메뉴 건너뛰기




Volumn 10, Issue 8, 2010, Pages 980-991

Prion amyloid structure explains templating: How proteins can be genes

Author keywords

Amyloid; In register parallel structure; Prion

Indexed keywords

AMYLOID; FUNGAL PROTEIN; PRION PROTEIN;

EID: 78349247103     PISSN: 15671356     EISSN: 15671364     Source Type: Journal    
DOI: 10.1111/j.1567-1364.2010.00666.x     Document Type: Review
Times cited : (62)

References (119)
  • 1
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A & Lindquist S (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137: 146-158.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 2
    • 0014004625 scopus 로고
    • The exceptionally small size of the scrapie agent
    • Alper T, Haig DA & Clarke MC (1966) The exceptionally small size of the scrapie agent. Biochem Bioph Res Co 22: 278-284.
    • (1966) Biochem Bioph Res Co , vol.22 , pp. 278-284
    • Alper, T.1    Haig, D.A.2    Clarke, M.C.3
  • 3
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper T, Cramp WA, Haig DA & Clarke MC (1967) Does the agent of scrapie replicate without nucleic acid? Nature 214: 764-766.
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 4
    • 9644287905 scopus 로고    scopus 로고
    • The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms
    • Bai M, Zhou JM & Perrett S (2004) The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J Biol Chem 279: 50025-50030.
    • (2004) J Biol Chem , vol.279 , pp. 50025-50030
    • Bai, M.1    Zhou, J.M.2    Perrett, S.3
  • 6
    • 0022476747 scopus 로고
    • Scrapie and cellular PrP isoforms are encoded by the same chromosomal locus
    • Basler K, Oesch B, Scott M et al. (1986) Scrapie and cellular PrP isoforms are encoded by the same chromosomal locus. Cell 46: 417-428.
    • (1986) Cell , vol.46 , pp. 417-428
    • Basler, K.1    Oesch, B.2    Scott, M.3
  • 7
    • 0037117485 scopus 로고    scopus 로고
    • Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein
    • Baxa U, Speransky V, Steven AC & Wickner RB (2002) Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein. P Natl Acad Sci USA 99: 5253-5260.
    • (2002) P Natl Acad Sci USA , vol.99 , pp. 5253-5260
    • Baxa, U.1    Speransky, V.2    Steven, A.C.3    Wickner, R.B.4
  • 9
    • 20944436593 scopus 로고    scopus 로고
    • Filaments of the Ure2p prion protein have a cross-beta core structure
    • Baxa U, Cheng N, Winkler DC et al. (2005) Filaments of the Ure2p prion protein have a cross-beta core structure. J Struct Biol 150: 170-179.
    • (2005) J Struct Biol , vol.150 , pp. 170-179
    • Baxa, U.1    Cheng, N.2    Winkler, D.C.3
  • 10
    • 36048969163 scopus 로고    scopus 로고
    • Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance
    • Baxa U, Wickner RB, Steven AC, Anderson D, Marekov L, Yau W-M & Tycko R (2007) Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance. Biochemistry 46: 13149-13162.
    • (2007) Biochemistry , vol.46 , pp. 13149-13162
    • Baxa, U.1    Wickner, R.B.2    Steven, A.C.3    Anderson, D.4    Marekov, L.5    Yau, W.6    Tycko, R.7
  • 12
    • 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
  • 13
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton DC, McKinley MP & Prusiner SB (1982) Identification of a protein that purifies with the scrapie prion. Science 218: 1309-1311.
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 16
    • 70349612496 scopus 로고    scopus 로고
    • A heritable switch in carbon source utilization driven by an unusual yeast prion
    • Brown JC & Lindquist S (2009) A heritable switch in carbon source utilization driven by an unusual yeast prion. Gene Dev 23: 2320-2332.
    • (2009) Gene Dev , vol.23 , pp. 2320-2332
    • Brown, J.C.1    Lindquist, S.2
  • 17
    • 0027740178 scopus 로고
    • Scrapie strain variation and mutation
    • Bruce ME (1993) Scrapie strain variation and mutation. Brit Med Bull 49: 822-838.
    • (1993) Brit Med Bull , vol.49 , pp. 822-838
    • Bruce, M.E.1
  • 18
    • 0022530549 scopus 로고
    • Linkagae of prion protein and scrapie incubation time genes
    • Carlson GA, Kingsbury DT, Goodman PA et al. (1986) Linkagae of prion protein and scrapie incubation time genes. Cell 46: 503-511.
    • (1986) Cell , vol.46 , pp. 503-511
    • Carlson, G.A.1    Kingsbury, D.T.2    Goodman, P.A.3
  • 19
    • 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: 32230-32235.
    • (1998) J Biol Chem , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 20
    • 23244449092 scopus 로고    scopus 로고
    • Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p
    • Chan JCC, Oyler NA, Yau W-M & Tycko R (2005) Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Biochemistry 44: 10669-10680.
    • (2005) Biochemistry , vol.44 , pp. 10669-10680
    • Chan, J.C.C.1    Oyler, N.A.2    Yau, W.3    Tycko, R.4
  • 21
    • 49749206702 scopus 로고
    • Encephalopathy in mice produced by inoculation with scrapie brain material
    • Chandler RL (1961) Encephalopathy in mice produced by inoculation with scrapie brain material. Lancet 1: 107-108.
    • (1961) Lancet , vol.1 , pp. 107-108
    • Chandler, R.L.1
  • 22
    • 33847307713 scopus 로고    scopus 로고
    • Prion species barrier between the closely related yeast proteins is detected despite coaggregation
    • Chen B, Newnam GP & Chernoff YO (2007) Prion species barrier between the closely related yeast proteins is detected despite coaggregation. P Natl Acad Sci USA 104: 2791-2796.
    • (2007) P Natl Acad Sci USA , vol.104 , pp. 2791-2796
    • Chen, B.1    Newnam, G.P.2    Chernoff, Y.O.3
  • 23
    • 70149087962 scopus 로고    scopus 로고
    • Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy
    • Chen B, Thurber KR, Shewmaker F, Wickner RB & Tycko R (2009) Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy. P Natl Acad Sci USA, 106: 14339-14344.
    • (2009) P Natl Acad Sci USA , vol.106 , pp. 14339-14344
    • Chen, B.1    Thurber, K.R.2    Shewmaker, F.3    Wickner, R.B.4    Tycko, R.5
  • 25
    • 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
  • 27
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • Coustou V, Deleu C, Saupe S & Begueret J (1997) The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. P Natl Acad Sci USA 94: 9773-9778.
    • (1997) P Natl Acad Sci USA , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 28
    • 84966138908 scopus 로고
    • PSI, a cytoplasmic suppressor of super-suppressor in yeast
    • Cox BS (1965) PSI, a cytoplasmic suppressor of super-suppressor in yeast. Heredity 20: 505-521.
    • (1965) Heredity , vol.20 , pp. 505-521
    • Cox, B.S.1
  • 29
    • 0001289828 scopus 로고
    • Pathologie animale. La maladie dite tremblant du mouton est-elle inoculable?
    • Cuille J & Chelle PL (1936) Pathologie animale. La maladie dite tremblant du mouton est-elle inoculable? CR Acad Sci 203: 1552-1554.
    • (1936) CR Acad Sci , vol.203 , pp. 1552-1554
    • Cuille, J.1    Chelle, P.L.2
  • 30
    • 0000049491 scopus 로고
    • Experimental transmission of trembling to the goat
    • Cuille J & Chelle PL (1939) Experimental transmission of trembling to the goat. CR Seances Acad Sci 208: 1058-1060.
    • (1939) CR Seances Acad Sci , vol.208 , pp. 1058-1060
    • Cuille, J.1    Chelle, P.L.2
  • 34
    • 0030833388 scopus 로고    scopus 로고
    • Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae
    • Derkatch IL, Bradley ME, Zhou P, Chernoff YO & Liebman SW (1997) Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147: 507-519.
    • (1997) Genetics , vol.147 , pp. 507-519
    • Derkatch, I.L.1    Bradley, M.E.2    Zhou, P.3    Chernoff, Y.O.4    Liebman, S.W.5
  • 36
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of α-synuclein fibrils studied by site-directed spin labeling
    • Der-Sarkissian A, Jao CC, Chen J & Langen R (2003) Structural organization of α-synuclein fibrils studied by site-directed spin labeling. J Biol Chem 278: 37530-37535.
    • (2003) J Biol Chem , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 38
    • 0014305661 scopus 로고
    • Identification of a gene which controls the incubation period of some strains of scrapie in mice
    • Dickinson AG, Meikle VMH & Fraser H (1968) Identification of a gene which controls the incubation period of some strains of scrapie in mice. J Comp Pathol 78: 293-299.
    • (1968) J Comp Pathol , vol.78 , pp. 293-299
    • Dickinson, A.G.1    Meikle, V.M.H.2    Fraser, H.3
  • 40
    • 0028174948 scopus 로고
    • - mutation which eliminates the [PSI] factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene
    • - mutation which eliminates the [PSI] factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137: 659-670.
    • (1994) Genetics , vol.137 , pp. 659-670
    • Doel, S.M.1    McCready, S.J.2    Nierras, C.R.3    Cox, B.S.4
  • 41
    • 41349087784 scopus 로고    scopus 로고
    • Newly identified prion linked to the chromatin-remodeling factor swi1 in Saccharomyces cerevisiae
    • Du Z, Park K-W, Yu H, Fan Q & Li L (2008) Newly identified prion linked to the chromatin-remodeling factor swi1 in Saccharomyces cerevisiae. Nat Genet 40: 460-465.
    • (2008) Nat Genet , vol.40 , pp. 460-465
    • Du, Z.1    Park, K.2    Yu, H.3    Fan, Q.4    Li, L.5
  • 42
    • 0033118934 scopus 로고    scopus 로고
    • Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
    • Eaglestone SS, Cox BS & Tuite MF (1999) Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J 18: 1974-1981.
    • (1999) EMBO J , vol.18 , pp. 1974-1981
    • Eaglestone, S.S.1    Cox, B.S.2    Tuite, M.F.3
  • 43
    • 0037058949 scopus 로고    scopus 로고
    • Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein
    • Edskes HK & Wickner RB (2002) Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. P Natl Acad Sci USA 99 (suppl 4): 16384-16391.
    • (2002) P Natl Acad Sci USA , vol.99 , Issue.SUPPL 4 , pp. 16384-16391
    • Edskes, H.K.1    Wickner, R.B.2
  • 44
    • 62549130374 scopus 로고    scopus 로고
    • Prion variants and species barriers among Saccharomyces Ure2 proteins
    • Edskes HK, McCann LM, Hebert AM & Wickner RB (2009) Prion variants and species barriers among Saccharomyces Ure2 proteins. Genetics 181: 1159-1167.
    • (2009) Genetics , vol.181 , pp. 1159-1167
    • Edskes, H.K.1    McCann, L.M.2    Hebert, A.M.3    Wickner, R.B.4
  • 45
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith JS (1967) Self-replication and scrapie. Nature 215: 1043-1044.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 46
    • 0033546405 scopus 로고    scopus 로고
    • The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-poly(A) tail of mRNA
    • Hoshino S, Imai M, Kobayashi T, Uchida N & Katada T (1999) The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-poly(A) tail of mRNA. J Biol Chem 274: 16677-16680.
    • (1999) J Biol Chem , vol.274 , pp. 16677-16680
    • Hoshino, S.1    Imai, M.2    Kobayashi, T.3    Uchida, N.4    Katada, T.5
  • 47
    • 0141866883 scopus 로고    scopus 로고
    • Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation
    • Hosoda N, Kobayashii T, Uchida N, Funakoshi Y, Kikuchi Y, Hoshino S & Katada T (2003) Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation. J Biol Chem 278: 38287-38291.
    • (2003) J Biol Chem , vol.278 , pp. 38287-38291
    • Hosoda, N.1    Kobayashii, T.2    Uchida, N.3    Funakoshi, Y.4    Kikuchi, Y.5    Hoshino, S.6    Katada, T.7
  • 48
    • 0024519771 scopus 로고
    • Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome
    • Hsiao K, Baker HF, Crow TJ et al. (1989) Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature 338: 342-345.
    • (1989) Nature , vol.338 , pp. 342-345
    • Hsiao, K.1    Baker, H.F.2    Crow, T.J.3
  • 49
    • 0023430390 scopus 로고
    • Linkage of the scrapie-associated fibril protein (PrP) gene and Sinc using congenic mice and restriction fragment length polymorphism analysis
    • Hunter N, Hope J, McConnell I & Dickinson AG (1987) Linkage of the scrapie-associated fibril protein (PrP) gene and Sinc using congenic mice and restriction fragment length polymorphism analysis. J Gen Virol 68: 2711-2716.
    • (1987) J Gen Virol , vol.68 , pp. 2711-2716
    • Hunter, N.1    Hope, J.2    McConnell, I.3    Dickinson, A.G.4
  • 50
    • 0025871691 scopus 로고
    • Three proteolytic systems in the yeast Saccharomyces cerevisiae
    • Jones EW (1991) Three proteolytic systems in the yeast Saccharomyces cerevisiae. J Biol Chem 266: 7963-7966.
    • (1991) J Biol Chem , vol.266 , pp. 7963-7966
    • Jones, E.W.1
  • 51
    • 0035853292 scopus 로고    scopus 로고
    • Supporting the structural basis of prion strains
    • J Mol Biol
    • King CY (2001) Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J Mol Biol 307: 1247-1260.
    • (2001) induction and identification of [PSI] variants , vol.307 , pp. 1247-1260
    • King, C.Y.1
  • 52
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King CY & Diaz-Avalos R (2004) Protein-only transmission of three yeast prion strains. Nature 428: 319-323.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 53
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King C-Y, Tittmann P, Gross H, Gebert R, Aebi M & Wuthrich K (1997) Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. P Natl Acad Sci USA 94: 6618-6622.
    • (1997) P Natl Acad Sci USA , vol.94 , pp. 6618-6622
    • King, C.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5    Wuthrich, K.6
  • 54
    • 0141593548 scopus 로고    scopus 로고
    • A quantitative, highly sensitive cell-based infectivity assay for mouse scrapie prions
    • Klohn PC, Stoltze L, Flechsig E, Enari M & Weissmann C (2003) A quantitative, highly sensitive cell-based infectivity assay for mouse scrapie prions. P Natl Acad Sci USA 100: 11666-11671.
    • (2003) P Natl Acad Sci USA , vol.100 , pp. 11666-11671
    • Klohn, P.C.1    Stoltze, L.2    Flechsig, E.3    Enari, M.4    Weissmann, C.5
  • 56
    • 33847266871 scopus 로고    scopus 로고
    • Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain
    • Krzewska J, Tanaka M, Burston SG & Melki R (2007) Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain. J Biol Chem 282: 1679-1686.
    • (2007) J Biol Chem , vol.282 , pp. 1679-1686
    • Krzewska, J.1    Tanaka, M.2    Burston, S.G.3    Melki, R.4
  • 59
    • 0015056102 scopus 로고
    • Non-mendelian mutation allowing ureidosuccinic acid uptake in yeast
    • Lacroute F (1971) Non-mendelian mutation allowing ureidosuccinic acid uptake in yeast. J Bacteriol 106: 519-522.
    • (1971) J Bacteriol , vol.106 , pp. 519-522
    • Lacroute, F.1
  • 61
    • 0023001210 scopus 로고
    • Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent
    • Locht C, Chesebro B, Race R & Keith JM (1986) Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. P Natl Acad Sci USA 83: 6372-6376.
    • (1986) P Natl Acad Sci USA , vol.83 , pp. 6372-6376
    • Locht, C.1    Chesebro, B.2    Race, R.3    Keith, J.M.4
  • 62
    • 70350185406 scopus 로고    scopus 로고
    • Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded molecules
    • Loquet A, Bousset L, Gardiennet C et al. (2009) Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded molecules. J Mol Biol 394: 108-118.
    • (2009) J Mol Biol , vol.394 , pp. 108-118
    • Loquet, A.1    Bousset, L.2    Gardiennet, C.3
  • 63
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils
    • &, Biochemistry
    • Luca S, Yau W-M, Leapman R & Tycko R (2007) Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry 46: 13505-13522.
    • (2007) constraints from solid-state NMR , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.2    Leapman, R.3    Tycko, R.4
  • 65
    • 77449142074 scopus 로고    scopus 로고
    • Recombinant prion protein induces a new transmissible prion disease in wild-type animals
    • Makarava N, Kovacs GG, Bocharova O et al. (2010) Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol 119: 177-187.
    • (2010) Acta Neuropathol , vol.119 , pp. 177-187
    • Makarava, N.1    Kovacs, G.G.2    Bocharova, O.3
  • 68
    • 0019778656 scopus 로고
    • Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Straussler syndrome with an analysis of the various forms of amyloid plaque deposition in the virus-induced spongiform encephalopathies
    • Masters CL, Gajdusek DC & Gibbs CJ (1981) Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Straussler syndrome with an analysis of the various forms of amyloid plaque deposition in the virus-induced spongiform encephalopathies. Brain 104: 559-588.
    • (1981) Brain , vol.104 , pp. 559-588
    • Masters, C.L.1    Gajdusek, D.C.2    Gibbs, C.J.3
  • 69
    • 0242684410 scopus 로고    scopus 로고
    • Balancing selection at the prion protein gene consistent with prehistoric kurulike epidemics
    • Mead S, Stumpf MP, Whitfield J et al. (2003) Balancing selection at the prion protein gene consistent with prehistoric kurulike epidemics. Science 300: 640-643.
    • (2003) Science , vol.300 , pp. 640-643
    • Mead, S.1    Stumpf, M.P.2    Whitfield, J.3
  • 73
    • 60549101873 scopus 로고    scopus 로고
    • A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen
    • Nemecek J, Nakayashiki T & Wickner RB (2009) A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. P Natl Acad Sci USA 106: 1892-1896.
    • (2009) P Natl Acad Sci USA , vol.106 , pp. 1892-1896
    • Nemecek, J.1    Nakayashiki, T.2    Wickner, R.B.3
  • 74
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • Paravastu AK, Leapman RD, Yau WM & Tycko R (2008) Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. P Natl Acad Sci USA 105: 18349-18354.
    • (2008) P Natl Acad Sci USA , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 75
    • 0003782542 scopus 로고
    • Scrapie Disease in Sheep - Historical, Clinical, Epidemiological, Pathological and Practical Aspects of the Natural Disease
    • () Academic Press, London.
    • Parry HB (1983) Scrapie Disease in Sheep - Historical, Clinical, Epidemiological, Pathological and Practical Aspects of the Natural Disease. Academic Press, London.
    • (1983)
    • Parry, H.B.1
  • 76
    • 0034727080 scopus 로고    scopus 로고
    • Evolving evolvability
    • Partridge L & Barton NH (2000) Evolving evolvability. Nature 407: 457-458.
    • (2000) Nature , vol.407 , pp. 457-458
    • Partridge, L.1    Barton, N.H.2
  • 78
    • 61849091420 scopus 로고    scopus 로고
    • The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion
    • Patel BK, Gavin-Smyth J & Liebman SW (2009) The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat Cell Biol 11: 344-349.
    • (2009) Nat Cell Biol , vol.11 , pp. 344-349
    • Patel, B.K.1    Gavin-Smyth, J.2    Liebman, S.W.3
  • 81
    • 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
  • 82
    • 0025244011 scopus 로고
    • Transgenic studies implicate interactions between homologous PrP isoforms in scrapie prion replication
    • Prusiner SB, Scott M, Foster D et al. (1990) Transgenic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63: 673-686.
    • (1990) Cell , vol.63 , pp. 673-686
    • Prusiner, S.B.1    Scott, M.2    Foster, D.3
  • 84
    • 20444458341 scopus 로고    scopus 로고
    • Correlation of structural elements and infectivity of the HET-s prion
    • Ritter C, Maddelein ML, Siemer AB et al. (2005) Correlation of structural elements and infectivity of the HET-s prion. Nature 435: 844-848.
    • (2005) Nature , vol.435 , pp. 844-848
    • Ritter, C.1    Maddelein, M.L.2    Siemer, A.B.3
  • 85
    • 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. Gene Dev 17: 2083-2087.
    • (2003) Gene Dev , vol.17 , pp. 2083-2087
    • Roberts, B.T.1    Wickner, R.B.2
  • 86
    • 3543022080 scopus 로고    scopus 로고
    • Scrambled prion domains form prions and amyloid
    • Ross ED, Baxa U & Wickner RB (2004) Scrambled prion domains form prions and amyloid. Mol Cell Biol 24: 7206-7213.
    • (2004) Mol Cell Biol , vol.24 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3
  • 89
    • 0034695569 scopus 로고    scopus 로고
    • Molecular basis of a yeast prion species barrier
    • Santoso A, Chien P, Osherovich LZ & Weissman JS (2000) Molecular basis of a yeast prion species barrier. Cell 100: 277-288.
    • (2000) Cell , vol.100 , pp. 277-288
    • Santoso, A.1    Chien, P.2    Osherovich, L.Z.3    Weissman, J.S.4
  • 93
    • 67650168748 scopus 로고    scopus 로고
    • Hsp70 structure, function, regulation and influence on yeast prions
    • Sharma D & Masison DC (2009) Hsp70 structure, function, regulation and influence on yeast prions. Protein Peptide Lett 16: 571-581.
    • (2009) Protein Peptide Lett , vol.16 , pp. 571-581
    • Sharma, D.1    Masison, D.C.2
  • 94
    • 33845938549 scopus 로고    scopus 로고
    • Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure
    • Shewmaker F, Wickner RB & Tycko R (2006) Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure. P Natl Acad Sci USA 103: 19754-19759.
    • (2006) P Natl Acad Sci USA , vol.103 , pp. 19754-19759
    • Shewmaker, F.1    Wickner, R.B.2    Tycko, R.3
  • 95
    • 34547136725 scopus 로고    scopus 로고
    • Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae
    • Shewmaker F, Mull L, Nakayashiki T, Masison DC & Wickner RB (2007) Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae. Genetics 176: 1557-1565.
    • (2007) Genetics , vol.176 , pp. 1557-1565
    • Shewmaker, F.1    Mull, L.2    Nakayashiki, T.3    Masison, D.C.4    Wickner, R.B.5
  • 96
    • 41449106103 scopus 로고    scopus 로고
    • Amyloids of shuffled prion domains that form prions have a parallel in-register β-sheet structure
    • Shewmaker F, Ross ED, Tycko R & Wickner RB (2008) Amyloids of shuffled prion domains that form prions have a parallel in-register β-sheet structure. Biochemistry 47: 4000-4007.
    • (2008) Biochemistry , vol.47 , pp. 4000-4007
    • Shewmaker, F.1    Ross, E.D.2    Tycko, R.3    Wickner, R.B.4
  • 97
    • 67049087912 scopus 로고    scopus 로고
    • Two prion variants of Sup35p have in-register β-sheet structures, independent of hydration
    • Shewmaker F, Kryndushkin D, Chen B, Tycko R & Wickner RB (2009) Two prion variants of Sup35p have in-register β-sheet structures, independent of hydration. Biochemistry 48: 5074-5082.
    • (2009) Biochemistry , vol.48 , pp. 5074-5082
    • Shewmaker, F.1    Kryndushkin, D.2    Chen, B.3    Tycko, R.4    Wickner, R.B.5
  • 99
    • 26444520003 scopus 로고    scopus 로고
    • The [URE3] prion is not conserved among Saccharomyces species
    • Talarek N, Maillet L, Cullin C & Aigle M (2005) The [URE3] prion is not conserved among Saccharomyces species. Genetics 171: 23-54.
    • (2005) Genetics , vol.171 , pp. 23-54
    • Talarek, N.1    Maillet, L.2    Cullin, C.3    Aigle, M.4
  • 100
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, Cooke R & Weissman JS (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428: 323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 101
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor KL, Cheng N, Williams RW, Steven AC & Wickner RB (1999) Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283: 1339-1343.
    • (1999) Science , vol.283 , pp. 1339-1343
    • Taylor, K.L.1    Cheng, N.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 102
    • 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: 233-237.
    • (2007) Nature , vol.449 , pp. 233-237
    • Toyama, B.H.1    Kelly, M.J.2    Gross, J.D.3    Weissman, J.S.4
  • 103
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • True HL & Lindquist SL (2000) A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407: 477-483.
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 104
    • 0023217646 scopus 로고
    • Ureidosuccinate is transported by the allantoate transport system in Saccharomyces cerevisiae
    • Turoscy V & Cooper TG (1987) Ureidosuccinate is transported by the allantoate transport system in Saccharomyces cerevisiae. J Bacteriol 169: 2598-2600.
    • (1987) J Bacteriol , vol.169 , pp. 2598-2600
    • Turoscy, V.1    Cooper, T.G.2
  • 105
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils
    • Q Rev Biophys
    • Tycko R (2006) Molecular structure of amyloid fibrils: insights from solid-state NMR. Q Rev Biophys 1: 1-55.
    • (2006) insights from solid-state NMR , vol.1 , pp. 1-55
    • Tycko, R.1
  • 106
    • 33847064253 scopus 로고    scopus 로고
    • Symmetry-based constant-time homonuclear dipolar recoupling in solid-state NMR
    • Tycko R (2007) Symmetry-based constant-time homonuclear dipolar recoupling in solid-state NMR. J Chem Phys 126: 064506.
    • (2007) J Chem Phys , vol.126 , pp. 064506
    • Tycko, R.1
  • 107
    • 56849099636 scopus 로고    scopus 로고
    • Prion switching in response to environmental stress
    • Tyedmers J, Madariaga ML & Lindquist S (2008) Prion switching in response to environmental stress. PLoS Biol 6: e294.
    • (2008) PLoS Biol , vol.6
    • Tyedmers, J.1    Madariaga, M.L.2    Lindquist, S.3
  • 108
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F, Wang X, Yuan C-G & 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.3    Ma, J.4
  • 109
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-279) 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(218-279) prion form a beta solenoid with a triangular hydrophobic core. Science 319: 1523-1526.
    • (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
  • 111
    • 0030987607 scopus 로고    scopus 로고
    • A new prion controls fungal cell fusion incompatibility
    • Wickner RB (1997) A new prion controls fungal cell fusion incompatibility. P Natl Acad Sci USA 94: 10012-10014.
    • (1997) P Natl Acad Sci USA , vol.94 , pp. 10012-10014
    • Wickner, R.B.1
  • 112
    • 23244448234 scopus 로고    scopus 로고
    • Scrapie in ancient China?
    • Wickner RB (2005) Scrapie in ancient China? Science 309: 874.
    • (2005) Science , vol.309 , pp. 874
    • Wickner, R.B.1
  • 114
  • 115
    • 53149116688 scopus 로고    scopus 로고
    • Protein inheritance (prions) based on parallel in-register β-sheet amyloid structures
    • Wickner RB, Shewmaker F, Kryndushkin D & Edskes HK (2008b) Protein inheritance (prions) based on parallel in-register β-sheet amyloid structures. Bioessays 30: 955-964.
    • (2008) Bioessays , vol.30 , pp. 955-964
    • Wickner, R.B.1    Shewmaker, F.2    Kryndushkin, D.3    Edskes, H.K.4
  • 116
    • 0024291136 scopus 로고
    • Bovine spongiform encephalopathy
    • Wilesmith JW (1988) Bovine spongiform encephalopathy. Vet Rec 122: 614.
    • (1988) Vet Rec , vol.122 , pp. 614
    • Wilesmith, J.W.1
  • 117
    • 0342951746 scopus 로고    scopus 로고
    • A new variant of Creutzfeldt-Jakob disease in the UK
    • Will RG, Ironside JW, Zeidler M et al. (1996) A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347: 921-925.
    • (1996) Lancet , vol.347 , pp. 921-925
    • Will, R.G.1    Ironside, J.W.2    Zeidler, M.3
  • 118
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart DS, Sykes BD & Richards FM (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222: 311-333.
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 119
    • 0020340108 scopus 로고
    • Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae
    • Zubenko GS, Park FJ & Jones EW (1982) Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae. Genetics 102: 679-690.
    • (1982) Genetics , vol.102 , pp. 679-690
    • Zubenko, G.S.1    Park, F.J.2    Jones, E.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.