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Volumn 14, Issue 5, 2004, Pages 541-552

Propagating prions in fungi and mammals

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; PRION PROTEIN;

EID: 2942620539     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.05.012     Document Type: Review
Times cited : (32)

References (116)
  • 3
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid
    • Balbirnie M., Grothe R., Eisenberg D.S. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc. Natl. Acad. Sci. USA. 98:2001;2375-2380
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 5
    • 0035903461 scopus 로고    scopus 로고
    • Changing a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers
    • Barron R.M., Thomson V., Jamieson E., Melton D.W., Ironside J., Will R., Manson J.C. Changing a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers. EMBO J. 20:2001;5070-5078
    • (2001) EMBO J. , vol.20 , pp. 5070-5078
    • Barron, R.M.1    Thomson, V.2    Jamieson, E.3    Melton, D.W.4    Ironside, J.5    Will, R.6    Manson, J.C.7
  • 8
    • 0037124337 scopus 로고    scopus 로고
    • The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro
    • Bousset L., Thomson N.H., Radford S.E., Melki R. The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J. 21:2002;2903-2911
    • (2002) EMBO J. , vol.21 , pp. 2903-2911
    • Bousset, L.1    Thomson, N.H.2    Radford, S.E.3    Melki, R.4
  • 10
    • 0027740178 scopus 로고
    • Scrapie strain variation and mutation
    • Bruce M.E. Scrapie strain variation and mutation. Br. Med. Bull. 49:1993;822-838
    • (1993) Br. Med. Bull. , vol.49 , pp. 822-838
    • Bruce, M.E.1
  • 11
    • 0141849856 scopus 로고    scopus 로고
    • Prion protein conversions: Insight into mechanisms, TSE transmission barriers and strains
    • Caughey B. Prion protein conversions. insight into mechanisms, TSE transmission barriers and strains Br. Med. Bull. 66:2003;109-120
    • (2003) Br. Med. Bull. , vol.66 , pp. 109-120
    • Caughey, B.1
  • 12
    • 0142215488 scopus 로고    scopus 로고
    • Prion diseases: A nucleic-acid accomplice?
    • Caughey B., Kocisko D.A. Prion diseases. a nucleic-acid accomplice? Nature. 425:2003;673-674
    • (2003) Nature , vol.425 , pp. 673-674
    • Caughey, B.1    Kocisko, D.A.2
  • 13
    • 0032557457 scopus 로고    scopus 로고
    • Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides
    • Chabry J., Caughey B., Chesebro B. Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides. J. Biol. Chem. 273:1998;13203-13207
    • (1998) J. Biol. Chem. , vol.273 , pp. 13203-13207
    • Chabry, J.1    Caughey, B.2    Chesebro, B.3
  • 15
    • 0032472239 scopus 로고    scopus 로고
    • BSE and prions: Uncertainties about the agent
    • Chesebro B. BSE and prions. uncertainties about the agent Science. 279:1998;42-43
    • (1998) Science , vol.279 , pp. 42-43
    • Chesebro, B.1
  • 16
    • 0035826236 scopus 로고    scopus 로고
    • Conformational diversity in a yeast prion dictates its seeding specificity
    • Chien P., Weissman J.S. Conformational diversity in a yeast prion dictates its seeding specificity. Nature. 410:2001;223-227
    • (2001) Nature , vol.410 , pp. 223-227
    • Chien, P.1    Weissman, J.S.2
  • 17
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge J. Prion diseases of humans and animals. Their causes and molecular basis Annu. Rev. Neurosci. 24:2001;519-550
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-550
    • Collinge, J.1
  • 18
    • 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. 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. 94:1997;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
  • 20
    • 0038714894 scopus 로고    scopus 로고
    • +], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104
    • +], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104. Genes Cells. 8:2003;603-618
    • (2003) Genes Cells , vol.8 , pp. 603-618
    • Crist, C.G.1    Nakayashiki, T.2    Kurahashi, H.3    Nakamura, Y.4
  • 21
    • 0031443433 scopus 로고    scopus 로고
    • Chaperone-supervised conversion of prion protein to its protease-resistant form
    • DebBurman S.K., Raymond G.J., Caughey B., Lindquist S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl. Acad. Sci.USA. 94:1997;13938-13943
    • (1997) Proc. Natl. Acad. Sci.USA , vol.94 , pp. 13938-13943
    • Debburman, S.K.1    Raymond, G.J.2    Caughey, B.3    Lindquist, S.4
  • 22
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault N.R., Lucassen R.W., Supattapone S. RNA molecules stimulate prion protein conversion. Nature. 425:2003;717-720
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 23
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DePace A.H., Santoso A., Hillner P., Weissman J.S. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell. 93:1998;1241-1252
    • (1998) Cell , vol.93 , pp. 1241-1252
    • Depace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 24
    • 0036233931 scopus 로고    scopus 로고
    • Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
    • DePace A.H., Weissman J.S. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nat. Struct. Biol. 9:2002;389-396
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 389-396
    • Depace, A.H.1    Weissman, J.S.2
  • 28
    • 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. 137:1994;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
  • 30
    • 0037155213 scopus 로고    scopus 로고
    • The HET-s prion protein of the filamentous fungus Podospora sparagi aggregates in vitro into amyloid-like fibrils
    • Dos Reis S., Coulary-Salin B., Forge V., Lascu I., Begueret J., Saupe S.J. The HET-s prion protein of the filamentous fungus Podospora sparagi aggregates in vitro into amyloid-like fibrils. J. Biol. Chem. 277:2002;5703-5706
    • (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
  • 33
    • 0036303942 scopus 로고    scopus 로고
    • Global analysis of tandem aromatic octapeptide repeats: The significance of the aromatic-glycine motif
    • Gazit E. Global analysis of tandem aromatic octapeptide repeats. the significance of the aromatic-glycine motif Bioinformatics. 18:2002;880-883
    • (2002) Bioinformatics , vol.18 , pp. 880-883
    • Gazit, E.1
  • 34
    • 1942471926 scopus 로고    scopus 로고
    • Mechanism of intestinal entry of infectious prion protein in the pathogenesis of variant Creutzfeldt-Jakob disease
    • Ghosh S. Mechanism of intestinal entry of infectious prion protein in the pathogenesis of variant Creutzfeldt-Jakob disease. Adv. Drug Deliv. Rev. 56:2004;915-920
    • (2004) Adv. Drug Deliv. Rev. , vol.56 , pp. 915-920
    • Ghosh, S.1
  • 35
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., Lindquist S. Hsp104, Hsp70, and Hsp40. A novel chaperone system that rescues previously aggregated proteins Cell. 94:1998;73-82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 38
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith J.S. Self-replication and scrapie. Nature. 215:1967;1043-1044
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 39
    • 1542380028 scopus 로고    scopus 로고
    • The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104
    • Grimminger V., Richter K., Imhof A., Buchner J., Walter S. The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J. Biol. Chem. 279:2004;7378-7383
    • (2004) J. Biol. Chem. , vol.279 , pp. 7378-7383
    • Grimminger, V.1    Richter, K.2    Imhof, A.3    Buchner, J.4    Walter, S.5
  • 40
    • 0037269316 scopus 로고    scopus 로고
    • Mutant prion protein-mediated aggregation of normal prion protein in the endoplasmic reticulum: Implications for prion propagation and neurotoxicity
    • Gu Y., Verghese S., Mishra R.S., Xu X., Shi Y., Singh N. Mutant prion protein-mediated aggregation of normal prion protein in the endoplasmic reticulum. implications for prion propagation and neurotoxicity J. Neurochem. 84:2003;10-22
    • (2003) J. Neurochem. , vol.84 , pp. 10-22
    • Gu, Y.1    Verghese, S.2    Mishra, R.S.3    Xu, X.4    Shi, Y.5    Singh, N.6
  • 42
    • 0033301552 scopus 로고    scopus 로고
    • Cell biological studies of the prion protein
    • Harris D.A. Cell biological studies of the prion protein. Curr. Issues Mol. Biol. 1:1999;65-75
    • (1999) Curr. Issues Mol. Biol. , vol.1 , pp. 65-75
    • Harris, D.A.1
  • 44
    • 0032892306 scopus 로고    scopus 로고
    • Protease-resistant prion protein produced in vitro lacks detectable infectivity
    • Hill A.F., Antoniou M., Collinge J. Protease-resistant prion protein produced in vitro lacks detectable infectivity. J. Gen. Virol. 80:1999;11-14
    • (1999) J. Gen. Virol. , vol.80 , pp. 11-14
    • Hill, A.F.1    Antoniou, M.2    Collinge, J.3
  • 46
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • Hornshaw M.P., McDermott J.R., Candy J.M., Lakey J.H. Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein. structural studies using synthetic peptides Biochem. Biophys. Res. Commun. 214:1995;993-999
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 47
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett J.T., Lansbury P.T. Seeding "one-dimensional crystallization" of amyloid. a pathogenic mechanism in Alzheimer's disease and scrapie? Cell. 73:1993;1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 48
    • 0037297381 scopus 로고    scopus 로고
    • +] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of
    • +] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of. Genetics. 163:2003;495-506
    • (2003) Genetics , vol.163 , pp. 495-506
    • Jones, G.W.1    Masison, D.C.2
  • 49
    • 0041825135 scopus 로고    scopus 로고
    • Analysis of yeast prion aggregates with amyloid-staining compound in vivo
    • Kimura Y., Koitabashi S., Fujita T. Analysis of yeast prion aggregates with amyloid-staining compound in vivo. Cell Struct. Funct. 28:2003;187-193
    • (2003) Cell Struct. Funct. , vol.28 , pp. 187-193
    • Kimura, Y.1    Koitabashi, S.2    Fujita, T.3
  • 50
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King C.Y., Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature. 428:2004;319-323
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 51
    • 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. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad. Sci. USA. 94:1997;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    Wuthrich, K.6
  • 53
    • 0141632823 scopus 로고    scopus 로고
    • New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products
    • Kocisko D.A., Baron G.S., Rubenstein R., Chen J., Kuizon S., Caughey B. New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products. J. Virol. 77:2003;10288-10294
    • (2003) J. Virol. , vol.77 , pp. 10288-10294
    • Kocisko, D.A.1    Baron, G.S.2    Rubenstein, R.3    Chen, J.4    Kuizon, S.5    Caughey, B.6
  • 54
    • 0037189549 scopus 로고    scopus 로고
    • Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions
    • Kryndushkin D.S., Smirnov V.N., Ter-Avanesyan M.D., Kushnirov V.V. Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J. Biol. Chem. 277:2002;23702-23708
    • (2002) J. Biol. Chem. , vol.277 , pp. 23702-23708
    • Kryndushkin, D.S.1    Smirnov, V.N.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 56
    • 0142091396 scopus 로고    scopus 로고
    • Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: Structural clues for prion propagation
    • Kundu B., Maiti N.R., Jones E.M., Surewicz K.A., Vanik D.L., Surewicz W.K. Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein. structural clues for prion propagation Proc. Natl. Acad. Sci. USA. 100:2003;12069-12074
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12069-12074
    • Kundu, B.1    Maiti, N.R.2    Jones, E.M.3    Surewicz, K.A.4    Vanik, D.L.5    Surewicz, W.K.6
  • 57
    • 0032503963 scopus 로고    scopus 로고
    • Structure and replication of yeast prions
    • Kushnirov V.V., Ter-Avanesyan M.D. Structure and replication of yeast prions. Cell. 94:1998;13-16
    • (1998) Cell , vol.94 , pp. 13-16
    • Kushnirov, V.V.1    Ter-Avanesyan, M.D.2
  • 58
    • 0035929635 scopus 로고    scopus 로고
    • N-terminal truncation of prion protein affects both formation and conformation of abnormal protease-resistant prion protein generated in vitro
    • Lawson V.A., Priola S.A., Wehrly K., Chesebro B. N-terminal truncation of prion protein affects both formation and conformation of abnormal protease-resistant prion protein generated in vitro. J. Biol. Chem. 276:2001;35265-35271
    • (2001) J. Biol. Chem. , vol.276 , pp. 35265-35271
    • Lawson, V.A.1    Priola, S.A.2    Wehrly, K.3    Chesebro, B.4
  • 59
    • 1842791529 scopus 로고    scopus 로고
    • Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro
    • Lawson V.A., Priola S.A., Meade-White K., Lawson M., Chesebro B. Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro. J. Biol. Chem. 279:2004;13689-13695
    • (2004) J. Biol. Chem. , vol.279 , pp. 13689-13695
    • Lawson, V.A.1    Priola, S.A.2    Meade-White, K.3    Lawson, M.4    Chesebro, B.5
  • 60
    • 0030799062 scopus 로고    scopus 로고
    • Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells
    • Lehmann S., Harris D.A. Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 272:1997;21479-21487
    • (1997) J. Biol. Chem. , vol.272 , pp. 21479-21487
    • Lehmann, S.1    Harris, D.A.2
  • 61
    • 0034723391 scopus 로고    scopus 로고
    • Creating a protein-based element of inheritance
    • Li L., Lindquist S. Creating a protein-based element of inheritance. Science. 287:2000;661-664
    • (2000) Science , vol.287 , pp. 661-664
    • Li, L.1    Lindquist, S.2
  • 62
    • 0033527045 scopus 로고    scopus 로고
    • Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast
    • Liu J.J., Lindquist S. Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature. 400:1999;573-576
    • (1999) Nature , vol.400 , pp. 573-576
    • Liu, J.J.1    Lindquist, S.2
  • 64
    • 0028859540 scopus 로고
    • Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
    • Masison D.C., Wickner R.B. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science. 270:1995;93-95
    • (1995) Science , vol.270 , pp. 93-95
    • Masison, D.C.1    Wickner, R.B.2
  • 65
    • 0242438133 scopus 로고    scopus 로고
    • A solid-phase assay for identification of modulators of prion protein interactions
    • Maxson L., Wong C., Herrmann L.M., Caughey B., Baron G.S. A solid-phase assay for identification of modulators of prion protein interactions. Anal. Biochem. 323:2003;54-64
    • (2003) Anal. Biochem. , vol.323 , pp. 54-64
    • Maxson, L.1    Wong, C.2    Herrmann, L.M.3    Caughey, B.4    Baron, G.S.5
  • 66
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley M.P., Bolton D.C., Prusiner S.B. A protease-resistant protein is a structural component of the scrapie prion. Cell. 35:1983;57-62
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 68
    • 0034462603 scopus 로고    scopus 로고
    • [URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • Moriyama H., Edskes H.K., Wickner R.B. [URE3] prion propagation in Saccharomyces cerevisiae. requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p Mol. Cell. Biol. 20:2000;8916-8922
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 69
    • 0041345995 scopus 로고    scopus 로고
    • Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora sparagi analyzed by hydrogen/deuterium exchange and mass spectrometry
    • Nazabal A., Dos Reis S., Bonneu M., Saupe S.J., Schmitter J.M. Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora sparagi analyzed by hydrogen/deuterium exchange and mass spectrometry. Biochemistry. 42:2003;8852-8861
    • (2003) Biochemistry , vol.42 , pp. 8852-8861
    • Nazabal, A.1    Dos Reis, S.2    Bonneu, M.3    Saupe, S.J.4    Schmitter, J.M.5
  • 70
    • 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 B.S., Tuite M.F. Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol. Cell. Biol. 22:2002;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
  • 71
    • 0035871295 scopus 로고    scopus 로고
    • Beyond the Qs in the polyglutamine diseases
    • Orr H.T. Beyond the Qs in the polyglutamine diseases. Genes Dev. 15:2001;925-932
    • (2001) Genes Dev. , vol.15 , pp. 925-932
    • Orr, H.T.1
  • 74
    • 0035341212 scopus 로고    scopus 로고
    • Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions
    • Parham S.N., Resende C.G., Tuite M.F. Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J. 20:2001;2111-2119
    • (2001) EMBO J. , vol.20 , pp. 2111-2119
    • Parham, S.N.1    Resende, C.G.2    Tuite, M.F.3
  • 75
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino M.M., Liu J.J., Glover J.R., Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science. 273:1996;622-626
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.J.2    Glover, J.R.3    Lindquist, S.4
  • 76
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P.C., Harris D.A. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273:1998;33107-33110
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 77
  • 78
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and sparagines-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques
    • Perutz M.F., Pope B.J., Owen D., Wanker E.E., Scherzinger E. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and sparagines-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proc. Natl. Acad. Sci. USA. 99:2002;5596-5600
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 80
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science. 216:1982;136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 81
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner S.B. Molecular biology of prion diseases. Science. 252:1991;1515-1522
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 83
    • 0141891211 scopus 로고    scopus 로고
    • Characterization of 2′-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion
    • Rhie A., Kirby L., Sayer N., Wellesley R., Disterer P., Sylvester I., Gill A., Hope J., James W., Tahiri-Alaoui A. Characterization of 2′-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. J. Biol. Chem. 278:2003;39697-39705
    • (2003) J. Biol. Chem. , vol.278 , pp. 39697-39705
    • Rhie, A.1    Kirby, L.2    Sayer, N.3    Wellesley, R.4    Disterer, P.5    Sylvester, I.6    Gill, A.7    Hope, J.8    James, W.9    Tahiri-Alaoui, A.10
  • 84
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Riek R., Hornemann S., Wider G., Glockshuber R., Wuthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett.s. 413:1997;282-288
    • (1997) FEBS Lett.s. , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 85
    • 0141864665 scopus 로고    scopus 로고
    • The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products
    • Ripaud L., Maillet L., Cullin C. The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products. EMBO J. 22:2003;5251-5259
    • (2003) EMBO J. , vol.22 , pp. 5251-5259
    • Ripaud, L.1    Maillet, L.2    Cullin, C.3
  • 87
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio G.P., Permanne B., Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature. 411:2001;810-813
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 88
    • 0033542142 scopus 로고    scopus 로고
    • Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone
    • Saborio G.P., Soto C., Kascsak R.J., Levy E., Kascsak R., Harris D.A., Frangione B. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem. Biophys. Res. Commun. 258:1999;470-475
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 470-475
    • Saborio, G.P.1    Soto, C.2    Kascsak, R.J.3    Levy, E.4    Kascsak, R.5    Harris, D.A.6    Frangione, B.7
  • 89
    • 0242643749 scopus 로고    scopus 로고
    • New anti-prion drugs make yeast blush
    • Saupe S.J. New anti-prion drugs make yeast blush. Trends Biotechnol. 21:2003;516-519
    • (2003) Trends Biotechnol. , vol.21 , pp. 516-519
    • Saupe, S.J.1
  • 90
    • 0034758487 scopus 로고    scopus 로고
    • The role of conformational flexibility in prion propagation and maintenance for Sup35p
    • Scheibel T., Lindquist S.L. The role of conformational flexibility in prion propagation and maintenance for Sup35p. Nat. Struct. Biol. 8:2001;958-962
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 958-962
    • Scheibel, T.1    Lindquist, S.L.2
  • 91
    • 0035814918 scopus 로고    scopus 로고
    • Bidirectional amyloid fiber growth for a yeast prion determinant
    • Scheibel T., Kowal A.S., Bloom J.D., Lindquist S.L. Bidirectional amyloid fiber growth for a yeast prion determinant. Curr. Biol. 11:2001;366-369
    • (2001) Curr. Biol. , vol.11 , pp. 366-369
    • Scheibel, T.1    Kowal, A.S.2    Bloom, J.D.3    Lindquist, S.L.4
  • 92
    • 0031441886 scopus 로고    scopus 로고
    • Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP
    • Schirmer E.C., Lindquist S. Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. Proc. Natl. Acad. Sci. USA. 94:1997;13932-13937
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13932-13937
    • Schirmer, E.C.1    Lindquist, S.2
  • 95
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • Sondheimer N., Lindquist S. Rnq1. an epigenetic modifier of protein function in yeast Mol. Cell. 5:2000;163-172
    • (2000) Mol. Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 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 J.S. Conformational variations in an infectious protein determine prion strain differences. Nature. 428:2004;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 K.L., Cheng N., Williams R.W., Steven A.C., Wickner R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science. 283:1999;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
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling G.C., Scott M., Mastrianni J., Gabizon R., Torchia M., Cohen F.E., DeArmond S.J., Prusiner S.B. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell. 83:1995;79-90
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    Dearmond, S.J.7    Prusiner, S.B.8
  • 104
    • 0034603218 scopus 로고    scopus 로고
    • Yeast prions and their prion-forming domain
    • Tuite M.F. Yeast prions and their prion-forming domain. Cell. 100:2000;289-292
    • (2000) Cell , vol.100 , pp. 289-292
    • Tuite, M.F.1
  • 106
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain S.M., Lindquist S. Prions as protein-based genetic elements. Annu. Rev. Microbiol. 56:2002;703-741
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 109
    • 0032923522 scopus 로고    scopus 로고
    • Molecular genetics of transmissible spongiform encephalopathies
    • Weissmann C. Molecular genetics of transmissible spongiform encephalopathies. J. Biol. Chem. 274:1999;3-6
    • (1999) J. Biol. Chem. , vol.274 , pp. 3-6
    • Weissmann, C.1
  • 110
    • 0001489266 scopus 로고    scopus 로고
    • Knockouts, transgenics and transplants in prion research
    • S.B. Prusiner, ed. (New York, Cold Spring Harbor Laboratory Press)
    • Weissmann, C., Raeber, A.J., Shmerling, D., Aguzzi, A., and Manson, J.C. (1999). Knockouts, transgenics and transplants in prion research. In Prion Biology and Diseases, S.B. Prusiner, ed. (New York, Cold Spring Harbor Laboratory Press), pp. 273-305.
    • (1999) Prion Biology and Diseases , pp. 273-305
    • Weissmann, C.1    Raeber, A.J.2    Shmerling, D.3    Aguzzi, A.4    Manson, J.C.5
  • 111
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner R.B. [URE3] as an altered URE2 protein. evidence for a prion analog in Saccharomyces cerevisiae Science. 264:1994;566-569
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 112
    • 0036366021 scopus 로고    scopus 로고
    • Prions of yeast as epigenetic phenomena: High protein "copy number" inducing protein "silencing
    • Wickner R.B., Edskes H.K., Roberts B.T., Pierce M., Baxa U. Prions of yeast as epigenetic phenomena. high protein "copy number" inducing protein "silencing Adv. Genet. 46:2002;485-525
    • (2002) Adv. Genet. , vol.46 , pp. 485-525
    • Wickner, R.B.1    Edskes, H.K.2    Roberts, B.T.3    Pierce, M.4    Baxa, U.5
  • 114
    • 2542434845 scopus 로고    scopus 로고
    • Calpain-dependent endoproteolytic cleavage of PrPSc modulates scrapie prion propagation
    • in press
    • Yadavalli R., Guttmann R.P., Seward T., A.P C., Williamson R.A., Telling G.C. Calpain-dependent endoproteolytic cleavage of PrPSc modulates scrapie prion propagation. J. Biol. Chem. 279:2004;. in press
    • (2004) J. Biol. Chem. , vol.279
    • Yadavalli, R.1    Guttmann, R.P.2    Seward, T.3    Williamson, R.A.4    Telling, G.C.5
  • 115
    • 1642340527 scopus 로고    scopus 로고
    • Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation
    • Yamanaka K., Okubo Y., Suzaki T., Ogura T. Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation. J. Struct. Biol. 146:2004;242-250
    • (2004) J. Struct. Biol. , vol.146 , pp. 242-250
    • Yamanaka, K.1    Okubo, Y.2    Suzaki, T.3    Ogura, T.4


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