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Volumn 78, Issue , 2009, Pages 177-204

Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions

Author keywords

Exosomes; Glycophosphatidylinositol anchor; Protein misfolding diseases; Tunneling nanotubes

Indexed keywords

AMYLOID; OLIGOMER; PRION PROTEIN;

EID: 67650747654     PISSN: 00664154     EISSN: 00664154     Source Type: Book Series    
DOI: 10.1146/annurev.biochem.78.082907.145410     Document Type: Review
Times cited : (286)

References (161)
  • 1
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith JS. 1967. Self-replication and scrapie. Nature 215:1043-44
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 2
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216:136-44
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 3
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J, Saá P, Hetz C, Soto C. 2005. In vitro generation of infectious scrapie prions. Cell 121:195-206
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saá, P.2    Hetz, C.3    Soto, C.4
  • 5
    • 0028308104 scopus 로고
    • URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisia
    • Wickner RB. 1994. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisia. Science 264:566-69
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 6
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien P, Weissman JS, DePace AH. 2004. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73:617-56
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 7
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner SB, Groth DF, Bolton DC, Kent SB, Hood LE. 1984. Purification and structural studies of a major scrapie prion protein. Cell 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
  • 10
    • 0029066886 scopus 로고
    • Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie spcies barrier
    • Kocisko DA, Priola SA, Raymond GJ, Chesebro B, LansburyPTJr, Caughey B. 1995. Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie spcies barrier. Proc. Natl. Acad. Sci. USA 92:3923-27
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3923-3927
    • Kocisko, D.A.1    Priola, S.A.2    Raymond, G.J.3    Chesebro, B.4    LansburyPTJr, C.B.5
  • 11
    • 0030802361 scopus 로고    scopus 로고
    • Molecular assessment of the transmissibilities of BSE and scrapie to humans
    • Raymond GJ, Hope J, Kocisko DA, Priola SA, Raymond LD, et al. 1997. Molecular assessment of the transmissibilities of BSE and scrapie to humans. Nature 388:285-88
    • (1997) Nature , vol.388 , pp. 285-288
    • Raymond, G.J.1    Hope, J.2    Kocisko, D.A.3    Priola, S.A.4    Raymond, L.D.5
  • 12
    • 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, Lansbury PT. 1995. Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem. Biol. 2:807-17
    • (1995) Chem. Biol , vol.2 , pp. 807-817
    • Caughey, B.1    Kocisko, D.A.2    Raymond, G.J.3    Lansbury, P.T.4
  • 14
    • 0035958977 scopus 로고    scopus 로고
    • Reversibility of scrapie-associated prion protein aggregation
    • Callahan MA, Xiong L, Caughey B. 2001. Reversibility of scrapie-associated prion protein aggregation. J. Biol. Chem. 276:28022-28
    • (2001) J. Biol. Chem , vol.276 , pp. 28022-28028
    • Callahan, M.A.1    Xiong, L.2    Caughey, B.3
  • 15
    • 0024211952 scopus 로고
    • Transmissible and nontransmissible amyloidoses: Autocatalytic post-translational conversion of host precursor proteins to beta-pleated configurations
    • Gadjusek DC. 1988. Transmissible and nontransmissible amyloidoses: autocatalytic post-translational conversion of host precursor proteins to beta-pleated configurations. J. Neuroimmunol. 20:95-110
    • (1988) J. Neuroimmunol , vol.20 , pp. 95-110
    • Gadjusek, D.C.1
  • 16
    • 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 73:1055-58
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 17
    • 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, Lansbury PT Jr. 1997. Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies. J. Virol. 71:4107-10
    • (1997) J. Virol , vol.71 , pp. 4107-4110
    • Caughey, B.1    Raymond, G.J.2    Kocisko, D.A.3    Lansbury Jr., P.T.4
  • 18
    • 0032892306 scopus 로고    scopus 로고
    • Protease-resistant prion protein produced in vitro lacks detectable infectivity
    • Hill AF, Antoniou M, Collinge J. 1999. Protease-resistant prion protein produced in vitro lacks detectable infectivity. J. Gen. Virol. 80:11-14
    • (1999) J. Gen. Virol , vol.80 , pp. 11-14
    • Hill, A.F.1    Antoniou, M.2    Collinge, J.3
  • 21
    • 0028608963 scopus 로고
    • Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein
    • Hsiao KK, Groth D, Scott M, Yang SL, Serban H, et al. 1994. Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc. Natl. Acad. Sci. USA 91:9126-30
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9126-9130
    • Hsiao, K.K.1    Groth, D.2    Scott, M.3    Yang, S.L.4    Serban, H.5
  • 22
    • 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 411:810-13
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 24
    • 33845944898 scopus 로고    scopus 로고
    • Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
    • Saá P, Castilla J, Soto C. 2006. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J. Biol. Chem. 281:35245-52
    • (2006) J. Biol. Chem , vol.281 , pp. 35245-35252
    • Saá, P.1    Castilla, J.2    Soto, C.3
  • 26
    • 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 5:211-12
    • (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
  • 27
    • 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 4:645-50
    • (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
    • 20344394154 scopus 로고    scopus 로고
    • Anchorless prion protein results in infectious amyloid disease without clinical scrapie
    • Chesebro B, Trifilo M, Race R, Meade-White K, Teng C, et al. 2005. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308:1435-39
    • (2005) Science , vol.308 , pp. 1435-1439
    • Chesebro, B.1    Trifilo, M.2    Race, R.3    Meade-White, K.4    Teng, C.5
  • 30
    • 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
  • 31
    • 11144221186 scopus 로고    scopus 로고
    • Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections
    • Neuendorf E,Weber A, Saalmueller A, Schatzl H, Reifenberg K, et al. 2004. Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections. J. Biol. Chem. 279:53306-16
    • (2004) J. Biol. Chem , vol.279 , pp. 53306-53316
    • Neuendorf, E.1    Weber, A.2    Saalmueller, A.3    Schatzl, H.4    Reifenberg, K.5
  • 34
    • 70349858126 scopus 로고    scopus 로고
    • Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils
    • doi:10.1016/j.neurobiolaging.2008.02.016
    • Sim VL, Caughey B. 2008. Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils. Neurobiol. Aging doi:10.1016/j.neurobiolaging.2008.02.016
    • (2008) Neurobiol. Aging
    • Sim, V.L.1    Caughey, B.2
  • 35
    • 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, Ernst D, Hayes SF, Caughey WS. 1991. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30:7672-80
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 36
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into betasheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, et al. 1993. Conversion of alpha-helices into betasheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90:10962-66
    • (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
  • 37
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in beta-sheet conformations of abnormal prion protein
    • Caughey B, Raymond GJ, Bessen RA. 1998. Strain-dependent differences in beta-sheet conformations of abnormal prion protein. J. Biol. Chem. 273:32230-35
    • (1998) J. Biol. Chem , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 38
    • 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 1760:1138-49
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1138-1149
    • Spassov, S.1    Beekes, M.2    Naumann, D.3
  • 39
    • 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. 68:7859-68
    • (1994) J. Virol , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 40
    • 11444251657 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathy strain, PrP genotype and brain region all affect the degree of glycosylation of PrPSc
    • Somerville RA, Hamilton S, Fernie K. 2005. Transmissible spongiform encephalopathy strain, PrP genotype and brain region all affect the degree of glycosylation of PrPSc. J. Gen. Virol. 86:241-46
    • (2005) J. Gen. Virol , vol.86 , pp. 241-246
    • Somerville, R.A.1    Hamilton, S.2    Fernie, K.3
  • 42
    • 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. 39:767-78
    • (1996) Ann. Neurol , vol.39 , pp. 767-778
    • Parchi, P.1    Castellani, R.2    Capellari, S.3    Ghetti, B.4    Young, K.5
  • 43
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of "new variant" CJD
    • Collinge J, Sidle KCL, Meads J, Ironside J, Hill AF. 1996. Molecular analysis of prion strain variation and the aetiology of "new variant" CJD. Nature 383:685-90
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.L.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 44
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrP(Sc) molecules with different conformations
    • Safar J, Wille H, Itri V, Groth D, Serban H, et al. 1998. Eight prion strains have PrP(Sc) molecules with different conformations. Nat. Med. 4:1157-65
    • (1998) Nat. Med , vol.4 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3    Groth, D.4    Serban, H.5
  • 47
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: Protofibril formation of the prion protein
    • Demarco ML, Daggett V. 2004. From conversion to aggregation: protofibril formation of the prion protein. Proc. Natl. Acad. Sci. USA 101:2293-98
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2293-2298
    • Demarco, M.L.1    Daggett, V.2
  • 48
    • 33845932931 scopus 로고    scopus 로고
    • Structural properties of prion protein protofibrils and fibrils: An experimental assessment of atomic models
    • Demarco ML, Silveira J, Caughey B, Daggett V. 2006. Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models. Biochemistry 45:15573-82
    • (2006) Biochemistry , vol.45 , pp. 15573-15582
    • Demarco, M.L.1    Silveira, J.2    Caughey, B.3    Daggett, V.4
  • 49
    • 33846811599 scopus 로고    scopus 로고
    • Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange
    • Lu X, Wintrode PL, Surewicz WK. 2007. Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc. Natl. Acad. Sci. USA 104:1510-15
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 50
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure
    • Cobb NJ, Sonnichsen FD, McHaourab H, Surewicz WK. 2007. Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure. Proc. Natl. Acad. Sci. USA 104:18946-51
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18946-18951
    • Cobb, N.J.1    Sonnichsen, F.D.2    McHaourab, H.3    Surewicz, W.K.4
  • 51
  • 52
    • 29144451322 scopus 로고    scopus 로고
    • Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L)
    • Lim KH, Nguyen TN, Damo SM, Mazur T, Ball HL, et al. 2006. Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L). Solid State Nucl. Magn. Reson. 29:183-90
    • (2006) Solid State Nucl. Magn. Reson , vol.29 , pp. 183-190
    • Lim, K.H.1    Nguyen, T.N.2    Damo, S.M.3    Mazur, T.4    Ball, H.L.5
  • 53
    • 36048969163 scopus 로고    scopus 로고
    • Characterization of betasheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance
    • Baxa U, Wickner RB, Steven AC, Anderson DE, Marekov LN, et al. 2007. Characterization of betasheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance. Biochemistry 46:13149-62
    • (2007) Biochemistry , vol.46 , pp. 13149-13162
    • Baxa, U.1    Wickner, R.B.2    Steven, A.C.3    Anderson, D.E.4    Marekov, L.N.5
  • 54
    • 41449106103 scopus 로고    scopus 로고
    • Amyloids of shuffled prion domains that form prions have a parallel in-register beta-sheet structure
    • Shewmaker F, Ross ED, Tycko R, Wickner RB. 2008. Amyloids of shuffled prion domains that form prions have a parallel in-register beta-sheet structure. Biochemistry 47:4000-7
    • (2008) Biochemistry , vol.47 , pp. 4000-4007
    • Shewmaker, F.1    Ross, E.D.2    Tycko, R.3    Wickner, R.B.4
  • 55
    • 33845938549 scopus 로고    scopus 로고
    • Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure
    • Shewmaker F,Wickner RB, Tycko R. 2006. Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc. Natl. Acad. Sci. USA 103:19754-59
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19754-19759
    • Shewmaker, F.1    Wickner, R.B.2    Tycko, R.3
  • 56
    • 40649098246 scopus 로고    scopus 로고
    • Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure
    • Wickner RB, Dyda F, Tycko R. 2008. Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure. Proc. Natl. Acad. Sci. USA 105:2403-8
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2403-2408
    • Wickner, R.B.1    Dyda, F.2    Tycko, R.3
  • 57
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan R, Lindquist SL. 2005. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435:765-72
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 59
    • 20444458341 scopus 로고    scopus 로고
    • Correlation of structural elements and infectivity of the HET-s prion
    • Ritter C, Maddelein ML, Siemer AB, Lührs T, Ernst M, et al. 2005. Correlation of structural elements and infectivity of the HET-s prion. Nature 435:844-48
    • (2005) Nature , vol.435 , pp. 844-848
    • Ritter, C.1    Maddelein, M.L.2    Siemer, A.B.3    Lührs, T.4    Ernst, M.5
  • 60
    • 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, Siemer AB, Riek R, Meier BH. 2008. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 319:1523-26
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 61
    • 34548615995 scopus 로고    scopus 로고
    • The structural basis of yeast prion strain variants
    • Toyama BH, Kelly MJ, Gross JD,Weissman JS. 2007. The structural basis of yeast prion strain variants. Nature 449:233-37
    • (2007) Nature , vol.449 , pp. 233-237
    • Toyama, B.H.1    Kelly, M.J.2    Gross, J.D.3    Weissman, J.S.4
  • 62
    • 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 442:585-89
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 63
    • 34247856087 scopus 로고    scopus 로고
    • Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure
    • Sun Y, Breydo L, Makarava N, Yang Q, Bocharova OV, Baskakov IV. 2007. Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure. J. Biol. Chem. 282:9090-97
    • (2007) J. Biol. Chem , vol.282 , pp. 9090-9097
    • Sun, Y.1    Breydo, L.2    Makarava, N.3    Yang, Q.4    Bocharova, O.V.5    Baskakov, I.V.6
  • 64
    • 33646093028 scopus 로고    scopus 로고
    • Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy
    • Anderson M, Bocharova OV, Makarava N, Breydo L, Salnikov VV, Baskakov IV. 2006. Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy. J. Mol. Biol. 358:580-96
    • (2006) J. Mol. Biol , vol.358 , pp. 580-596
    • Anderson, M.1    Bocharova, O.V.2    Makarava, N.3    Breydo, L.4    Salnikov, V.V.5    Baskakov, I.V.6
  • 65
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-beta spine of amyloid-like fibrils
    • Nelson R, Sawaya MR, Balbirnie M, Madsen AØ, Riekel C, et al. 2005. Structure of the cross-beta spine of amyloid-like fibrils. Nature 435:773-78
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.4    Riekel, C.5
  • 66
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, et al. 2007. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447:453-57
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3    Ivanova, M.I.4    Sievers, S.A.5
  • 67
    • 0035168351 scopus 로고    scopus 로고
    • Prion diseases: What is the neurotoxic molecule?
    • Chiesa R, Harris DA. 2001. Prion diseases: What is the neurotoxic molecule? Neurobiol. Dis. 8:743-63
    • (2001) Neurobiol. Dis , vol.8 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 68
    • 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. 1991. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase- sensitive. J. Biol. Chem. 266:18217-23
    • (1991) J. Biol. Chem , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 69
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey B, Raymond GJ, Ernst D, Race RE. 1991. N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J. Virol. 65:6597-603
    • (1991) J. Virol , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 70
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion protein in the endocytic pathway
    • Borchelt DR, Taraboulos A, Prusiner SB. 1992. Evidence for synthesis of scrapie prion protein in the endocytic pathway. J. Biol. Chem. 267:16188-99
    • (1992) J. Biol. Chem , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 72
    • 19444376451 scopus 로고    scopus 로고
    • Heparan sulfate is a cellular receptor for purified infectious prions
    • Horonchik L, Tzaban S, Ben-Zaken O, Yedidia Y, Rouvinski A, et al. 2005. Heparan sulfate is a cellular receptor for purified infectious prions. J. Biol. Chem. 280:17062-67
    • (2005) J. Biol. Chem , vol.280 , pp. 17062-17067
    • Horonchik, L.1    Tzaban, S.2    Ben-Zaken, O.3    Yedidia, Y.4    Rouvinski, A.5
  • 73
    • 0035957944 scopus 로고    scopus 로고
    • Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods
    • Shaked GM, Meiner Z, Avraham I, Taraboulos A, Gabizon R. 2001. Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods. J. Biol. Chem. 276:14324-28
    • (2001) J. Biol. Chem , vol.276 , pp. 14324-14328
    • Shaked, G.M.1    Meiner, Z.2    Avraham, I.3    Taraboulos, A.4    Gabizon, R.5
  • 74
    • 0242585507 scopus 로고    scopus 로고
    • The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells
    • 4:290-95
    • Leucht C, Simoneau S, Rey C, Vana K, Rieger R, et al. 2003. The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. EMBO Rep. 4:290-95
    • (2003) EMBO Rep
    • Leucht, C.1    Simoneau, S.2    Rey, C.3    Vana, K.4    Rieger, R.5
  • 75
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Taraboulos A, Scott M, Semenov A, Avraham D, Laszlo L, Prusiner SB. 1995. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J. Cell. Biol. 129:121-32
    • (1995) J. Cell. Biol , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avraham, D.4    Laszlo, L.5    Prusiner, S.B.6
  • 76
    • 35848936977 scopus 로고    scopus 로고
    • Antiprion activity of cholesterol esteri-fication modulators: A comparative study using ex vivo sheep fibroblasts and lymphocytes and mouse neuroblastoma cell lines
    • Pani A, Norfo C, Abete C, Mulas C, Putzolu M, et al. 2007. Antiprion activity of cholesterol esteri-fication modulators: a comparative study using ex vivo sheep fibroblasts and lymphocytes and mouse neuroblastoma cell lines. Antimicrob. Agents Chemother. 51:4141-47
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 4141-4147
    • Pani, A.1    Norfo, C.2    Abete, C.3    Mulas, C.4    Putzolu, M.5
  • 77
    • 0033597931 scopus 로고    scopus 로고
    • Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions
    • Naslavsky N, Shmeeda H, Friedlander G, Yanai A, Futerman AH, et al. 1999. Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions. J. Biol. Chem. 274:20763-71
    • (1999) J. Biol. Chem , vol.274 , pp. 20763-20771
    • Naslavsky, N.1    Shmeeda, H.2    Friedlander, G.3    Yanai, A.4    Futerman, A.H.5
  • 78
    • 57449121226 scopus 로고    scopus 로고
    • Strain-associated variations in abnormal PrP trafficking of sheep scrapie
    • Jeffrey M, McGovern G, Goodsir CM, González L. 2009. Strain-associated variations in abnormal PrP trafficking of sheep scrapie. Brain Pathol. 19:1-11
    • (2009) Brain Pathol , vol.19 , pp. 1-11
    • Jeffrey, M.1    McGovern, G.2    Goodsir, C.M.3    González, L.4
  • 79
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley MP, Meyer RK, Kenaga L, Rahbar F, Cotter R, et al. 1991. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65:1340-51
    • (1991) J. Virol , vol.65 , pp. 1340-1351
    • McKinley, M.P.1    Meyer, R.K.2    Kenaga, L.3    Rahbar, F.4    Cotter, R.5
  • 81
    • 22844438894 scopus 로고    scopus 로고
    • Proteaseresistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions
    • Deleault NR, Geoghegan JC, Nishina K, Kascsak R, Williamson RA, Supattapone S. 2005. Proteaseresistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J. Biol. Chem. 280:26873-79
    • (2005) J. Biol. Chem , vol.280 , pp. 26873-26879
    • Deleault, N.R.1    Geoghegan, J.C.2    Nishina, K.3    Kascsak, R.4    Williamson, R.A.5    Supattapone, S.6
  • 82
    • 0141994735 scopus 로고    scopus 로고
    • Cellular heparan sulfate participates in the metabolism of prions
    • Ben-Zaken O, Tzaban S, Tal Y, Horonchik L, Esko JD, et al. 2003. Cellular heparan sulfate participates in the metabolism of prions. J. Biol. Chem. 278:40041-49
    • (2003) J. Biol. Chem , vol.278 , pp. 40041-40049
    • Ben-Zaken, O.1    Tzaban, S.2    Tal, Y.3    Horonchik, L.4    Esko, J.D.5
  • 83
    • 33646000833 scopus 로고    scopus 로고
    • Prions and their lethal journey to the brain
    • Mabbott NA, MacPherson GG. 2006. Prions and their lethal journey to the brain. Nat. Rev. Microbiol. 4:201-11
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 201-211
    • Mabbott, N.A.1    MacPherson, G.G.2
  • 85
    • 0242499506 scopus 로고    scopus 로고
    • Positioning of follicular dendritic cells within the spleen controls prion neuroinvasion
    • Prinz M, Heikenwalder M, Junt T, Schwarz P, Glatzel M, et al. 2003. Positioning of follicular dendritic cells within the spleen controls prion neuroinvasion. Nature 425:957-62
    • (2003) Nature , vol.425 , pp. 957-962
    • Prinz, M.1    Heikenwalder, M.2    Junt, T.3    Schwarz, P.4    Glatzel, M.5
  • 86
    • 65349151298 scopus 로고    scopus 로고
    • Neuroinvasion in sheep TSEs: The role of the haematogenous route
    • Sisó S, Jeffrey M, González L. 2009. Neuroinvasion in sheep TSEs: the role of the haematogenous route. Neuropathol. Appl. Neurobiol. 35:232-46
    • (2009) Neuropathol. Appl. Neurobiol , vol.35 , pp. 232-246
    • Sisó, S.1    Jeffrey, M.2    González, L.3
  • 87
    • 58149378573 scopus 로고    scopus 로고
    • Prion diseases are efficiently transmitted by blood transfusion in sheep
    • Houston F, McCutcheon S, Goldmann W, Chong A, Foster J, et al. 2008. Prion diseases are efficiently transmitted by blood transfusion in sheep. Blood 112:4739-45
    • (2008) Blood , vol.112 , pp. 4739-4745
    • Houston, F.1    McCutcheon, S.2    Goldmann, W.3    Chong, A.4    Foster, J.5
  • 88
    • 0037213933 scopus 로고    scopus 로고
    • Rapid prion neuroinvasion following tongue infection
    • Bartz JC, Kincaid AE, Bessen RA. 2003. Rapid prion neuroinvasion following tongue infection. J. Virol. 77:583-91
    • (2003) J. Virol , vol.77 , pp. 583-591
    • Bartz, J.C.1    Kincaid, A.E.2    Bessen, R.A.3
  • 89
    • 19444374721 scopus 로고    scopus 로고
    • Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells
    • Magalhães AC, Baron GS, Lee KS, Steele-Mortimer O, Dorward D, et al. 2005. Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells. J. Neurosci. 25:5207-16
    • (2005) J. Neurosci , vol.25 , pp. 5207-5216
    • Magalhães, A.C.1    Baron, G.S.2    Lee, K.S.3    Steele-Mortimer, O.4    Dorward, D.5
  • 91
    • 19444376065 scopus 로고    scopus 로고
    • PrPSc incorporation to cells requires endogenous glycosaminoglycan expression
    • Hijazi N, Kariv-Inbal Z, Gasset M, Gabizon R. 2005. PrPSc incorporation to cells requires endogenous glycosaminoglycan expression. J. Biol. Chem. 280:17057-61
    • (2005) J. Biol. Chem , vol.280 , pp. 17057-17061
    • Hijazi, N.1    Kariv-Inbal, Z.2    Gasset, M.3    Gabizon, R.4
  • 93
    • 33748074456 scopus 로고    scopus 로고
    • The 37-kDa/67-kDa laminin receptor acts as a receptor for infectious prions and is inhibited by polysulfated glycanes
    • Gauczynski S, Nikles D, El-Gogo S, Papy-Garcia D, Rey C, et al. 2006. The 37-kDa/67-kDa laminin receptor acts as a receptor for infectious prions and is inhibited by polysulfated glycanes. J. Infect. Dis. 194:702-9
    • (2006) J. Infect. Dis , vol.194 , pp. 702-709
    • Gauczynski, S.1    Nikles, D.2    El-Gogo, S.3    Papy-Garcia, D.4    Rey, C.5
  • 94
    • 0037384208 scopus 로고    scopus 로고
    • Cell-associated variants of disease-specific prion protein immunolabelling are found in different sources of sheep transmissible spongiform encephalopathy
    • Jeffrey M, Martin S, Gonzalez L. 2003. Cell-associated variants of disease-specific prion protein immunolabelling are found in different sources of sheep transmissible spongiform encephalopathy. J. Gen. Virol. 84:1033-45
    • (2003) J. Gen. Virol , vol.84 , pp. 1033-1045
    • Jeffrey, M.1    Martin, S.2    Gonzalez, L.3
  • 95
    • 33144469836 scopus 로고    scopus 로고
    • Mouse-adapted scrapie infection of SN56 cells: Greater efficiency with microsome-associated versus purified PrP-res
    • Baron GS, Magalhães AC, Prado MA, Caughey B. 2006. Mouse-adapted scrapie infection of SN56 cells: greater efficiency with microsome-associated versus purified PrP-res. J. Virol. 80:2106-17
    • (2006) J. Virol , vol.80 , pp. 2106-2117
    • Baron, G.S.1    Magalhães, A.C.2    Prado, M.A.3    Caughey, B.4
  • 96
    • 0038013717 scopus 로고    scopus 로고
    • Effect of glycosylphosphatidylinositol anchor-dependent and - independent prion protein association with model raft membranes on conversion to the protease-resistant isoform
    • Baron GS, Caughey B. 2003. Effect of glycosylphosphatidylinositol anchor-dependent and - independent prion protein association with model raft membranes on conversion to the protease-resistant isoform. J. Biol. Chem. 278:14883-92
    • (2003) J. Biol. Chem , vol.278 , pp. 14883-14892
    • Baron, G.S.1    Caughey, B.2
  • 100
  • 102
    • 33947709328 scopus 로고    scopus 로고
    • Packaging of prions into exosomes is associated with a novel pathway of PrP processing
    • Vella LJ, Sharples RA, Lawson VA, Masters CL, Cappai R, Hill AF. 2007. Packaging of prions into exosomes is associated with a novel pathway of PrP processing. J. Pathol. 211:582-90
    • (2007) J. Pathol , vol.211 , pp. 582-590
    • Vella, L.J.1    Sharples, R.A.2    Lawson, V.A.3    Masters, C.L.4    Cappai, R.5    Hill, A.F.6
  • 103
    • 44949098577 scopus 로고    scopus 로고
    • Scrapie-specific pathology of sheep lymphoid tissues
    • McGovern G, Jeffrey M. 2007. Scrapie-specific pathology of sheep lymphoid tissues. PLoSONE2:e1304
    • (2007) PLoSONE2
    • McGovern, G.1    Jeffrey, M.2
  • 105
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey B, Baron GS. 2006. Prions and their partners in crime. Nature 443:803-10
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 106
    • 47149114386 scopus 로고    scopus 로고
    • Intercellular transfer mediated by tunneling nanotubes
    • Gerdes HH, Carvalho RN. 2008. Intercellular transfer mediated by tunneling nanotubes. Curr. Opin. Cell Biol. 20:470-75
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 470-475
    • Gerdes, H.H.1    Carvalho, R.N.2
  • 108
    • 33745565356 scopus 로고    scopus 로고
    • Retrovirus infection strongly enhances scrapie infectivity release in cell culture
    • Leblanc P, Alais S, Porto-Carreiro I, Lehmann S, Grassi J, et al. 2006. Retrovirus infection strongly enhances scrapie infectivity release in cell culture. EMBO J. 25:2674-85
    • (2006) EMBO J , vol.25 , pp. 2674-2685
    • Leblanc, P.1    Alais, S.2    Porto-Carreiro, I.3    Lehmann, S.4    Grassi, J.5
  • 109
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT. 2003. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:267-98
    • (2003) Annu. Rev. Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 110
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers-a decade of discovery
    • Walsh DM, Selkoe DJ. 2007. Aβ oligomers-a decade of discovery. J. Neurochem. 101:1172-84
    • (2007) J. Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 112
    • 42949175211 scopus 로고    scopus 로고
    • Dynamics of the microglial/amyloid interaction indicate a role in plaque maintenance
    • Bolmont T, Haiss F, Eicke D, Radde R, Mathis CA, et al. 2008. Dynamics of the microglial/amyloid interaction indicate a role in plaque maintenance. J. Neurosci. 28:4283-92
    • (2008) J. Neurosci , vol.28 , pp. 4283-4292
    • Bolmont, T.1    Haiss, F.2    Eicke, D.3    Radde, R.4    Mathis, C.A.5
  • 113
    • 0000158060 scopus 로고    scopus 로고
    • Dendritic and synaptic alterations of hippocampal pyramidal neurones in scrapie-infected mice
    • Belichenko PV, Brown D, Jeffrey M, Fraser JR. 2000. Dendritic and synaptic alterations of hippocampal pyramidal neurones in scrapie-infected mice. Neuropathol. Appl. Neurobiol. 26:143-49
    • (2000) Neuropathol. Appl. Neurobiol , vol.26 , pp. 143-149
    • Belichenko, P.V.1    Brown, D.2    Jeffrey, M.3    Fraser, J.R.4
  • 114
    • 2542638001 scopus 로고    scopus 로고
    • Scrapie-specific neuronal lesions are independent of neuronal PrP expression
    • Jeffrey M, Goodsir CM, Race RE, Chesebro B. 2004. Scrapie-specific neuronal lesions are independent of neuronal PrP expression. Ann. Neurol. 55:781-92
    • (2004) Ann. Neurol , vol.55 , pp. 781-792
    • Jeffrey, M.1    Goodsir, C.M.2    Race, R.E.3    Chesebro, B.4
  • 115
    • 41749093035 scopus 로고    scopus 로고
    • The tubulovesicular structures-the ultrastructural hallmark for all prion diseases
    • Liberski P. 2008. The tubulovesicular structures-the ultrastructural hallmark for all prion diseases. Acta Neurobiol. Exp. 68:113-21
    • (2008) Acta Neurobiol. Exp , vol.68 , pp. 113-121
    • Liberski, P.1
  • 116
    • 2942595817 scopus 로고    scopus 로고
    • Characterization of recombinant, membrane-attached full-length prion protein
    • Eberl H, Tittmann P, Glockshuber R. 2004. Characterization of recombinant, membrane-attached full-length prion protein. J. Biol. Chem. 279:25058-65
    • (2004) J. Biol. Chem , vol.279 , pp. 25058-25065
    • Eberl, H.1    Tittmann, P.2    Glockshuber, R.3
  • 117
    • 33644747643 scopus 로고    scopus 로고
    • Synthesis and structural characterization of a mimetic membrane-anchored prion protein
    • Hicks MR, Gill AC, Bath IK, Rullay AK, Sylvester ID, et al. 2006. Synthesis and structural characterization of a mimetic membrane-anchored prion protein. FEBS J. 273:1285-99
    • (2006) FEBS J , vol.273 , pp. 1285-1299
    • Hicks, M.R.1    Gill, A.C.2    Bath, I.K.3    Rullay, A.K.4    Sylvester, I.D.5
  • 119
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • Morillas M, Swietnicki W, Gambetti P, Surewicz WK. 1999. Membrane environment alters the conformational structure of the recombinant human prion protein. J. Biol. Chem. 274:36859-65
    • (1999) J. Biol. Chem , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 120
    • 0141679530 scopus 로고    scopus 로고
    • Channels formed with a mutant prion protein PrP(82-146) homologous to a 7-kDa fragment in diseased brain of GSS patients
    • Bahadi R, Farrelly PV, Kenna BL, Kourie JI, Tagliavini F, et al. 2003. Channels formed with a mutant prion protein PrP(82-146) homologous to a 7-kDa fragment in diseased brain of GSS patients. Am. J. Physiol. Cell Physiol. 285:C862-72
    • (2003) Am. J. Physiol. Cell Physiol , vol.285
    • Bahadi, R.1    Farrelly, P.V.2    Kenna, B.L.3    Kourie, J.I.4    Tagliavini, F.5
  • 121
    • 33744961080 scopus 로고    scopus 로고
    • The interaction between cytoplasmic prion protein and the hydrophobic lipid core of membrane correlates with neurotoxicity
    • Wang X,Wang F, Arterburn L,Wollmann R, Ma J. 2006. The interaction between cytoplasmic prion protein and the hydrophobic lipid core of membrane correlates with neurotoxicity. J. Biol. Chem. 281:13559-65
    • (2006) J. Biol. Chem , vol.281 , pp. 13559-13565
    • Wang, X.1    Wang, F.2    Arterburn, L.3    Wollmann, R.4    Ma, J.5
  • 122
    • 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, Wang X, Wang X, et al. 2007. Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions. Biochemistry 46:7045-53
    • (2007) Biochemistry , vol.46 , pp. 7045-7053
    • Wang, F.1    Yang, F.2    Hu, Y.3    Wang, X.4    Wang, X.5
  • 123
    • 0037465821 scopus 로고    scopus 로고
    • Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization
    • Kazlauskaite J, Sanghera N, Sylvester I, Venien-Bryan C, Pinheiro TJ. 2003. Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization. Biochemistry 42:3295-304
    • (2003) Biochemistry , vol.42 , pp. 3295-3304
    • Kazlauskaite, J.1    Sanghera, N.2    Sylvester, I.3    Venien-Bryan, C.4    Pinheiro, T.J.5
  • 124
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • Sanghera N, Pinheiro TJ. 2002. Binding of prion protein to lipid membranes and implications for prion conversion. J. Mol. Biol. 315:1241-56
    • (2002) J. Mol. Biol , vol.315 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 126
    • 0025091084 scopus 로고
    • Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein
    • Stahl N, Baldwin MA, Burlingame AL, Prusiner SB. 1990. Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry 29:8879-84
    • (1990) Biochemistry , vol.29 , pp. 8879-8884
    • Stahl, N.1    Baldwin, M.A.2    Burlingame, A.L.3    Prusiner, S.B.4
  • 127
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death?
    • Caughey B. 2001. Interactions between prion protein isoforms: The kiss of death? Trends Biochem. Sci. 26:235-42
    • (2001) Trends Biochem. Sci , vol.26 , pp. 235-242
    • Caughey, B.1
  • 129
    • 0026600865 scopus 로고
    • Normal development and behavior of mice lacking the neuronal cell-surface PrP protein
    • Bueler H, Fischer M, Lang Y, Bluethmann H, Lipp H-P, et al. 1992. Normal development and behavior of mice lacking the neuronal cell-surface PrP protein. Nature 356:577-82
    • (1992) Nature , vol.356 , pp. 577-582
    • Bueler, H.1    Fischer, M.2    Lang, Y.3    Bluethmann, H.4    Lipp, H.-P.5
  • 130
    • 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, Linehan J, Gowland I, et al. 2002. Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J. 21:202-10
    • (2002) EMBO J , vol.21 , pp. 202-210
    • Mallucci, G.R.1    Ratte, S.2    Asante, E.A.3    Linehan, J.4    Gowland, I.5
  • 131
    • 34249995984 scopus 로고    scopus 로고
    • Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice
    • Li A, Piccardo P, Barmada SJ, Ghetti B, Harris DA. 2007. Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice. EMBO J. 26:2777-85
    • (2007) EMBO J , vol.26 , pp. 2777-2785
    • Li, A.1    Piccardo, P.2    Barmada, S.J.3    Ghetti, B.4    Harris, D.A.5
  • 132
    • 0030054010 scopus 로고    scopus 로고
    • Normal host prion protein necessary for scrapie-induced neurotoxicity
    • Brandner S, Isenmann S, Raeber A, Fischer M, Sailer A, et al. 1996. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 379:339-43
    • (1996) Nature , vol.379 , pp. 339-343
    • Brandner, S.1    Isenmann, S.2    Raeber, A.3    Fischer, M.4    Sailer, A.5
  • 133
  • 134
    • 0033987842 scopus 로고    scopus 로고
    • Entry versus blockade of brain infection following oral or intraperitoneal scrapie administration: Role of prion protein expression in peripheral nerves and spleen
    • Race R, Oldstone M, Chesebro B. 2000. Entry versus blockade of brain infection following oral or intraperitoneal scrapie administration: role of prion protein expression in peripheral nerves and spleen. J. Virol. 74:828-33
    • (2000) J. Virol , vol.74 , pp. 828-833
    • Race, R.1    Oldstone, M.2    Chesebro, B.3
  • 135
    • 0030684056 scopus 로고    scopus 로고
    • Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie
    • Raeber AJ, Race RE, Brandner S, Priola SA, Sailer A, et al. 1997. Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie. EMBO J. 16:6057-65
    • (1997) EMBO J , vol.16 , pp. 6057-6065
    • Raeber, A.J.1    Race, R.E.2    Brandner, S.3    Priola, S.A.4    Sailer, A.5
  • 136
    • 12544257289 scopus 로고    scopus 로고
    • Pathological prion protein exposure switches on neuronal mitogen-activated protein kinase pathway resulting in microglia recruitment
    • Marella M, Gaggioli C, Batoz M, Deckert M, Tartare-Deckert S, Chabry J. 2005. Pathological prion protein exposure switches on neuronal mitogen-activated protein kinase pathway resulting in microglia recruitment. J. Biol. Chem. 280:1529-34
    • (2005) J. Biol. Chem , vol.280 , pp. 1529-1534
    • Marella, M.1    Gaggioli, C.2    Batoz, M.3    Deckert, M.4    Tartare-Deckert, S.5    Chabry, J.6
  • 138
    • 33646126278 scopus 로고    scopus 로고
    • New insights into prion structure and toxicity
    • Harris DA, True HL. 2006. New insights into prion structure and toxicity. Neuron 50:353-57
    • (2006) Neuron , vol.50 , pp. 353-357
    • Harris, D.A.1    True, H.L.2
  • 140
    • 12144291519 scopus 로고    scopus 로고
    • Cross-linking cellular prion protein triggers neuronal apoptosis in vivo
    • Solforosi L, Criado JR, McGavern DB, Wirz S, Sanchez-Alavez M, et al. 2004. Cross-linking cellular prion protein triggers neuronal apoptosis in vivo. Science 303:1514-16
    • (2004) Science , vol.303 , pp. 1514-1516
    • Solforosi, L.1    Criado, J.R.2    McGavern, D.B.3    Wirz, S.4    Sanchez-Alavez, M.5
  • 141
    • 34249937435 scopus 로고    scopus 로고
    • The prion protein family: Diversity, rivalry, and dysfunction
    • Watts JC, Westaway D. 2007. The prion protein family: diversity, rivalry, and dysfunction. Biochim. Biophys. Acta 1772:654-72
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 654-672
    • Watts, J.C.1    Westaway, D.2
  • 144
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-66
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 146
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: The story of [PIN(+)]
    • Derkatch IL, Bradley ME, Hong JY, Liebman SW. 2001. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106:171-82
    • (2001) Cell , vol.106 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 147
    • 0035725458 scopus 로고    scopus 로고
    • In vivo aggregation of the HET-s prion protein of the fungus Podospora anserina
    • Coustou-Linares V, Maddelein ML, Begueret J, Saupe SJ. 2001. In vivo aggregation of the HET-s prion protein of the fungus Podospora anserina. Mol. Microbiol. 42:1325-35
    • (2001) Mol. Microbiol , vol.42 , pp. 1325-1335
    • Coustou-Linares, V.1    Maddelein, M.L.2    Begueret, J.3    Saupe, S.J.4
  • 148
    • 0041319637 scopus 로고    scopus 로고
    • A class of prions that propagate via covalent auto-activation
    • Roberts BT, Wickner RB. 2003. A class of prions that propagate via covalent auto-activation. Genes Dev. 17:2083-87
    • (2003) Genes Dev , vol.17 , pp. 2083-2087
    • Roberts, B.T.1    Wickner, R.B.2
  • 150
    • 22844449525 scopus 로고    scopus 로고
    • Preparation and propagation of amyloid-enhancing factor
    • Kisilevsky R. 2005. Preparation and propagation of amyloid-enhancing factor. Methods Mol. Biol. 299:237-41
    • (2005) Methods Mol. Biol , vol.299 , pp. 237-241
    • Kisilevsky, R.1
  • 152
  • 153
    • 27744502798 scopus 로고    scopus 로고
    • Extrinsic factors significantly affect patterns of disease in free-ranging and captive cheetah (Acinonyx jubatus) populations
    • Munson L,Terio KA,Worley M, Jago M, Bagot-Smith A, Marker L. 2005. Extrinsic factors significantly affect patterns of disease in free-ranging and captive cheetah (Acinonyx jubatus) populations. J. Wildl. Dis. 41:542-48
    • (2005) J. Wildl. Dis , vol.41 , pp. 542-548
    • Munson, L.1    Terio, K.A.2    Worley, M.3    Jago, M.4    Bagot-Smith, A.5    Marker, L.6
  • 154
    • 44449092737 scopus 로고    scopus 로고
    • Fecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease
    • Zhang B, Une Y, Fu X, Yan J, Ge F, et al. 2008. Fecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease. Proc. Natl. Acad. Sci. USA 105:7263-68
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7263-7268
    • Zhang, B.1    Une, Y.2    Fu, X.3    Yan, J.4    Ge, F.5
  • 156
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann M, Coomaraswamy J, Bolmont T, Kaeser S, Schaefer C, et al. 2006. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 313:1781-84
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3    Kaeser, S.4    Schaefer, C.5
  • 157
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • Si K, Lindquist S, Kandel ER. 2003. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 115:879-91
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 160
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma J, Wollmann R, Lindquist S. 2002. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298:1781-85
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 161
    • 33644677579 scopus 로고    scopus 로고
    • Disease-related prion protein forms aggresomes in neuronal cells leading to caspase activation and apoptosis
    • Kristiansen M, Messenger MJ, Klohn PC, Brandner S, Wadsworth JD, et al. 2005. Disease-related prion protein forms aggresomes in neuronal cells leading to caspase activation and apoptosis. J. Biol. Chem. 280:38851-61
    • (2005) J. Biol. Chem , vol.280 , pp. 38851-38861
    • Kristiansen, M.1    Messenger, M.J.2    Klohn, P.C.3    Brandner, S.4    Wadsworth, J.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.