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Volumn 9, Issue 10, 2013, Pages

Quaternary Structure of Pathological Prion Protein as a Determining Factor of Strain-Specific Prion Replication Dynamics

Author keywords

[No Author keywords available]

Indexed keywords

DIGITONIN; PRION PROTEIN;

EID: 84887275537     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003702     Document Type: Article
Times cited : (49)

References (84)
  • 2
    • 84858978818 scopus 로고    scopus 로고
    • Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships
    • Bemporad F, Chiti F, (2012) Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem Biol 19: 315-327.
    • (2012) Chem Biol , vol.19 , pp. 315-327
    • Bemporad, F.1    Chiti, F.2
  • 3
    • 84861315209 scopus 로고    scopus 로고
    • High-resolution structure of infectious prion protein: the final frontier
    • Diaz-Espinoza R, Soto C, (2012) High-resolution structure of infectious prion protein: the final frontier. Nat Struct Mol Biol 19: 370-377.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 370-377
    • Diaz-Espinoza, R.1    Soto, C.2
  • 5
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB, (1982) Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 6
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles TP, Waudby CA, Devlin GL, Cohen SI, Aguzzi A, et al. (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326: 1533-1537.
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.1    Waudby, C.A.2    Devlin, G.L.3    Cohen, S.I.4    Aguzzi, A.5
  • 7
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue WF, Homans SW, Radford SE, (2008) Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci U S A 105: 8926-8931.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 8
    • 80054745655 scopus 로고    scopus 로고
    • De novo generation of prion strains
    • Colby DW, Prusiner SB, (2011) De novo generation of prion strains. Nat Rev Microbiol 9: 771-777.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 771-777
    • Colby, D.W.1    Prusiner, S.B.2
  • 9
    • 79952449094 scopus 로고    scopus 로고
    • Prion hypothesis: the end of the controversy?
    • Soto C, (2011) Prion hypothesis: the end of the controversy? Trends Biochem Sci 36: 151-158.
    • (2011) Trends Biochem Sci , vol.36 , pp. 151-158
    • Soto, C.1
  • 10
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: their causes and molecular basis
    • Collinge J, (2001) Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 24: 519-550.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 519-550
    • Collinge, J.1
  • 11
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen RA, Marsh RF, (1994) Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 68: 7859-7868.
    • (1994) J Virol , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 12
    • 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, Cortelli P, Montagna P, et al. (1996) Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274: 2079-2082.
    • (1996) Science , vol.274 , pp. 2079-2082
    • Telling, G.C.1    Parchi, P.2    DeArmond, S.J.3    Cortelli, P.4    Montagna, P.5
  • 13
    • 70349858126 scopus 로고    scopus 로고
    • Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils
    • Sim VL, Caughey B, (2009) Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils. Neurobiol Aging 30: 2031-2042.
    • (2009) Neurobiol Aging , vol.30 , pp. 2031-2042
    • Sim, V.L.1    Caughey, B.2
  • 14
    • 33745058355 scopus 로고    scopus 로고
    • Structural differences between TSEs strains investigated by FT-IR spectroscopy
    • Spassov S, Beekes M, Naumann D, (2006) Structural differences between TSEs strains investigated by FT-IR spectroscopy. Biochim Biophys Acta 1760: 1138-1149.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 1138-1149
    • Spassov, S.1    Beekes, M.2    Naumann, D.3
  • 15
    • 4043137988 scopus 로고    scopus 로고
    • Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein
    • Thomzig A, Spassov S, Friedrich M, Naumann D, Beekes M, (2004) Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein. J Biol Chem 279: 33847-33854.
    • (2004) J Biol Chem , vol.279 , pp. 33847-33854
    • Thomzig, A.1    Spassov, S.2    Friedrich, M.3    Naumann, D.4    Beekes, M.5
  • 16
    • 50049099543 scopus 로고    scopus 로고
    • Prion agent diversity and species barrier
    • Beringue V, Vilotte JL, Laude H, (2008) Prion agent diversity and species barrier. Vet Res 39: 47.
    • (2008) Vet Res , vol.39 , pp. 47
    • Beringue, V.1    Vilotte, J.L.2    Laude, H.3
  • 17
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge J, Clarke AR, (2007) A general model of prion strains and their pathogenicity. Science 318: 930-936.
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 19
    • 77649205447 scopus 로고    scopus 로고
    • Biochemistry. What makes a prion infectious?
    • Supattapone S, (2010) Biochemistry. What makes a prion infectious? Science 327: 1091-1092.
    • (2010) Science , vol.327 , pp. 1091-1092
    • Supattapone, S.1
  • 20
    • 77954051480 scopus 로고    scopus 로고
    • The physical relationship between infectivity and prion protein aggregates is strain-dependent
    • Tixador P, Herzog L, Reine F, Jaumain E, Chapuis J, et al. (2010) The physical relationship between infectivity and prion protein aggregates is strain-dependent. PLoS Pathog 6: e1000859.
    • (2010) PLoS Pathog , vol.6
    • Tixador, P.1    Herzog, L.2    Reine, F.3    Jaumain, E.4    Chapuis, J.5
  • 21
    • 27644492381 scopus 로고    scopus 로고
    • A newly identified type of scrapie agent can naturally infect sheep with resistant PrP genotypes
    • Le Dur A, Beringue V, Andreoletti O, Reine F, Lai TL, et al. (2005) A newly identified type of scrapie agent can naturally infect sheep with resistant PrP genotypes. Proc Natl Acad Sci U S A 102: 16031-16036.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16031-16036
    • Le Dur, A.1    Beringue, V.2    Andreoletti, O.3    Reine, F.4    Lai, T.L.5
  • 22
    • 0035957345 scopus 로고    scopus 로고
    • Ex vivo propagation of infectious sheep scrapie agent in heterologous epithelial cells expressing ovine prion protein
    • Vilette D, Andreoletti O, Archer F, Madelaine MF, Vilotte JL, et al. (2001) Ex vivo propagation of infectious sheep scrapie agent in heterologous epithelial cells expressing ovine prion protein. Proc Natl Acad Sci U S A 98: 4055-4059.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4055-4059
    • Vilette, D.1    Andreoletti, O.2    Archer, F.3    Madelaine, M.F.4    Vilotte, J.L.5
  • 23
    • 33846818651 scopus 로고    scopus 로고
    • Efficient dissemination of prions through preferential transmission to nearby cells
    • Paquet S, Langevin C, Chapuis J, Jackson GS, Laude H, et al. (2007) Efficient dissemination of prions through preferential transmission to nearby cells. J Gen Virol 88: 706-713.
    • (2007) J Gen Virol , vol.88 , pp. 706-713
    • Paquet, S.1    Langevin, C.2    Chapuis, J.3    Jackson, G.S.4    Laude, H.5
  • 24
    • 24744446203 scopus 로고    scopus 로고
    • Detection of prions in blood
    • Castilla J, Saa P, Soto C, (2005) Detection of prions in blood. Nat Med 11: 982-985.
    • (2005) Nat Med , vol.11 , pp. 982-985
    • Castilla, J.1    Saa, P.2    Soto, C.3
  • 25
    • 80052702962 scopus 로고    scopus 로고
    • Relationship between conformational stability and amplification efficiency of prions
    • Gonzalez-Montalban N, Makarava N, Savtchenko R, Baskakov IV, (2011) Relationship between conformational stability and amplification efficiency of prions. Biochemistry 50: 7933-7940.
    • (2011) Biochemistry , vol.50 , pp. 7933-7940
    • Gonzalez-Montalban, N.1    Makarava, N.2    Savtchenko, R.3    Baskakov, I.V.4
  • 26
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • London E, Brown DA, (2000) Insolubility of lipids in triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim Biophys Acta 1508: 182-195.
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 182-195
    • London, E.1    Brown, D.A.2
  • 27
    • 71549138062 scopus 로고    scopus 로고
    • Determination of size, molecular weight, and presence of subunits
    • Rhodes DG, Bossio RE, Laue TM, (2009) Determination of size, molecular weight, and presence of subunits. Methods Enzymol 463: 691-723.
    • (2009) Methods Enzymol , vol.463 , pp. 691-723
    • Rhodes, D.G.1    Bossio, R.E.2    Laue, T.M.3
  • 28
    • 0013874701 scopus 로고
    • Quantitative precipitation of various 3-beta-hydroxysterols with digitonin
    • Huaust HL, Kuksis A, Beveridge JM, (1966) Quantitative precipitation of various 3-beta-hydroxysterols with digitonin. Can J Biochem 44: 119-128.
    • (1966) Can J Biochem , vol.44 , pp. 119-128
    • Huaust, H.L.1    Kuksis, A.2    Beveridge, J.M.3
  • 29
    • 0014515315 scopus 로고
    • Interaction of saponins with cholesterol, lecithin, and albumin
    • Schlosser E, (1969) Interaction of saponins with cholesterol, lecithin, and albumin. Can J Physiol Pharmacol 47: 487-490.
    • (1969) Can J Physiol Pharmacol , vol.47 , pp. 487-490
    • Schlosser, E.1
  • 30
    • 0023718731 scopus 로고
    • Drug solubilizers to aid pharmacologists: amorphous cyclodextrin derivatives
    • Pitha J, Irie T, Sklar PB, Nye JS, (1988) Drug solubilizers to aid pharmacologists: amorphous cyclodextrin derivatives. Life Sci 43: 493-502.
    • (1988) Life Sci , vol.43 , pp. 493-502
    • Pitha, J.1    Irie, T.2    Sklar, P.B.3    Nye, J.S.4
  • 31
    • 33845915792 scopus 로고    scopus 로고
    • Isolation and characterization of a proteinase K-sensitive PrPSc fraction
    • Pastrana MA, Sajnani G, Onisko B, Castilla J, Morales R, et al. (2006) Isolation and characterization of a proteinase K-sensitive PrPSc fraction. Biochemistry 45: 15710-15717.
    • (2006) Biochemistry , vol.45 , pp. 15710-15717
    • Pastrana, M.A.1    Sajnani, G.2    Onisko, B.3    Castilla, J.4    Morales, R.5
  • 32
    • 0037159185 scopus 로고    scopus 로고
    • Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes
    • Tzaban S, Friedlander G, Schonberger O, Horonchik L, Yedidia Y, et al. (2002) Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes. Biochemistry 41: 12868-12875.
    • (2002) Biochemistry , vol.41 , pp. 12868-12875
    • Tzaban, S.1    Friedlander, G.2    Schonberger, O.3    Horonchik, L.4    Yedidia, Y.5
  • 33
    • 77249149930 scopus 로고    scopus 로고
    • Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins
    • Silva JL, Vieira TC, Gomes MP, Bom AP, Lima LM, et al. (2010) Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins. Acc Chem Res 43: 271-279.
    • (2010) Acc Chem Res , vol.43 , pp. 271-279
    • Silva, J.L.1    Vieira, T.C.2    Gomes, M.P.3    Bom, A.P.4    Lima, L.M.5
  • 34
    • 3543030409 scopus 로고    scopus 로고
    • Hydration and packing effects on prion folding and beta-sheet conversion. High pressure spectroscopy and pressure perturbation calorimetry studies
    • Cordeiro Y, Kraineva J, Ravindra R, Lima LM, Gomes MP, et al. (2004) Hydration and packing effects on prion folding and beta-sheet conversion. High pressure spectroscopy and pressure perturbation calorimetry studies. J Biol Chem 279: 32354-32359.
    • (2004) J Biol Chem , vol.279 , pp. 32354-32359
    • Cordeiro, Y.1    Kraineva, J.2    Ravindra, R.3    Lima, L.M.4    Gomes, M.P.5
  • 35
    • 19644385843 scopus 로고    scopus 로고
    • Prion and water: tight and dynamical hydration sites have a key role in structural stability
    • De Simone A, Dodson GG, Verma CS, Zagari A, Fraternali F, (2005) Prion and water: tight and dynamical hydration sites have a key role in structural stability. Proc Natl Acad Sci U S A 102: 7535-7540.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 7535-7540
    • De Simone, A.1    Dodson, G.G.2    Verma, C.S.3    Zagari, A.4    Fraternali, F.5
  • 36
    • 0029075988 scopus 로고
    • Oligomeric structure of caveolin: implications for caveolae membrane organization
    • Sargiacomo M, Scherer PE, Tang Z, Kubler E, Song KS, et al. (1995) Oligomeric structure of caveolin: implications for caveolae membrane organization. Proc Natl Acad Sci U S A 92: 9407-9411.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9407-9411
    • Sargiacomo, M.1    Scherer, P.E.2    Tang, Z.3    Kubler, E.4    Song, K.S.5
  • 40
    • 4644311920 scopus 로고    scopus 로고
    • Average protein density is a molecular-weight-dependent function
    • Fischer H, Polikarpov I, Craievich AF, (2004) Average protein density is a molecular-weight-dependent function. Protein Sci 13: 2825-2828.
    • (2004) Protein Sci , vol.13 , pp. 2825-2828
    • Fischer, H.1    Polikarpov, I.2    Craievich, A.F.3
  • 41
    • 77951217018 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent
    • Dron M, Moudjou M, Chapuis J, Salamat MK, Bernard J, et al. (2010) Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent. J Biol Chem 285: 10252-10264.
    • (2010) J Biol Chem , vol.285 , pp. 10252-10264
    • Dron, M.1    Moudjou, M.2    Chapuis, J.3    Salamat, M.K.4    Bernard, J.5
  • 42
    • 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, Aguzzi A, Kincaid AE, et al. (2011) The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease. PLoS Pathog 7: e1001317.
    • (2011) PLoS Pathog , vol.7
    • Ayers, J.I.1    Schutt, C.R.2    Shikiya, R.A.3    Aguzzi, A.4    Kincaid, A.E.5
  • 43
    • 78651252313 scopus 로고    scopus 로고
    • Cellular and sub-cellular pathology of animal prion diseases: relationship between morphological changes, accumulation of abnormal prion protein and clinical disease
    • Jeffrey M, McGovern G, Siso S, Gonzalez L, (2011) Cellular and sub-cellular pathology of animal prion diseases: relationship between morphological changes, accumulation of abnormal prion protein and clinical disease. Acta Neuropathol 121: 113-134.
    • (2011) Acta Neuropathol , vol.121 , pp. 113-134
    • Jeffrey, M.1    McGovern, G.2    Siso, S.3    Gonzalez, L.4
  • 44
    • 25844472720 scopus 로고    scopus 로고
    • The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation
    • Cordeiro Y, Kraineva J, Gomes MP, Lopes MH, Martins VR, et al. (2005) The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation. Biophys J 89: 2667-2676.
    • (2005) Biophys J , vol.89 , pp. 2667-2676
    • Cordeiro, Y.1    Kraineva, J.2    Gomes, M.P.3    Lopes, M.H.4    Martins, V.R.5
  • 45
    • 59049099079 scopus 로고    scopus 로고
    • A comprehensive model for packing and hydration for amyloid fibrils of beta2-microglobulin
    • Lee YH, Chatani E, Sasahara K, Naiki H, Goto Y, (2009) A comprehensive model for packing and hydration for amyloid fibrils of beta2-microglobulin. J Biol Chem 284: 2169-2175.
    • (2009) J Biol Chem , vol.284 , pp. 2169-2175
    • Lee, Y.H.1    Chatani, E.2    Sasahara, K.3    Naiki, H.4    Goto, Y.5
  • 46
    • 27544484009 scopus 로고    scopus 로고
    • Thermodynamic properties underlying the alpha-helix-to-beta-sheet transition, aggregation, and amyloidogenesis of polylysine as probed by calorimetry, densimetry, and ultrasound velocimetry
    • Smirnovas V, Winter R, Funck T, Dzwolak W, (2005) Thermodynamic properties underlying the alpha-helix-to-beta-sheet transition, aggregation, and amyloidogenesis of polylysine as probed by calorimetry, densimetry, and ultrasound velocimetry. J Phys Chem B 109: 19043-19045.
    • (2005) J Phys Chem B , vol.109 , pp. 19043-19045
    • Smirnovas, V.1    Winter, R.2    Funck, T.3    Dzwolak, W.4
  • 47
    • 0043194011 scopus 로고    scopus 로고
    • Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities
    • Foguel D, Suarez MC, Ferrao-Gonzales AD, Porto TC, Palmieri L, et al. (2003) Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities. Proc Natl Acad Sci U S A 100: 9831-9836.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9831-9836
    • Foguel, D.1    Suarez, M.C.2    Ferrao-Gonzales, A.D.3    Porto, T.C.4    Palmieri, L.5
  • 48
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey B, Baron GS, (2006) Prions and their partners in crime. Nature 443: 803-810.
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 49
    • 84863913395 scopus 로고    scopus 로고
    • Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions
    • Deleault NR, Walsh DJ, Piro JR, Wang F, Wang X, et al. (2012) Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions. Proc Natl Acad Sci U S A 109: E1938-1946.
    • (2012) Proc Natl Acad Sci U S A , vol.109
    • Deleault, N.R.1    Walsh, D.J.2    Piro, J.R.3    Wang, F.4    Wang, X.5
  • 50
    • 0023769532 scopus 로고
    • Solubilization and hydrodynamic properties of pig atrial muscarinic acetylcholine receptor in dodecyl beta-D-maltoside
    • Peterson GL, Rosenbaum LC, Schimerlik MI, (1988) Solubilization and hydrodynamic properties of pig atrial muscarinic acetylcholine receptor in dodecyl beta-D-maltoside. Biochem J 255: 553-560.
    • (1988) Biochem J , vol.255 , pp. 553-560
    • Peterson, G.L.1    Rosenbaum, L.C.2    Schimerlik, M.I.3
  • 51
    • 33646180878 scopus 로고    scopus 로고
    • Solubilization and immunopurification of rat brain synaptic vesicle protein 2A with maintained binding properties
    • Lambeng N, Grossmann M, Chatelain P, Fuks B, (2006) Solubilization and immunopurification of rat brain synaptic vesicle protein 2A with maintained binding properties. Neurosci Lett 398: 107-112.
    • (2006) Neurosci Lett , vol.398 , pp. 107-112
    • Lambeng, N.1    Grossmann, M.2    Chatelain, P.3    Fuks, B.4
  • 52
    • 0017286349 scopus 로고
    • Partial purification of the scrapie agent from mouse brain by pressure disruption and zonal centrifugation in sucrose-sodium chloride gradients
    • Siakotos AN, Gajdusek DC, Gibbs CJ Jr, Traub RD, Bucana C, (1976) Partial purification of the scrapie agent from mouse brain by pressure disruption and zonal centrifugation in sucrose-sodium chloride gradients. Virology 70: 230-237.
    • (1976) Virology , vol.70 , pp. 230-237
    • Siakotos, A.N.1    Gajdusek, D.C.2    Gibbs Jr., C.J.3    Traub, R.D.4    Bucana, C.5
  • 53
    • 0024551140 scopus 로고
    • Physical properties of the Creutzfeldt-Jakob disease agent
    • Sklaviadis T, Manuelidis L, Manuelidis EE, (1989) Physical properties of the Creutzfeldt-Jakob disease agent. J Virol 63: 1212-1222.
    • (1989) J Virol , vol.63 , pp. 1212-1222
    • Sklaviadis, T.1    Manuelidis, L.2    Manuelidis, E.E.3
  • 54
    • 0030019508 scopus 로고    scopus 로고
    • The association between PrP and infectivity in scrapie and BSE infected mouse brain
    • Somerville RA, Dunn AJ, (1996) The association between PrP and infectivity in scrapie and BSE infected mouse brain. Arch Virol 141: 275-289.
    • (1996) Arch Virol , vol.141 , pp. 275-289
    • Somerville, R.A.1    Dunn, A.J.2
  • 55
    • 0037040886 scopus 로고    scopus 로고
    • Apolipoprotein A-I induces translocation of cholesterol, phospholipid, and caveolin-1 to cytosol in rat astrocytes
    • Ito J, Nagayasu Y, Kato K, Sato R, Yokoyama S, (2002) Apolipoprotein A-I induces translocation of cholesterol, phospholipid, and caveolin-1 to cytosol in rat astrocytes. J Biol Chem 277: 7929-7935.
    • (2002) J Biol Chem , vol.277 , pp. 7929-7935
    • Ito, J.1    Nagayasu, Y.2    Kato, K.3    Sato, R.4    Yokoyama, S.5
  • 56
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrPsc molecules with different conformations
    • Safar J, Wille H, Itri V, Groth D, Serban H, et al. (1998) Eight prion strains have PrPsc molecules with different conformations. Nat Med 4: 1157-1165.
    • (1998) Nat Med , vol.4 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3    Groth, D.4    Serban, H.5
  • 57
    • 58149280203 scopus 로고    scopus 로고
    • Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin
    • Cronier S, Gros N, Tattum MH, Jackson GS, Clarke AR, et al. (2008) Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin. Biochem J 416: 297-305.
    • (2008) Biochem J , vol.416 , pp. 297-305
    • Cronier, S.1    Gros, N.2    Tattum, M.H.3    Jackson, G.S.4    Clarke, A.R.5
  • 59
    • 84861209811 scopus 로고    scopus 로고
    • PK-sensitive PrP is infectious and shares basic structural features with PK-resistant PrP
    • Sajnani G, Silva CJ, Ramos A, Pastrana MA, Onisko BC, et al. (2012) PK-sensitive PrP is infectious and shares basic structural features with PK-resistant PrP. PLoS Pathog 8: e1002547.
    • (2012) PLoS Pathog , vol.8
    • Sajnani, G.1    Silva, C.J.2    Ramos, A.3    Pastrana, M.A.4    Onisko, B.C.5
  • 60
    • 33645305159 scopus 로고    scopus 로고
    • Preparation of soluble infectious samples from scrapie-infected brain: a new tool to study the clearance of transmissible spongiform encephalopathy agents during plasma fractionation
    • Berardi VA, Cardone F, Valanzano A, Lu M, Pocchiari M, (2006) Preparation of soluble infectious samples from scrapie-infected brain: a new tool to study the clearance of transmissible spongiform encephalopathy agents during plasma fractionation. Transfusion 46: 652-658.
    • (2006) Transfusion , vol.46 , pp. 652-658
    • Berardi, V.A.1    Cardone, F.2    Valanzano, A.3    Lu, M.4    Pocchiari, M.5
  • 61
    • 54449083425 scopus 로고    scopus 로고
    • The effects of prion protein proteolysis and disaggregation on the strain properties of hamster scrapie
    • Deleault AM, Deleault NR, Harris BT, Rees JR, Supattapone S, (2008) The effects of prion protein proteolysis and disaggregation on the strain properties of hamster scrapie. J Gen Virol 89: 2642-2650.
    • (2008) J Gen Virol , vol.89 , pp. 2642-2650
    • Deleault, A.M.1    Deleault, N.R.2    Harris, B.T.3    Rees, J.R.4    Supattapone, S.5
  • 62
    • 84866183670 scopus 로고    scopus 로고
    • Small Protease Sensitive Oligomers of PrP(Sc) in Distinct Human Prions Determine Conversion Rate of PrP(C)
    • Kim C, Haldiman T, Surewicz K, Cohen Y, Chen W, et al. (2012) Small Protease Sensitive Oligomers of PrP(Sc) in Distinct Human Prions Determine Conversion Rate of PrP(C). PLoS Pathog 8: e1002835.
    • (2012) PLoS Pathog , vol.8
    • Kim, C.1    Haldiman, T.2    Surewicz, K.3    Cohen, Y.4    Chen, W.5
  • 63
    • 34648819293 scopus 로고    scopus 로고
    • Molecular profiling of ovine prion diseases by using thermolysin-resistant PrPSc and endogenous C2 PrP fragments
    • Owen JP, Rees HC, Maddison BC, Terry LA, Thorne L, et al. (2007) Molecular profiling of ovine prion diseases by using thermolysin-resistant PrPSc and endogenous C2 PrP fragments. J Virol 81: 10532-10539.
    • (2007) J Virol , vol.81 , pp. 10532-10539
    • Owen, J.P.1    Rees, H.C.2    Maddison, B.C.3    Terry, L.A.4    Thorne, L.5
  • 64
    • 11844286389 scopus 로고    scopus 로고
    • Efficient inhibition of prion replication by PrP-Fc(2) suggests that the prion is a PrP(Sc) oligomer
    • Masel J, Genoud N, Aguzzi A, (2005) Efficient inhibition of prion replication by PrP-Fc(2) suggests that the prion is a PrP(Sc) oligomer. J Mol Biol 345: 1243-1251.
    • (2005) J Mol Biol , vol.345 , pp. 1243-1251
    • Masel, J.1    Genoud, N.2    Aguzzi, A.3
  • 65
    • 84864009032 scopus 로고    scopus 로고
    • Assessment of strain-specific PrP(Sc) elongation rates revealed a transformation of PrP(Sc) properties during protein misfolding cyclic amplification
    • Gonzalez-Montalban N, Baskakov IV, (2012) Assessment of strain-specific PrP(Sc) elongation rates revealed a transformation of PrP(Sc) properties during protein misfolding cyclic amplification. PLoS One 7: e41210.
    • (2012) PLoS One , vol.7
    • Gonzalez-Montalban, N.1    Baskakov, I.V.2
  • 66
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr, (1993) Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73: 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 67
    • 0032968132 scopus 로고    scopus 로고
    • Quantifying the kinetic parameters of prion replication
    • Masel J, Jansen VA, Nowak MA, (1999) Quantifying the kinetic parameters of prion replication. Biophys Chem 77: 139-152.
    • (1999) Biophys Chem , vol.77 , pp. 139-152
    • Masel, J.1    Jansen, V.A.2    Nowak, M.A.3
  • 68
    • 0030155687 scopus 로고    scopus 로고
    • Prion replication and secondary nucleation
    • Orgel LE, (1996) Prion replication and secondary nucleation. Chem Biol 3: 413-414.
    • (1996) Chem Biol , vol.3 , pp. 413-414
    • Orgel, L.E.1
  • 70
    • 0035794531 scopus 로고    scopus 로고
    • Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form
    • Leclerc E, Peretz D, Ball H, Sakurai H, Legname G, et al. (2001) Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form. EMBO J 20: 1547-1554.
    • (2001) EMBO J , vol.20 , pp. 1547-1554
    • Leclerc, E.1    Peretz, D.2    Ball, H.3    Sakurai, H.4    Legname, G.5
  • 71
    • 34447639732 scopus 로고    scopus 로고
    • Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes
    • Legname G, Nguyen HO, Peretz D, Cohen FE, DeArmond SJ, et al. (2006) Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci U S A 103: 19105-19110.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19105-19110
    • Legname, G.1    Nguyen, H.O.2    Peretz, D.3    Cohen, F.E.4    DeArmond, S.J.5
  • 72
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • Tanaka M, Collins SR, Toyama BH, Weissman JS, (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442: 585-589.
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 73
    • 34250681413 scopus 로고    scopus 로고
    • Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage
    • Eghiaian F, Daubenfeld T, Quenet Y, van Audenhaege M, Bouin AP, et al. (2007) Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage. Proc Natl Acad Sci U S A 104: 7414-7419.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7414-7419
    • Eghiaian, F.1    Daubenfeld, T.2    Quenet, Y.3    van Audenhaege, M.4    Bouin, A.P.5
  • 74
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid
    • Gosal WS, Morten IJ, Hewitt EW, Smith DA, Thomson NH, et al. (2005) Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J Mol Biol 351: 850-864.
    • (2005) J Mol Biol , vol.351 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5
  • 75
    • 0037066715 scopus 로고    scopus 로고
    • Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH
    • Souillac PO, Uversky VN, Millett IS, Khurana R, Doniach S, et al. (2002) Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH. J Biol Chem 277: 12666-12679.
    • (2002) J Biol Chem , vol.277 , pp. 12666-12679
    • Souillac, P.O.1    Uversky, V.N.2    Millett, I.S.3    Khurana, R.4    Doniach, S.5
  • 78
    • 0018215610 scopus 로고
    • Unusual resistance to ionizing radiation of the viruses of kuru, Creutzfeldt-Jakob disease, and scrapie
    • Gibbs CJ Jr, Gajdusek DC, Latarjet R, (1978) Unusual resistance to ionizing radiation of the viruses of kuru, Creutzfeldt-Jakob disease, and scrapie. Proc Natl Acad Sci U S A 75: 6268-6270.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 6268-6270
    • Gibbs Jr., C.J.1    Gajdusek, D.C.2    Latarjet, R.3
  • 79
    • 0030026759 scopus 로고    scopus 로고
    • Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity
    • Riesner D, Kellings K, Post K, Wille H, Serban H, et al. (1996) Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity. J Virol 70: 1714-1722.
    • (1996) J Virol , vol.70 , pp. 1714-1722
    • Riesner, D.1    Kellings, K.2    Post, K.3    Wille, H.4    Serban, H.5
  • 81
    • 79953127836 scopus 로고    scopus 로고
    • Recovery of small infectious PrP(res) aggregates from prion-infected cultured cells
    • Anaya ZE, Savistchenko J, Massonneau V, Lacroux C, Andreoletti O, et al. (2011) Recovery of small infectious PrP(res) aggregates from prion-infected cultured cells. J Biol Chem 286: 8141-8148.
    • (2011) J Biol Chem , vol.286 , pp. 8141-8148
    • Anaya, Z.E.1    Savistchenko, J.2    Massonneau, V.3    Lacroux, C.4    Andreoletti, O.5
  • 82
    • 84865786047 scopus 로고    scopus 로고
    • Endogenous prion protein conversion is required for prion-induced neuritic alterations and neuronal death
    • Cronier S, Carimalo J, Schaeffer B, Jaumain E, Beringue V, et al. (2012) Endogenous prion protein conversion is required for prion-induced neuritic alterations and neuronal death. FASEB J 26: 3854-3861.
    • (2012) FASEB J , vol.26 , pp. 3854-3861
    • Cronier, S.1    Carimalo, J.2    Schaeffer, B.3    Jaumain, E.4    Beringue, V.5
  • 83
    • 84863986886 scopus 로고    scopus 로고
    • Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity
    • Fandrich M, (2012) Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity. J Mol Biol 421: 427-440.
    • (2012) J Mol Biol , vol.421 , pp. 427-440
    • Fandrich, M.1
  • 84
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker M, Walker LC, (2011) Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann Neurol 70: 532-540.
    • (2011) Ann Neurol , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2


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