메뉴 건너뛰기




Volumn 38, Issue , 2004, Pages 681-707

Prion genetics: New rules for a new kind of gene

Author keywords

Het s ; PIN ; PSI ; URE3 ; Amyloid; PrP

Indexed keywords

AMYLOID; CHAPERONE; MKS1P PROTEIN; NUCLEIC ACID; PRION PROTEIN; PROTEIN; RAS PROTEIN; RECOMBINANT PROTEIN; SUP35P PROTEIN; UNCLASSIFIED DRUG;

EID: 10944228369     PISSN: 00664197     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.genet.38.072902.092200     Document Type: Review
Times cited : (74)

References (144)
  • 1
    • 10944229158 scopus 로고    scopus 로고
    • Prions for physicians
    • 2003. Prions for physicians. Br. Med. Bull. 66:1-316
    • Br. Med. Bull. , vol.66 , pp. 1-316
  • 2
    • 0344021409 scopus 로고    scopus 로고
    • Prions and the immune system: A journey through gut, spleen and nerves
    • Aguzzi A. 2003. Prions and the immune system: a journey through gut, spleen and nerves. Adv. Immunol. 81:123-71
    • (2003) Adv. Immunol. , vol.81 , pp. 123-171
    • Aguzzi, A.1
  • 3
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology, one century of evolving concepts
    • Aguzzi A, Polymenidou M. 2004. Mammalian prion biology, one century of evolving concepts. Cell 116:313-27
    • (2004) Cell , vol.116 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 5
    • 0016669719 scopus 로고
    • Genetical aspects of [URE3], anon-Mendelian, cytoplasmically inherited mutation in y east
    • Aigle M, Lacroute F. 1975. Genetical aspects of [URE3], anon-Mendelian, cytoplasmically inherited mutation in y east. Mol. Gen. Genet. 136:327-35
    • (1975) Mol. Gen. Genet. , vol.136 , pp. 327-335
    • Aigle, M.1    Lacroute, F.2
  • 6
    • 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 214:764-66
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 7
    • 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 21:1075-81
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1075-1081
    • Bach, S.1    Talarek, N.2    Andrieu, T.3    Vierfond, J.M.4    Mettey, Y.5
  • 8
    • 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. 22:2071-81
    • (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
  • 9
    • 0037117485 scopus 로고    scopus 로고
    • Mechanism of inactivation on prion conversion of the Sacchammyces cerevisiae Ure2 protein
    • Baxa U, Speransky V, Steven AC, Wickner RB. 2002. Mechanism of inactivation on prion conversion of the Sacchammyces cerevisiae Ure2 protein. Proc. Natl. Acad. Sci. USA 99:5253-60
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5253-5260
    • Baxa, U.1    Speransky, V.2    Steven, A.C.3    Wickner, R.B.4
  • 10
    • 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. 278:43717-27
    • (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
  • 11
    • 0033540030 scopus 로고    scopus 로고
    • The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors
    • Beck T, Hall MN. 1999. The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors. Nature 402:689-92
    • (1999) Nature , vol.402 , pp. 689-692
    • Beck, T.1    Hall, M.N.2
  • 12
    • 0027985296 scopus 로고
    • Vegetative incompatibility in filamentous fungi: Het genes begin to talk
    • Begueret J, Turq B, Clave C. 1994. Vegetative incompatibility in filamentous fungi: het genes begin to talk. Trends Genet. 10:441-46
    • (1994) Trends Genet. , vol.10 , pp. 441-446
    • Begueret, J.1    Turq, B.2    Clave, C.3
  • 14
    • 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 218:1309-11
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 15
    • 0035156642 scopus 로고    scopus 로고
    • Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
    • Bousset L, Beirhali H, Janin J, Melki R, Morera S. 2001. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 9:39-46
    • (2001) Structure , vol.9 , pp. 39-46
    • Bousset, L.1    Beirhali, H.2    Janin, J.3    Melki, R.4    Morera, S.5
  • 16
    • 0037124337 scopus 로고    scopus 로고
    • The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro
    • Bousset L, Thomson NH, Radford SE, Melki R. 2002. The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro. EMBO J. 21:2903-11
    • (2002) EMBO J. , vol.21 , pp. 2903-2911
    • Bousset, L.1    Thomson, N.H.2    Radford, S.E.3    Melki, R.4
  • 17
    • 0028235176 scopus 로고
    • Human spongiform encephalopathy: The National Institutes of Health series of 300 cases of experimentally transmitted disease
    • Brown P, Gibbs CJ, Rogers-Johnson P, Asher DM, Sulima MP, et al. 1994. Human spongiform encephalopathy: the National Institutes of Health series of 300 cases of experimentally transmitted disease. Ann. Neurol. 35:513-29
    • (1994) Ann. Neurol. , vol.35 , pp. 513-529
    • Brown, P.1    Gibbs, C.J.2    Rogers-Johnson, P.3    Asher, D.M.4    Sulima, M.P.5
  • 18
    • 0141515178 scopus 로고    scopus 로고
    • TSE strain variation
    • Bruce ME. 2003. TSE strain variation. Br. Med. Bull. 66:99-108
    • (2003) Br. Med. Bull. , vol.66 , pp. 99-108
    • Bruce, M.E.1
  • 20
    • 0026099887 scopus 로고
    • The disease characteristics of different strains of scrapie in Sinc congenic mouse lines: Implications for the nature of the agent and host control of pathogenesis
    • Bruce ME, McConnell I, Fraser H, Dickinson AG. 1991. The disease characteristics of different strains of scrapie in Sinc congenic mouse lines: implications for the nature of the agent and host control of pathogenesis. J. Gen. Virol. 72:595-603
    • (1991) J. Gen. Virol. , vol.72 , pp. 595-603
    • Bruce, M.E.1    McConnell, I.2    Fraser, H.3    Dickinson, A.G.4
  • 22
    • 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 HP, 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
  • 24
  • 26
    • 0036468673 scopus 로고    scopus 로고
    • Role of Escherichia coli Curli operons in directing amyloid fiber formation
    • Chapman MR, Robinson LS, Pinkner JS, Roth R, Heuser J, et al. 2002. Role of Escherichia coli Curli operons in directing amyloid fiber formation. Science 295:851-55
    • (2002) Science , vol.295 , pp. 851-855
    • Chapman, M.R.1    Robinson, L.S.2    Pinkner, J.S.3    Roth, R.4    Heuser, J.5
  • 27
    • 0027483882 scopus 로고
    • Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae
    • Chernoff YO, Derkach IL, Inge-Vechtomov SG. 1993. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr. Genet. 24:268-70
    • (1993) Curr. Genet. , vol.24 , pp. 268-270
    • Chernoff, Y.O.1    Derkach, I.L.2    Inge-Vechtomov, S.G.3
  • 31
    • 0002933976 scopus 로고
    • Dosage-dependent modifiers of PSI-dependent omnipotent suppression in yeast
    • ed. AJP Brown, MF Tuite, JEG McCarthy. Berlin: Springer-Verlag
    • Chernoff YO, Ono B-I. 1992. Dosage-dependent modifiers of PSI-dependent omnipotent suppression in yeast. In Protein Synthesis and Targeting in Yeast, ed. AJP Brown, MF Tuite, JEG McCarthy, pp. 101-7. Berlin: Springer-Verlag
    • (1992) Protein Synthesis and Targeting in Yeast , pp. 101-107
    • Chernoff, Y.O.1    Ono, B.-I.2
  • 33
    • 0021884354 scopus 로고
    • Identification of scrapie prion protein-specific mRNA in scrapie-infected brain
    • Chesebro B, Race R, Wehrly K, Nishio J, Bloom M, et al. 1985. Identification of scrapie prion protein-specific mRNA in scrapie-infected brain. Nature 315:331-33
    • (1985) Nature , vol.315 , pp. 331-333
    • Chesebro, B.1    Race, R.2    Wehrly, K.3    Nishio, J.4    Bloom, M.5
  • 34
    • 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. Rev. 26:223-38
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 223-238
    • Cooper, T.G.1
  • 35
    • 0025959235 scopus 로고
    • The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione S-transferases
    • Coschigano PW, Magasanik B. 1991. The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione S-transferases. Mol. Cell. Biol. 11:822-32
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 822-832
    • Coschigano, P.W.1    Magasanik, B.2
  • 36
    • 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 94:9773-78
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 37
    • 0032711226 scopus 로고    scopus 로고
    • Mutational analysis of the [Het-s] prion analog of Podospora anserina: A short N-terminal peptide allows prion propagation
    • Coustou V, Deleu C, Saupe SJ, Begueret J. 1999. Mutational analysis of the [Het-s] prion analog of Podospora anserina: A short N-terminal peptide allows prion propagation. Genetics 153:1629-40
    • (1999) Genetics , vol.153 , pp. 1629-1640
    • Coustou, V.1    Deleu, C.2    Saupe, S.J.3    Begueret, J.4
  • 38
    • 0035725458 scopus 로고    scopus 로고
    • In vivo aggreg ation of the HET-s prion protein of the fungus Podospora anserina
    • Coustou-Linares V, Maddelein ML, Begueret J, Saupe SJ. 2001. In vivo aggreg ation 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
  • 39
    • 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 20:505-21
    • (1965) Heredity , vol.20 , pp. 505-521
    • Cox, B.S.1
  • 40
    • 0015051303 scopus 로고
    • A recessive lethal super-suppressor mutation in yeast and other PSI phenomena
    • Cox BS. 1971. A recessive lethal super-suppressor mutation in yeast and other PSI phenomena. Heredity 26:211-32
    • (1971) Heredity , vol.26 , pp. 211-232
    • Cox, B.S.1
  • 41
    • 0038714894 scopus 로고    scopus 로고
    • +], a novel Sup35-prion variant propagated with non-G1n/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104
    • +], a novel Sup35-prion variant propagated with non-G1n/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104. Genes Cells 8:603-18
    • (2003) Genes Cells , vol.8 , pp. 603-618
    • Crist, C.G.1    Nakayashiki, T.2    Kurahashi, H.3    Nakamura, Y.4
  • 42
    • 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? C. R. Acad. Sci. 203:1552-54
    • (1936) C. R. Acad. Sci. , vol.203 , pp. 1552-1554
    • Cuille, J.1    Chelle, P.L.2
  • 44
    • 0027234098 scopus 로고
    • A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina
    • Deleu C, Clave C, Begueret J. 1993. A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina. Genetics 135:45-52
    • (1993) Genetics , vol.135 , pp. 45-52
    • Deleu, C.1    Clave, C.2    Begueret, J.3
  • 45
    • 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 93:1241-52
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 46
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: The story of [PIN]
    • Derkatch BL, 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, B.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 50
    • 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. 78:293-99
    • (1968) J. Comp. Pathol. , vol.78 , pp. 293-299
    • Dickinson, A.G.1    Meikle, V.M.H.2    Fraser, H.3
  • 52
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-32
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 53
    • 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 137:659-70
    • (1994) Genetics , vol.137 , pp. 659-670
    • Doel, S.M.1    McCready, S.J.2    Nierras, C.R.3    Cox, B.S.4
  • 54
    • 0037155213 scopus 로고    scopus 로고
    • The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils
    • Dos Reis S, Coulary-Salin B, Forge V, Lascu I, Begueret J, Saupe SJ. 2002. The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils. J. Biol. Chem. 277:5703-6
    • (2002) J. Biol. Chem. , vol.277 , pp. 5703-5706
    • Dos Reis, S.1    Coulary-Salin, B.2    Forge, V.3    Lascu, I.4    Begueret, J.5    Saupe, S.J.6
  • 55
    • 0015260033 scopus 로고
    • Ureido-succinic acid uptake in yeast and some aspects of its regulation
    • Drillien R, Lacroute F. 1972. Ureido-succinic acid uptake in yeast and some aspects of its regulation. J. Bacteriol. 109:203-8
    • (1972) J. Bacteriol. , vol.109 , pp. 203-208
    • Drillien, R.1    Lacroute, F.2
  • 57
    • 0033574042 scopus 로고    scopus 로고
    • The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
    • Edskes HK, Gray VT, Wickner RB. 1999. The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc. Natl. Acad. Sci. USA 96:1498-503
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1498-1503
    • Edskes, H.K.1    Gray, V.T.2    Wickner, R.B.3
  • 58
    • 0034612316 scopus 로고    scopus 로고
    • A protein required for prion generation: [URE3] induction requires the Ras-regulated Mks1 protein
    • Edskes HK, Wickner RB. 2000. A protein required for prion generation: [URE3] induction requires the Ras-regulated Mks1 protein. Proc. Natl. Acad. Sci. USA 97:6625-29
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6625-6629
    • Edskes, H.K.1    Wickner, R.B.2
  • 60
    • 0028581973 scopus 로고
    • A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor
    • Frolova L, LeGoff X, Rasmussen HH, Cheperegin S, Drugeon G, et al. 1994. A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor. Nature 372:701-3
    • (1994) Nature , vol.372 , pp. 701-703
    • Frolova, L.1    LeGoff, X.2    Rasmussen, H.H.3    Cheperegin, S.4    Drugeon, G.5
  • 61
    • 0002313311 scopus 로고    scopus 로고
    • Infectious amyloidosis: Subacute spongiform encephalopathies as transmissible cerebral amyloidoses
    • ed. BN Fields, DM Knipe, PM Howley. Philadelphia: Raven
    • Gajdusek DC. 1996. Infectious amyloidosis: subacute spongiform encephalopathies as transmissible cerebral amyloidoses. In Fields Virology, ed. BN Fields, DM Knipe, PM Howley, pp. 2851-900. Philadelphia: Raven
    • (1996) Fields Virology , pp. 2851-2900
    • Gajdusek, D.C.1
  • 62
    • 0014201286 scopus 로고
    • Transmission and passage of experimental "kuru" to chimpanzees
    • Gajdusek DC, Gibbs CJ, Alpers M. 1967. Transmission and passage of experimental "kuru" to chimpanzees. Science 155:212-14
    • (1967) Science , vol.155 , pp. 212-214
    • Gajdusek, D.C.1    Gibbs, C.J.2    Alpers, M.3
  • 64
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover JR, Lindquist S. 1998. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94:73-82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 65
    • 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
  • 66
    • 1542380028 scopus 로고    scopus 로고
    • The prion curing agent guanidinium chloride specifically inibits ATP hydrolysis by Hsp104
    • Grimminger V, Richter K, Imhof A, Buchner J, Walter S. 2004. The prion curing agent guanidinium chloride specifically inibits ATP hydrolysis by Hsp104. J. Biol. Chem. 279:7378-83
    • (2004) J. Biol. Chem. , vol.279 , pp. 7378-7383
    • Grimminger, V.1    Richter, K.2    Imhof, A.3    Buchner, J.4    Walter, S.5
  • 67
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada C, Gardiner K, Marsh T, Pace N, Altman S. 1983. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35:849-57
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 68
    • 0024519771 scopus 로고
    • Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome
    • Hsiao K, Baker HF, Crow TJ, Poulter M, Owen F, et al. 1989. Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature 338:342-45
    • (1989) Nature , vol.338 , pp. 342-345
    • Hsiao, K.1    Baker, H.F.2    Crow, T.J.3    Poulter, M.4    Owen, F.5
  • 69
    • 0033583190 scopus 로고    scopus 로고
    • Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations
    • Jackson GS, Hosszu LL, Power A, Hill AF, Kenny J, et al. 1999. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science 283:1935-37
    • (1999) Science , vol.283 , pp. 1935-1937
    • Jackson, G.S.1    Hosszu, L.L.2    Power, A.3    Hill, A.F.4    Kenny, J.5
  • 70
    • 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. 266:7963-66
    • (1991) J. Biol. Chem. , vol.266 , pp. 7963-7966
    • Jones, E.W.1
  • 73
    • 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 99:9936-41
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9936-9941
    • Jung, G.1    Jones, G.2    Masison, D.C.3
  • 75
    • 0034974996 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits Hsp 104 activity in vivo: A possible explanation for its effect in curing yeast prions
    • Jung G, Masison DC. 2001. Guanidine hydrochloride inhibits Hsp 104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr. Microbiol. 43:7-10
    • (2001) Curr. Microbiol. , vol.43 , pp. 7-10
    • Jung, G.1    Masison, D.C.2
  • 76
    • 0026604959 scopus 로고
    • Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis (RRGE)
    • Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D. 1992. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis (RRGE). J. Gen. Microbiol. 73:1025-29
    • (1992) J. Gen. Microbiol. , vol.73 , pp. 1025-1029
    • Kellings, K.1    Meyer, N.2    Mirenda, C.3    Prusiner, S.B.4    Riesner, D.5
  • 77
    • 1942421791 scopus 로고    scopus 로고
    • PaASK1, a mitogen-activated protein kinase kinase kinase that controls cell degeneration and cell differentiation in Podospora anserina
    • Kicka S, Silar P. 2004. PaASK1, a mitogen-activated protein kinase kinase kinase that controls cell degeneration and cell differentiation in Podospora anserina. Genetics 166:1241-52
    • (2004) Genetics , vol.166 , pp. 1241-1252
    • Kicka, S.1    Silar, P.2
  • 78
    • 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. 307:1247-60
    • (2001) J. Mol. Biol. , vol.307 , pp. 1247-1260
    • King, C.Y.1
  • 79
    • 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 428:319-23
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 80
    • 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. Proc. Natl. Acad. Sci. USA 94:6618-22
    • (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    Wuthrich, K.6
  • 84
    • 0029066886 scopus 로고
    • Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier
    • Kocisko DA, Priola SA, Raymond GJ, Chesebro B, Landsbury PT, Caughey B. 1995. Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species 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    Landsbury, P.T.5    Caughey, B.6
  • 85
    • 0020417286 scopus 로고
    • Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of Tetrahymena
    • Kruger K, Grabowski PJ, Zaug AJ, Sands J, Gottschling DE, Cech TR. 1982. Self-splicing RNA: autoexcision and autocyclization of the ribosomal RNA intervening sequence of Tetrahymena. Cell 31:147-57
    • (1982) Cell , vol.31 , pp. 147-157
    • Kruger, K.1    Grabowski, P.J.2    Zaug, A.J.3    Sands, J.4    Gottschling, D.E.5    Cech, T.R.6
  • 86
    • 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. 106:519-22
    • (1971) J. Bacteriol. , vol.106 , pp. 519-522
    • Lacroute, F.1
  • 88
    • 0034723391 scopus 로고    scopus 로고
    • Creating a protein-based element of inheritance
    • Li L, Lindquist S. 2000. Creating a protein-based element of inheritance. Science 287:661-64
    • (2000) Science , vol.287 , pp. 661-664
    • Li, L.1    Lindquist, S.2
  • 89
    • 0033527045 scopus 로고    scopus 로고
    • Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast
    • Liu JJ, Lindquist S. 1999. Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature 400:573-76
    • (1999) Nature , vol.400 , pp. 573-576
    • Liu, J.J.1    Lindquist, S.2
  • 90
    • 0019411527 scopus 로고
    • -] mutations in Saccharomyces cerevisiae
    • -] mutations in Saccharomyces cerevisiae. Genet. Res. 37:173-82
    • (1981) Genet. Res. , vol.37 , pp. 173-182
    • Lund, P.M.1    Cox, B.S.2
  • 92
    • 0032974451 scopus 로고    scopus 로고
    • Two prion-inducing regions of Ure2p are non-overlapping
    • Maddelein M-L, Wickner RB. 1999. Two prion-inducing regions of Ure2p are non-overlapping. Mol. Cell. Biol. 19:4516-24
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4516-4524
    • Maddelein, M.-L.1    Wickner, R.B.2
  • 93
    • 0037094434 scopus 로고    scopus 로고
    • Nitrogen regulation in Saccharomyces cerevisiae
    • Magasanik B, Kaiser CA. 2002. Nitrogen regulation in Saccharomyces cerevisiae. Gene 290:1-18
    • (2002) Gene , vol.290 , pp. 1-18
    • Magasanik, B.1    Kaiser, C.A.2
  • 94
    • 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 94:12503-8
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12503-12508
    • Masison, D.C.1    Maddelein, M.-L.2    Wickner, R.B.3
  • 95
    • 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
  • 96
    • 0027276617 scopus 로고
    • Characterization of the MKS1 gene, a new negative regulator of the ras-cyclic AMP pathway in Saccharomyces cerevisiae
    • Matsuura A, Anraku Y. 1993. Characterization of the MKS1 gene, a new negative regulator of the ras-cyclic AMP pathway in Saccharomyces cerevisiae. Mol. Gen. Genet. 238:6-16
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 6-16
    • Matsuura, A.1    Anraku, Y.2
  • 98
    • 0025174149 scopus 로고
    • Consequences of growth media, gene copy number and regulatory mutations on the expression of the PRB1 bene of Saccharomyces cerevisiae
    • Moehle CM, Jones EW. 1990. Consequences of growth media, gene copy number and regulatory mutations on the expression of the PRB1 bene of Saccharomyces cerevisiae. Genetics 124:39-55
    • (1990) Genetics , vol.124 , pp. 39-55
    • Moehle, C.M.1    Jones, E.W.2
  • 99
    • 0023463750 scopus 로고
    • Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases
    • Moehle CM, Tizard R, Lemmon SK, Smart J, Jones EW. 1987. Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases. Mol. Cell Biol 7:4390-99
    • (1987) Mol. Cell Biol. , vol.7 , pp. 4390-4399
    • Moehle, C.M.1    Tizard, R.2    Lemmon, S.K.3    Smart, J.4    Jones, E.W.5
  • 100
    • 0034462603 scopus 로고    scopus 로고
    • [URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by over-expressed chaperone Ydj1p
    • Moriyama H, Edskes HK, Wickner RB. 2000. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by over-expressed chaperone Ydj1p. Mol. Cell. Biol. 20:8916-22
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 101
    • 0026317974 scopus 로고
    • Activation of the proteinase B precursor of the yeast Saccharomyces cerevisiae by autocatalysis and by an internal sequence
    • Nebes VL, Jones EW. 1991. Activation of the proteinase B precursor of the yeast Saccharomyces cerevisiae by autocatalysis and by an internal sequence. J. Biol. Chem. 266:22851-57
    • (1991) J. Biol. Chem. , vol.266 , pp. 22851-22857
    • Nebes, V.L.1    Jones, E.W.2
  • 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. 22:5593-605
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5593-5605
    • Ness, F.1    Ferreira, P.2    Cox, B.S.3    Tuite, M.F.4
  • 103
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO. 1999. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol. 19:1325-33
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1325-1333
    • Newnam, G.P.1    Wegrzyn, R.D.2    Lindquist, S.L.3    Chernoff, Y.O.4
  • 105
    • 0024530897 scopus 로고
    • Insertion in prion protein gene in familial Creutzfeldt-Jakob disease
    • Owen F, Poulter M, Lofthouse R, Collinge J, Crow TJ, et al. 1989. Insertion in prion protein gene in familial Creutzfeldt-Jakob disease. Lancet1:51-52
    • (1989) Lancet , vol.1 , pp. 51-52
    • Owen, F.1    Poulter, M.2    Lofthouse, R.3    Collinge, J.4    Crow, T.J.5
  • 106
    • 0035341212 scopus 로고    scopus 로고
    • Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions
    • Parham SN, Resende CG, Tuite MF. 2001. Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J. 20:2111-19
    • (2001) EMBO J. , vol.20 , pp. 2111-2119
    • Parham, S.N.1    Resende, C.G.2    Tuite, M.F.3
  • 107
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a pheno-typic trait in yeast
    • Patino MM, Liu J-J, Glover JR, Lindquist S. 1996. Support for the prion hypothesis for inheritance of a pheno-typic trait in yeast. Science 273:622-26
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.-J.2    Glover, J.R.3    Lindquist, S.4
  • 110
    • 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 99:16742-47
    • (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
  • 112
    • 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
  • 113
    • 0003661592 scopus 로고    scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press. 1050 pp.
    • Prusiner SB, ed. 2004. Prion Biology and Diseases. Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press. 1050 pp.
    • (2004) Prion Biology and Diseases
    • Prusiner, S.B.1
  • 114
    • 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
  • 115
    • 0036891092 scopus 로고    scopus 로고
    • Subclinical scrapie infection in a resistant species: Persistence, replication, and adaptation of infectivity during four passages
    • Race R, Meade-White K, Raines A, Raymond GJ, Caughey B, Chesebro B. 2002. Subclinical scrapie infection in a resistant species: persistence, replication, and adaptation of infectivity during four passages. J. Infect. Dis. 186:8166-70
    • (2002) J. Infect. Dis. , vol.186 , pp. 8166-8170
    • Race, R.1    Meade-White, K.2    Raines, A.3    Raymond, G.J.4    Caughey, B.5    Chesebro, B.6
  • 117
    • 0001909765 scopus 로고
    • Les phénomènes de barrage chez Podospora anserina: Analyse génétique des barrages entre les souches s et S
    • Rizet G. 1952. Les phénomènes de barrage chez Podospora anserina: analyse génétique 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
  • 118
    • 1242296312 scopus 로고    scopus 로고
    • [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast
    • Roberts BT, Moriyama H, Wickner RB. 2004. [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast 21:107-17
    • (2004) Yeast , vol.21 , pp. 107-117
    • Roberts, B.T.1    Moriyama, H.2    Wickner, R.B.3
  • 119
    • 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
  • 120
    • 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. 24:7206-13
    • (2004) Mol. Cell Biol. , vol.24 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3
  • 121
    • 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. Rev. 64:489-502
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 489-502
    • Saupe, S.J.1
  • 122
    • 0033661670 scopus 로고    scopus 로고
    • Vegetative incompatibility in filamentous fungi: Podospora and Neurospora provide some clues
    • Saupe SJ, Clave C, Begueret J. 2000. Vegetative incompatibility in filamentous fungi: Podospora and Neurospora provide some clues. Curr. Opin. Microbiol. 3:608-12
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 608-612
    • Saupe, S.J.1    Clave, C.2    Begueret, J.3
  • 124
    • 0036096777 scopus 로고    scopus 로고
    • +] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssalp but not by Ssa2p
    • +] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssalp but not by Ssa2p. Mol. Cell. Biol. 22:3590-98
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3590-3598
    • Schwimmer, C.1    Masison, D.C.2
  • 125
    • 0032919691 scopus 로고    scopus 로고
    • Propagation of a novel cytoplasmic, infectious and deleterious determinant is controlled by translational accuracy in Podospora anserina
    • Silar P, Haedens V, Rossingnol M, Lalucque H. 1999. Propagation of a novel cytoplasmic, infectious and deleterious determinant is controlled by translational accuracy in Podospora anserina. Genetics 151:87-95
    • (1999) Genetics , vol.151 , pp. 87-95
    • Silar, P.1    Haedens, V.2    Rossingnol, M.3    Lalucque, H.4
  • 127
    • 0037192848 scopus 로고    scopus 로고
    • Characterization of thermodynamic diversity between transmissible spongiform encephalopathy agent strains and its theoretical implications
    • Somerville RA, Oberthur RC, Havekost U, MacDonald F, Taylor DM, Dickinson AG. 2002. Characterization of thermodynamic diversity between transmissible spongiform encephalopathy agent strains and its theoretical implications. J. Biol. Chem. 277:11084-89
    • (2002) J. Biol. Chem. , vol.277 , pp. 11084-11089
    • Somerville, R.A.1    Oberthur, R.C.2    Havekost, U.3    MacDonald, F.4    Taylor, D.M.5    Dickinson, A.G.6
  • 128
    • 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. Mol. Cell 5:163-72
    • (2000) Mol. Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 130
    • 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. 14:4365-73
    • (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
  • 131
    • 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 428:323-28
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 132
    • 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 283:1339-43
    • (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
  • 136
    • 0025304230 scopus 로고
    • Isolation of two alleles incompatibility genes J and S of the fungus Podospora anserina
    • Turcq B, Denayrolles M, Begueret J. 1990. Isolation of two alleles incompatibility genes J and S of the fungus Podospora anserina. Curr. Genet. 17:297-303
    • (1990) Curr. Genet. , vol.17 , pp. 297-303
    • Turcq, B.1    Denayrolles, M.2    Begueret, J.3
  • 137
    • 0037465708 scopus 로고    scopus 로고
    • Insights into the amyloid folding problem from solid-state NMR
    • Tycko R. 2003. Insights into the amyloid folding problem from solid-state NMR. Biochemistry 42:3151-59
    • (2003) Biochemistry , vol.42 , pp. 3151-3159
    • Tycko, R.1
  • 138
    • 0035852745 scopus 로고    scopus 로고
    • The crystal structure of the nitrogen catabolite regulatory fragment of the yeast prion protein Ure2p
    • Umland TC, Taylor KL, Rhee S, Wickner RB, Davies DR. 2001. The crystal structure of the nitrogen catabolite regulatory fragment of the yeast prion protein Ure2p. Proc. Natl. Acad. Sci. USA 98:1459-64
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1459-1464
    • Umland, T.C.1    Taylor, K.L.2    Rhee, S.3    Wickner, R.B.4    Davies, D.R.5
  • 140
    • 0028308104 scopus 로고
    • Evidence for a prion analog in S. cerevisiae: The [URE3] non-Mendelian genetic element as an altered URE2 protein
    • Wickner RB. 1994. Evidence for a prion analog in S. cerevisiae: the [URE3] non-Mendelian genetic element as an altered URE2 protein. Science 264:566-69
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 141
    • 0030443751 scopus 로고    scopus 로고
    • Prions and RNA viruses of Saccharomyces cerevisiae
    • Wickner RB. 1996. Prions and RNA viruses of Saccharomyces cerevisiae. Annu. Rev. Genet. 30:109-35
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 109-135
    • Wickner, R.B.1
  • 142
    • 0012176129 scopus 로고    scopus 로고
    • Viruses of yeasts, fungi and parasitic microorganisms
    • ed. DM Knipe, PM Howley. Philadelphia: Lippincott, Williams & Wilkins
    • Wickner RB. 2001. Viruses of yeasts, fungi and parasitic microorganisms. In Fields Virology, ed. DM Knipe, PM Howley, pp. 629-58. Philadelphia: Lippincott, Williams & Wilkins
    • (2001) Fields Virology , pp. 629-658
    • Wickner, R.B.1
  • 144
    • 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 102:679-90
    • (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.