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Volumn 270, Issue 1, 2011, Pages 1-14

Prions and protein-folding diseases

Author keywords

Iatrogenic disease; Prions; Protein folding

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; AMYLOID A PROTEIN; AMYLOID BETA PROTEIN; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 9; CELL PROTEIN; DNA; GROWTH HORMONE; HISTONE; METHIONINE; NUCLEIC ACID; POLYGLUTAMINE; POLYPEPTIDE; PRION PROTEIN; SYNTHETIC PEPTIDE; UNTRANSLATED RNA; VALINE; YELLOW FEVER VACCINE;

EID: 79959366068     PISSN: 09546820     EISSN: 13652796     Source Type: Journal    
DOI: 10.1111/j.1365-2796.2011.02387.x     Document Type: Review
Times cited : (56)

References (80)
  • 1
    • 78651041685 scopus 로고
    • Degenerative disease of the central nervous system in New Guinea: the endemic occurrence of "kuru" in the native population
    • Gajdusek DC, Zigas V. Degenerative disease of the central nervous system in New Guinea: the endemic occurrence of "kuru" in the native population. N Engl J Med 1957; 257: 974-8.
    • (1957) N Engl J Med , vol.257 , pp. 974-978
    • Gajdusek, D.C.1    Zigas, V.2
  • 2
    • 49749220574 scopus 로고
    • Scrapie and kuru
    • Hadlow WJ. Scrapie and kuru. Lancet 1959; 2: 289-90.
    • (1959) Lancet , vol.2 , pp. 289-290
    • Hadlow, W.J.1
  • 3
    • 0014021742 scopus 로고
    • Experimental transmission of a kuru-like syndrome to chimpanzees
    • Gajdusek DC, Gibbs CJ Jr, Alpers M. Experimental transmission of a kuru-like syndrome to chimpanzees. Nature 1966; 209: 794-6.
    • (1966) Nature , vol.209 , pp. 794-796
    • Gajdusek, D.C.1    Gibbs Jr, C.J.2    Alpers, M.3
  • 4
    • 0014430962 scopus 로고
    • Creutzfeldt-Jakob disease (spongiform encephalopathy): transmission to the chimpanzee
    • Gibbs CJ Jr, Gajdusek DC, Asher DM et al. Creutzfeldt-Jakob disease (spongiform encephalopathy): transmission to the chimpanzee. Science 1968; 161: 388-9.
    • (1968) Science , vol.161 , pp. 388-389
    • Gibbs Jr, C.J.1    Gajdusek, D.C.2    Asher, D.M.3
  • 5
    • 0014080385 scopus 로고
    • Cannibalism in the kuru region of New Guinea
    • Glasse RM. Cannibalism in the kuru region of New Guinea. Trans N Y Acad Sci 1967; 29: 748-54.
    • (1967) Trans N Y Acad Sci , vol.29 , pp. 748-754
    • Glasse, R.M.1
  • 6
    • 33745440706 scopus 로고    scopus 로고
    • st century - an acquired human prion disease with very long incubation periods
    • st century - an acquired human prion disease with very long incubation periods. Lancet 2006; 367: 2068-74.
    • (2006) Lancet , vol.367 , pp. 2068-2074
    • Collinge, J.1    Whitfield, J.2    McKintosh, E.3
  • 7
    • 65349173916 scopus 로고    scopus 로고
    • Lack of evidence of transfusion transmission of Creutzfeldt-Jakob disease in a US surveillance study
    • Dorsey KA, Zou S, Schonberger LB et al. Lack of evidence of transfusion transmission of Creutzfeldt-Jakob disease in a US surveillance study. Transfusion 2009; 49: 977-84.
    • (2009) Transfusion , vol.49 , pp. 977-984
    • Dorsey, K.A.1    Zou, S.2    Schonberger, L.B.3
  • 8
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner SB, Groth DF, Bolton DC, Kent SB, Hood LE. Purification and structural studies of a major scrapie prion protein. Cell 1984; 38: 127-34.
    • (1984) Cell , vol.38 , pp. 127-134
    • Prusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3    Kent, S.B.4    Hood, L.E.5
  • 9
    • 0002812673 scopus 로고    scopus 로고
    • Prions
    • In: Frängsmyr T, ed. Stockholm: Almqvist & Wiksell International
    • Prusiner SB. Prions. In: Frängsmyr T, ed. Nobel Lecture. Stockholm: Almqvist & Wiksell International, 1997; 268-323.
    • (1997) Nobel Lecture , pp. 268-323
    • Prusiner, S.B.1
  • 10
    • 77951969247 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 1986; 46: 417-28.
    • (1986) Cell , vol.46 , pp. 417-428
    • Oesch, B.1    Westaway, D.2    Wälchli, M.3
  • 11
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Büeler H, Fischer M, Lang Y et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992; 356: 577-82.
    • (1992) Nature , vol.356 , pp. 577-582
    • Büeler, H.1    Fischer, M.2    Lang, Y.3
  • 12
    • 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: 1339-47.
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Büeler, H.1    Aguzzi, A.2    Sailer, A.3
  • 13
    • 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 USA 1993; 90: 10608-12.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10608-10612
    • Prusiner, S.B.1    Groth, D.2    Serban, A.3
  • 14
    • 0033850051 scopus 로고    scopus 로고
    • Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein
    • Wille H, Prusiner SB, Cohen FE. Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein. J Struct Biol 2000; 130: 323-38.
    • (2000) J Struct Biol , vol.130 , pp. 323-338
    • Wille, H.1    Prusiner, S.B.2    Cohen, F.E.3
  • 15
    • 0031456947 scopus 로고    scopus 로고
    • Structure of the recombinant full-length hamster 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 protein PrP (29-231): the N terminus is highly flexible. Proc Natl Acad Sci USA 1997; 94: 7279-82.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7279-7282
    • Donne, D.G.1    Viles, J.H.2    Groth, D.3
  • 16
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP (23-231)
    • Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP (23-231). FEBS Lett 1997; 413: 282-8.
    • (1997) FEBS Lett , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wüthrich, K.5
  • 17
    • 0030728039 scopus 로고    scopus 로고
    • Deadly conformations - Protein misfolding in prion disease
    • Horwich AL, Weissman JS. Deadly conformations - Protein misfolding in prion disease. Cell 1997; 89: 499-510.
    • (1997) Cell , vol.89 , pp. 499-510
    • Horwich, A.L.1    Weissman, J.S.2
  • 18
    • 58149378573 scopus 로고    scopus 로고
    • Prion diseases are effectively transmitted by blood transfusion in sheep
    • Houston F, McCutcheon S, Goldmnann W et al. Prion diseases are effectively transmitted by blood transfusion in sheep. Blood 2008; 112: 4739-45.
    • (2008) Blood , vol.112 , pp. 4739-4745
    • Houston, F.1    McCutcheon, S.2    Goldmnann, W.3
  • 19
    • 37149043763 scopus 로고    scopus 로고
    • Creutzfeldt-Jakob disease: reflections on the risk from blood product therapy
    • Brown P. Creutzfeldt-Jakob disease: reflections on the risk from blood product therapy. Haemophilia 2007; 13: 33-40.
    • (2007) Haemophilia , vol.13 , pp. 33-40
    • Brown, P.1
  • 21
    • 0020077296 scopus 로고
    • Evidence for case-to-case transmission of Creutzfeldt-Jakob disease
    • Will RG, Mathews WB. Evidence for case-to-case transmission of Creutzfeldt-Jakob disease. J Neurol Neurosurg Psychiatry 1982; 45: 235-8.
    • (1982) J Neurol Neurosurg Psychiatry , vol.45 , pp. 235-238
    • Will, R.G.1    Mathews, W.B.2
  • 22
    • 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: 921-5.
    • (1996) Lancet , vol.347 , pp. 921-925
    • Will, R.G.1    Ironside, J.W.2    Zeidler, M.3
  • 23
    • 79959333840 scopus 로고    scopus 로고
    • The National Creutzfeldt-Jakob Disease Surveillance Unit (NCJDSU), University of Edinburgh, UK, Available at:, Accessed November 30, 2010.
    • The National Creutzfeldt-Jakob Disease Surveillance Unit (NCJDSU), University of Edinburgh, UK, Available at:, Accessed November 30, 2010.
  • 24
    • 72249109696 scopus 로고    scopus 로고
    • Variant CJD in an individual heterozygous for PRNP codon 129
    • Kaski D, Mead S, Hyare H et al. Variant CJD in an individual heterozygous for PRNP codon 129. Lancet 2009; 374: 2128.
    • (2009) Lancet , vol.374 , pp. 2128
    • Kaski, D.1    Mead, S.2    Hyare, H.3
  • 25
    • 1142273431 scopus 로고    scopus 로고
    • Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion
    • Llewelyn CA, Hewitt RE, Knight RSG et al. Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet 2004; 363: 417-21.
    • (2004) Lancet , vol.363 , pp. 417-421
    • Llewelyn, C.A.1    Hewitt, R.E.2    Knight, R.S.G.3
  • 26
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • Peden AH, Head MW, Ritchie DL, Bell JE, Ironside JW. Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 2004; 364: 527-9.
    • (2004) Lancet , vol.364 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3    Bell, J.E.4    Ironside, J.W.5
  • 27
    • 0020522298 scopus 로고
    • Creutzfeldt-Jakob disease in mice: persistent viremia and preferential replication of virus in low-density lymphocytes
    • Kuroda Y, Gibbs CJ Jr, Amyx HL, Gajdusek DC. Creutzfeldt-Jakob disease in mice: persistent viremia and preferential replication of virus in low-density lymphocytes. Infect Immunol 1983; 41: 154-61.
    • (1983) Infect Immunol , vol.41 , pp. 154-161
    • Kuroda, Y.1    Gibbs Jr, C.J.2    Amyx, H.L.3    Gajdusek, D.C.4
  • 28
    • 4043054277 scopus 로고    scopus 로고
    • Effectiveness of leucoreduction for removal of infectivity of transmissible spongiform encephalopathies from blood
    • Gregori L, McCombie DP, Palmer D, Sowemimo-Coker AO, Giulivi A, Rohwer RG. Effectiveness of leucoreduction for removal of infectivity of transmissible spongiform encephalopathies from blood. Lancet 2004; 264: 529-31.
    • (2004) Lancet , vol.264 , pp. 529-531
    • Gregori, L.1    McCombie, D.P.2    Palmer, D.3    Sowemimo-Coker, A.O.4    Giulivi, A.5    Rohwer, R.G.6
  • 29
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper T, Cramp WA, Haig DA, Clarke MC. Does the agent of scrapie replicate without nucleic acid? Nature 1967; 214: 764-6.
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 30
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith JS. Self-replication and scrapie. Nature 1967; 215: 1043-4.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 31
    • 40749088877 scopus 로고    scopus 로고
    • A new liquid intravenous immunoglobulin with three dedicated virus reduction steps: virus and prion reduction capacity
    • Poelser G, Berting A, Kindermann J et al. A new liquid intravenous immunoglobulin with three dedicated virus reduction steps: virus and prion reduction capacity. Vox Sang 2008; 94: 184-92.
    • (2008) Vox Sang , vol.94 , pp. 184-192
    • Poelser, G.1    Berting, A.2    Kindermann, J.3
  • 32
    • 47349084677 scopus 로고    scopus 로고
    • Prion safety of transfusion plasma and plasma-derivatives typically used for prophylactic treatment
    • Svae T-E, Neisser-Svae A, Bailey A et al. Prion safety of transfusion plasma and plasma-derivatives typically used for prophylactic treatment. Transf Apheres Sci 2008; 39: 59-67.
    • (2008) Transf Apheres Sci , vol.39 , pp. 59-67
    • Svae, T.-E.1    Neisser-Svae, A.2    Bailey, A.3
  • 33
    • 33746501354 scopus 로고    scopus 로고
    • Reduction of transmissible spongiform encephalopathy infectivity from human red blood cells with prion protein affinity ligands
    • Gregori L, Lambert B, Gurgel P et al. Reduction of transmissible spongiform encephalopathy infectivity from human red blood cells with prion protein affinity ligands. Transfusion 2009; 46: 1152-61.
    • (2009) Transfusion , vol.46 , pp. 1152-1161
    • Gregori, L.1    Lambert, B.2    Gurgel, P.3
  • 34
    • 70349559216 scopus 로고    scopus 로고
    • Prion removal effect of a specific affinity ligand introduced into the manufacturing process of the pharmaceutical quality solvent/detergent(S/D)-treated plasma OctaplasLG
    • Neisser-Svae A, Bailey A, Gregori L et al. Prion removal effect of a specific affinity ligand introduced into the manufacturing process of the pharmaceutical quality solvent/detergent(S/D)-treated plasma OctaplasLG. Vox Sang 2009; 97: 226-33.
    • (2009) Vox Sang , vol.97 , pp. 226-233
    • Neisser-Svae, A.1    Bailey, A.2    Gregori, L.3
  • 36
    • 79959346994 scopus 로고    scopus 로고
    • Health Protection Agency. Variant CJD and plasma products
    • Health Protection Agency. Variant CJD and plasma products, 2009.
    • (2009)
  • 37
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: one century of evolving concepts
    • Aguzzi A, Polymenidou M. Mammalian prion biology: one century of evolving concepts. Cell 2004; 116: 313-27.
    • (2004) Cell , vol.116 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 38
    • 70349705441 scopus 로고    scopus 로고
    • Prions: Protein aggregation and infectious disease
    • Aguzzi A, Calella AM. Prions: Protein aggregation and infectious disease. Physiol Rev 2009; 89: 1105-52.
    • (2009) Physiol Rev , vol.89 , pp. 1105-1152
    • Aguzzi, A.1    Calella, A.M.2
  • 39
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey B, Baron GS. Prions and their partners in crime. Nature 2006; 443: 803-10.
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 40
    • 51649087972 scopus 로고    scopus 로고
    • Physiological role of the cellular prion protein (PrP-C): protein profiling study in two cell culture systems
    • Ramijak S, Asif AR, Armstrong VW et al. Physiological role of the cellular prion protein (PrP-C): protein profiling study in two cell culture systems. J Proteome Res 2008; 7: 2681-95.
    • (2008) J Proteome Res , vol.7 , pp. 2681-2695
    • Ramijak, S.1    Asif, A.R.2    Armstrong, V.W.3
  • 42
    • 79959340884 scopus 로고    scopus 로고
    • Prions. In: Morimoto R, Kelly J, Selkoe D, ed. Additional Perspectives on Protein Homeostasis. Cold Spring Harb Perspect Biol doi:
    • Colby DW, Prusiner SB. Prions. In: Morimoto R, Kelly J, Selkoe D, ed. Additional Perspectives on Protein Homeostasis. Cold Spring Harb Perspect Biol doi:
    • Colby, D.W.1    Prusiner, S.B.2
  • 43
    • 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; 104: 1435-9.
    • (2005) Science , vol.104 , pp. 1435-1439
    • Chesebro, B.1    Trifilo, M.2    Race, R.3
  • 44
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter Jw. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009; 457: 1128-33.
    • (2009) Nature , vol.457 , pp. 1128-1133
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, J.5
  • 45
    • 77649091387 scopus 로고    scopus 로고
    • Axonal prion protein is required for peripheral myelin maintenance
    • Bremer J, Baumann F, Tiberi C et al. Axonal prion protein is required for peripheral myelin maintenance. Nat Neurosci 2010; 13: 310-18. doi:.
    • (2010) Nat Neurosci , vol.13 , pp. 310-318
    • Bremer, J.1    Baumann, F.2    Tiberi, C.3
  • 46
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien P, Weissman JS, De Pace AH. Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 2004; 73: 617-56.
    • (2004) Annu Rev Biochem , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    De Pace, A.H.3
  • 47
    • 33644817188 scopus 로고    scopus 로고
    • Prion domains: sequences, structures and interactions
    • Ross ED, Minton A, Wickner RB. Prion domains: sequences, structures and interactions. Nat Cell Biol 2005; 7: 1039-44.
    • (2005) Nat Cell Biol , vol.7 , pp. 1039-1044
    • Ross, E.D.1    Minton, A.2    Wickner, R.B.3
  • 48
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137: 146-58.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 49
    • 77249122579 scopus 로고    scopus 로고
    • Prions, protein homeostasis, and phenotypic diversity
    • Halfmann R, Alberti S, Lindquist S. Prions, protein homeostasis, and phenotypic diversity. Trends Cell Biol 2010; 20: 125-34.
    • (2010) Trends Cell Biol , vol.20 , pp. 125-134
    • Halfmann, R.1    Alberti, S.2    Lindquist, S.3
  • 50
    • 78049361927 scopus 로고    scopus 로고
    • Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits
    • Halfmann R, Lindquist S. Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits. Science 2010; 330: 629-32.
    • (2010) Science , vol.330 , pp. 629-632
    • Halfmann, R.1    Lindquist, S.2
  • 51
    • 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
  • 53
    • 77950379326 scopus 로고    scopus 로고
    • Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion 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 membrane anchoring. PLoS Pathog 2010; 6: e1000800.
    • (2010) PLoS Pathog , vol.6
    • Chesebro, B.1    Race, B.2    Meade-White, K.3
  • 54
    • 78951477465 scopus 로고    scopus 로고
    • Crucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infection
    • PubMed PMID: 21123371.
    • Klingeborn M, Race B, Meade-White KD, Rosenke R, Striebel JF, Chesebro B Crucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infection. J Virol 2011; 85: 1484-94. PubMed PMID: 21123371.
    • (2011) J Virol , vol.85 , pp. 1484-1494
    • Klingeborn, M.1    Race, B.2    Meade-White, K.D.3    Rosenke, R.4    Striebel, J.F.5    Chesebro, B.6
  • 55
    • 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: 773-8.
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3
  • 56
    • 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: 453-7.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3
  • 57
    • 69949187643 scopus 로고    scopus 로고
    • Molecular mechanisms of protein-encoded inheritance
    • Wiltzius JJ, Landau M, Nelson R et al. Molecular mechanisms of protein-encoded inheritance. Nat Struct Mol Biol 2009; 16: 973-8.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 973-978
    • Wiltzius, J.J.1    Landau, M.2    Nelson, R.3
  • 59
    • 58549102983 scopus 로고    scopus 로고
    • De novo generation of a transmissible spongiform encephalopathy by mouse transgenesis
    • Sigurdson CJ, Nilsson KP, Hornemann S et al. De novo generation of a transmissible spongiform encephalopathy by mouse transgenesis. Proc Natl Acad Sci 2009; 106: 304-9.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 304-309
    • Sigurdson, C.J.1    Nilsson, K.P.2    Hornemann, S.3
  • 60
    • 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: 810-3.
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 61
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J, Saá P, Hetz C, Soto C. In vitro generation of infectious scrapie prions. Cell 2005; 121: 136-44.
    • (2005) Cell , vol.121 , pp. 136-144
    • Castilla, J.1    Saá, P.2    Hetz, C.3    Soto, C.4
  • 63
    • 67249123069 scopus 로고    scopus 로고
    • De novo generation of infectious prions in vitro produces a new disease phenotype
    • Barria MA, Mukherjee A, Gonzales-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
    • Barria, M.A.1    Mukherjee, A.2    Gonzales-Romero, D.3
  • 64
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with a bacterially expressed recombinant prion protein
    • Wang F, Wang X, Yuan CG, Ma J. Generating a prion with a bacterially expressed recombinant prion protein. Science 2010; 327: 1132-5.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 65
    • 0031586212 scopus 로고    scopus 로고
    • Molecular properties of complexes formed between the prion protein and synthetic peptides
    • Kaneko K, Wille H, Mehlhorn I et al. Molecular properties of complexes formed between the prion protein and synthetic peptides. J Mol Biol 1997; 270: 574-86.
    • (1997) J Mol Biol , vol.270 , pp. 574-586
    • Kaneko, K.1    Wille, H.2    Mehlhorn, I.3
  • 67
    • 34447639732 scopus 로고    scopus 로고
    • Continuum of prion protein structures enciphers a multitude of prion isolate-specific phenotypes
    • Legname G, Nguyen H-OB, Peretz D et al. Continuum of prion protein structures enciphers a multitude of prion isolate-specific phenotypes. Proc Natl Acad Sci 2006; 103: 19105-10.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 19105-19110
    • Legname, G.1    Nguyen, H.-O.2    Peretz, D.3
  • 68
    • 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 2009; 106: 20417-22.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 20417-20422
    • Colby, D.W.1    Giles, K.2    Legname, G.3
  • 70
    • 77956276348 scopus 로고    scopus 로고
    • Spontaneous generation of mammalian prions
    • Edgeworth JA, Gros N, Alden J et al. Spontaneous generation of mammalian prions. Proc Natl Acad Sci 2010; 107: 14402-6. DOI:.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 14402-14406
    • Edgeworth, J.A.1    Gros, N.2    Alden, J.3
  • 72
    • 67649286622 scopus 로고    scopus 로고
    • Beyond the prion principle
    • Aguzzi A. Beyond the prion principle. Nature 2009; 459: 924-5.
    • (2009) Nature , vol.459 , pp. 924-925
    • Aguzzi, A.1
  • 73
    • 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: 1781-4.
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3
  • 74
    • 69149098707 scopus 로고    scopus 로고
    • Indiction of cerebral beta-amyloidosis: intracerebral versus systemic A-beta inoculation
    • Eisele YS, Bolmont T, Heikenwalder M et al. Indiction of cerebral beta-amyloidosis: intracerebral versus systemic A-beta inoculation. Proc Natl Acad Sci 2009; 106: 12926-31.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 12926-12931
    • Eisele, Y.S.1    Bolmont, T.2    Heikenwalder, M.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: 909-13.
    • (2009) Nat Cell Biol , vol.11 , pp. 909-913
    • Clavaguera, F.1    Bolmont, T.2    Crowther, R.A.3
  • 76
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren PH, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, Kopito RR. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 2009; 11: 209-25.
    • (2009) Nat Cell Biol , vol.11 , pp. 209-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 77
    • 17844367336 scopus 로고    scopus 로고
    • Protein fibrils in nature can enhance amyloid protein a amyloidosis in mice: cross-seeding as a disease mechanism
    • Lundmark K, Westermark GT, Olsen A, Westermark P. Protein fibrils in nature can enhance amyloid protein a amyloidosis in mice: cross-seeding as a disease mechanism. Proc Natl Acad Sci USA 2005; 102: 6098-102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6098-6102
    • Lundmark, K.1    Westermark, G.T.2    Olsen, A.3    Westermark, P.4
  • 78
    • 69149088365 scopus 로고    scopus 로고
    • Is Parkinson's disease a prion disorder?
    • Olanow CW, Prusiner SB. Is Parkinson's disease a prion disorder? Proc Natl Acad Sci 2009; 106: 12571-2.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 12571-12572
    • Olanow, C.W.1    Prusiner, S.B.2
  • 79
    • 0034632806 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes mellitus
    • Höppener JW, Ahren B, Lips CJ. Islet amyloid and type 2 diabetes mellitus. N Engl J Med 2000; 343: 411-9.
    • (2000) N Engl J Med , vol.343 , pp. 411-419
    • Höppener, J.W.1    Ahren, B.2    Lips, C.J.3
  • 80
    • 75749134925 scopus 로고    scopus 로고
    • Aplysia CFEB can form prion-like multimers in sensory neurons that contribute to long-tem facilitation
    • Si K, Choi YB, White-Grindley E, Majumdar A, Kandel ER. Aplysia CFEB can form prion-like multimers in sensory neurons that contribute to long-tem facilitation. Cell 2010; 140: 421-35.
    • (2010) Cell , vol.140 , pp. 421-435
    • Si, K.1    Choi, Y.B.2    White-Grindley, E.3    Majumdar, A.4    Kandel, E.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.