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Volumn 6, Issue 7, 2011, Pages

[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; PRION PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN; UNCLASSIFIED DRUG; HEAT SHOCK PROTEIN; HSP104 PROTEIN, S CEREVISIAE; HYBRID PROTEIN; MUTANT PROTEIN; OLIGOPEPTIDE; SUP35 PROTEIN, S CEREVISIAE; TRANSLATION TERMINATION FACTOR;

EID: 79960104526     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021953     Document Type: Article
Times cited : (30)

References (54)
  • 2
    • 66849099684 scopus 로고    scopus 로고
    • Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]
    • Tessier PM, Lindquist S, (2009) Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]. Nat Struct Mol Biol 16: 598-605.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 598-605
    • Tessier, P.M.1    Lindquist, S.2
  • 3
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner RB, (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264: 566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 4
    • 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
  • 5
    • 0029145925 scopus 로고
    • Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
    • Zhouravleva G, Frolova L, Le Goff X, Le Guellec R, Inge-Vechtomov 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    Le Goff, X.3    Le Guellec, R.4    Inge-Vechtomov, S.5
  • 6
    • 0028200770 scopus 로고
    • The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae
    • Ter-Avanesyan MD, 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
    • Ter-Avanesyan, M.D.1    Dagkesamanskaya, A.R.2    Kushnirov, V.V.3    Smirnov, V.N.4
  • 7
    • 0027513128 scopus 로고
    • Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein
    • Ter-Avanesyan MD, Kushnirov VV, Dagkesamanskaya AR, Didichenko SA, Chernoff YO, et al. (1993) Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol Microbiol 7: 683-692.
    • (1993) Mol Microbiol , vol.7 , pp. 683-692
    • Ter-Avanesyan, M.D.1    Kushnirov, V.V.2    Dagkesamanskaya, A.R.3    Didichenko, S.A.4    Chernoff, Y.O.5
  • 8
    • 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
  • 9
    • 0037059016 scopus 로고    scopus 로고
    • Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]
    • Liu JJ, Sondheimer N, Lindquist SL, (2002) Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc Natl Acad Sci USA 99 (Suppl 4): 16446-16453.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.SUPPL. 4 , pp. 16446-16453
    • Liu, J.J.1    Sondheimer, N.2    Lindquist, S.L.3
  • 11
    • 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: 573-576.
    • (1999) Nature , vol.400 , pp. 573-576
    • Liu, J.J.1    Lindquist, S.2
  • 12
    • 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: 2111-2119.
    • (2001) EMBO J , vol.20 , pp. 2111-2119
    • Parham, S.N.1    Resende, C.G.2    Tuite, M.F.3
  • 13
    • 33644760407 scopus 로고    scopus 로고
    • The role of the N-terminal oligopeptide repeats of the yeast sup35 prion protein in propagation and transmission of prion variants
    • Shkundina IS, Kushnirov VV, Tuite MF, Ter-Avanesyan MD, (2006) The role of the N-terminal oligopeptide repeats of the yeast sup35 prion protein in propagation and transmission of prion variants. Genetics 172: 827-835.
    • (2006) Genetics , vol.172 , pp. 827-835
    • Shkundina, I.S.1    Kushnirov, V.V.2    Tuite, M.F.3    Ter-Avanesyan, M.D.4
  • 14
    • 77249124926 scopus 로고    scopus 로고
    • Differences in prion strain conformations result from non-native interactions in a nucleus
    • Ohhashi Y, Ito K, Toyama BH, Weissman JS, Tanaka M, (2010) Differences in prion strain conformations result from non-native interactions in a nucleus. Nature 6: 225-230.
    • (2010) Nature , vol.6 , pp. 225-230
    • Ohhashi, Y.1    Ito, K.2    Toyama, B.H.3    Weissman, J.S.4    Tanaka, M.5
  • 15
    • 0038714894 scopus 로고    scopus 로고
    • [PHI+], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104
    • Crist CG, Nakayashiki T, Kurahashi H, Nakamura Y, (2003) [PHI+], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104. Genes Cells 8: 603-618.
    • (2003) Genes Cells , vol.8 , pp. 603-618
    • Crist, C.G.1    Nakayashiki, T.2    Kurahashi, H.3    Nakamura, Y.4
  • 16
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW, (1995) Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268: 880-884.
    • (1995) Science , vol.268 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 17
    • 78049408567 scopus 로고    scopus 로고
    • A size threshold limits prion transmission and establishes phenotypic diversity
    • Derdowski A, Sindi SS, Klaips CL, DiSalvo S, Serio TR, (2010) A size threshold limits prion transmission and establishes phenotypic diversity. Science 330: 680-683.
    • (2010) Science , vol.330 , pp. 680-683
    • Derdowski, A.1    Sindi, S.S.2    Klaips, C.L.3    DiSalvo, S.4    Serio, T.R.5
  • 19
    • 0029888121 scopus 로고    scopus 로고
    • Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
    • Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD, (1996) Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 15: 3127-3134.
    • (1996) EMBO J , vol.15 , pp. 3127-3134
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 20
    • 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
  • 21
    • 0034964442 scopus 로고    scopus 로고
    • Yeast [PSI+] "prions" that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state
    • Nakayashiki T, Ebihara K, Bannai H, Nakamura Y, (2001) Yeast [PSI+] "prions" that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol Cell 7: 1121-1130.
    • (2001) Mol Cell , vol.7 , pp. 1121-1130
    • Nakayashiki, T.1    Ebihara, K.2    Bannai, H.3    Nakamura, Y.4
  • 23
    • 0033529861 scopus 로고    scopus 로고
    • Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone
    • Street AG, Mayo SL, (1999) Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone. Proc Natl Acad Sci U S A 96: 9074-9076.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9074-9076
    • Street, A.G.1    Mayo, S.L.2
  • 24
    • 73549115633 scopus 로고    scopus 로고
    • Compositional determinants of prion formation in yeast
    • Toombs JA, McCarty BR, Ross ED, (2010) Compositional determinants of prion formation in yeast. Mol Cell Biol 30: 319-332.
    • (2010) Mol Cell Biol , vol.30 , pp. 319-332
    • Toombs, J.A.1    McCarty, B.R.2    Ross, E.D.3
  • 25
    • 0141849458 scopus 로고    scopus 로고
    • Molecular and clinical classification of human prion disease
    • Wadsworth JD, Hill AF, Beck JA, Collinge J, (2003) Molecular and clinical classification of human prion disease. Br Med Bull 66: 241-254.
    • (2003) Br Med Bull , vol.66 , pp. 241-254
    • Wadsworth, J.D.1    Hill, A.F.2    Beck, J.A.3    Collinge, J.4
  • 27
    • 0033695126 scopus 로고    scopus 로고
    • Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice
    • Flechsig E, Shmerling D, Hegyi I, Raeber AJ, Fischer M, et al. (2000) Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice. Neuron 27: 399-408.
    • (2000) Neuron , vol.27 , pp. 399-408
    • Flechsig, E.1    Shmerling, D.2    Hegyi, I.3    Raeber, A.J.4    Fischer, M.5
  • 28
    • 36348975285 scopus 로고    scopus 로고
    • Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions
    • Dong J, Bloom JD, Goncharov V, Chattopadhyay M, Millhauser GL, et al. (2007) Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions. J Biol Chem 282: 34204-34212.
    • (2007) J Biol Chem , vol.282 , pp. 34204-34212
    • Dong, J.1    Bloom, J.D.2    Goncharov, V.3    Chattopadhyay, M.4    Millhauser, G.L.5
  • 29
    • 34547204037 scopus 로고    scopus 로고
    • Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability
    • Tank EM, Harris DA, Desai AA, True HL, (2007) Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability. Mol Cell Biol 27: 5445-5455.
    • (2007) Mol Cell Biol , vol.27 , pp. 5445-5455
    • Tank, E.M.1    Harris, D.A.2    Desai, A.A.3    True, H.L.4
  • 30
    • 41549105426 scopus 로고    scopus 로고
    • Prion protein insertional mutations increase aggregation propensity but not fiber stability
    • Kalastavadi T, True HL, (2008) Prion protein insertional mutations increase aggregation propensity but not fiber stability. BMC Biochem 9: 7.
    • (2008) BMC Biochem , vol.9 , pp. 7
    • Kalastavadi, T.1    True, H.L.2
  • 31
    • 34247211144 scopus 로고    scopus 로고
    • Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP
    • Epub 2007 Apr 2006
    • Vitrenko YA, Pavon ME, Stone SI, Liebman SW, (2007) Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP. Curr Genet 51: 309-319. Epub 2007 Apr 2006.
    • (2007) Curr Genet , vol.51 , pp. 309-319
    • Vitrenko, Y.A.1    Pavon, M.E.2    Stone, S.I.3    Liebman, S.W.4
  • 32
    • 60549101873 scopus 로고    scopus 로고
    • A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen
    • Nemecek J, Nakayashiki T, Wickner RB, (2009) A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. Proc Natl Acad Sci U S A 106: 1892-1896.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 1892-1896
    • Nemecek, J.1    Nakayashiki, T.2    Wickner, R.B.3
  • 33
    • 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: 163-172.
    • (2000) Mol Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 35
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter J, Lindquist S, (2004) Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304: 1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 37
    • 3543033720 scopus 로고
    • PSI, a cytoplasmic suppressor of super-suppressor in yeast
    • Cox BS, (1965) PSI, a cytoplasmic suppressor of super-suppressor in yeast. Heredity 26: 211-232.
    • (1965) Heredity , vol.26 , pp. 211-232
    • Cox, B.S.1
  • 38
    • 0019604156 scopus 로고
    • Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae
    • Tuite MF, Mundy CR, Cox BS, (1981) Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. Genetics 98: 691-711.
    • (1981) Genetics , vol.98 , pp. 691-711
    • Tuite, M.F.1    Mundy, C.R.2    Cox, B.S.3
  • 39
    • 0034932879 scopus 로고    scopus 로고
    • The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation
    • Ferreira PC, Ness F, Edwards SR, Cox BS, Tuite MF, (2001) The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol Microbiol 40: 1357-1369.
    • (2001) Mol Microbiol , vol.40 , pp. 1357-1369
    • Ferreira, P.C.1    Ness, F.2    Edwards, S.R.3    Cox, B.S.4    Tuite, M.F.5
  • 40
    • 0034974996 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions
    • Jung G, Masison DC, (2001) Guanidine hydrochloride inhibits Hsp104 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
  • 41
    • 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
  • 42
    • 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
  • 43
    • 28044457195 scopus 로고    scopus 로고
    • The amyloid stretch hypothesis: Recruiting proteins toward the dark side
    • Esteras-Chopo A, Serrano L, de la Paz ML, (2005) The amyloid stretch hypothesis: Recruiting proteins toward the dark side. Proc Natl Acad Sci USA 102: 16672-16677.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16672-16677
    • Esteras-Chopo, A.1    Serrano, L.2    de la Paz, M.L.3
  • 44
    • 77955629284 scopus 로고    scopus 로고
    • The effects of amino acid composition on yeast prion formation and prion domain interactions
    • Ross ED, Toombs JA, (2010) The effects of amino acid composition on yeast prion formation and prion domain interactions. Prion 4: 60-65.
    • (2010) Prion , vol.4 , pp. 60-65
    • Ross, E.D.1    Toombs, J.A.2
  • 45
    • 0037168446 scopus 로고    scopus 로고
    • Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance
    • Antzutkin ON, Leapman RD, Balbach JJ, Tycko R, (2002) Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 41: 15436-15450.
    • (2002) Biochemistry , vol.41 , pp. 15436-15450
    • Antzutkin, O.N.1    Leapman, R.D.2    Balbach, J.J.3    Tycko, R.4
  • 46
    • 33846218303 scopus 로고    scopus 로고
    • Identification of an amyloidogenic region on keratoepithelin via synthetic peptides
    • Yuan C, Berscheit HL, Huang AJW, (2007) Identification of an amyloidogenic region on keratoepithelin via synthetic peptides. FEBS Letters 581: 241-247.
    • (2007) FEBS Letters , vol.581 , pp. 241-247
    • Yuan, C.1    Berscheit, H.L.2    Huang, A.J.W.3
  • 47
    • 47249095058 scopus 로고    scopus 로고
    • Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentation
    • Alexandrov IM, Vishnevskaya AB, Ter-Avanesyan MD, Kushnirov VV, (2008) Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentation. J Biol Chem 283: 15185-15192.
    • (2008) J Biol Chem , vol.283 , pp. 15185-15192
    • Alexandrov, I.M.1    Vishnevskaya, A.B.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 49
    • 37349102454 scopus 로고    scopus 로고
    • Hsp104: a weapon to combat diverse neurodegenerative disorders
    • Epub 2007 Dec 2005
    • Shorter J, (2008) Hsp104: a weapon to combat diverse neurodegenerative disorders. Neurosignals 16: 63-74. Epub 2007 Dec 2005.
    • (2008) Neurosignals , vol.16 , pp. 63-74
    • Shorter, J.1
  • 50
    • 0026650443 scopus 로고
    • Inherited prion disease with 144 base pair gene insertion. 2. Clinical and pathological features
    • Collinge J, Brown J, Hardy J, Mullan M, Rossor MN, et al. (1992) Inherited prion disease with 144 base pair gene insertion. 2. Clinical and pathological features. Brain 115: 687-710.
    • (1992) Brain , vol.115 , pp. 687-710
    • Collinge, J.1    Brown, J.2    Hardy, J.3    Mullan, M.4    Rossor, M.N.5
  • 51
    • 0026636605 scopus 로고
    • Inherited prion disease with 144 base pair gene insertion. 1. Genealogical and molecular studies
    • Poulter M, Baker HF, Frith CD, Leach M, Lofthouse R, et al. (1992) Inherited prion disease with 144 base pair gene insertion. 1. Genealogical and molecular studies. Brain 115: 675-685.
    • (1992) Brain , vol.115 , pp. 675-685
    • Poulter, M.1    Baker, H.F.2    Frith, C.D.3    Leach, M.4    Lofthouse, R.5
  • 52
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman F, (1991) Getting started with yeast. Methods Enzymol 194: 3-21.
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 53
    • 13844313010 scopus 로고    scopus 로고
    • Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication
    • Song Y, Wu YX, Jung G, Tutar Y, Eisenberg E, et al. (2005) Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication. Eukaryot Cell 4: 289-297.
    • (2005) Eukaryot Cell , vol.4 , pp. 289-297
    • Song, Y.1    Wu, Y.X.2    Jung, G.3    Tutar, Y.4    Eisenberg, E.5
  • 54
    • 72449146732 scopus 로고    scopus 로고
    • A promiscuous prion: Efficient induction of [URE3] prion formation by heterologous prion domains
    • Ross CD, McCarty BM, Hamilton M, Ben-Hur A, Ross ED, (2009) A promiscuous prion: Efficient induction of [URE3] prion formation by heterologous prion domains. Genetics 183: 929-940.
    • (2009) Genetics , vol.183 , pp. 929-940
    • Ross, C.D.1    McCarty, B.M.2    Hamilton, M.3    Ben-Hur, A.4    Ross, E.D.5


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