메뉴 건너뛰기




Volumn 30, Issue 10, 2008, Pages 955-964

Protein inheritance (prions) based on parallel in-register β-sheet amyloid structures

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; CHAPERONE; PRION PROTEIN; AMYLOID; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE; URE2 PROTEIN, S CEREVISIAE;

EID: 53149116688     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20821     Document Type: Review
Times cited : (82)

References (111)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 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
  • 4
    • 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 Path 78:293-299.
    • (1968) J Comp Path , vol.78 , pp. 293-299
    • Dickinson, A.G.1    Meikle, V.M.H.2    Fraser, H.3
  • 5
    • 0024272862 scopus 로고
    • Genetics and polymorphism of the mouse prion gene complex: Control of scrapie incubation time
    • Carlson GA, Goodman PA, Lovett M, Taylor BA, Marshall ST, et al. 1988. Genetics and polymorphism of the mouse prion gene complex: control of scrapie incubation time. Mol Cell Biol 8:5528-5540.
    • (1988) Mol Cell Biol , vol.8 , pp. 5528-5540
    • Carlson, G.A.1    Goodman, P.A.2    Lovett, M.3    Taylor, B.A.4    Marshall, S.T.5
  • 9
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J, Saa 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    Saa, P.2    Hetz, C.3    Soto, C.4
  • 11
    • 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
  • 12
    • 0024085209 scopus 로고
    • The Psi factor of yeast: A problem in inheritance
    • Cox BS, Tuite MF, McLaughlin CS. 1988. The Psi factor of yeast: a problem in inheritance. Yeast 4:159-179.
    • (1988) Yeast , vol.4 , pp. 159-179
    • Cox, B.S.1    Tuite, M.F.2    McLaughlin, C.S.3
  • 13
    • 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
  • 14
    • 0016669719 scopus 로고
    • Genetical aspects of [URE3], a non-Mendelian, cytoplasmically inherited mutation in yeast
    • Aigle M, Lacroute F. 1975. Genetical aspects of [URE3], a non-Mendelian, cytoplasmically inherited mutation in yeast. Molec Gen Genet 136:327-335.
    • (1975) Molec Gen Genet , vol.136 , pp. 327-335
    • Aigle, M.1    Lacroute, F.2
  • 15
    • 0028308104 scopus 로고
    • URE3] as an altered URE2 protein: Evidence for a prion analog in S. cerevisiae
    • Wickner RB. 1994. [URE3] as an altered URE2 protein: evidence for a prion analog in S. cerevisiae. Science 264:566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 16
    • 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
  • 17
    • 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 106:171-182.
    • (2001) Cell , vol.106 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 18
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • Sondheimer N, Lindquist S. 2000. Rnq1: an epigenetic modifier of protein function in yeast. Molec Cell 5:163-172.
    • (2000) Molec Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 19
    • 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.-W.2    Yu, H.3    Fan, Q.4    Li, L.5
  • 20
    • 0036024577 scopus 로고    scopus 로고
    • Transmitting the signal of excess nitrogen in Saccharomyces cerevisiae from the Tor proteins to th GATA factors: Connecting the dots
    • Cooper TG. 2002. Transmitting the signal of excess nitrogen in Saccharomyces cerevisiae from the Tor proteins to th GATA factors: connecting the dots. FEMS Microbiol Revs 26:223-238.
    • (2002) FEMS Microbiol Revs , vol.26 , pp. 223-238
    • Cooper, T.G.1
  • 21
    • 0015260033 scopus 로고
    • Ureidosuccinic acid uptake in yeast and some aspects of its regulation
    • Drillien R, Lacroute F. 1972. Ureidosuccinic acid uptake in yeast and some aspects of its regulation. J Bacteriol 109:203-208.
    • (1972) J Bacteriol , vol.109 , pp. 203-208
    • Drillien, R.1    Lacroute, F.2
  • 22
    • 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
  • 23
    • 0029165882 scopus 로고
    • The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae
    • Stansfield I, Jones KM, Kushnirov VV, Dagkesamanskaya AR, Poznyakovski AI, et al. 1995. The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J 14:4365-4373.
    • (1995) EMBO J , vol.14 , pp. 4365-4373
    • Stansfield, I.1    Jones, K.M.2    Kushnirov, V.V.3    Dagkesamanskaya, A.R.4    Poznyakovski, A.I.5
  • 24
    • 0029145925 scopus 로고
    • Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
    • Zhouravleva G, Frolova L, LeGoff X, LeGuellec R, Inge-Vectomov S, et al. 1995. Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J 14:4065-4072.
    • (1995) EMBO J , vol.14 , pp. 4065-4072
    • Zhouravleva, G.1    Frolova, L.2    LeGoff, X.3    LeGuellec, R.4    Inge-Vectomov, S.5
  • 25
    • 0033823006 scopus 로고    scopus 로고
    • Molecular genetics of heterokaryon incompatibility in filamentous ascomycetes
    • Saupe SJ. 2000. Molecular genetics of heterokaryon incompatibility in filamentous ascomycetes. Microbiol Mol Biol Revs 64:489-502.
    • (2000) Microbiol Mol Biol Revs , vol.64 , pp. 489-502
    • Saupe, S.J.1
  • 26
    • 0001909765 scopus 로고
    • Les phenomenes de barrage chez Podospora anserina: Analyse genetique des barrages entre les souches s et S
    • Rizet G. 1952. Les phenomenes de barrage chez Podospora anserina: analyse genetique des barrages entre les souches s et S Rev. Cytol Biol Veg 13:51-92.
    • (1952) Rev. Cytol Biol Veg , vol.13 , pp. 51-92
    • Rizet, G.1
  • 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. Proc Natl Acad Sci USA 94:9773-9778.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 28
    • 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 17:2083-2087.
    • (2003) Genes Dev , vol.17 , pp. 2083-2087
    • Roberts, B.T.1    Wickner, R.B.2
  • 29
    • 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
  • 30
    • 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
  • 32
    • 0028859540 scopus 로고
    • Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
    • Masison DC, Wickner RB. 1995. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270:93-95.
    • (1995) Science , vol.270 , pp. 93-95
    • Masison, D.C.1    Wickner, R.B.2
  • 33
    • 0030780097 scopus 로고    scopus 로고
    • The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation
    • Masison DC, Maddelein M-L, Wickner RB. 1997. The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. Proc Natl Acad Sci USA 94:12503-12508.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12503-12508
    • Masison, D.C.1    Maddelein, M.-L.2    Wickner, R.B.3
  • 34
    • 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
  • 35
    • 0242353209 scopus 로고    scopus 로고
    • Architecture of Ure2p prion filaments: The N-terminal domain forms a central core fiber
    • Baxa U, Taylor KL, Wall JS, Simon MN, Cheng N, et al. 2003. Architecture of Ure2p prion filaments: the N-terminal domain forms a central core fiber. J Biol Chem 278:43717-43727.
    • (2003) J Biol Chem , vol.278 , pp. 43717-43727
    • Baxa, U.1    Taylor, K.L.2    Wall, J.S.3    Simon, M.N.4    Cheng, N.5
  • 36
    • 27144451227 scopus 로고    scopus 로고
    • Prion generation in vitro: Amyloid of Ure2p is infectious
    • Brachmann A, Baxa U, Wickner RB. 2005. Prion generation in vitro: amyloid of Ure2p is infectious. Embo J 24:3082-3092.
    • (2005) Embo J , vol.24 , pp. 3082-3092
    • Brachmann, A.1    Baxa, U.2    Wickner, R.B.3
  • 37
    • 0028200770 scopus 로고
    • The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae
    • TerAvanesyan A, Dagkesamanskaya AR, Kushnirov VV, Smirnov VN. 1994. The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics 137:671-676.
    • (1994) Genetics , vol.137 , pp. 671-676
    • TerAvanesyan, A.1    Dagkesamanskaya, A.R.2    Kushnirov, V.V.3    Smirnov, V.N.4
  • 38
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain2-114of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King C-Y, Tittmann P, Gross H, Gebert R, Aebi M, et al. 1997. Prion-inducing domain2-114of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc Natl Acad Sci USA 94:6618-6622.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6618-6622
    • King, C.-Y.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5
  • 39
    • 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
  • 40
    • 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
  • 42
    • 36048969163 scopus 로고    scopus 로고
    • Characterization of β-sheet structure in Ure2p1-89yeast prion fibrils by solid state nuclear magnetic resonance
    • Baxa U, Wickner RB, Steven AC, Anderson D, Marekov L, et al. 2007. Characterization of β-sheet structure in Ure2p1-89yeast 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
  • 44
    • 33845605514 scopus 로고    scopus 로고
    • Prion proof for [PIN+]: Infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+]
    • Patel BK, Liebman SW. 2007. "Prion proof" for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+]. J Mol Biol 365:773-782.
    • (2007) J Mol Biol , vol.365 , pp. 773-782
    • Patel, B.K.1    Liebman, S.W.2
  • 45
    • 0038219626 scopus 로고    scopus 로고
    • Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina
    • Balguerie A, Dos Reis S, Ritter C, Chaignepain S, Coulary-Salin B, et al. 2003. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. Embo J 22:2071-2081.
    • (2003) Embo J , vol.22 , pp. 2071-2081
    • Balguerie, A.1    Dos Reis, S.2    Ritter, C.3    Chaignepain, S.4    Coulary-Salin, B.5
  • 47
    • 0030987607 scopus 로고    scopus 로고
    • A new prion controls fungal cell fusion incompatibility
    • Wickner RB. 1997. A new prion controls fungal cell fusion incompatibility. Proc Natl Acad Sci USA 94:10012-10014.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10012-10014
    • Wickner, R.B.1
  • 48
    • 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
  • 49
    • 33947390044 scopus 로고    scopus 로고
    • Evolution of budding yeast prion-determinant sequences across diverse fungi
    • doi:10.1016/j.jmb.2007.01.070
    • Harrison LB, Yu Z, Stajich JE, Dietrich FS, Harrison PM. 2007. Evolution of budding yeast prion-determinant sequences across diverse fungi. J Mol Biol. doi:10.1016/j.jmb.2007.01.070.
    • (2007) J Mol Biol
    • Harrison, L.B.1    Yu, Z.2    Stajich, J.E.3    Dietrich, F.S.4    Harrison, P.M.5
  • 50
    • 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
  • 51
    • 33750436582 scopus 로고    scopus 로고
    • N-terminal region of Saccharomyces cerevisiae eRF3 is essential for the functioning of the eRF1/eRF3 complex beyond translation termination
    • Urakov VN, Valouev IA, Kochneva-Pervukhova NV, Pakeiser AN, Vishnevsky AY, et al. 2006. N-terminal region of Saccharomyces cerevisiae eRF3 is essential for the functioning of the eRF1/eRF3 complex beyond translation termination. BMC Mol Biol 7:34-46.
    • (2006) BMC Mol Biol , vol.7 , pp. 34-46
    • Urakov, V.N.1    Valouev, I.A.2    Kochneva-Pervukhova, N.V.3    Pakeiser, A.N.4    Vishnevsky, A.Y.5
  • 52
    • 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
  • 54
    • 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. Proc Natl Acad Sci USA 99:16384-16391.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16384-16391
    • Edskes, H.K.1    Wickner, R.B.2
  • 55
    • 0025820942 scopus 로고
    • Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease
    • Palmer MS, Dryden AJ, Hughes JT, Collinge J. 1991. Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 352:340-342.
    • (1991) Nature , vol.352 , pp. 340-342
    • Palmer, M.S.1    Dryden, A.J.2    Hughes, J.T.3    Collinge, J.4
  • 56
    • 0242684410 scopus 로고    scopus 로고
    • Balancing selection at the prion protein gene consistent with prehistoric kurulike epidemics
    • Mead S, Stumpf MP, Whitfield J, Beck JA, Poulter M, 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    Beck, J.A.4    Poulter, M.5
  • 57
    • 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. Proc Natl Acad Sci USA 104:2791-2796.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2791-2796
    • Chen, B.1    Newnam, G.P.2    Chernoff, Y.O.3
  • 59
    • 0024292298 scopus 로고
    • SUF12 suppressor protein of yeast: A fusion protein related to the EF-1 family of elongation factors
    • Wilson PG, Culbertson MR. 1988. SUF12 suppressor protein of yeast: a fusion protein related to the EF-1 family of elongation factors. J Mol Biol 199:559-573.
    • (1988) J Mol Biol , vol.199 , pp. 559-573
    • Wilson, P.G.1    Culbertson, M.R.2
  • 60
    • 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
  • 62
    • 0028364192 scopus 로고
    • Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells
    • Priola SA, Caughey B, Race RE, Chesebro B. 1994. Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells. J Virol 68:4873-4878.
    • (1994) J Virol , vol.68 , pp. 4873-4878
    • Priola, S.A.1    Caughey, B.2    Race, R.E.3    Chesebro, B.4
  • 63
    • 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
  • 64
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DePace AH, Santoso A, Hillner P, Weissman JS. 1998. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93:1241-1252.
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 65
    • 33644817188 scopus 로고    scopus 로고
    • Prion domains: Sequences, structures and interactions
    • Ross ED, Minton AP, Wickner RB. 2005. Prion domains: sequences, structures and interactions. Nat. Cell Biol 7:1039-1044.
    • (2005) Nat. Cell Biol , vol.7 , pp. 1039-1044
    • Ross, E.D.1    Minton, A.P.2    Wickner, R.B.3
  • 67
    • 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 447:453-457.
    • (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
  • 68
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, et al. 2004. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc Natl Acad Sci USA 101:711-716.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 711-716
    • Jaroniec, C.P.1    MacPhee, C.E.2    Bajaj, V.S.3    McMahon, M.T.4    Dobson, C.M.5
  • 69
    • 0026320119 scopus 로고
    • An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: Application of solid state NMR to the determination of protein secondary structure
    • Spencer RGS, Halverson KJ, Auger M, McDermott AE, Griffin RG, et al. 1991. An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid state NMR to the determination of protein secondary structure. Biochemistry 30:10382-10387.
    • (1991) Biochemistry , vol.30 , pp. 10382-10387
    • Spencer, R.G.S.1    Halverson, K.J.2    Auger, M.3    McDermott, A.E.4    Griffin, R.G.5
  • 70
    • 0028804827 scopus 로고
    • Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
    • Lansbury PT Jr, Costa PR, Griffiths JM, Simon EJ, Auger M, at al. 1995. Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat Struct Biol 2:990-998.
    • (1995) Nat Struct Biol , vol.2 , pp. 990-998
    • Lansbury Jr, P.T.1    Costa, P.R.2    Griffiths, J.M.3    Simon, E.J.4    Auger, M.5    at al6
  • 71
    • 0032506114 scopus 로고    scopus 로고
    • Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register
    • Benzinger TL, Gregory DM, Burkoth TS, Miller-Auer H, Lynn DG, et al. 1998. Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register, Proc Natl Acad Sci USA 95:13407-13412.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13407-13412
    • Benzinger, T.L.1    Gregory, D.M.2    Burkoth, T.S.3    Miller-Auer, H.4    Lynn, D.G.5
  • 72
    • 0034700129 scopus 로고    scopus 로고
    • Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils
    • Antzutkin ON, Balbach JJ, Leapman RD, Rizzo NW, Reed J, at al. 2000. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci USA 97:13045-13050.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13045-13050
    • Antzutkin, O.N.1    Balbach, J.J.2    Leapman, R.D.3    Rizzo, N.W.4    Reed, J.5    at al6
  • 73
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko R. 2006. Molecular structure of amyloid fibrils: insights from solid-state NMR. Quart Revs Biophys 1:1-55.
    • (2006) Quart Revs Biophys , vol.1 , pp. 1-55
    • Tycko, R.1
  • 74
    • 20444458341 scopus 로고    scopus 로고
    • Correlation of structural elements and infectivity of the HET-s prion
    • Ritter C, Maddelein ML, Siemer AB, Luhrs T, Ernst M, 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    Luhrs, T.4    Ernst, M.5
  • 75
    • 33645473793 scopus 로고    scopus 로고
    • 13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form
    • Siemer AB, Ritter C, Steinmetz MO, Ernst M, Riek R, et al. 2006. 13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form. J Biomol NMR 34:75-87.
    • (2006) J Biomol NMR , vol.34 , pp. 75-87
    • Siemer, A.B.1    Ritter, C.2    Steinmetz, M.O.3    Ernst, M.4    Riek, R.5
  • 76
    • 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, et al. 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
  • 77
    • 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. Proc Natl Acad Sci USA 103:19754-19759.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 19754-19759
    • Shewmaker, F.1    Wickner, R.B.2    Tycko, R.3
  • 78
    • 0037059016 scopus 로고    scopus 로고
    • Changes in the middle region of Sup35p profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]
    • Liu J-J, Sondheimer N, Lindquist S. 2002. Changes in the middle region of Sup35p profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc Natl Acad Sci USA 99:16446-16453.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16446-16453
    • Liu, J.-J.1    Sondheimer, N.2    Lindquist, S.3
  • 79
    • 1642524541 scopus 로고    scopus 로고
    • The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+[prions
    • Bradley ME, Liebman SW. 2004, The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+[prions. Mol Microbiol 51:1649-1659.
    • (2004) Mol Microbiol , vol.51 , pp. 1649-1659
    • Bradley, M.E.1    Liebman, S.W.2
  • 81
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, et al. 2002. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 99:16742-16747.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Balbach, J.J.3    Antzutkin, O.N.4    Leapman, R.D.5
  • 82
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR
    • 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) Biochemistry , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.-M.2    Leapman, R.3    Tycko, R.4
  • 83
    • 0027740178 scopus 로고
    • Scrapie strain variation and mutation
    • Bruce ME. 1993. Scrapie strain variation and mutation. Br Med Bull 49: 822-838.
    • (1993) Br Med Bull , vol.49 , pp. 822-838
    • Bruce, M.E.1
  • 84
    • 0026583834 scopus 로고
    • Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent
    • Bessen RA, Marsh RF. 1992. Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 66:2096-2101.
    • (1992) J Virol , vol.66 , pp. 2096-2101
    • Bessen, R.A.1    Marsh, R.F.2
  • 88
    • 0035853292 scopus 로고    scopus 로고
    • Supporting the structural basis of prion strains: Induction and identification of [PSI] variants
    • King CY. 2001. Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J Mol Biol 307:1247-1260.
    • (2001) J Mol Biol , vol.307 , pp. 1247-1260
    • King, C.Y.1
  • 89
    • 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
  • 92
    • 34447526217 scopus 로고    scopus 로고
    • Stress and prions: Lessons from the yeast model
    • Chernoff YO. 2007. Stress and prions: lessons from the yeast model. FEBS Lett 581:3695-3701.
    • (2007) FEBS Lett , vol.581 , pp. 3695-3701
    • Chernoff, Y.O.1
  • 93
    • 0033500152 scopus 로고    scopus 로고
    • Evidence for a protein mutator in yeast: Role of the Hsp70-related chaperone Ssb in formation, stability and toxicity of the [PSI+] prion
    • Chernoff YO, Newnam GP, Kumar J, Allen K, Zink AD. 1999. Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone Ssb in formation, stability and toxicity of the [PSI+] prion. Mol Cell Biol 19:8103-8112.
    • (1999) Mol Cell Biol , vol.19 , pp. 8103-8112
    • Chernoff, Y.O.1    Newnam, G.P.2    Kumar, J.3    Allen, K.4    Zink, A.D.5
  • 94
    • 0033786333 scopus 로고    scopus 로고
    • A role for cytosolic Hsp70 in yeast [PSI+] prion propagation and [PSI+] as a cellular stress
    • Jung G, Jones G, Wegrzyn RD, Masison DC. 2000. A role for cytosolic Hsp70 in yeast [PSI+] prion propagation and [PSI+] as a cellular stress. Genetics 156:559-570.
    • (2000) Genetics , vol.156 , pp. 559-570
    • Jung, G.1    Jones, G.2    Wegrzyn, R.D.3    Masison, D.C.4
  • 96
    • 0037189549 scopus 로고    scopus 로고
    • Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions
    • Kryndushkin D, Smirnov VN, Ter-Avanesyan MD, Kushnirov VV. 2002. Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277:23702-23708.
    • (2002) J Biol Chem , vol.277 , pp. 23702-23708
    • Kryndushkin, D.1    Smirnov, V.N.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 97
    • 1942518319 scopus 로고    scopus 로고
    • Propagation of yeast [PSI+] prion impaired by factors that regulate Hsp70 substrate binding
    • Jones G, Song Y, Chung S, Masison DC. 2004. Propagation of yeast [PSI+] prion impaired by factors that regulate Hsp70 substrate binding. Mol Cell Biol 24:3928-3937.
    • (2004) Mol Cell Biol , vol.24 , pp. 3928-3937
    • Jones, G.1    Song, Y.2    Chung, S.3    Masison, D.C.4
  • 98
    • 0034462603 scopus 로고    scopus 로고
    • URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • Moriyama H, Edskes HK, Wickner RB. 2000. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol Cell Biol 20:8916-8922.
    • (2000) Mol Cell Biol , vol.20 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 99
    • 34548101963 scopus 로고    scopus 로고
    • J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds for prion propagation
    • Aron R, Higurashi T, Sahi C, Craig EA. 2007. J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds for prion propagation. EMBO J 26:3794-3803.
    • (2007) EMBO J , vol.26 , pp. 3794-3803
    • Aron, R.1    Higurashi, T.2    Sahi, C.3    Craig, E.A.4
  • 100
    • 37049025592 scopus 로고    scopus 로고
    • Role of Hsp104 in the propagation and inheritance of the [Het-s] prion
    • Malato L, Dos Reis S, Benkemoun L, Sabate R, Saupe SJ. 2007. Role of Hsp104 in the propagation and inheritance of the [Het-s] prion. Mol Biol Cell 18:4803-4812.
    • (2007) Mol Biol Cell , vol.18 , pp. 4803-4812
    • Malato, L.1    Dos Reis, S.2    Benkemoun, L.3    Sabate, R.4    Saupe, S.J.5
  • 101
  • 102
    • 0036310663 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast
    • Ness F, Ferreira P, Cox BS, Tuite MF. 2002. Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol Cell Biol 22:5593-5605.
    • (2002) Mol Cell Biol , vol.22 , pp. 5593-5605
    • Ness, F.1    Ferreira, P.2    Cox, B.S.3    Tuite, M.F.4
  • 103
    • 0037162510 scopus 로고    scopus 로고
    • Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance
    • Jung G, Jones G, Masison DC. 2002. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc Natl Acad Sci USA 99:9936-9941.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9936-9941
    • Jung, G.1    Jones, G.2    Masison, D.C.3
  • 104
    • 34249689651 scopus 로고    scopus 로고
    • Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils
    • Lian HY, Zhang H, Zhang ZR, Loovers HM, Jones GW, et al. 2007. Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils. J Biol Chem 282:11931-11940.
    • (2007) J Biol Chem , vol.282 , pp. 11931-11940
    • Lian, H.Y.1    Zhang, H.2    Zhang, Z.R.3    Loovers, H.M.4    Jones, G.W.5
  • 105
    • 0032832981 scopus 로고    scopus 로고
    • Genetic study of interactions between the cytoskeletal assembly protein Sla1 and prion - forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae
    • Bailleul PA, Newnam GP, Steenbergen JN, Chernoff YO. 1999. Genetic study of interactions between the cytoskeletal assembly protein Sla1 and prion - forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Genetics 153:81-94.
    • (1999) Genetics , vol.153 , pp. 81-94
    • Bailleul, P.A.1    Newnam, G.P.2    Steenbergen, J.N.3    Chernoff, Y.O.4
  • 106
    • 30644474711 scopus 로고    scopus 로고
    • Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast
    • Ganusova EE, Ozolins LN, Bhagat S, Newnam GP, Wegrzyn RD, et al. 2006. Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Mol Cell Biol 26:617-629.
    • (2006) Mol Cell Biol , vol.26 , pp. 617-629
    • Ganusova, E.E.1    Ozolins, L.N.2    Bhagat, S.3    Newnam, G.P.4    Wegrzyn, R.D.5
  • 107
  • 108
    • 10744225913 scopus 로고    scopus 로고
    • Isolation of drugs active against mammalian prions using a yeast-based screening assay
    • Bach S, Talarek N, Andrieu T, Vierfond JM, Mettey Y, et al. 2003. Isolation of drugs active against mammalian prions using a yeast-based screening assay. Nat. Biotechnol 21:1075-1081.
    • (2003) Nat. Biotechnol , vol.21 , pp. 1075-1081
    • Bach, S.1    Talarek, N.2    Andrieu, T.3    Vierfond, J.M.4    Mettey, Y.5
  • 109
    • 48249101576 scopus 로고    scopus 로고
    • Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs
    • Tribouillard-Tanvier D, Dos Reis S, Gug F, Voisset C, Beringue V, et al. 2008. Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs. Plos One 3:e2174.
    • (2008) Plos One , vol.3
    • Tribouillard-Tanvier, D.1    Dos Reis, S.2    Gug, F.3    Voisset, C.4    Beringue, V.5
  • 110
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses
    • Johnson SM, Wiseman RL, Sekijima Y, Green NS, Adamski-Werner SL, et al. 2005. Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. Acc Chem Res 38:911-921.
    • (2005) Acc Chem Res , vol.38 , pp. 911-921
    • Johnson, S.M.1    Wiseman, R.L.2    Sekijima, Y.3    Green, N.S.4    Adamski-Werner, S.L.5
  • 111
    • 17444417025 scopus 로고    scopus 로고
    • Hsp70 chaperones as modulators of prion life cycle: Novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]
    • Allen KD, Wegrzyn RD, Chernova TA, Muller S, Newnam GP, et al. 2005. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 169:1227-1242.
    • (2005) Genetics , vol.169 , pp. 1227-1242
    • Allen, K.D.1    Wegrzyn, R.D.2    Chernova, T.A.3    Muller, S.4    Newnam, G.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.