메뉴 건너뛰기




Volumn 8, Issue 8, 2012, Pages

Small Protease Sensitive Oligomers of PrPSc in Distinct Human Prions Determine Conversion Rate of PrPC

Author keywords

[No Author keywords available]

Indexed keywords

OLIGOMER; PRION PROTEIN;

EID: 84866183670     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002835     Document Type: Article
Times cited : (69)

References (63)
  • 1
    • 3442881123 scopus 로고    scopus 로고
    • Transmission and replication of prions
    • In: Prusiner SB, editor 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Prusiner SB, Scott MR, DeArmond SJ, Carlson G (2004) Transmission and replication of prions. In: Prusiner SB, editor. Prion Biology and Diseases. 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 187-242.
    • (2004) Prion Biology and Diseases , pp. 187-242
    • Prusiner, S.B.1    Scott, M.R.2    DeArmond, S.J.3    Carlson, G.4
  • 2
    • 0014021742 scopus 로고
    • Experimental transmission of a kuru-like syndrome to chimpanzees
    • Gajdusek DC, Gibbs CJ Jr, Alpers M, (1966) Experimental transmission of a kuru-like syndrome to chimpanzees. Nature 209: 794-796.
    • (1966) Nature , vol.209 , pp. 794-796
    • Gajdusek, D.C.1    Gibbs Jr., C.J.2    Alpers, M.3
  • 3
    • 0014430962 scopus 로고
    • Creutzfeldt-Jakob disease (spongiform encephalopathy): transmission to the chimpanzee
    • Gibbs CJ Jr, Gajdusek DC, Asher DM, Alpers MP, Beck E, et al. (1968) Creutzfeldt-Jakob disease (spongiform encephalopathy): transmission to the chimpanzee. Science 161: 388-389.
    • (1968) Science , vol.161 , pp. 388-389
    • Gibbs Jr., C.J.1    Gajdusek, D.C.2    Asher, D.M.3    Alpers, M.P.4    Beck, E.5
  • 4
    • 80053451037 scopus 로고    scopus 로고
    • Protease-Sensitive Conformers in Broad Spectrum of Distinct PrP Structures in Sporadic Creutzfeldt-Jakob Disease Are Indicator of Progression Rate
    • Kim C, Haldiman T, Cohen Y, Chen W, Blevins J, et al. (2011) Protease-Sensitive Conformers in Broad Spectrum of Distinct PrP Structures in Sporadic Creutzfeldt-Jakob Disease Are Indicator of Progression Rate. PLoS Pathog 7: e1002242.
    • (2011) PLoS Pathog , vol.7
    • Kim, C.1    Haldiman, T.2    Cohen, Y.3    Chen, W.4    Blevins, J.5
  • 6
    • 77955344991 scopus 로고    scopus 로고
    • Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties
    • Bishop MT, Will RG, Manson JC, (2010) Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties. Proc Natl Acad Sci U S A 107: 12005-12010.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 12005-12010
    • Bishop, M.T.1    Will, R.G.2    Manson, J.C.3
  • 7
    • 80054774250 scopus 로고    scopus 로고
    • Prion protein and its conformational conversion: a structural perspective
    • Surewicz WK, Apostol MI, (2011) Prion protein and its conformational conversion: a structural perspective. Top Curr Chem 305: 135-167.
    • (2011) Top Curr Chem , vol.305 , pp. 135-167
    • Surewicz, W.K.1    Apostol, M.I.2
  • 8
    • 79953785159 scopus 로고    scopus 로고
    • Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange
    • Smirnovas V, Baron GS, Offerdahl DK, Raymond GJ, Caughey B, et al. (2011) Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol 18: 504-506.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 504-506
    • Smirnovas, V.1    Baron, G.S.2    Offerdahl, D.K.3    Raymond, G.J.4    Caughey, B.5
  • 9
    • 82755176171 scopus 로고    scopus 로고
    • Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils
    • Jones EM, Wu B, Surewicz K, Nadaud PS, Helmus JJ, et al. (2011) Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils. J Biol Chem 286: 42777-42784.
    • (2011) J Biol Chem , vol.286 , pp. 42777-42784
    • Jones, E.M.1    Wu, B.2    Surewicz, K.3    Nadaud, P.S.4    Helmus, J.J.5
  • 10
    • 0141514771 scopus 로고    scopus 로고
    • Sporadic and familial CJD: classification and characterisation
    • Gambetti P, Kong Q, Zou W, Parchi P, Chen SG, (2003) Sporadic and familial CJD: classification and characterisation. Br Med Bull 66: 213-239.
    • (2003) Br Med Bull , vol.66 , pp. 213-239
    • Gambetti, P.1    Kong, Q.2    Zou, W.3    Parchi, P.4    Chen, S.G.5
  • 11
    • 46749121818 scopus 로고    scopus 로고
    • A novel human disease with abnormal prion protein sensitive to protease
    • Gambetti P, Dong Z, Yuan J, Xiao X, Zheng M, et al. (2008) A novel human disease with abnormal prion protein sensitive to protease. Ann Neurol 63: 697-708.
    • (2008) Ann Neurol , vol.63 , pp. 697-708
    • Gambetti, P.1    Dong, Z.2    Yuan, J.3    Xiao, X.4    Zheng, M.5
  • 12
    • 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
  • 14
    • 0029937271 scopus 로고    scopus 로고
    • NMR structure of the mouse prion protein domain PrP(121-231)
    • Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, et al. (1996) NMR structure of the mouse prion protein domain PrP(121-231). Nature 382: 180-182.
    • (1996) Nature , vol.382 , pp. 180-182
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Billeter, M.4    Glockshuber, R.5
  • 16
    • 0027332116 scopus 로고
    • Conversion of a-helices into b-sheets features in the formation of the scrapie prion proteins
    • Pan K-M, Baldwin M, Nguyen J, Gasset M, Serban A, et al. (1993) Conversion of a-helices into b-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90: 10962-10966.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.-M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5
  • 17
    • 0027182522 scopus 로고
    • Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein
    • Safar J, Roller PP, Gajdusek DC, Gibbs CJ Jr, (1993) Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J Biol Chem 268: 20276-20284.
    • (1993) J Biol Chem , vol.268 , pp. 20276-20284
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 18
    • 3442879322 scopus 로고    scopus 로고
    • Development of the prion concept
    • In: Prusiner SB, editor 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Prusiner SB (2004) Development of the prion concept. In: Prusiner SB, editor. Prion Biology and Diseases. 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 89-141.
    • (2004) Prion Biology and Diseases , pp. 89-141
    • Prusiner, S.B.1
  • 20
    • 80055020932 scopus 로고    scopus 로고
    • High CJD infectivity remains after prion protein is destroyed
    • Miyazawa K, Emmerling K, Manuelidis L, (2011) High CJD infectivity remains after prion protein is destroyed. J Cell Biochem 112: 3630-3637.
    • (2011) J Cell Biochem , vol.112 , pp. 3630-3637
    • Miyazawa, K.1    Emmerling, K.2    Manuelidis, L.3
  • 21
    • 43249086837 scopus 로고    scopus 로고
    • Host PrP glycosylation: a major factor determining the outcome of prion infection
    • Tuzi NL, Cancellotti E, Baybutt H, Blackford L, Bradford B, et al. (2008) Host PrP glycosylation: a major factor determining the outcome of prion infection. PLoS Biol 6: e100.
    • (2008) PLoS Biol , vol.6
    • Tuzi, N.L.1    Cancellotti, E.2    Baybutt, H.3    Blackford, L.4    Bradford, B.5
  • 22
    • 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
  • 24
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio GP, Permanne B, Soto C, (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411: 810-813.
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 25
    • 82755197344 scopus 로고    scopus 로고
    • Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions
    • Klingeborn M, Race B, Meade-White KD, Chesebro B, (2011) Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions. Proc Natl Acad Sci U S A 108: E1244-53.
    • (2011) Proc Natl Acad Sci U S A , vol.108
    • Klingeborn, M.1    Race, B.2    Meade-White, K.D.3    Chesebro, B.4
  • 27
    • 40149090017 scopus 로고    scopus 로고
    • Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking
    • Atarashi R, Wilham JM, Christensen L, Hughson AG, Moore RA, et al. (2008) Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking. Nat Methods 5: 211-212.
    • (2008) Nat Methods , vol.5 , pp. 211-212
    • Atarashi, R.1    Wilham, J.M.2    Christensen, L.3    Hughson, A.G.4    Moore, R.A.5
  • 28
    • 34547638271 scopus 로고    scopus 로고
    • Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein
    • Atarashi R, Moore RA, Sim VL, Hughson AG, Dorward DW, et al. (2007) Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat Methods 4: 645-650.
    • (2007) Nat Methods , vol.4 , pp. 645-650
    • Atarashi, R.1    Moore, R.A.2    Sim, V.L.3    Hughson, A.G.4    Dorward, D.W.5
  • 29
    • 77951979579 scopus 로고    scopus 로고
    • Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors
    • Kim JI, Cali I, Surewicz K, Kong Q, Raymond GJ, et al. (2010) Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 285: 14083-14087.
    • (2010) J Biol Chem , vol.285 , pp. 14083-14087
    • Kim, J.I.1    Cali, I.2    Surewicz, K.3    Kong, Q.4    Raymond, G.J.5
  • 30
    • 79751535822 scopus 로고    scopus 로고
    • Ultrasensitive human prion detection in cerebrospinal fluid by real-time quaking-induced conversion
    • Atarashi R, Satoh K, Sano K, Fuse T, Yamaguchi N, et al. (2011) Ultrasensitive human prion detection in cerebrospinal fluid by real-time quaking-induced conversion. Nat Med 17: 175-178.
    • (2011) Nat Med , vol.17 , pp. 175-178
    • Atarashi, R.1    Satoh, K.2    Sano, K.3    Fuse, T.4    Yamaguchi, N.5
  • 31
    • 78651249792 scopus 로고    scopus 로고
    • Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays
    • Wilham JM, Orru CD, Bessen RA, Atarashi R, Sano K, et al. (2010) Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays. PLoS Pathog 6: e1001217.
    • (2010) PLoS Pathog , vol.6
    • Wilham, J.M.1    Orru, C.D.2    Bessen, R.A.3    Atarashi, R.4    Sano, K.5
  • 34
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F, Wang X, Yuan CG, Ma J, (2010) Generating a prion with bacterially expressed recombinant prion protein. Science 327: 1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 36
    • 80054733246 scopus 로고    scopus 로고
    • Prion seeded conversion and amplification assays
    • Orru CD, Caughey B, (2011) Prion seeded conversion and amplification assays. Top Curr Chem 305: 121-133.
    • (2011) Top Curr Chem , vol.305 , pp. 121-133
    • Orru, C.D.1    Caughey, B.2
  • 37
    • 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, Deering C, Didorenko S, et al. (2002) Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice. Nat Biotechnol 20: 1147-1150.
    • (2002) Nat Biotechnol , vol.20 , pp. 1147-1150
    • Safar, J.G.1    Scott, M.2    Monaghan, J.3    Deering, C.4    Didorenko, S.5
  • 38
    • 70349937836 scopus 로고    scopus 로고
    • Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: its effect on the phenotype and prion-type characteristics
    • Cali I, Castellani R, Alshekhlee A, Cohen Y, Blevins J, et al. (2009) Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: its effect on the phenotype and prion-type characteristics. Brain 132: 2643-2658.
    • (2009) Brain , vol.132 , pp. 2643-2658
    • Cali, I.1    Castellani, R.2    Alshekhlee, A.3    Cohen, Y.4    Blevins, J.5
  • 40
    • 0029962468 scopus 로고    scopus 로고
    • Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains
    • Vey M, Pilkuhn S, Wille H, Nixon R, DeArmond SJ, et al. (1996) Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc Natl Acad Sci USA 93: 14945-14949.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14945-14949
    • Vey, M.1    Pilkuhn, S.2    Wille, H.3    Nixon, R.4    DeArmond, S.J.5
  • 41
    • 0031843985 scopus 로고    scopus 로고
    • Prion rods contain small amounts of two sphingolipids as revealed by thin-layer chromatography and mass spectrometry
    • Klein TR, Kirsch D, Kaufmann R, Riesner D, (1998) Prion rods contain small amounts of two sphingolipids as revealed by thin-layer chromatography and mass spectrometry. J Biol Chem 379: 655-666.
    • (1998) J Biol Chem , vol.379 , pp. 655-666
    • Klein, T.R.1    Kirsch, D.2    Kaufmann, R.3    Riesner, D.4
  • 42
    • 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, Heye N, Telling G, et al. (2003) Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene. Proc Natl Acad Sci USA 100: 4784-4789.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4784-4789
    • Korth, C.1    Kaneko, K.2    Groth, D.3    Heye, N.4    Telling, G.5
  • 44
    • 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
  • 45
    • 33845915792 scopus 로고    scopus 로고
    • Isolation and characterization of a proteinase K-sensitive PrP(Sc) fraction
    • Pastrana MA, Sajnani G, Onisko B, Castilla J, Morales R, et al. (2006) Isolation and characterization of a proteinase K-sensitive PrP(Sc) 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
  • 47
    • 34548394607 scopus 로고    scopus 로고
    • In vitro amplification and detection of variant Creutzfeldt-Jakob disease PrP(Sc)
    • Jones M, Peden A, Prowse C, Groner A, Manson J, et al. (2007) In vitro amplification and detection of variant Creutzfeldt-Jakob disease PrP(Sc). J Pathol 213: 21-26.
    • (2007) J Pathol , vol.213 , pp. 21-26
    • Jones, M.1    Peden, A.2    Prowse, C.3    Groner, A.4    Manson, J.5
  • 48
    • 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
  • 49
    • 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, Cohen FE, DeArmond SJ, et al. (2006) Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci USA 103: 19105-19110.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 19105-19110
    • Legname, G.1    Nguyen, H.-O.B.2    Peretz, D.3    Cohen, F.E.4    DeArmond, S.J.5
  • 50
    • 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
  • 53
    • 8944259890 scopus 로고    scopus 로고
    • Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease
    • Parchi P, Castellani R, Capellari S, Ghetti B, Young K, et al. (1996) Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann Neurol 39: 767-778.
    • (1996) Ann Neurol , vol.39 , pp. 767-778
    • Parchi, P.1    Castellani, R.2    Capellari, S.3    Ghetti, B.4    Young, K.5
  • 54
    • 66549125845 scopus 로고    scopus 로고
    • Prion proteins in subpopulations of white blood cells from patients with sporadic Creutzfeldt-Jakob disease
    • Choi EM, Geschwind MD, Deering C, Pomeroy K, Kuo A, et al. (2009) Prion proteins in subpopulations of white blood cells from patients with sporadic Creutzfeldt-Jakob disease. Lab Invest 89: 624-635.
    • (2009) Lab Invest , vol.89 , pp. 624-635
    • Choi, E.M.1    Geschwind, M.D.2    Deering, C.3    Pomeroy, K.4    Kuo, A.5
  • 55
    • 13144256747 scopus 로고    scopus 로고
    • Prion protein expression in different species: Analysis with a panel of new mAbs
    • Zanusso G, Liu D, Ferrari S, Hegyi I, Yin X, et al. (1998) Prion protein expression in different species: Analysis with a panel of new mAbs. Proc Natl Acad Sci USA 95: 8812-8816.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8812-8816
    • Zanusso, G.1    Liu, D.2    Ferrari, S.3    Hegyi, I.4    Yin, X.5
  • 56
    • 0023499868 scopus 로고
    • Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins
    • Kascsak RJ, Rubenstein R, Merz PA, Tonna-DeMasi M, Fersko R, et al. (1987) Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J Virol 61: 3688-3693.
    • (1987) J Virol , vol.61 , pp. 3688-3693
    • Kascsak, R.J.1    Rubenstein, R.2    Merz, P.A.3    Tonna-DeMasi, M.4    Fersko, R.5
  • 57
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
    • Swietnicki W, Morillas M, Chen SG, Gambetti P, Surewicz WK, (2000) Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 39: 424-431.
    • (2000) Biochemistry , vol.39 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 59
    • 24344492256 scopus 로고    scopus 로고
    • Chronic wasting disease of elk: transmissibility to humans examined by transgenic mouse models
    • Kong Q, Huang S, Zou W, Vanegas D, Wang M, et al. (2005) Chronic wasting disease of elk: transmissibility to humans examined by transgenic mouse models. J Neurosci 25: 7944-7999.
    • (2005) J Neurosci , vol.25 , pp. 7944-7999
    • Kong, Q.1    Huang, S.2    Zou, W.3    Vanegas, D.4    Wang, M.5
  • 60
    • 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, Gabizon R, Torchia M, et al. (1995) Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83: 79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5
  • 61
    • 0033030954 scopus 로고    scopus 로고
    • Ultrastructural studies on scrapie prion protein crystals obtained from reverse micellar solutions
    • Wille H, Prusiner SB, (1999) Ultrastructural studies on scrapie prion protein crystals obtained from reverse micellar solutions. Biophys J 76: 1048-1062.
    • (1999) Biophys J , vol.76 , pp. 1048-1062
    • Wille, H.1    Prusiner, S.B.2
  • 62
    • 0018171392 scopus 로고
    • Sedimentation characteristics of the scrapie agent from murine spleen and brain
    • Prusiner SB, Hadlow WJ, Eklund CM, Race RE, Cochran SP, (1978) Sedimentation characteristics of the scrapie agent from murine spleen and brain. Biochemistry 17: 4987-4992.
    • (1978) Biochemistry , vol.17 , pp. 4987-4992
    • Prusiner, S.B.1    Hadlow, W.J.2    Eklund, C.M.3    Race, R.E.4    Cochran, S.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.