dong Z, Yuan J, et al. A novel human disease with abnormal prion protein sensitive to protease. Ann Neurol 2008;63:697-708.
    • (2008) Ann Neurol , vol.63 , pp. 697-708
    • Gambetti, P.1    Dong, Z.2    Yuan, J.3
  • 122
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
    • Games D, Adams D, Alessandrini R, et al. Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature 1995;373:523-527.
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 123
    • 0027388993 scopus 로고
    • Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
    • Gasset M, Baldwin MA, Fletterick RJ, et al. Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc Natl Acad Sci U S A 1993;90:1-5.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 1-5
    • Gasset, M.1    Baldwin, M.A.2    Fletterick, R.J.3
  • 124
    • 14644389457 scopus 로고    scopus 로고
    • A possible pharmacological explanation for quinacrine failure to treat prion diseases: pharmacokinetic investigations in a ovine model of scrapie
    • Gayrard V, Picard-Hagen N, Viguie C, et al. A possible pharmacological explanation for quinacrine failure to treat prion diseases: pharmacokinetic investigations in a ovine model of scrapie. Br J Pharmacol 2005;144:386-393.
    • (2005) Br J Pharmacol , vol.144 , pp. 386-393
    • Gayrard, V.1    Picard-Hagen, N.2    Viguie, C.3
  • 125
    • 0037709838 scopus 로고    scopus 로고
    • Challenging the clinical utility of the 14-3-3 protein for the diagnosis of sporadic Creutzfeldt-Jakob disease
    • Geschwind MD, Martindale J, Miller D, et al. Challenging the clinical utility of the 14-3-3 protein for the diagnosis of sporadic Creutzfeldt-Jakob disease. Arch Neurol 2003;60:813-816.
    • (2003) Arch Neurol , vol.60 , pp. 813-816
    • Geschwind, M.D.1    Martindale, J.2    Miller, D.3
  • 126
    • 72649091794 scopus 로고    scopus 로고
    • Continuous quinacrine treatment results in the formation of drug-resistant prions
    • Ghaemmaghami S, Ahn M, Lessard P, et al. Continuous quinacrine treatment results in the formation of drug-resistant prions. PLoS Pathog 2009;5:e1000673.
    • (2009) PLoS Pathog , vol.5 , pp. e1000673
    • Ghaemmaghami, S.1    Ahn, M.2    Lessard, P.3
  • 127
    • 77949357105 scopus 로고    scopus 로고
    • Discovery of 2-aminothiazoles as potent antiprion compounds
    • Ghaemmaghami S, May BCH, Renslo AR, et al. Discovery of 2-aminothiazoles as potent antiprion compounds. J Virol 2010;84:3408-3412.
    • (2010) J Virol , vol.84 , pp. 3408-3412
    • Ghaemmaghami, S.1    May, B.C.H.2    Renslo, A.R.3
  • 128
    • 77951237722 scopus 로고    scopus 로고
    • Chemical induction of misfolded prion protein conformers in cell culture
    • Ghaemmaghami S, Ullman J, Ahn M, et al. Chemical induction of misfolded prion protein conformers in cell culture. J Biol Chem 2010;285:10415-10423.
    • (2010) J Biol Chem , vol.285 , pp. 10415-10423
    • Ghaemmaghami, S.1    Ullman, J.2    Ahn, M.3
  • 129
    • 80054685349 scopus 로고    scopus 로고
    • Conformational transformation and selection of synthetic prion strains
    • Ghaemmaghami S, Watts JC, Nguyen H-O, et al. Conformational transformation and selection of synthetic prion strains. J Mol Biol 2011;413:527-542.
    • (2011) J Mol Biol , vol.413 , pp. 527-542
    • Ghaemmaghami, S.1    Watts, J.C.2    Nguyen, H.-O.3
  • 130
    • 0034632711 scopus 로고    scopus 로고
    • Predicted vCJD mortality in Great Britain
    • Ghani AC, Ferguson NM, Donnelly CA, et al. Predicted vCJD mortality in Great Britain. Nature 2000;406:583-584.
    • (2000) Nature , vol.406 , pp. 583-584
    • Ghani, A.C.1    Ferguson, N.M.2    Donnelly, C.A.3
  • 131
    • 84855498241 scopus 로고    scopus 로고
    • Hereditary prion protein amyloidosis
    • Brown DR, ed, New York: Springer Science+Business Media, Inc.
    • Ghetti B, Piccardo P, Bugiani O, et al. Hereditary prion protein amyloidosis. In: Brown DR, ed. Neurodegeneration and Prion Disease. New York: Springer Science+Business Media, Inc.; 2005:83-109.
    • (2005) Neurodegeneration and Prion Disease , pp. 83-109
    • Ghetti, B.1    Piccardo, P.2    Bugiani, O.3
  • 132
    • 0037118259 scopus 로고    scopus 로고
    • Neuronal α-synucleinopathy with severe movement disorder in mice expressing A53T human α-synuclein
    • Giasson BI, Duda JE, Quinn SM, et al. Neuronal α-synucleinopathy with severe movement disorder in mice expressing A53T human α-synuclein. Neuron 2002;34:521-533.
    • (2002) Neuron , vol.34 , pp. 521-533
    • Giasson, B.I.1    Duda, J.E.2    Quinn, S.M.3
  • 133
    • 57149118018 scopus 로고    scopus 로고
    • Resistance of bovine spongiform encephalopathy (BSE) prions to inactivation
    • Giles K, Glidden DV, Beckwith R, et al. Resistance of bovine spongiform encephalopathy (BSE) prions to inactivation. PLoS Pathog 2008;4:e1000206.
    • (2008) PLoS Pathog , vol.4 , pp. e1000206
    • Giles, K.1    Glidden, D.V.2    Beckwith, R.3
  • 134
    • 77955298267 scopus 로고    scopus 로고
    • Human prion strain selection in transgenic mice
    • Giles K, Glidden DV, Patel S, et al. Human prion strain selection in transgenic mice. Ann Neurol 2010;68:151-161.
    • (2010) Ann Neurol , vol.68 , pp. 151-161
    • Giles, K.1    Glidden, D.V.2    Patel, S.3
  • 136
    • 0242361687 scopus 로고    scopus 로고
    • Extraneural pathologic prion protein in sporadic Creutzfeldt-Jakob disease
    • Glatzel M, Abela E, Maissen M, et al. Extraneural pathologic prion protein in sporadic Creutzfeldt-Jakob disease. N Engl J Med 2003;349:1812-1820.
    • (2003) N Engl J Med , vol.349 , pp. 1812-1820
    • Glatzel, M.1    Abela, E.2    Maissen, M.3
  • 137
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 1984;122:1131-1135.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 138
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A, Chartier-Harlin M-C, Mullan M, et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991;349:704-706.
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.-C.2    Mullan, M.3
  • 139
    • 0025918142 scopus 로고
    • Creutzfeldt-Jacob disease associated with the PRNP codon 200Lys mutation: an analysis of 45 families
    • Goldfarb LG, Brown P, Mitrova E, et al. Creutzfeldt-Jacob disease associated with the PRNP codon 200Lys mutation: an analysis of 45 families. Eur J Epidemiol 1991;7:477-486.
    • (1991) Eur J Epidemiol , vol.7 , pp. 477-486
    • Goldfarb, L.G.1    Brown, P.2    Mitrova, E.3
  • 140
    • 0024992359 scopus 로고
    • Mutation in codon 200 of scrapie amyloid precursor gene linked to Creutzfeldt-Jakob disease in Sephardic Jews of Libyan and non-Libyan origin
    • Goldfarb LG, Korczyn AD, Brown P, et al. Mutation in codon 200 of scrapie amyloid precursor gene linked to Creutzfeldt-Jakob disease in Sephardic Jews of Libyan and non-Libyan origin. Lancet 1990;336:637-638.
    • (1990) Lancet , vol.336 , pp. 637-638
    • Goldfarb, L.G.1    Korczyn, A.D.2    Brown, P.3
  • 142
    • 0026017096 scopus 로고
    • Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon
    • Goldmann W, Hunter N, Martin T, et al. Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon. J Gen Virol 1991;72:201-204.
    • (1991) J Gen Virol , vol.72 , pp. 201-204
    • Goldmann, W.1    Hunter, N.2    Martin, T.3
  • 143
    • 0028349264 scopus 로고
    • PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie
    • Goldmann W, Hunter N, Smith G, et al. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J Gen Virol 1994;75:989-995.
    • (1994) J Gen Virol , vol.75 , pp. 989-995
    • Goldmann, W.1    Hunter, N.2    Smith, G.3
  • 144
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • Gorodinsky A, Harris DA. Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J Cell Biol 1995;129:619-627.
    • (1995) J Cell Biol , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 145
    • 14144253104 scopus 로고    scopus 로고
    • Prion protein NMR structures of elk and of mouse/elk hybrids
    • Gossert AD, Bonjour S, Lysek DA, et al. Prion protein NMR structures of elk and of mouse/elk hybrids. Proc Natl Acad Sci U S A 2005;102:646-650.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 646-650
    • Gossert, A.D.1    Bonjour, S.2    Lysek, D.A.3
  • 146
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β-helices into trimers
    • Govaerts C, Wille H, Prusiner SB, et al. Evidence for assembly of prions with left-handed β-helices into trimers. Proc Natl Acad Sci U S A 2004;101:8342-8347.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3
  • 147
    • 77955504368 scopus 로고    scopus 로고
    • The mechanism of prion inhibition by HET-S
    • Greenwald J, Buhtz C, Ritter C, et al. The mechanism of prion inhibition by HET-S. Mol Cell 2010;38:889-899.
    • (2010) Mol Cell , vol.38 , pp. 889-899
    • Greenwald, J.1    Buhtz, C.2    Ritter, C.3
  • 148
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I, Iqbal K, Tung Y-C, et al. Abnormal phosphorylation of the microtubule-associated protein (tau) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci U S A 1986;83:4913-4917.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.-C.3
  • 149
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal tau by pathological tau conformers drives pathogenesis of Alzheimer-like tangles
    • Guo JL, Lee VM-Y. Seeding of normal tau by pathological tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem 2011;286:15317-15331.
    • (2011) J Biol Chem , vol.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.-Y.2
  • 150
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway
    • Haass C, Lemere CA, Capell A, et al. The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Nat Med 1995;1:1291-1296.
    • (1995) Nat Med , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3
  • 151
    • 1242272068 scopus 로고    scopus 로고
    • The crystal structure of the globular domain of sheep prion protein
    • Haire LF, Whyte SM, Vasisht N, et al. The crystal structure of the globular domain of sheep prion protein. J Mol Biol 2004;336:1175-1183.
    • (2004) J Mol Biol , vol.336 , pp. 1175-1183
    • Haire, L.F.1    Whyte, S.M.2    Vasisht, N.3
  • 152
    • 62849123278 scopus 로고    scopus 로고
    • Detection of CWD prions in urine and saliva of deer by transgenic mouse bioassay
    • Haley NJ, Seelig DM, Zabel MD, et al. Detection of CWD prions in urine and saliva of deer by transgenic mouse bioassay. PLoS One 2009;4:e4848.
    • (2009) PLoS One , vol.4 , pp. e4848
    • Haley, N.J.1    Seelig, D.M.2    Zabel, M.D.3
  • 153
    • 0035233928 scopus 로고    scopus 로고
    • Preliminary findings on the experimental transmission of chronic wasting disease agent of mule deer to cattle
    • Hamir AN, Cutlip RC, Miller JM, et al. Preliminary findings on the experimental transmission of chronic wasting disease agent of mule deer to cattle. J Vet Diagn Invest 2001;13:91-96.
    • (2001) J Vet Diagn Invest , vol.13 , pp. 91-96
    • Hamir, A.N.1    Cutlip, R.C.2    Miller, J.M.3
  • 154
    • 0032488777 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein in neurodegenerative disease
    • Hegde RS, Mastrianni JA, Scott MR, et al. A transmembrane form of the prion protein in neurodegenerative disease. Science 1998;279:827-834.
    • (1998) Science , vol.279 , pp. 827-834
    • Hegde, R.S.1    Mastrianni, J.A.2    Scott, M.R.3
  • 155
    • 13844259181 scopus 로고    scopus 로고
    • Chronic lymphocytic inflammation specifies the organ tropism of prions
    • Heikenwalder M, Zeller N, Seeger H, et al. Chronic lymphocytic inflammation specifies the organ tropism of prions. Science 2005;307:1107-1110.
    • (2005) Science , vol.307 , pp. 1107-1110
    • Heikenwalder, M.1    Zeller, N.2    Seeger, H.3
  • 156
    • 0035812752 scopus 로고    scopus 로고
    • Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies
    • Heppner FL, Musahl C, Arrighi I, et al. Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies. Science 2001;294:178-182.
    • (2001) Science , vol.294 , pp. 178-182
    • Heppner, F.L.1    Musahl, C.2    Arrighi, I.3
  • 157
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C, Russelakis-Carneiro M, Maundrell K, et al. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 2003;22:5435-5445.
    • (2003) EMBO J , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3
  • 158
    • 0030820354 scopus 로고    scopus 로고
    • The same prion strain causes vCJD and BSE
    • Hill AF, Desbruslais M, Joiner S, et al. The same prion strain causes vCJD and BSE. Nature 1997;389:448-450.
    • (1997) Nature , vol.389 , pp. 448-450
    • Hill, A.F.1    Desbruslais, M.2    Joiner, S.3
  • 159
    • 3242716876 scopus 로고    scopus 로고
    • Prevalence of lymphoreticular prion protein accumulation in UK tissue samples
    • Hilton DA, Ghani AC, Conyers L, et al. Prevalence of lymphoreticular prion protein accumulation in UK tissue samples. J Pathol 2004;203:733-739.
    • (2004) J Pathol , vol.203 , pp. 733-739
    • Hilton, D.A.1    Ghani, A.C.2    Conyers, L.3
  • 160
    • 12144271772 scopus 로고    scopus 로고
    • NMR structure of the bovine prion protein isolated from healthy calf brains
    • Hornemann S, Schorn C, Wuthrich K. NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO Rep 2004;5:1159-1164.
    • (2004) EMBO Rep , vol.5 , pp. 1159-1164
    • Hornemann, S.1    Schorn, C.2    Wuthrich, K.3
  • 161
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides
    • Hornshaw MP, McDermott JR, Candy JM, et al. Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem Biophys Res Commun 1995;214:993-999.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 162
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou F, Sun L, Zheng H, et al. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 2011;146:448-461.
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3
  • 163
    • 0038700808 scopus 로고    scopus 로고
    • Prion diseases: BSE in sheep bred for resistance to infection
    • Houston F, Goldmann W, Chong A, et al. Prion diseases: BSE in sheep bred for resistance to infection. Nature 2003;423:498.
    • (2003) Nature , vol.423 , pp. 498
    • Houston, F.1    Goldmann, W.2    Chong, A.3
  • 164
    • 0024519771 scopus 로고
    • Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome
    • Hsiao K, Baker HF, Crow TJ, et al. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature 1989;338:342-345.
    • (1989) Nature , vol.338 , pp. 342-345
    • Hsiao, K.1    Baker, H.F.2    Crow, T.J.3
  • 165
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • Hsiao K, Chapman P, Nilsen S, et al. Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science 1996;274:99-102.
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 166
    • 0025869213 scopus 로고
    • Mutation of the prion protein in Libyan Jews with Creutzfeldt-Jakob disease
    • Hsiao K, Meiner Z, Kahana E, et al. Mutation of the prion protein in Libyan Jews with Creutzfeldt-Jakob disease. N Engl J Med 1991;324:1091-1097.
    • (1991) N Engl J Med , vol.324 , pp. 1091-1097
    • Hsiao, K.1    Meiner, Z.2    Kahana, E.3
  • 167
    • 0025896970 scopus 로고
    • Restriction fragment length polymorphisms of the scrapie-associated fibril protein (PrP) gene and their association with susceptiblity to natural scrapie in British sheep
    • Hunter N, Foster JD, Benson G, et al. Restriction fragment length polymorphisms of the scrapie-associated fibril protein (PrP) gene and their association with susceptiblity to natural scrapie in British sheep. J Gen Virol 1991;72:1287-1292.
    • (1991) J Gen Virol , vol.72 , pp. 1287-1292
    • Hunter, N.1    Foster, J.D.2    Benson, G.3
  • 168
    • 0028778780 scopus 로고
    • Frequencies of PrP gene variants in healthy cattle and cattle with BSE in Scotland
    • Hunter N, Goldmann W, Smith G, et al. Frequencies of PrP gene variants in healthy cattle and cattle with BSE in Scotland. Vet Rec 1994;135:400-403.
    • (1994) Vet Rec , vol.135 , pp. 400-403
    • Hunter, N.1    Goldmann, W.2    Smith, G.3
  • 169
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M, Lendon CL, Rizzu P, et al. Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 1998;393:702-705.
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 170
    • 77955367206 scopus 로고    scopus 로고
    • NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features
    • Ilc G, Giachin G, Jaremko M, et al. NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. PLoS One 2010;5:e11715.
    • (2010) PLoS One , vol.5 , pp. e11715
    • Ilc, G.1    Giachin, G.2    Jaremko, M.3
  • 171
    • 85005785942 scopus 로고    scopus 로고
    • The new variant form of Creutzfeldt-Jakob disease: a novel prion protein amyloid disorder (Editorial)
    • Ironside JW. The new variant form of Creutzfeldt-Jakob disease: a novel prion protein amyloid disorder (Editorial). Amyloid 1997;4:66-69.
    • (1997) Amyloid , vol.4 , pp. 66-69
    • Ironside, J.W.1
  • 173
    • 20044392285 scopus 로고    scopus 로고
    • An enzyme-detergent method for effective prion decontamination of surgical steel
    • Jackson GS, McKintosh E, Flechsig E, et al. An enzyme-detergent method for effective prion decontamination of surgical steel. J Gen Virol 2005;86:869-878.
    • (2005) J Gen Virol , vol.86 , pp. 869-878
    • Jackson, G.S.1    McKintosh, E.2    Flechsig, E.3
  • 174
    • 68949163542 scopus 로고    scopus 로고
    • Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice
    • Jackson WS, Borkowski AW, Faas H, et al. Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice. Neuron 2009;63:438-450.
    • (2009) Neuron , vol.63 , pp. 438-450
    • Jackson, W.S.1    Borkowski, A.W.2    Faas, H.3
  • 175
    • 0030967895 scopus 로고    scopus 로고
    • Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
    • James TL, Liu H, Ulyanov NB, et al. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci U S A 1997;94:10086-10091.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10086-10091
    • James, T.L.1    Liu, H.2    Ulyanov, N.B.3
  • 176
    • 77449089995 scopus 로고    scopus 로고
    • Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP
    • Jansen C, Parchi P, Capellari S, et al. Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP. Acta Neuropathol 2010;119:189-197.
    • (2010) Acta Neuropathol , vol.119 , pp. 189-197
    • Jansen, C.1    Parchi, P.2    Capellari, S.3
  • 177
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993;73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 178
    • 0026069894 scopus 로고
    • Proteinase-resistant prion protein accumulation in Syrian hamster brain correlates with regional pathology and scrapie infectivity
    • Jendroska K, Heinzel FP, Torchia M, et al. Proteinase-resistant prion protein accumulation in Syrian hamster brain correlates with regional pathology and scrapie infectivity. Neurology 1991;41:1482-1490.
    • (1991) Neurology , vol.41 , pp. 1482-1490
    • Jendroska, K.1    Heinzel, F.P.2    Torchia, M.3
  • 179
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • Jin M, Shepardson N, Yang T, et al. Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc Natl Acad Sci U S A 2011;108:5819-5824.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3
  • 180
    • 0032478215 scopus 로고    scopus 로고
    • Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils
    • Johan K, Westermark G, Engstrom U, et al. Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils. Proc Natl Acad Sci U S A 1998;95:2558-2563.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2558-2563
    • Johan, K.1    Westermark, G.2    Engstrom, U.3
  • 181
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson BS, Snead D, Lee JJ, et al. TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 2009;284:20329-20339.
    • (2009) J Biol Chem , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3
  • 182
    • 0016389681 scopus 로고
    • Creutzfeldt-Jakob disease: focus among Libyan Jews in Israel
    • Kahana E, Milton A, Braham J, et al. Creutzfeldt-Jakob disease: focus among Libyan Jews in Israel. Science 1974;183:90-91.
    • (1974) Science , vol.183 , pp. 90-91
    • Kahana, E.1    Milton, A.2    Braham, J.3
  • 183
    • 38349185509 scopus 로고    scopus 로고
    • Molecular model of an alpha-helical prion protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations
    • Kaimann T, Metzger S, Kuhlmann K, et al. Molecular model of an alpha-helical prion protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations. J Mol Biol 2008;376:582-596.
    • (2008) J Mol Biol , vol.376 , pp. 582-596
    • Kaimann, T.1    Metzger, S.2    Kuhlmann, K.3
  • 184
    • 77952305367 scopus 로고    scopus 로고
    • Beta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrils
    • Kajava AV, Baxa U, Steven AC. Beta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrils. FASEB J 2010;24:1311-1319.
    • (2010) FASEB J , vol.24 , pp. 1311-1319
    • Kajava, A.V.1    Baxa, U.2    Steven, A.C.3
  • 185
    • 28844477599 scopus 로고    scopus 로고
    • Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro
    • Kanaani J, Prusiner SB, Diacovo J, et al. Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro. J Neurochem 2005;95:1373-1386.
    • (2005) J Neurochem , vol.95 , pp. 1373-1386
    • Kanaani, J.1    Prusiner, S.B.2    Diacovo, J.3
  • 186
    • 0034723133 scopus 로고    scopus 로고
    • A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice
    • Kaneko K, Ball HL, Wille H, et al. A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice. J Mol Biol 2000;295:997-1007.
    • (2000) J Mol Biol , vol.295 , pp. 997-1007
    • Kaneko, K.1    Ball, H.L.2    Wille, H.3
  • 187
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
    • Kaneko K, Zulianello L, Scott M, et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc Natl Acad Sci U S A 1997;94:10069-10074.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10069-10074
    • Kaneko, K.1    Zulianello, L.2    Scott, M.3
  • 188
    • 0033527583 scopus 로고    scopus 로고
    • Antibody binding defines a structure for an epitope that participates in the PrPC-> PrPSc conformational change
    • Kanyo ZF, Pan K-M, Williamson A, et al. Antibody binding defines a structure for an epitope that participates in the PrPC-> PrPSc conformational change. J Mol Biol 1999;293:855-863.
    • (1999) J Mol Biol , vol.293 , pp. 855-863
    • Kanyo, Z.F.1    Pan, K.-M.2    Williamson, A.3
  • 189
    • 36348929457 scopus 로고    scopus 로고
    • Orally administered amyloidophilic compound is effective in prolonging the incubation periods of animals cerebrally infected with prion diseases in a prion strain-dependent manner
    • Kawasaki Y, Kawagoe K, Chen CJ, et al. Orally administered amyloidophilic compound is effective in prolonging the incubation periods of animals cerebrally infected with prion diseases in a prion strain-dependent manner. J Virol 2007;81:12889-12898.
    • (2007) J Virol , vol.81 , pp. 12889-12898
    • Kawasaki, Y.1    Kawagoe, K.2    Chen, C.J.3
  • 190
    • 78650575242 scopus 로고    scopus 로고
    • Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP
    • Khan MQ, Sweeting B, Mulligan VK, et al. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proc Natl Acad Sci U S A 2010;107:19808-19813.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19808-19813
    • Khan, M.Q.1    Sweeting, B.2    Mulligan, V.K.3
  • 191
    • 15744398507 scopus 로고    scopus 로고
    • Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor
    • Kiachopoulos S, Bracher A, Winklhofer KF, et al. Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor. J Biol Chem 2005;280:9320-9329.
    • (2005) J Biol Chem , vol.280 , pp. 9320-9329
    • Kiachopoulos, S.1    Bracher, A.2    Winklhofer, K.F.3
  • 192
    • 0017336439 scopus 로고
    • Characteristics of a short incubation model of scrapie in the golden hamster
    • Kimberlin R, Walker C. Characteristics of a short incubation model of scrapie in the golden hamster. J Gen Virol 1977;34:295-304.
    • (1977) J Gen Virol , vol.34 , pp. 295-304
    • Kimberlin, R.1    Walker, C.2
  • 193
    • 0021046367 scopus 로고
    • The antiviral compound HPA-23 can prevent scrapie when administered at the time of infection
    • Kimberlin RH, Walker CA. The antiviral compound HPA-23 can prevent scrapie when administered at the time of infection. Arch Virol 1983;78:9-18.
    • (1983) Arch Virol , vol.78 , pp. 9-18
    • Kimberlin, R.H.1    Walker, C.A.2
  • 194
    • 0024325787 scopus 로고
    • The genomic identity of different strains of mouse scrapie is expressed in hamsters and preserved on reisolation in mice
    • Kimberlin RH, Walker CA, Fraser H. The genomic identity of different strains of mouse scrapie is expressed in hamsters and preserved on reisolation in mice. J Gen Virol 1989;70:2017-2025.
    • (1989) J Gen Virol , vol.70 , pp. 2017-2025
    • Kimberlin, R.H.1    Walker, C.A.2    Fraser, H.3
  • 195
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King CY, Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 2004;428:319-323.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 196
    • 0025983158 scopus 로고
    • Abnormal isoform of prion protein accumulates in follicular dendritic cells in mice with Creutzfeldt-Jakob disease
    • Kitamoto T, Muramoto T, Mohri S, et al. Abnormal isoform of prion protein accumulates in follicular dendritic cells in mice with Creutzfeldt-Jakob disease. J Virol 1991;65:6292-6295.
    • (1991) J Virol , vol.65 , pp. 6292-6295
    • Kitamoto, T.1    Muramoto, T.2    Mohri, S.3
  • 198
    • 0021711247 scopus 로고
    • The natural incubation period of kuru and the episodes of transmission in three clusters of patients
    • Klitzman RL, Alpers MP, Gajdusek DC. The natural incubation period of kuru and the episodes of transmission in three clusters of patients. Neuroepidemiology 1984;3:3-20.
    • (1984) Neuroepidemiology , vol.3 , pp. 3-20
    • Klitzman, R.L.1    Alpers, M.P.2    Gajdusek, D.C.3
  • 199
    • 0034869693 scopus 로고    scopus 로고
    • Crystal structure of the human prion protein reveals a mechanism for oligomerization
    • Knaus KJ, Morillas M, Swietnicki W, et al. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat Struct Biol 2001;8:770-774.
    • (2001) Nat Struct Biol , vol.8 , pp. 770-774
    • Knaus, K.J.1    Morillas, M.2    Swietnicki, W.3
  • 200
    • 33644655659 scopus 로고    scopus 로고
    • Potent antiscrapie activities of degenerate phosphorothioate oligonucleotides
    • Kocisko DA, Vaillant A, Lee KS, et al. Potent antiscrapie activities of degenerate phosphorothioate oligonucleotides. Antimicrob Agents Chemother 2006;50:1034-1044.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1034-1044
    • Kocisko, D.A.1    Vaillant, A.2    Lee, K.S.3
  • 201
    • 1942470550 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S
    • Kong C, Ito K, Walsh MA, et al. Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Mol Cell 2004;14:233-245.
    • (2004) pombe. Mol Cell , vol.14 , pp. 233-245
    • Kong, C.1    Ito, K.2    Walsh, M.A.3
  • 202
    • 24344492256 scopus 로고    scopus 로고
    • Chronic wasting disease of elk: transmissibility to humans examined by transgenic mouse models
    • Kong Q, Huang S, Zou W, et al. Chronic wasting disease of elk: transmissibility to humans examined by transgenic mouse models. J Neurosci 2005;25:7944-7999.
    • (2005) J Neurosci , vol.25 , pp. 7944-7999
    • Kong, Q.1    Huang, S.2    Zou, W.3
  • 203
    • 1842644947 scopus 로고    scopus 로고
    • Inherited prion diseases
    • Prusiner SB, ed, 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Kong Q, Surewicz WK, Petersen RB, et al. Inherited prion diseases. In: Prusiner SB, ed. Prion Biology and Diseases. 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; 2004:673-775.
    • (2004) Prion Biology and Diseases , pp. 673-775
    • Kong, Q.1    Surewicz, W.K.2    Petersen, R.B.3
  • 204
    • 0037447071 scopus 로고    scopus 로고
    • Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene
    • Korth C, Kaneko K, Groth D, et al. Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene. Proc Natl Acad Sci U S A 2003;100:4784-4789.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4784-4789
    • Korth, C.1    Kaneko, K.2    Groth, D.3
  • 205
    • 0035859806 scopus 로고    scopus 로고
    • Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
    • Korth C, May BCH, Cohen FE, et al. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc Natl Acad Sci U S A 2001;98:9836-9841.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9836-9841
    • Korth, C.1    May, B.C.H.2    Cohen, F.E.3
  • 206
    • 0030613755 scopus 로고    scopus 로고
    • Prion (PrPSc)-specific epitope defined by a monoclonal antibody
    • Korth C, Stierli B, Streit P, et al. Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 1997;389:74-77.
    • (1997) Nature , vol.389 , pp. 74-77
    • Korth, C.1    Stierli, B.2    Streit, P.3
  • 207
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ. Microtubule-associated protein tau is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci U S A 1986;83:4044-4048.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 208
    • 0035824517 scopus 로고    scopus 로고
    • Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution
    • Kozin SA, Bertho G, Mazur AK, et al. Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution. J Biol Chem 2001;276:46364-46370.
    • (2001) J Biol Chem , vol.276 , pp. 46364-46370
    • Kozin, S.A.1    Bertho, G.2    Mazur, A.K.3
  • 209
    • 0028894604 scopus 로고
    • Codon 178 mutation of the human prion protein gene in a German family (Backer family): sequencing data from 72 year-old celloidin-embedded brain tissue
    • Kretzschmar HA, Neumann M, Stavrou D. Codon 178 mutation of the human prion protein gene in a German family (Backer family): sequencing data from 72 year-old celloidin-embedded brain tissue. Acta Neuropathol 1995;89:96-98.
    • (1995) Acta Neuropathol , vol.89 , pp. 96-98
    • Kretzschmar, H.A.1    Neumann, M.2    Stavrou, D.3
  • 211
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, et al. Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A 1998;95:6448-6453.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 212
    • 0027350787 scopus 로고
    • French autochthonous scrapied sheep without the 136Val PrP polymorphism
    • Laplanche J-L, Chatelain J, Beaudry P, et al. French autochthonous scrapied sheep without the 136Val PrP polymorphism. Mamm Genome 1993;4:463-464.
    • (1993) Mamm Genome , vol.4 , pp. 463-464
    • Laplanche, J.-L.1    Chatelain, J.2    Beaudry, P.3
  • 215
    • 0014963710 scopus 로고
    • Inactivation of the scrapie agent by near monochromatic ultraviolet light
    • Latarjet R, Muel B, Haig DA, et al. Inactivation of the scrapie agent by near monochromatic ultraviolet light. Nature 1970;227:1341-1343.
    • (1970) Nature , vol.227 , pp. 1341-1343
    • Latarjet, R.1    Muel, B.2    Haig, D.A.3
  • 216
    • 44749083979 scopus 로고    scopus 로고
    • Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein
    • Lee H-J, Suk J-E, Bae E-J, et al. Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein. Int J Biochem Cell Biol 2008;40:1835-1849.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1835-1849
    • Lee, H.-J.1    Suk, J.-E.2    Bae, E.-J.3
  • 217
    • 26444434251 scopus 로고    scopus 로고
    • Selective precipitation of prions by polyoxometalate complexes
    • Lee IS, Long JR, Prusiner SB, et al. Selective precipitation of prions by polyoxometalate complexes. J Am Chem Soc 2005;127:13802-13803.
    • (2005) J Am Chem Soc , vol.127 , pp. 13802-13803
    • Lee, I.S.1    Long, J.R.2    Prusiner, S.B.3
  • 218
    • 75649120399 scopus 로고    scopus 로고
    • Conformational diversity in prion protein variants influences intermolecular beta-sheet formation
    • Lee S, Antony L, Hartmann R, et al. Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. EMBO J 2010;29:251-262.
    • (2010) EMBO J , vol.29 , pp. 251-262
    • Lee, S.1    Antony, L.2    Hartmann, R.3
  • 219
    • 0025904444 scopus 로고
    • A68: a major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee VM-Y, Balin BJ, Orvos IJ, et al. A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science 1991;251:645-678.
    • (1991) Science , vol.251 , pp. 645-678
    • Lee, V.M.-Y.1    Balin, B.J.2    Orvos, I.J.3
  • 221
  • 222
    • 34447639732 scopus 로고    scopus 로고
    • Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes
    • Legname G, Nguyen H-OB, Peretz D, et al. Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci U S A 2006;103:19105-19110.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19105-19110
    • Legname, G.1    Nguyen, H.-O.B.2    Peretz, D.3
  • 223
    • 0033609035 scopus 로고    scopus 로고
    • Solution structure of Syrian hamster prion protein rPrP(90-231)
    • Liu H, Farr-Jones S, Ulyanov NB, et al. Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry 1999;38:5362-5377.
    • (1999) Biochemistry , vol.38 , pp. 5362-5377
    • Liu, H.1    Farr-Jones, S.2    Ulyanov, N.B.3
  • 224
    • 1142273431 scopus 로고    scopus 로고
    • Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion
    • Llewelyn CA, Hewitt PE, Knight RS, et al. Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet 2004;363:417-421.
    • (2004) Lancet , vol.363 , pp. 417-421
    • Llewelyn, C.A.1    Hewitt, P.E.2    Knight, R.S.3
  • 226
    • 33748793940 scopus 로고    scopus 로고
    • Directed evolution of an anti-prion protein scFv fragment to an affinity of 1 pM and its structural interpretation
    • Luginbuhl B, Kanyo Z, Jones RM, et al. Directed evolution of an anti-prion protein scFv fragment to an affinity of 1 pM and its structural interpretation. J Mol Biol 2006;363:75-97.
    • (2006) J Mol Biol , vol.363 , pp. 75-97
    • Luginbuhl, B.1    Kanyo, Z.2    Jones, R.M.3
  • 227
    • 0037424610 scopus 로고    scopus 로고
    • NMR structure of the human doppel protein
    • Lührs T, Riek R, Guntert P, et al. NMR structure of the human doppel protein. J Mol Biol 2003;326:1549-1557.
    • (2003) J Mol Biol , vol.326 , pp. 1549-1557
    • Lührs, T.1    Riek, R.2    Guntert, P.3
  • 228
    • 20044367104 scopus 로고    scopus 로고
    • Prion protein NMR structures of cats, dogs, pigs, and sheep
    • Lysek DA, Schorn C, Nivon LG, et al. Prion protein NMR structures of cats, dogs, pigs, and sheep. Proc Natl Acad Sci U S A 2005;102:640-645.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 640-645
    • Lysek, D.A.1    Schorn, C.2    Nivon, L.G.3
  • 229
    • 0037195617 scopus 로고    scopus 로고
    • Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
    • Ma J, Lindquist S. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 2002;298:1785-1788.
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 231
    • 77449142074 scopus 로고    scopus 로고
    • Recombinant prion protein induces a new transmissible prion disease in wild-type animals
    • Makarava N, Kovacs GG, Bocharova O, et al. Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol 2010;119:177-187.
    • (2010) Acta Neuropathol , vol.119 , pp. 177-187
    • Makarava, N.1    Kovacs, G.G.2    Bocharova, O.3
  • 232
    • 65949115708 scopus 로고    scopus 로고
    • Regulation of embryonic cell adhesion by the prion protein
    • Málaga-Trillo E, Solis GP, Schrock Y, et al. Regulation of embryonic cell adhesion by the prion protein. PLoS Biol 2009;7:e55.
    • (2009) PLoS Biol , vol.7 , pp. e55
    • Málaga-Trillo, E.1    Solis, G.P.2    Schrock, Y.3
  • 233
    • 0242363656 scopus 로고    scopus 로고
    • Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis
    • Mallucci G, Dickinson A, Linehan J, et al. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 2003;302:871-874.
    • (2003) Science , vol.302 , pp. 871-874
    • Mallucci, G.1    Dickinson, A.2    Linehan, J.3
  • 234
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • Mallucci GR, Ratte S, Asante EA, et al. Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J 2002;21:202-210.
    • (2002) EMBO J , vol.21 , pp. 202-210
    • Mallucci, G.R.1    Ratte, S.2    Asante, E.A.3
  • 235
    • 33846538022 scopus 로고    scopus 로고
    • Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice
    • Mallucci GR, White MD, Farmer M, et al. Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice. Neuron 2007;53:325-335.
    • (2007) Neuron , vol.53 , pp. 325-335
    • Mallucci, G.R.1    White, M.D.2    Farmer, M.3
  • 236
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • Manson JC, Clarke AR, Hooper ML, et al. 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 1994;8:121-127.
    • (1994) Mol Neurobiol , vol.8 , pp. 121-127
    • Manson, J.C.1    Clarke, A.R.2    Hooper, M.L.3
  • 238
    • 0032092220 scopus 로고    scopus 로고
    • OH-radical formation by ultrasound in aqueous solution-Part II: Terephthalate and Fricke dosimetry and the influence of various conditions on the sonolytic yield
    • Mark G, Tauber A, Laupert R, et al. OH-radical formation by ultrasound in aqueous solution-Part II: Terephthalate and Fricke dosimetry and the influence of various conditions on the sonolytic yield. Ultrason Sonochem 1998;5:41-52.
    • (1998) Ultrason Sonochem , vol.5 , pp. 41-52
    • Mark, G.1    Tauber, A.2    Laupert, R.3
  • 239
    • 0026012059 scopus 로고
    • Epidemiological and experimental studies on a new incident of transmissible mink encephalopathy
    • Marsh RF, Bessen RA, Lehmann S, et al. Epidemiological and experimental studies on a new incident of transmissible mink encephalopathy. J Gen Virol 1991;72:589-594.
    • (1991) J Gen Virol , vol.72 , pp. 589-594
    • Marsh, R.F.1    Bessen, R.A.2    Lehmann, S.3
  • 240
    • 0019778656 scopus 로고
    • Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Sträussler syndrome
    • Masters CL, Gajdusek DC, Gibbs CJ Jr. Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Sträussler syndrome. Brain 1981;104:559-588.
    • (1981) Brain , vol.104 , pp. 559-588
    • Masters, C.L.1    Gajdusek, D.C.2    Gibbs, C.J.3
  • 241
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • Masters CL, Simms G, Weinman NA, et al. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc Natl Acad Sci U S A 1985;82:4245-4249.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 4245-4249
    • Masters, C.L.1    Simms, G.2    Weinman, N.A.3
  • 242
    • 33749618609 scopus 로고    scopus 로고
    • Infectious prions in the saliva and blood of deer with chronic wasting disease
    • Mathiason CK, Powers JG, Dahmes SJ, et al. Infectious prions in the saliva and blood of deer with chronic wasting disease. Science 2006;314:133-136.
    • (2006) Science , vol.314 , pp. 133-136
    • Mathiason, C.K.1    Powers, J.G.2    Dahmes, S.J.3
  • 243
    • 0037452925 scopus 로고    scopus 로고
    • Potent inhibition of scrapie prion replication in cultured cells by bis-acridines
    • May BCH, Fafarman AT, Hong SB, et al. Potent inhibition of scrapie prion replication in cultured cells by bis-acridines. Proc Natl Acad Sci U S A 2003;100:3416-3421.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3416-3421
    • May, B.C.H.1    Fafarman, A.T.2    Hong, S.B.3
  • 245
    • 68249157080 scopus 로고    scopus 로고
    • Chronic traumatic encephalopathy in athletes: progressive tauopathy after repetitive head injury
    • McKee AC, Cantu RC, Nowinski CJ, et al. Chronic traumatic encephalopathy in athletes: progressive tauopathy after repetitive head injury. J Neuropathol Exp Neurol 2009;68:709-735.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 709-735
    • McKee, A.C.1    Cantu, R.C.2    Nowinski, C.J.3
  • 246
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley MP, Bolton DC, Prusiner SB. A protease-resistant protein is a structural component of the scrapie prion. Cell 1983;35:57-62.
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 247
    • 0022494814 scopus 로고
    • Molecular characteristics of prion rods purified from scrapie-infected hamster brains
    • McKinley MP, Braunfeld MB, Bellinger CG, et al. Molecular characteristics of prion rods purified from scrapie-infected hamster brains. J Infect Dis 1986;154:110-120.
    • (1986) J Infect Dis , vol.154 , pp. 110-120
    • McKinley, M.P.1    Braunfeld, M.B.2    Bellinger, C.G.3
  • 248
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley MP, Meyer RK, Kenaga L, et al. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 1991;65:1340-1351.
    • (1991) J Virol , vol.65 , pp. 1340-1351
    • McKinley, M.P.1    Meyer, R.K.2    Kenaga, L.3
  • 249
    • 33645147707 scopus 로고    scopus 로고
    • Prion disease genetics
    • Mead S. Prion disease genetics. Eur J Hum Genet 2006;14:273-281.
    • (2006) Eur J Hum Genet , vol.14 , pp. 273-281
    • Mead, S.1
  • 250
    • 9344258589 scopus 로고    scopus 로고
    • Possible role of region 152-156 in the structural duality of a peptide fragment from sheep prion protein
    • Megy S, Bertho G, Kozin SA, et al. Possible role of region 152-156 in the structural duality of a peptide fragment from sheep prion protein. Protein Sci 2004;13:3151-3160.
    • (2004) Protein Sci , vol.13 , pp. 3151-3160
    • Megy, S.1    Bertho, G.2    Kozin, S.A.3
  • 251
    • 0037418828 scopus 로고    scopus 로고
    • Soluble dimeric prion protein binds PrPSc in vivo and antagonizes prion disease
    • Meier P, Genoud N, Prinz M, et al. Soluble dimeric prion protein binds PrPSc in vivo and antagonizes prion disease. Cell 2003;113:49-60.
    • (2003) Cell , vol.113 , pp. 49-60
    • Meier, P.1    Genoud, N.2    Prinz, M.3
  • 252
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann M, Coomaraswamy J, Bolmont T, et al. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 2006;313:1781-1784.
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3
  • 253
    • 0035099673 scopus 로고    scopus 로고
    • A novel erythroid-specific marker of transmissible spongiform encephalopathies
    • Miele G, Manson J, Clinton M. A novel erythroid-specific marker of transmissible spongiform encephalopathies. Nat Med 2001;7:361-364.
    • (2001) Nat Med , vol.7 , pp. 361-364
    • Miele, G.1    Manson, J.2    Clinton, M.3
  • 254
    • 0034303243 scopus 로고    scopus 로고
    • Epizootiology of chronic wasting disease in free-ranging cervids in Colorado and Wyoming
    • Miller MW, Williams ES, McCarty CW, et al. Epizootiology of chronic wasting disease in free-ranging cervids in Colorado and Wyoming. J Wildl Dis 2000;36:676-690.
    • (2000) J Wildl Dis , vol.36 , pp. 676-690
    • Miller, M.W.1    Williams, E.S.2    McCarty, C.W.3
  • 255
    • 1842502935 scopus 로고    scopus 로고
    • Long-term mortality in the United States cohort of pituitary-derived growth hormone recipients
    • Mills JL, Schonberger LB, Wysowski DK, et al. Long-term mortality in the United States cohort of pituitary-derived growth hormone recipients. J Pediatr 2004;144:430-436.
    • (2004) J Pediatr , vol.144 , pp. 430-436
    • Mills, J.L.1    Schonberger, L.B.2    Wysowski, D.K.3
  • 256
    • 0016915917 scopus 로고
    • The physico-chemical nature of the scrapie agent
    • Kimberlin RH, ed, New York: American Elsevier
    • Millson GC, Hunter GD, Kimberlin RH. The physico-chemical nature of the scrapie agent. In: Kimberlin RH, ed. Slow Virus Diseases of Animals and Man. New York: American Elsevier; 1976:243-266.
    • (1976) Slow Virus Diseases of Animals and Man , pp. 243-266
    • Millson, G.C.1    Hunter, G.D.2    Kimberlin, R.H.3
  • 257
    • 2942694110 scopus 로고    scopus 로고
    • Standards for the assay of Creutz{reversed not sign}feldt-Jakob disease specimens
    • Minor P, Newham J, Jones N, et al. Standards for the assay of Creutz{reversed not sign}feldt-Jakob disease specimens. J Gen Virol 2004;85:1777-1784.
    • (2004) J Gen Virol , vol.85 , pp. 1777-1784
    • Minor, P.1    Newham, J.2    Jones, N.3
  • 258
    • 0037025370 scopus 로고    scopus 로고
    • Cell surface accumulation of a truncated transmembrane prion protein in Gerstmann-Straussler-Scheinker disease P102L
    • Mishra RS, Gu Y, Bose S, et al. Cell surface accumulation of a truncated transmembrane prion protein in Gerstmann-Straussler-Scheinker disease P102L. J Biol Chem 2002;277:24554-24561.
    • (2002) J Biol Chem , vol.277 , pp. 24554-24561
    • Mishra, R.S.1    Gu, Y.2    Bose, S.3
  • 259
    • 0035957003 scopus 로고    scopus 로고
    • Two different neurodegenerative diseases caused by proteins with similar structures
    • Mo H, Moore RC, Cohen FE, et al. Two different neurodegenerative diseases caused by proteins with similar structures. Proc Natl Acad Sci U S A 2001;98:2352-2357.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2352-2357
    • Mo, H.1    Moore, R.C.2    Cohen, F.E.3
  • 260
    • 0031942579 scopus 로고    scopus 로고
    • Mice with gene targetted prion protein alterations show that Prnp, Sinc and Prni are congruent
    • Moore RC, Hope J, McBride PA, et al. Mice with gene targetted prion protein alterations show that Prnp, Sinc and Prni are congruent. Nat Genet 1998;18:118-125.
    • (1998) Nat Genet , vol.18 , pp. 118-125
    • Moore, R.C.1    Hope, J.2    McBride, P.A.3
  • 261
    • 0033215478 scopus 로고    scopus 로고
    • Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel
    • Moore RC, Lee IY, Silverman GL, et al. Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J Mol Biol 1999;292:797-817.
    • (1999) J Mol Biol , vol.292 , pp. 797-817
    • Moore, R.C.1    Lee, I.Y.2    Silverman, G.L.3
  • 262
  • 263
    • 84870067233 scopus 로고    scopus 로고
    • De novo induction of amyloid-β deposition in vivo
    • Morales R, Duran-Aniotz C, Castilla J, et al. De novo induction of amyloid-β deposition in vivo. Mol Psychiatry 2012;17(12)1347-1353.
    • (2012) Mol Psychiatry , vol.17 , Issue.12 , pp. 1347-1353
    • Morales, R.1    Duran-Aniotz, C.2    Castilla, J.3
  • 264
    • 84863433677 scopus 로고    scopus 로고
    • Prion-like acceleration of a synucleinopathy in a transgenic mouse model
    • Mougenot AL, Nicot S, Bencsik A, et al. Prion-like acceleration of a synucleinopathy in a transgenic mouse model. Neurobiol Aging 2012;33(9):2225-2228.
    • (2012) Neurobiol Aging , vol.33 , Issue.9 , pp. 2225-2228
    • Mougenot, A.L.1    Nicot, S.2    Bencsik, A.3
  • 265
  • 266
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Münch C, O'Brien J, Bertolotti A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci U S A 2011;108:3548-3553.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3548-3553
    • Münch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 267
    • 0030811015 scopus 로고    scopus 로고
    • Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an α-helix
    • Muramoto T, DeArmond SJ, Scott M, et al. Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an α-helix. Nat Med 1997;3:750-755.
    • (1997) Nat Med , vol.3 , pp. 750-755
    • Muramoto, T.1    DeArmond, S.J.2    Scott, M.3
  • 268
    • 22744448690 scopus 로고    scopus 로고
    • Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice
    • Nazor KE, Kuhn F, Seward T, et al. Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice. EMBO J 2005;24:2472-2480.
    • (2005) EMBO J , vol.24 , pp. 2472-2480
    • Nazor, K.E.1    Kuhn, F.2    Seward, T.3
  • 269
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-beta spine of amyloid-like fibrils
    • Nelson R, Sawaya MR, Balbirnie M, et al. Structure of the cross-beta spine of amyloid-like fibrils. Nature 2005;435:773-778.
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3
  • 270
    • 70349766369 scopus 로고    scopus 로고
    • Detection of protease-resistant cervid prion protein in water from a CWD-endemic area
    • Nichols TA, Pulford B, Wyckoff AC, et al. Detection of protease-resistant cervid prion protein in water from a CWD-endemic area. Prion 2009;3:171-183.
    • (2009) Prion , vol.3 , pp. 171-183
    • Nichols, T.A.1    Pulford, B.2    Wyckoff, A.C.3
  • 271
    • 1542297705 scopus 로고    scopus 로고
    • In vitro prion protein conversion in detergent-solubilized membranes
    • Nishina K, Deleault NR, Lucassen RW, et al. In vitro prion protein conversion in detergent-solubilized membranes. Biochemistry 2004;43:2613-2621.
    • (2004) Biochemistry , vol.43 , pp. 2613-2621
    • Nishina, K.1    Deleault, N.R.2    Lucassen, R.W.3
  • 272
    • 33751572491 scopus 로고    scopus 로고
    • The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro
    • Nishina KA, Deleault NR, Mahal SP, et al. The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. Biochemistry 2006;45:14129-14139.
    • (2006) Biochemistry , vol.45 , pp. 14129-14139
    • Nishina, K.A.1    Deleault, N.R.2    Mahal, S.P.3
  • 273
    • 0030990920 scopus 로고    scopus 로고
    • PrP genotypes and experimental scrapie in orally inoculated Suffolk sheep in the United States
    • O'Rourke KI, Holyoak GR, Clark WW, et al. PrP genotypes and experimental scrapie in orally inoculated Suffolk sheep in the United States. J Gen Virol 1997;78:975-978.
    • (1997) J Gen Virol , vol.78 , pp. 975-978
    • O'Rourke, K.I.1    Holyoak, G.R.2    Clark, W.W.3
  • 274
    • 0022005315 scopus 로고
    • A cellular gene encodes scrapie PrP 27-30 protein
    • Oesch B, Westaway D, Wälchli M, et al. A cellular gene encodes scrapie PrP 27-30 protein. Cell 1985;40:735-746.
    • (1985) Cell , vol.40 , pp. 735-746
    • Oesch, B.1    Westaway, D.2    Wälchli, M.3
  • 275
  • 276
    • 82655180378 scopus 로고    scopus 로고
    • Chronic traumatic encephalopathy in an Iraqi war veteran with posttraumatic stress disorder who committed suicide
    • Omalu B, Hammers JL, Bailes J, et al. Chronic traumatic encephalopathy in an Iraqi war veteran with posttraumatic stress disorder who committed suicide. Neurosurg Focus 2011;31:E3.
    • (2011) Neurosurg Focus , vol.31 , pp. E3
    • Omalu, B.1    Hammers, J.L.2    Bailes, J.3
  • 277
    • 21744449747 scopus 로고    scopus 로고
    • Chronic traumatic encephalopathy in a National Football League player
    • Omalu BI, DeKosky ST, Minster RL, et al. Chronic traumatic encephalopathy in a National Football League player. Neurosurgery 2005;57:128-134.
    • (2005) Neurosurgery , vol.57 , pp. 128-134
    • Omalu, B.I.1    DeKosky, S.T.2    Minster, R.L.3
  • 278
    • 2442639172 scopus 로고    scopus 로고
    • Male infertility and DNA damage in Doppel knockout and prion protein/Doppel double-knockout mice
    • Paisley D, Banks S, Selfridge J, et al. Male infertility and DNA damage in Doppel knockout and prion protein/Doppel double-knockout mice. Am J Pathol 2004;164:2279-2288.
    • (2004) Am J Pathol , vol.164 , pp. 2279-2288
    • Paisley, D.1    Banks, S.2    Selfridge, J.3
  • 279
    • 0025820942 scopus 로고
    • Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease
    • Palmer MS, Dryden AJ, Hughes JT, et al. Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 1991;352:340-342.
    • (1991) Nature , vol.352 , pp. 340-342
    • Palmer, M.S.1    Dryden, A.J.2    Hughes, J.T.3
  • 280
    • 0027332116 scopus 로고
    • Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
    • Pan K-M, Baldwin M, Nguyen J, et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci U S A 1993;90:10962-10966.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10962-10966
    • Pan, K.-M.1    Baldwin, M.2    Nguyen, J.3
  • 281
    • 30144435044 scopus 로고    scopus 로고
    • NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles
    • Papadopoulos E, Oglecka K, Maler L, et al. NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles. Biochemistry 2006;45:159-166.
    • (2006) Biochemistry , vol.45 , pp. 159-166
    • Papadopoulos, E.1    Oglecka, K.2    Maler, L.3
  • 284
    • 0002977863 scopus 로고
    • Scrapie: a transmissible and hereditary disease of sheep
    • Parry HB. Scrapie: a transmissible and hereditary disease of sheep. Heredity 1962;17:75-105.
    • (1962) Heredity , vol.17 , pp. 75-105
    • Parry, H.B.1
  • 285
    • 0001074386 scopus 로고
    • Experiments with scrapie with special reference to the nature of the agent and the pathology of the disease
    • Gajdusek DC, Gibbs CJ Jr, Alpers MP, eds, Washington, D.C: Government Printing
    • Pattison IH. Experiments with scrapie with special reference to the nature of the agent and the pathology of the disease. In: Gajdusek DC, Gibbs CJ Jr, Alpers MP, eds. Slow, Latent and Temperate Virus Infections, NINDB Monograph 2. U.S. Washington, D.C: Government Printing; 1965:249-257.
    • (1965) Slow, Latent and Temperate Virus Infections, NINDB Monograph 2. U.S , pp. 249-257
    • Pattison, I.H.1
  • 286
    • 0015090051 scopus 로고
    • Clinical and histological observations on cuprizone toxicity and scrapie in mice
    • Pattison IH, Jebbett JN. Clinical and histological observations on cuprizone toxicity and scrapie in mice. Res Vet Sci 1971;12:378-380.
    • (1971) Res Vet Sci , vol.12 , pp. 378-380
    • Pattison, I.H.1    Jebbett, J.N.2
  • 287
    • 84961034678 scopus 로고
    • Scrapie produced experimentally in goats with special reference to the clinical syndrome
    • Pattison IH, Millson GC. Scrapie produced experimentally in goats with special reference to the clinical syndrome. J Comp Pathol 1961;71:101-108.
    • (1961) J Comp Pathol , vol.71 , pp. 101-108
    • Pattison, I.H.1    Millson, G.C.2
  • 288
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • Peden AH, Head MW, Ritchie DL, et al. Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 2004;364:527-529.
    • (2004) Lancet , vol.364 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3
  • 289
    • 33645959487 scopus 로고    scopus 로고
    • Inactivation of prions by acidic sodium dodecyl sulfate
    • Peretz D, Supattapone S, Giles K, et al. Inactivation of prions by acidic sodium dodecyl sulfate. J Virol 2006;80:322-331.
    • (2006) J Virol , vol.80 , pp. 322-331
    • Peretz, D.1    Supattapone, S.2    Giles, K.3
  • 290
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D, Williamson RA, Kaneko K, et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 2001;412:739-743.
    • (2001) Nature , vol.412 , pp. 739-743
    • Peretz, D.1    Williamson, R.A.2    Kaneko, K.3
  • 291
    • 0037071874 scopus 로고    scopus 로고
    • A change in the conformation of prions accompanies the emergence of a new prion strain
    • Peretz D, Williamson RA, Legname G, et al. A change in the conformation of prions accompanies the emergence of a new prion strain. Neuron 2002;34:921-932.
    • (2002) Neuron , vol.34 , pp. 921-932
    • Peretz, D.1    Williamson, R.A.2    Legname, G.3
  • 292
    • 0031592937 scopus 로고    scopus 로고
    • A conformational transition at the N-terminus of the prion protein features in formation of the scrapie isoform
    • Peretz D, Williamson RA, Matsunaga Y, et al. A conformational transition at the N-terminus of the prion protein features in formation of the scrapie isoform. J Mol Biol 1997;273:614-622.
    • (1997) J Mol Biol , vol.273 , pp. 614-622
    • Peretz, D.1    Williamson, R.A.2    Matsunaga, Y.3
  • 293
    • 77953808355 scopus 로고    scopus 로고
    • Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein
    • Pérez DR, Damberger FF, Wüthrich K. Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein. J Mol Biol 2010;400:121-128.
    • (2010) J Mol Biol , vol.400 , pp. 121-128
    • Pérez, D.R.1    Damberger, F.F.2    Wüthrich, K.3
  • 294
    • 0036791019 scopus 로고    scopus 로고
    • Dominant-negative inhibition of prion replication in transgenic mice
    • Perrier V, Kaneko K, Safar J, et al. Dominant-negative inhibition of prion replication in transgenic mice. Proc Natl Acad Sci U S A 2002;99:13079-13084.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13079-13084
    • Perrier, V.1    Kaneko, K.2    Safar, J.3
  • 295
    • 0034705043 scopus 로고    scopus 로고
    • Mimicking dominant negative inhibition of prion replication through structure-based drug design
    • Perrier V, Wallace AC, Kaneko K, et al. Mimicking dominant negative inhibition of prion replication through structure-based drug design. Proc Natl Acad Sci U S A 2000;97:6073-6078.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6073-6078
    • Perrier, V.1    Wallace, A.C.2    Kaneko, K.3
  • 296
    • 33845346122 scopus 로고    scopus 로고
    • Lentivector-mediated RNAi efficiently suppresses prion protein and prolongs survival of scrapie-infected mice
    • Pfeifer A, Eigenbrod S, Al-Khadra S, et al. Lentivector-mediated RNAi efficiently suppresses prion protein and prolongs survival of scrapie-infected mice. J Clin Invest 2006;116:3204-3210.
    • (2006) J Clin Invest , vol.116 , pp. 3204-3210
    • Pfeifer, A.1    Eigenbrod, S.2    Al-Khadra, S.3
  • 298
    • 9944257937 scopus 로고    scopus 로고
    • Breakage of PrP aggregates is essential for efficient autocatalytic propagation of misfolded prion protein
    • Piening N, Weber P, Giese A, et al. Breakage of PrP aggregates is essential for efficient autocatalytic propagation of misfolded prion protein. Biochem Biophys Res Commun 2005;326:339-343.
    • (2005) Biochem Biophys Res Commun , vol.326 , pp. 339-343
    • Piening, N.1    Weber, P.2    Giese, A.3
  • 299
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, et al. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 1997;276:2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3
  • 300
    • 79960982077 scopus 로고    scopus 로고
    • A survey of antiprion compounds reveals the prevalence of non-PrP molecular targets
    • Poncet-Montange G, St.-Martin SJ, Bogatova OV, et al. A survey of antiprion compounds reveals the prevalence of non-PrP molecular targets. J Biol Chem 2011;286:27718-27728.
    • (2011) J Biol Chem , vol.286 , pp. 27718-27728
    • Poncet-Montange, G.1    St-Martin, S.J.2    Bogatova, O.V.3
  • 301
    • 28444477767 scopus 로고    scopus 로고
    • Neurotoxicity but not infectivity of prion proteins can be induced reversibly in vitro
    • Post K, Brown DR, Groschup M, et al. Neurotoxicity but not infectivity of prion proteins can be induced reversibly in vitro. Arch Virol Suppl 2000;(16):265-273.
    • (2000) Arch Virol Suppl , Issue.16 , pp. 265-273
    • Post, K.1    Brown, D.R.2    Groschup, M.3
  • 302
    • 0026636605 scopus 로고
    • Inherited prion disease with 144 base pair gene insertion. 1. Genealogical and molecular studies
    • Poulter M, Baker HF, Frith CD, et al. Inherited prion disease with 144 base pair gene insertion. 1. Genealogical and molecular studies. Brain 1992;115:675-685.
    • (1992) Brain , vol.115 , pp. 675-685
    • Poulter, M.1    Baker, H.F.2    Frith, C.D.3
  • 303
    • 0141760321 scopus 로고    scopus 로고
    • Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein
    • Premzl M, Sangiorgio L, Strumbo B, et al. Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein. Gene 2003;314:89-102.
    • (2003) Gene , vol.314 , pp. 89-102
    • Premzl, M.1    Sangiorgio, L.2    Strumbo, B.3
  • 304
    • 0034711993 scopus 로고    scopus 로고
    • Porphyrin and phthalocyanine antiscrapie compounds
    • Priola SA, Raines A, Caughey WS. Porphyrin and phthalocyanine antiscrapie compounds. Science 2000;287:1503-1506.
    • (2000) Science , vol.287 , pp. 1503-1506
    • Priola, S.A.1    Raines, A.2    Caughey, W.S.3
  • 305
    • 0036902277 scopus 로고    scopus 로고
    • Prion-protein-specific aptamer reduces PrPSc formation
    • Proske D, Gilch S, Wopfner F, et al. Prion-protein-specific aptamer reduces PrPSc formation. Chembiochem 2002;3:717-725.
    • (2002) Chembiochem , vol.3 , pp. 717-725
    • Proske, D.1    Gilch, S.2    Wopfner, F.3
  • 306
    • 3142624750 scopus 로고    scopus 로고
    • Detecting mad cow disease
    • Prusiner SB. Detecting mad cow disease. Sci Am 2004;291:86-93.
    • (2004) Sci Am , vol.291 , pp. 86-93
    • Prusiner, S.B.1
  • 307
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB. Molecular biology of prion diseases. Science 1991;252:1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 308
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982;216:136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 309
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner SB. Prion diseases and the BSE crisis. Science 1997;278:245-251.
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 310
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck Lecture-Neurodegenerative diseases and prions
    • Prusiner SB. Shattuck Lecture-Neurodegenerative diseases and prions. N Engl J Med 2001;344:1516-1526.
    • (2001) N Engl J Med , vol.344 , pp. 1516-1526
    • Prusiner, S.B.1
  • 311
    • 0021344124 scopus 로고
    • Some speculations about prions, amyloid, and Alzheimer's disease
    • Prusiner SB. Some speculations about prions, amyloid, and Alzheimer's disease. N Engl J Med 1984;310:661-663.
    • (1984) N Engl J Med , vol.310 , pp. 661-663
    • Prusiner, S.B.1
  • 312
    • 0027491308 scopus 로고
    • Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies
    • Prusiner SB, Groth D, Serban A, et al. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc Natl Acad Sci U S A 1993;90:10608-10612.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10608-10612
    • Prusiner, S.B.1    Groth, D.2    Serban, A.3
  • 313
    • 0018188825 scopus 로고
    • Partial purification and evidence for multiple molecular forms of the scrapie agent
    • Prusiner SB, Hadlow WJ, Garfin DE, et al. Partial purification and evidence for multiple molecular forms of the scrapie agent. Biochemistry 1978;17:4993-4997.
    • (1978) Biochemistry , vol.17 , pp. 4993-4997
    • Prusiner, S.B.1    Hadlow, W.J.2    Garfin, D.E.3
  • 314
    • 0001685843 scopus 로고
    • Prions: methods for assay, purification and characterization
    • Maramorosch K, Koprowski H, eds, New York: Academic Press
    • Prusiner SB, McKinley MP, Bolton DC, et al. Prions: methods for assay, purification and characterization. In: Maramorosch K, Koprowski H, eds. Methods in Virology. vol. 8. New York: Academic Press; 1984:293-345.
    • (1984) Methods in Virology , vol.8 , pp. 293-345
    • Prusiner, S.B.1    McKinley, M.P.2    Bolton, D.C.3
  • 315
    • 0021019026 scopus 로고
    • Scrapie prions aggregate to form amyloid-like birefringent rods
    • Prusiner SB, McKinley MP, Bowman KA, et al. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 1983;35:349-358.
    • (1983) Cell , vol.35 , pp. 349-358
    • Prusiner, S.B.1    McKinley, M.P.2    Bowman, K.A.3
  • 316
    • 0025244011 scopus 로고
    • Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication
    • Prusiner SB, Scott M, Foster D, et al. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 1990;63:673-686.
    • (1990) Cell , vol.63 , pp. 673-686
    • Prusiner, S.B.1    Scott, M.2    Foster, D.3
  • 317
    • 0842282785 scopus 로고    scopus 로고
    • Inactivation of transmissible spongiform encephalopathy (prion) agents by environ LpH
    • Race RE, Raymond GJ. Inactivation of transmissible spongiform encephalopathy (prion) agents by environ LpH. J Virol 2004;78:2164-2165.
    • (2004) J Virol , vol.78 , pp. 2164-2165
    • Race, R.E.1    Raymond, G.J.2
  • 318
    • 0033616564 scopus 로고    scopus 로고
    • Ectopic expression of prion protein (PrP) in T lymphocytes or hepatocytes of PrP knockout mice is insufficient to sustain prion replication
    • Raeber AJ, Sailer A, Hegyi I, et al. Ectopic expression of prion protein (PrP) in T lymphocytes or hepatocytes of PrP knockout mice is insufficient to sustain prion replication. Proc Natl Acad Sci U S A 1999;96:3987-3992.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3987-3992
    • Raeber, A.J.1    Sailer, A.2    Hegyi, I.3
  • 319
    • 0033998048 scopus 로고    scopus 로고
    • Nuclear Notch1 signaling and the regulation of dendritic development
    • Redmond L, Oh SR, Hicks C, et al. Nuclear Notch1 signaling and the regulation of dendritic development. Nat Neurosci 2000;3:30-40.
    • (2000) Nat Neurosci , vol.3 , pp. 30-40
    • Redmond, L.1    Oh, S.R.2    Hicks, C.3
  • 320
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren PH, Lauckner JE, Kachirskaia I, et al. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 2009;11:219-225.
    • (2009) Nat Cell Biol , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3
  • 321
    • 0035912772 scopus 로고    scopus 로고
    • Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein
    • Requena JR, Groth D, Legname G, et al. Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein. Proc Natl Acad Sci U S A 2001;98:7170-7175.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 7170-7175
    • Requena, J.R.1    Groth, D.2    Legname, G.3
  • 322
    • 0031436335 scopus 로고    scopus 로고
    • The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells
    • Rieger R, Edenhofer F, Lasmézas CI, et al. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat Med 1997;3:1383-1388.
    • (1997) Nat Med , vol.3 , pp. 1383-1388
    • Rieger, R.1    Edenhofer, F.2    Lasmézas, C.I.3
  • 323
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Riek R, Hornemann S, Wider G, et al. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 1997;413:282-288.
    • (1997) FEBS Lett , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3
  • 324
    • 0029937271 scopus 로고    scopus 로고
    • NMR structure of the mouse prion protein domain PrP(121-231)
    • Riek R, Hornemann S, Wider G, et al. NMR structure of the mouse prion protein domain PrP(121-231). Nature 1996;382:180-182.
    • (1996) Nature , vol.382 , pp. 180-182
    • Riek, R.1    Hornemann, S.2    Wider, G.3
  • 325
    • 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, Oidtmann B, Panagiotidis CH, et al. Disparate evolution of prion protein domains and the distinct origin of Doppel-and prion-related loci revealed by fish-to-mammal comparisons. FASEB J 2006;20:317-319.
    • (2006) FASEB J , vol.20 , pp. 317-319
    • Rivera-Milla, E.1    Oidtmann, B.2    Panagiotidis, C.H.3
  • 326
    • 0027520888 scopus 로고
    • Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells
    • Rogers M, Yehiely F, Scott M, et al. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc Natl Acad Sci U S A 1993;90:3182-3186.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3182-3186
    • Rogers, M.1    Yehiely, F.2    Scott, M.3
  • 327
    • 57849162808 scopus 로고    scopus 로고
    • Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein alpha 2-helical 180-195 segment, and comparison with full-length alpha 2-helix-derived peptides
    • Ronga L, Palladino P, Saviano G, et al. Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein alpha 2-helical 180-195 segment, and comparison with full-length alpha 2-helix-derived peptides. J Pept Sci 2008;14:1096-1102.
    • (2008) J Pept Sci , vol.14 , pp. 1096-1102
    • Ronga, L.1    Palladino, P.2    Saviano, G.3
  • 328
    • 0015549846 scopus 로고
    • The clinical characteristics of transmissible Creutzfeldt-Jakob disease
    • Roos R, Gajdusek DC, Gibbs CJ Jr. The clinical characteristics of transmissible Creutzfeldt-Jakob disease. Brain 1973;96:1-20.
    • (1973) Brain , vol.96 , pp. 1-20
    • Roos, R.1    Gajdusek, D.C.2    Gibbs, C.J.3
  • 329
    • 0035865398 scopus 로고    scopus 로고
    • Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain
    • Rossi D, Cozzio A, Flechsig E, et al. Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO J 2001;20:694-702.
    • (2001) EMBO J , vol.20 , pp. 694-702
    • Rossi, D.1    Cozzio, A.2    Flechsig, E.3
  • 330
    • 0038340656 scopus 로고    scopus 로고
    • Differential inhibition of prion propagation by enantiomers of quinacrine
    • Ryou C, Legname G, Peretz D, et al. Differential inhibition of prion propagation by enantiomers of quinacrine. Lab Invest 2003;83:837-843.
    • (2003) Lab Invest , vol.83 , pp. 837-843
    • Ryou, C.1    Legname, G.2    Peretz, D.3
  • 331
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001;411:810-813.
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 332
    • 0033542142 scopus 로고    scopus 로고
    • Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone
    • Saborío GP, Soto C, Kascsak RJ, et al. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem Biophys Res Commun 1999;258:470-475.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 470-475
    • Saborío, G.P.1    Soto, C.2    Kascsak, R.J.3
  • 333
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrPSc molecules with different conformations
    • Safar J, Wille H, Itri V, et al. Eight prion strains have PrPSc molecules with different conformations. Nat Med 1998;4:1157-1165.
    • (1998) Nat Med , vol.4 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3
  • 336
    • 23244431836 scopus 로고    scopus 로고
    • Search for a prion-specific nucleic acid
    • Safar JG, Kellings K, Serban A, et al. Search for a prion-specific nucleic acid. J Virol 2005;79:10796-10806.
    • (2005) J Virol , vol.79 , pp. 10796-10806
    • Safar, J.G.1    Kellings, K.2    Serban, A.3
  • 337
    • 0036843448 scopus 로고    scopus 로고
    • Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice
    • Safar JG, Scott M, Monaghan J, et al. Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice. Nat Biotechnol 2002;20:1147-1150.
    • (2002) Nat Biotechnol , vol.20 , pp. 1147-1150
    • Safar, J.G.1    Scott, M.2    Monaghan, J.3
  • 338
    • 13344282734 scopus 로고    scopus 로고
    • Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene
    • Sakaguchi S, Katamine S, Nishida N, et al. Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 1996;380:528-531.
    • (1996) Nature , vol.380 , pp. 528-531
    • Sakaguchi, S.1    Katamine, S.2    Nishida, N.3
  • 339
    • 0036457102 scopus 로고    scopus 로고
    • Developmental expression of the cellular prion protein in elongating axons
    • Sales N, Hassig R, Rodolfo K, et al. Developmental expression of the cellular prion protein in elongating axons. Eur J Neurosci 2002;15:1163-1177.
    • (2002) Eur J Neurosci , vol.15 , pp. 1163-1177
    • Sales, N.1    Hassig, R.2    Rodolfo, K.3
  • 340
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • Sandberg MK, Al-Doujaily H, Sharps B, et al. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 2011;470:540-542.
    • (2011) Nature , vol.470 , pp. 540-542
    • Sandberg, M.K.1    Al-Doujaily, H.2    Sharps, B.3
  • 341
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione A, Sytnyk V, Leshchyns'ka I, et al. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J Cell Biol 2005;169:341-354.
    • (2005) J Cell Biol , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'ka, I.3
  • 342
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R, et al. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 2007;447:453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3
  • 343
    • 70349669073 scopus 로고    scopus 로고
    • Evolutionary descent of prion genes from the ZIP family of metal ion transporters
    • Schmitt-Ulms G, Ehsani S, Watts JC, et al. Evolutionary descent of prion genes from the ZIP family of metal ion transporters. PLoS One 2009;4:e7208.
    • (2009) PLoS One , vol.4 , pp. e7208
    • Schmitt-Ulms, G.1    Ehsani, S.2    Watts, J.C.3
  • 344
    • 2542583141 scopus 로고    scopus 로고
    • Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues
    • Schmitt-Ulms G, Hansen K, Liu J, et al. Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues. Nat Biotechnol 2004;22:724-731.
    • (2004) Nat Biotechnol , vol.22 , pp. 724-731
    • Schmitt-Ulms, G.1    Hansen, K.2    Liu, J.3
  • 345
    • 0035861987 scopus 로고    scopus 로고
    • Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein
    • Schmitt-Ulms G, Legname G, Baldwin MA, et al. Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein. J Mol Biol 2001;314:1209-1225.
    • (2001) J Mol Biol , vol.314 , pp. 1209-1225
    • Schmitt-Ulms, G.1    Legname, G.2    Baldwin, M.A.3
  • 346
    • 0345687168 scopus 로고    scopus 로고
    • NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells
    • Schneider B, Mutel V, Pietri M, et al. NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells. Proc Natl Acad Sci U S A 2003;100:13326-13331.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13326-13331
    • Schneider, B.1    Mutel, V.2    Pietri, M.3
  • 347
  • 348
    • 0024820814 scopus 로고
    • Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques
    • Scott M, Foster D, Mirenda C, et al. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 1989;59:847-857.
    • (1989) Cell , vol.59 , pp. 847-857
    • Scott, M.1    Foster, D.2    Mirenda, C.3
  • 349
    • 0030731124 scopus 로고    scopus 로고
    • Propagation of prion strains through specific conformers of the prion protein
    • Scott MR, Groth D, Tatzelt J, et al. Propagation of prion strains through specific conformers of the prion protein. J Virol 1997;71:9032-9044.
    • (1997) J Virol , vol.71 , pp. 9032-9044
    • Scott, M.R.1    Groth, D.2    Tatzelt, J.3
  • 350
    • 17444393595 scopus 로고    scopus 로고
    • Transmission barriers for bovine, ovine, and human prions in transgenic mice
    • Scott MR, Peretz D, Nguyen HO, et al. Transmission barriers for bovine, ovine, and human prions in transgenic mice. J Virol 2005;79:5259-5271.
    • (2005) J Virol , vol.79 , pp. 5259-5271
    • Scott, M.R.1    Peretz, D.2    Nguyen, H.O.3
  • 351
    • 13144275223 scopus 로고    scopus 로고
    • Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice
    • Scott MR, Safar J, Telling G, et al. Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice. Proc Natl Acad Sci U S A 1997;94:14279-14284.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 14279-14284
    • Scott, M.R.1    Safar, J.2    Telling, G.3
  • 352
    • 0033592877 scopus 로고    scopus 로고
    • Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans
    • Scott MR, Will R, Ironside J, et al. Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans. Proc Natl Acad Sci U S A 1999;96:15137-15142.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 15137-15142
    • Scott, M.R.1    Will, R.2    Ironside, J.3
  • 353
    • 10344257549 scopus 로고    scopus 로고
    • Immunoglobulins in urine of hamsters with scrapie
    • Serban A, Legname G, Hansen K, et al. Immunoglobulins in urine of hamsters with scrapie. J Biol Chem 2004;279:48817-48820.
    • (2004) J Biol Chem , vol.279 , pp. 48817-48820
    • Serban, A.1    Legname, G.2    Hansen, K.3
  • 354
    • 0025103308 scopus 로고
    • Rapid detection of Creutzfeldt-Jakob disease and scrapie prion proteins
    • Serban D, Taraboulos A, DeArmond SJ, et al. Rapid detection of Creutzfeldt-Jakob disease and scrapie prion proteins. Neurology 1990;40:110-117.
    • (1990) Neurology , vol.40 , pp. 110-117
    • Serban, D.1    Taraboulos, A.2    DeArmond, S.J.3
  • 355
    • 0037143011 scopus 로고    scopus 로고
    • Postexposure prophylaxis against prion disease with a stimulator of innate immunity
    • Sethi S, Lipford G, Wagner H, et al. Postexposure prophylaxis against prion disease with a stimulator of innate immunity. Lancet 2002;360:229-230.
    • (2002) Lancet , vol.360 , pp. 229-230
    • Sethi, S.1    Lipford, G.2    Wagner, H.3
  • 356
    • 0036128896 scopus 로고    scopus 로고
    • Shedding light on proteins, nucleic acids, cells, humans and fish
    • Setlow RB. Shedding light on proteins, nucleic acids, cells, humans and fish. Mutat Res 2002;511:1-14.
    • (2002) Mutat Res , vol.511 , pp. 1-14
    • Setlow, R.B.1
  • 357
    • 0035943651 scopus 로고    scopus 로고
    • A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases
    • Shaked GM, Shaked Y, Kariv-Inbal Z, et al. A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases. J Biol Chem 2001;276:31479-31482.
    • (2001) J Biol Chem , vol.276 , pp. 31479-31482
    • Shaked, G.M.1    Shaked, Y.2    Kariv-Inbal, Z.3
  • 358
    • 77951996350 scopus 로고    scopus 로고
    • Coinfecting prion strains compete for a limiting cellular resource
    • Shikiya RA, Ayers JI, Schutt CR, et al. Coinfecting prion strains compete for a limiting cellular resource. J Virol 2010;84:5706-5714.
    • (2010) J Virol , vol.84 , pp. 5706-5714
    • Shikiya, R.A.1    Ayers, J.I.2    Schutt, C.R.3
  • 359
    • 0001552281 scopus 로고    scopus 로고
    • Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions
    • Shmerling D, Hegyi I, Fischer M, et al. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 1998;93:203-214.
    • (1998) Cell , vol.93 , pp. 203-214
    • Shmerling, D.1    Hegyi, I.2    Fischer, M.3
  • 360
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 2004;304:1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 361
    • 75749134925 scopus 로고    scopus 로고
    • Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation
    • Si K, Choi YB, White-Grindley E, et al. Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation. Cell 2010;140:421-435.
    • (2010) Cell , vol.140 , pp. 421-435
    • Si, K.1    Choi, Y.B.2    White-Grindley, E.3
  • 362
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • Si K, Lindquist S, Kandel ER. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 2003;115:879-891.
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 363
    • 0001168222 scopus 로고
    • Rida, a chronic encephalitis of sheep with general remarks on infections which develop slowly and some of their special characteristics
    • Sigurdsson B. Rida, a chronic encephalitis of sheep with general remarks on infections which develop slowly and some of their special characteristics. Br Vet J 1954;110:341-354.
    • (1954) Br Vet J , vol.110 , pp. 341-354
    • Sigurdsson, B.1
  • 364
    • 0037461583 scopus 로고    scopus 로고
    • Anti-prion antibodies for prophylaxis following prion exposure in mice
    • Sigurdsson EM, Sy MS, Li R, et al. Anti-prion antibodies for prophylaxis following prion exposure in mice. Neurosci Lett 2003;336:185-187.
    • (2003) Neurosci Lett , vol.336 , pp. 185-187
    • Sigurdsson, E.M.1    Sy, M.S.2    Li, R.3
  • 365
    • 24644448839 scopus 로고    scopus 로고
    • The most infectious prion protein particles
    • Silveira JR, Raymond GJ, Hughson AG, et al. The most infectious prion protein particles. Nature 2005;437:257-261.
    • (2005) Nature , vol.437 , pp. 257-261
    • Silveira, J.R.1    Raymond, G.J.2    Hughson, A.G.3
  • 366
    • 0242300619 scopus 로고    scopus 로고
    • α-Synuclein locus triplication causes Parkinson's disease
    • Singleton AB, Farrer M, Johnson J, et al. α-Synuclein locus triplication causes Parkinson's disease. Science 2003;302:841.
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1    Farrer, M.2    Johnson, J.3
  • 367
    • 79953785159 scopus 로고    scopus 로고
    • Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange
    • Smirnovas V, Baron GS, Offerdahl DK, et al. Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol 2011;18:504-506.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 504-506
    • Smirnovas, V.1    Baron, G.S.2    Offerdahl, D.K.3
  • 369
  • 370
    • 0011888936 scopus 로고
    • Assignment of the human and mouse prion protein genes to homologous chromosomes
    • Sparkes RS, Simon M, Cohn VH, et al. Assignment of the human and mouse prion protein genes to homologous chromosomes. Proc Natl Acad Sci U S A 1986;83:7358-7362.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 7358-7362
    • Sparkes, R.S.1    Simon, M.2    Cohn, V.H.3
  • 371
    • 0034725747 scopus 로고    scopus 로고
    • Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein
    • Sparrer HE, Santoso A, Szoka FC Jr, et al. Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein. Science 2000;289:595-599.
    • (2000) Science , vol.289 , pp. 595-599
    • Sparrer, H.E.1    Santoso, A.2    Szoka, F.C.3
  • 372
    • 0028981199 scopus 로고
    • Complete penetrance of Creutzfeldt-Jakob disease in Libyan Jews carrying the E200K mutation in the prion protein gene
    • Spudich S, Mastrianni JA, Wrensch M, et al. Complete penetrance of Creutzfeldt-Jakob disease in Libyan Jews carrying the E200K mutation in the prion protein gene. Mol Med 1995;1:607-613.
    • (1995) Mol Med , vol.1 , pp. 607-613
    • Spudich, S.1    Mastrianni, J.A.2    Wrensch, M.3
  • 373
    • 0025091084 scopus 로고
    • Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein
    • Stahl N, Baldwin MA, Burlingame AL, et al. Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry 1990;29:8879-8884.
    • (1990) Biochemistry , vol.29 , pp. 8879-8884
    • Stahl, N.1    Baldwin, M.A.2    Burlingame, A.L.3
  • 374
    • 0027534612 scopus 로고
    • Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl N, Baldwin MA, Teplow DB, et al. Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 1993;32:1991-2002.
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3
  • 375
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl N, Borchelt DR, Hsiao K, et al. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 1987;51:229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3
  • 376
    • 7244256224 scopus 로고    scopus 로고
    • Sonication of proteins causes formation of aggregates that resemble amyloid
    • Stathopulos PB, Scholz GA, Hwang YM, et al. Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Sci 2004;13:3017-3027.
    • (2004) Protein Sci , vol.13 , pp. 3017-3027
    • Stathopulos, P.B.1    Scholz, G.A.2    Hwang, Y.M.3
  • 377
    • 66349096914 scopus 로고    scopus 로고
    • Early onset prion disease from octarepeat expansion correlates with copper binding properties
    • Stevens DJ, Walter ED, Rodriguez A, et al. Early onset prion disease from octarepeat expansion correlates with copper binding properties. PLoS Pathog 2009;5:e1000390.
    • (2009) PLoS Pathog , vol.5 , pp. e1000390
    • Stevens, D.J.1    Walter, E.D.2    Rodriguez, A.3
  • 378
    • 0242412541 scopus 로고    scopus 로고
    • Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection
    • Stewart RS, Harris DA. Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection. J Biol Chem 2003;278:45960-45968.
    • (2003) J Biol Chem , vol.278 , pp. 45960-45968
    • Stewart, R.S.1    Harris, D.A.2
  • 379
    • 0037965529 scopus 로고    scopus 로고
    • Prion protein selectively binds copper (II) ions
    • Stöckel J, Safar J, Wallace AC, et al. Prion protein selectively binds copper (II) ions. Biochemistry 1998;37:7185-7193.
    • (1998) Biochemistry , vol.37 , pp. 7185-7193
    • Stöckel, J.1    Safar, J.2    Wallace, A.C.3
  • 380
    • 84855485942 scopus 로고    scopus 로고
    • Spontaneous generation of anchorless prions in transgenic mice
    • Stöhr J, Watts JC, Legname G, et al. Spontaneous generation of anchorless prions in transgenic mice. Proc Natl Acad Sci U S A 2011;08(52):21223-21228.
    • (2011) Proc Natl Acad Sci U S A , vol.8 , Issue.52 , pp. 21223-21228
    • Stöhr, J.1    Watts, J.C.2    Legname, G.3
  • 381
    • 9444229296 scopus 로고    scopus 로고
    • PrPC capping in T cells promotes its association with the lipid raft proteins reggie-1 and reggie-2 and leads to signal transduction
    • Stuermer CA, Langhorst MF, Wiechers MF, et al. PrPC capping in T cells promotes its association with the lipid raft proteins reggie-1 and reggie-2 and leads to signal transduction. FASEB J 2004;18:1731-1733.
    • (2004) FASEB J , vol.18 , pp. 1731-1733
    • Stuermer, C.A.1    Langhorst, M.F.2    Wiechers, M.F.3
  • 382
    • 0021967194 scopus 로고
    • Purification of proteins by IMAC
    • Sulkowski E. Purification of proteins by IMAC. Trends Biotechnol 1985;3:1-7.
    • (1985) Trends Biotechnol , vol.3 , pp. 1-7
    • Sulkowski, E.1
  • 383
    • 0035920226 scopus 로고    scopus 로고
    • Induction of neuronal cell death by Rab5A-dependent endocytosis of alpha-synuclein
    • Sung JY, Kim J, Paik SR, et al. Induction of neuronal cell death by Rab5A-dependent endocytosis of alpha-synuclein. J Biol Chem 2001;276:27441-27448.
    • (2001) J Biol Chem , vol.276 , pp. 27441-27448
    • Sung, J.Y.1    Kim, J.2    Paik, S.R.3
  • 384
    • 0033582935 scopus 로고    scopus 로고
    • Prion protein of 106 residues creates an artificial transmission barrier for prion replication in transgenic mice
    • Supattapone S, Bosque P, Muramoto T, et al. Prion protein of 106 residues creates an artificial transmission barrier for prion replication in transgenic mice. Cell 1999;96:869-878.
    • (1999) Cell , vol.96 , pp. 869-878
    • Supattapone, S.1    Bosque, P.2    Muramoto, T.3
  • 385
    • 0035099885 scopus 로고    scopus 로고
    • A protease-resistant 61-residue prion peptide causes neurodegeneration in transgenic mice
    • Supattapone S, Bouzamondo E, Ball HL, et al. A protease-resistant 61-residue prion peptide causes neurodegeneration in transgenic mice. Mol Cell Biol 2001;21:2608-2616.
    • (2001) Mol Cell Biol , vol.21 , pp. 2608-2616
    • Supattapone, S.1    Bouzamondo, E.2    Ball, H.L.3
  • 386
    • 0035152345 scopus 로고    scopus 로고
    • Identification of two prion protein regions that modify scrapie incubation time
    • Supattapone S, Muramoto T, Legname G, et al. Identification of two prion protein regions that modify scrapie incubation time. J Virol 2001;75:1408-1413.
    • (2001) J Virol , vol.75 , pp. 1408-1413
    • Supattapone, S.1    Muramoto, T.2    Legname, G.3
  • 387
    • 0033460187 scopus 로고    scopus 로고
    • Elimination of prions by branched polyamines and implications for therapeutics
    • Supattapone S, Nguyen H-OB, Cohen FE, et al. Elimination of prions by branched polyamines and implications for therapeutics. Proc Natl Acad Sci U S A 1999;96:14529-14534.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 14529-14534
    • Supattapone, S.1    Nguyen, H.-O.B.2    Cohen, F.E.3
  • 388
    • 0035108195 scopus 로고    scopus 로고
    • Branched polyamines cure prion-infected neuroblastoma cells
    • Supattapone S, Wille H, Uyechi L, et al. Branched polyamines cure prion-infected neuroblastoma cells. J Virol 2001;75:3453-3461.
    • (2001) J Virol , vol.75 , pp. 3453-3461
    • Supattapone, S.1    Wille, H.2    Uyechi, L.3
  • 389
    • 76549125306 scopus 로고    scopus 로고
    • 'Prion-Like' propagation of mouse and human tau aggregates in an inducible mouse model of tauopathy
    • Sydow A, Mandelkow EM. 'Prion-Like' propagation of mouse and human tau aggregates in an inducible mouse model of tauopathy. Neurodegener Dis 2010;7:28-31.
    • (2010) Neurodegener Dis , vol.7 , pp. 28-31
    • Sydow, A.1    Mandelkow, E.M.2
  • 391
    • 33748483636 scopus 로고    scopus 로고
    • Transmission of elk and deer prions to transgenic mice
    • Tamgüney G, Giles K, Bouzamondo-Bernstein E, et al. Transmission of elk and deer prions to transgenic mice. J Virol 2006;80:9104-9114.
    • (2006) J Virol , vol.80 , pp. 9104-9114
    • Tamgüney, G.1    Giles, K.2    Bouzamondo-Bernstein, E.3
  • 392
    • 70349466511 scopus 로고    scopus 로고
    • Asymptomatic deer excrete infectious prions in faeces
    • Tamgüney G, Miller MW, Wolfe LL, et al. Asymptomatic deer excrete infectious prions in faeces. Nature 2009;461:529-532.
    • (2009) Nature , vol.461 , pp. 529-532
    • Tamgüney, G.1    Miller, M.W.2    Wolfe, L.L.3
  • 393
    • 77955127153 scopus 로고    scopus 로고
    • Corrigendum: Asymptomatic deer excrete infectious prions in faeces
    • Tamgüney G, Miller MW, Wolfe LL, et al. Corrigendum: Asymptomatic deer excrete infectious prions in faeces. Nature 2010;466:652.
    • (2010) Nature , vol.466 , pp. 652
    • Tamgüney, G.1    Miller, M.W.2    Wolfe, L.L.3
  • 394
    • 84863393808 scopus 로고    scopus 로고
    • Salivary prions in sheep and deer
    • Tamgüney G, Richt JA, Hamir AN, et al. Salivary prions in sheep and deer. Prion 2012;6(1):52-61.
    • (2012) Prion , vol.6 , Issue.1 , pp. 52-61
    • Tamgüney, G.1    Richt, J.A.2    Hamir, A.N.3
  • 395
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, et al. Conformational variations in an infectious protein determine prion strain differences. Nature 2004;428:323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3
  • 396
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform
    • Taraboulos A, Scott M, Semenov A, et al. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform. J Cell Biol 1995;129:121-132.
    • (1995) J Cell Biol , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3
  • 397
    • 0027741446 scopus 로고
    • Developments in diagnosis for prion diseases
    • Tateishi J, Kitamoto T. Developments in diagnosis for prion diseases. Br Med Bull 1993;49:971-979.
    • (1993) Br Med Bull , vol.49 , pp. 971-979
    • Tateishi, J.1    Kitamoto, T.2
  • 398
    • 73249135395 scopus 로고    scopus 로고
    • Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan
    • Taubner LM, Bienkiewicz EA, Copie V, et al. Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. J Mol Biol 2010;395:475-490.
    • (2010) J Mol Biol , vol.395 , pp. 475-490
    • Taubner, L.M.1    Bienkiewicz, E.A.2    Copie, V.3
  • 399
    • 69249128689 scopus 로고    scopus 로고
    • Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein
    • Taylor DR, Parkin ET, Cocklin SL, et al. Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein. J Biol Chem 2009;284:22590-22600.
    • (2009) J Biol Chem , vol.284 , pp. 22590-22600
    • Taylor, D.R.1    Parkin, E.T.2    Cocklin, S.L.3
  • 400
    • 0029740354 scopus 로고    scopus 로고
    • Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice
    • Telling GC, Haga T, Torchia M, et al. Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes Dev 1996;10:1736-1750.
    • (1996) Genes Dev , vol.10 , pp. 1736-1750
    • Telling, G.C.1    Haga, T.2    Torchia, M.3
  • 401
    • 12644272790 scopus 로고    scopus 로고
    • Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity
    • Telling GC, Parchi P, DeArmond SJ, et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 1996;274:2079-2082.
    • (1996) Science , vol.274 , pp. 2079-2082
    • Telling, G.C.1    Parchi, P.2    DeArmond, S.J.3
  • 402
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling GC, Scott M, Mastrianni J, et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995;83:79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3
  • 403
    • 0038578675 scopus 로고    scopus 로고
    • Efficient and specific down-regulation of prion protein expression by RNAi
    • Tilly G, Chapuis J, Vilette D, et al. Efficient and specific down-regulation of prion protein expression by RNAi. Biochem Biophys Res Commun 2003;305:548-551.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 548-551
    • Tilly, G.1    Chapuis, J.2    Vilette, D.3
  • 404
    • 15844421385 scopus 로고    scopus 로고
    • Altered circadian activity rhythms and sleep in mice devoid of prion protein
    • Tobler I, Gaus SE, Deboer T, et al. Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 1996;380:639-642.
    • (1996) Nature , vol.380 , pp. 639-642
    • Tobler, I.1    Gaus, S.E.2    Deboer, T.3
  • 405
    • 0842304471 scopus 로고    scopus 로고
    • Mutant PrPSc conformers induced by a synthetic peptide and several prion strains
    • Tremblay P, Ball HL, Kaneko K, et al. Mutant PrPSc conformers induced by a synthetic peptide and several prion strains. J Virol 2004;78:2088-2099.
    • (2004) J Virol , vol.78 , pp. 2088-2099
    • Tremblay, P.1    Ball, H.L.2    Kaneko, K.3
  • 406
    • 0032514707 scopus 로고    scopus 로고
    • Doxycyline control of prion protein transgene expression modulates prion disease in mice
    • Tremblay P, Meiner Z, Galou M, et al. Doxycyline control of prion protein transgene expression modulates prion disease in mice. Proc Natl Acad Sci U S A 1998;95:12580-12585.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12580-12585
    • Tremblay, P.1    Meiner, Z.2    Galou, M.3
  • 407
    • 49349110821 scopus 로고    scopus 로고
    • Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases
    • Truant R, Atwal RS, Desmond C, et al. Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases. FEBS J 2008;275:4252-4262.
    • (2008) FEBS J , vol.275 , pp. 4252-4262
    • Truant, R.1    Atwal, R.S.2    Desmond, C.3
  • 408
    • 78651394950 scopus 로고    scopus 로고
    • Implications of the prion-related Q/N domains in TDP-43 and FUS
    • Udan M, Baloh RH. Implications of the prion-related Q/N domains in TDP-43 and FUS. Prion 2011;5:1-5.
    • (2011) Prion , vol.5 , pp. 1-5
    • Udan, M.1    Baloh, R.H.2
  • 409
    • 0035852745 scopus 로고    scopus 로고
    • The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p
    • Umland TC, Taylor KL, Rhee S, et al. The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc Natl Acad Sci U S A 2001;98:1459-1464.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1459-1464
    • Umland, T.C.1    Taylor, K.L.2    Rhee, S.3
  • 410
    • 70349195971 scopus 로고    scopus 로고
    • The consequences of pathogenic mutations to the human prion protein
    • van der Kamp MW, Daggett V. The consequences of pathogenic mutations to the human prion protein. Protein Eng Des Sel 2009;22:461-468.
    • (2009) Protein Eng Des Sel , vol.22 , pp. 461-468
    • van der Kamp, M.W.1    Daggett, V.2
  • 411
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy
    • Van Melckebeke H, Wasmer C, Lange A, et al. Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. J Am Chem Soc 2010;132:13765-13775.
    • (2010) J Am Chem Soc , vol.132 , pp. 13765-13775
    • Van Melckebeke, H.1    Wasmer, C.2    Lange, A.3
  • 412
    • 0035928432 scopus 로고    scopus 로고
    • Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay
    • Wadsworth JD, Joiner S, Hill AF, et al. Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay. Lancet 2001;358:171-180.
    • (2001) Lancet , vol.358 , pp. 171-180
    • Wadsworth, J.D.1    Joiner, S.2    Hill, A.F.3
  • 413
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F, Wang X, Yuan C-G, et al. Generating a prion with bacterially expressed recombinant prion protein. Science 2010;327:1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.-G.3
  • 414
    • 34250158426 scopus 로고    scopus 로고
    • Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions
    • Wang F, Yang F, Hu Y, et al. Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions. Biochemistry 2007;46:7045-7053.
    • (2007) Biochemistry , vol.46 , pp. 7045-7053
    • Wang, F.1    Yang, F.2    Hu, Y.3
  • 415
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
    • Wasmer C, Lange A, Van Melckebeke H, et al. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 2008;319:1523-1526.
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3
  • 416
    • 79952294595 scopus 로고    scopus 로고
    • Bioluminescence imaging of Abeta deposition in bigenic mouse models of Alzheimer's disease
    • Watts JC, Giles K, Grillo SK, et al. Bioluminescence imaging of Abeta deposition in bigenic mouse models of Alzheimer's disease. Proc Natl Acad Sci U S A 2011;108:2528-2533.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2528-2533
    • Watts, J.C.1    Giles, K.2    Grillo, S.K.3
  • 417
    • 81755166672 scopus 로고    scopus 로고
    • Protease-resistant prions selectively decrease Shadoo protein
    • Watts JC, Stöhr J, Bhardwaj S, et al. Protease-resistant prions selectively decrease Shadoo protein. PLoS Pathog 2011;7(11):e1002382.
    • (2011) PLoS Pathog , vol.7 , Issue.11 , pp. e1002382
    • Watts, J.C.1    Stöhr, J.2    Bhardwaj, S.3
  • 418
    • 34249937435 scopus 로고    scopus 로고
    • The prion protein family: diversity, rivalry, and dysfunction
    • Watts JC, Westaway D. The prion protein family: diversity, rivalry, and dysfunction. Biochim Biophys Acta 2007;1772:654-672.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 654-672
    • Watts, J.C.1    Westaway, D.2
  • 419
    • 0037385310 scopus 로고    scopus 로고
    • Studies of the transmissibility of the agent of bovine spongiform encephalopathy to pigs
    • Wells GA, Hawkins SA, Austin AR, et al. Studies of the transmissibility of the agent of bovine spongiform encephalopathy to pigs. J Gen Virol 2003;84:1021-1031.
    • (2003) J Gen Virol , vol.84 , pp. 1021-1031
    • Wells, G.A.1    Hawkins, S.A.2    Austin, A.R.3
  • 421
    • 78049286310 scopus 로고    scopus 로고
    • Solution structure and dynamics of the I214V mutant of the rabbit prion protein
    • Wen Y, Li J, Xiong M, et al. Solution structure and dynamics of the I214V mutant of the rabbit prion protein. PLoS One 2010;5:e13273.
    • (2010) PLoS One , vol.5 , pp. e13273
    • Wen, Y.1    Li, J.2    Xiong, M.3
  • 422
    • 77957793037 scopus 로고    scopus 로고
    • Unique structural characteristics of the rabbit prion protein
    • Wen Y, Li J, Yao W, et al. Unique structural characteristics of the rabbit prion protein. J Biol Chem 2010;285:31682-31693.
    • (2010) J Biol Chem , vol.285 , pp. 31682-31693
    • Wen, Y.1    Li, J.2    Yao, W.3
  • 423
    • 0028267507 scopus 로고
    • Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie
    • Westaway D, Zuliani V, Cooper CM, et al. Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie. Genes Dev 1994;8:959-969.
    • (1994) Genes Dev , vol.8 , pp. 959-969
    • Westaway, D.1    Zuliani, V.2    Cooper, C.M.3
  • 424
    • 78049285236 scopus 로고    scopus 로고
    • Prion-like aggregates: infectious agents in human disease
    • Westermark GT, Westermark P. Prion-like aggregates: infectious agents in human disease. Trends Mol Med 2010;16:501-507.
    • (2010) Trends Mol Med , vol.16 , pp. 501-507
    • Westermark, G.T.1    Westermark, P.2
  • 425
    • 0037422133 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit prion replication and delay the development of prion disease
    • White AR, Enever P, Tayebi M, et al. Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 2003;422:80-83.
    • (2003) Nature , vol.422 , pp. 80-83
    • White, A.R.1    Enever, P.2    Tayebi, M.3
  • 426
    • 48249108696 scopus 로고    scopus 로고
    • Single treatment with RNAi against prion protein rescues early neuronal dysfunction and prolongs survival in mice with prion disease
    • White MD, Farmer M, Mirabile I, et al. Single treatment with RNAi against prion protein rescues early neuronal dysfunction and prolongs survival in mice with prion disease. Proc Natl Acad Sci U S A 2008;105:10238-10243.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10238-10243
    • White, M.D.1    Farmer, M.2    Mirabile, I.3
  • 427
    • 1642322462 scopus 로고    scopus 로고
    • Prions of yeast and filamentous fungi: [URE3], [PSI+], [PIN+], and [Het-s]
    • Prusiner SB, ed, 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Wickner RB, Liebman SW, Saupe SJ. Prions of yeast and filamentous fungi: [URE3], [PSI+], [PIN+], and [Het-s]. In: Prusiner SB, ed. Prion Biology and Diseases. 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; 2004:305-372.
    • (2004) Prion Biology and Diseases , pp. 305-372
    • Wickner, R.B.1    Liebman, S.W.2    Saupe, S.J.3
  • 428
    • 0001091187 scopus 로고
    • The epidemiology of bovine spongiform encephalopathy
    • Wilesmith JW. The epidemiology of bovine spongiform encephalopathy. Semin Virol 1991;2:239-245.
    • (1991) Semin Virol , vol.2 , pp. 239-245
    • Wilesmith, J.W.1
  • 429
    • 3442882558 scopus 로고    scopus 로고
    • Infectious and sporadic prion diseases
    • Prusiner SB, ed, 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Will RG, Alpers MP, Dormont D, et al. Infectious and sporadic prion diseases. In: Prusiner SB, ed. Prion Biology and Diseases. 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; 2004:629-671.
    • (2004) Prion Biology and Diseases , pp. 629-671
    • Will, R.G.1    Alpers, M.P.2    Dormont, D.3
  • 430
    • 0342951746 scopus 로고    scopus 로고
    • A new variant of Creutzfeldt-Jakob disease in the UK
    • Will RG, Ironside JW, Zeidler M, et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 1996;347:921-925.
    • (1996) Lancet , vol.347 , pp. 921-925
    • Will, R.G.1    Ironside, J.W.2    Zeidler, M.3
  • 431
    • 70350134002 scopus 로고    scopus 로고
    • Natural and synthetic prion structure from X-ray fiber diffraction
    • Wille H, Bian W, McDonald M, et al. Natural and synthetic prion structure from X-ray fiber diffraction. Proc Natl Acad Sci U S A 2009;106:16990-16995.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16990-16995
    • Wille, H.1    Bian, W.2    McDonald, M.3
  • 432
    • 35748972976 scopus 로고    scopus 로고
    • Electron crystallography of the scrapie prion protein complexed with heavy metals
    • Wille H, Govaerts C, Borovinskiy A, et al. Electron crystallography of the scrapie prion protein complexed with heavy metals. Arch Biochem Biophys 2007;467:239-248.
    • (2007) Arch Biochem Biophys , vol.467 , pp. 239-248
    • Wille, H.1    Govaerts, C.2    Borovinskiy, A.3
  • 433
    • 0037133587 scopus 로고    scopus 로고
    • Structural studies of the scrapie prion protein by electron crystallography
    • Wille H, Michelitsch MD, Guénebaut V, et al. Structural studies of the scrapie prion protein by electron crystallography. Proc Natl Acad Sci U S A 2002;99:3563-3568.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3563-3568
    • Wille, H.1    Michelitsch, M.D.2    Guénebaut, V.3
  • 434
    • 62649147822 scopus 로고    scopus 로고
    • Surface charge of polyoxometalates modulates polymerization of the scrapie prion protein
    • Wille H, Shanmugam M, Murugesu M, et al. Surface charge of polyoxometalates modulates polymerization of the scrapie prion protein. Proc Natl Acad Sci U S A 2009;106:3740-3745.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3740-3745
    • Wille, H.1    Shanmugam, M.2    Murugesu, M.3
  • 435
    • 0036679120 scopus 로고    scopus 로고
    • Chronic wasting disease in deer and elk in North America
    • Williams ES, Miller MW. Chronic wasting disease in deer and elk in North America. Rev Sci Tech 2002;21:305-316.
    • (2002) Rev Sci Tech , vol.21 , pp. 305-316
    • Williams, E.S.1    Miller, M.W.2
  • 436
    • 0018871326 scopus 로고
    • Chronic wasting disease of captive mule deer: a spongiform encephalopathy
    • Williams ES, Young S. Chronic wasting disease of captive mule deer: a spongiform encephalopathy. J Wildl Dis 1980;16:89-98.
    • (1980) J Wildl Dis , vol.16 , pp. 89-98
    • Williams, E.S.1    Young, S.2
  • 437
    • 69949187643 scopus 로고    scopus 로고
    • Molecular mechanisms for protein-encoded inheritance
    • Wiltzius JJ, Landau M, Nelson R, et al. Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol 2009;16:973-978.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 973-978
    • Wiltzius, J.J.1    Landau, M.2    Nelson, R.3
  • 438
    • 1842685948 scopus 로고
    • Neurofibrillary tangles of Alzheimer's disease share antigenic determinants with the axonal microtubule-associated protein tau
    • Wood JG, Mirra SS, Pollock NJ, et al. Neurofibrillary tangles of Alzheimer's disease share antigenic determinants with the axonal microtubule-associated protein tau. Proc Natl Acad Sci U S A 1986;83:4040-4043.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4040-4043
    • Wood, J.G.1    Mirra, S.S.2    Pollock, N.J.3
  • 439
    • 0035048758 scopus 로고    scopus 로고
    • Transmission of mouse senile amyloidosis
    • Xing Y, Nakamura A, Chiba T, et al. Transmission of mouse senile amyloidosis. Lab Invest 2001;81:493-499.
    • (2001) Lab Invest , vol.81 , pp. 493-499
    • Xing, Y.1    Nakamura, A.2    Chiba, T.3
  • 440
    • 0037031915 scopus 로고    scopus 로고
    • Induction of protein conformational change in mouse senile amyloidosis
    • Xing Y, Nakamura A, Korenaga T, et al. Induction of protein conformational change in mouse senile amyloidosis. J Biol Chem 2002;277:33164-33169.
    • (2002) J Biol Chem , vol.277 , pp. 33164-33169
    • Xing, Y.1    Nakamura, A.2    Korenaga, T.3
  • 441
    • 18544397601 scopus 로고    scopus 로고
    • Directed evolution of high-affinity antibody mimics using mRNA display
    • Xu L, Aha P, Gu K, et al. Directed evolution of high-affinity antibody mimics using mRNA display. Chem Biol 2002;9:933-942.
    • (2002) Chem Biol , vol.9 , pp. 933-942
    • Xu, L.1    Aha, P.2    Gu, K.3
  • 442
    • 1142299412 scopus 로고    scopus 로고
    • Atypical proteinase K-resistant prion protein (PrPres) observed in an apparently healthy 23-month-old Holstein steer
    • Yamakawa Y, Hagiwara K, Nohtomi K, et al. Atypical proteinase K-resistant prion protein (PrPres) observed in an apparently healthy 23-month-old Holstein steer. Jpn J Infect Dis 2003;56:221-222.
    • (2003) Jpn J Infect Dis , vol.56 , pp. 221-222
    • Yamakawa, Y.1    Hagiwara, K.2    Nohtomi, K.3
  • 443
    • 0033863775 scopus 로고    scopus 로고
    • NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: a loop conformation with histidine and tryptophan in close proximity
    • Yoshida H, Matsushima N, Kumaki Y, et al. NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: a loop conformation with histidine and tryptophan in close proximity. J Biochem (Tokyo) 2000;128:271-281.
    • (2000) J Biochem (Tokyo) , vol.128 , pp. 271-281
    • Yoshida, H.1    Matsushima, N.2    Kumaki, Y.3
  • 444
    • 0242384747 scopus 로고    scopus 로고
    • Beta-catenin is critical for dendritic morphogenesis
    • Yu X, Malenka RC. Beta-catenin is critical for dendritic morphogenesis. Nat Neurosci 2003;6:1169-1177.
    • (2003) Nat Neurosci , vol.6 , pp. 1169-1177
    • Yu, X.1    Malenka, R.C.2
  • 445
    • 10144229414 scopus 로고    scopus 로고
    • Pharmacokinetics of quinacrine in the treatment of prion disease
    • Yung L, Huang Y, Lessard P, et al. Pharmacokinetics of quinacrine in the treatment of prion disease. BMC Infect Dis 2004;4:53-59.
    • (2004) BMC Infect Dis , vol.4 , pp. 53-59
    • Yung, L.1    Huang, Y.2    Lessard, P.3
  • 446
    • 0242662244 scopus 로고    scopus 로고
    • The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site
    • Zahn R. The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site. J Mol Biol 2003;334:477-488.
    • (2003) J Mol Biol , vol.334 , pp. 477-488
    • Zahn, R.1
  • 447
    • 0037423709 scopus 로고    scopus 로고
    • NMR structure of a variant human prion protein with two disulfide bridges
    • Zahn R, Guntert P, von Schroetter C, et al. NMR structure of a variant human prion protein with two disulfide bridges. J Mol Biol 2003;326:225-234.
    • (2003) J Mol Biol , vol.326 , pp. 225-234
    • Zahn, R.1    Guntert, P.2    von Schroetter, C.3
  • 448
    • 0012710491 scopus 로고    scopus 로고
    • NMR solution structure of the human prion protein
    • Zahn R, Liu A, Lührs T, et al. NMR solution structure of the human prion protein. Proc Natl Acad Sci U S A 2000;97:145-150.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 145-150
    • Zahn, R.1    Liu, A.2    Lührs, T.3
  • 449
    • 0034721767 scopus 로고    scopus 로고
    • Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases
    • Zhang Y, Swietnicki W, Zagorski MG, et al. Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J Biol Chem 2000;275:33650-33654.
    • (2000) J Biol Chem , vol.275 , pp. 33650-33654
    • Zhang, Y.1    Swietnicki, W.2    Zagorski, M.G.3
  • 450
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu H, Bilgin M, Bangham R, et al. Global analysis of protein activities using proteome chips. Science 2001;293:2101-2105.
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1    Bilgin, M.2    Bangham, R.3
  • 451
    • 4344659039 scopus 로고    scopus 로고
    • Non-invasive imaging of GFAP expression after neuronal damage in mice
    • Zhu L, Ramboz S, Hewitt D, et al. Non-invasive imaging of GFAP expression after neuronal damage in mice. Neurosci Lett 2004;367:210-212.
    • (2004) Neurosci Lett , vol.367 , pp. 210-212
    • Zhu, L.1    Ramboz, S.2    Hewitt, D.3
  • 452
    • 0033066555 scopus 로고    scopus 로고
    • Infectivity of scrapie prions bound to a stainless steel surface
    • Zobeley E, Flechsig E, Cozzio A, et al. Infectivity of scrapie prions bound to a stainless steel surface. Mol Med 1999;5:240-243.
    • (1999) Mol Med , vol.5 , pp. 240-243
    • Zobeley, E.1    Flechsig, E.2    Cozzio, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.