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Volumn 10, Issue 5, 2014, Pages

Extensive Diversity of Prion Strains Is Defined by Differential Chaperone Interactions and Distinct Amyloidogenic Regions

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; CHAPERONE; PROTEIN VARIANT; RNQ1 VIRUS PROTEIN; SIS1 PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; AMYLOID; PRION;

EID: 84901599537     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004337     Document Type: Article
Times cited : (33)

References (104)
  • 1
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ, (2003) Folding proteins in fatal ways. Nature 426: 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 2
    • 71549169557 scopus 로고    scopus 로고
    • Neurodegeneration. Could they all be prion diseases?
    • Miller G, (2009) Neurodegeneration. Could they all be prion diseases? Science 326: 1337-1339.
    • (2009) Science , vol.326 , pp. 1337-1339
    • Miller, G.1
  • 3
    • 84861559058 scopus 로고    scopus 로고
    • Transmissible Proteins: Expanding the Prion Heresy
    • Soto C, (2012) Transmissible Proteins: Expanding the Prion Heresy. Cell 149: 968-977.
    • (2012) Cell , vol.149 , pp. 968-977
    • Soto, C.1
  • 5
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, et al. (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90: 10962-10966.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5
  • 6
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447: 453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3    Ivanova, M.I.4    Sievers, S.A.5
  • 8
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau W-M, Mattson MP, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307: 262-265.
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5
  • 9
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge J, Clarke AR, (2007) A general model of prion strains and their pathogenicity. Science 318: 930-936.
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 10
    • 84879895467 scopus 로고    scopus 로고
    • Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons
    • Guo JL, Covell DJ, Daniels JP, Iba M, Stieber A, et al. (2013) Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons. Cell 154: 103-117.
    • (2013) Cell , vol.154 , pp. 103-117
    • Guo, J.L.1    Covell, D.J.2    Daniels, J.P.3    Iba, M.4    Stieber, A.5
  • 11
    • 84861747139 scopus 로고    scopus 로고
    • Molecular pathogenesis of sporadic prion diseases in man
    • Safar JG, (2012) Molecular pathogenesis of sporadic prion diseases in man. Prion 6: 108-115.
    • (2012) Prion , vol.6 , pp. 108-115
    • Safar, J.G.1
  • 13
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino MM, Liu JJ, Glover JR, Lindquist S, (1996) Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273: 622-626.
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.J.2    Glover, J.R.3    Lindquist, S.4
  • 14
    • 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
  • 18
    • 80053442711 scopus 로고    scopus 로고
    • Inter-Allelic Prion Propagation Reveals Conformational Relationships among a Multitude of [PSI] Strains
    • Lin J-Y, Liao T-Y, Lee H-C, King C-Y, (2011) Inter-Allelic Prion Propagation Reveals Conformational Relationships among a Multitude of [PSI] Strains. PLoS Genet 7: e1002297.
    • (2011) PLoS Genet , vol.7
    • Lin, J.-Y.1    Liao, T.-Y.2    Lee, H.-C.3    King, C.-Y.4
  • 19
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS, (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428: 323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 20
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • Tanaka M, Collins SR, Toyama BH, Weissman JS, (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442: 585-589.
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 21
  • 22
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan R, Lindquist SL, (2005) Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435: 765-772.
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 23
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King C-Y, Diaz-Avalos R, (2004) Protein-only transmission of three yeast prion strains. Nature 428: 319-323.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.-Y.1    Diaz-Avalos, R.2
  • 24
    • 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
  • 25
    • 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
  • 26
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King OD, Gitler AD, Shorter J, (2012) The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain research 1462: 61-80.
    • (2012) Brain Research , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 27
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S, (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137: 146-158.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 28
    • 1642524541 scopus 로고    scopus 로고
    • The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions
    • Bradley ME, Liebman SW, (2004) The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions. Mol Microbiol 51: 1649-1659.
    • (2004) Mol Microbiol , vol.51 , pp. 1649-1659
    • Bradley, M.E.1    Liebman, S.W.2
  • 29
    • 1542782213 scopus 로고    scopus 로고
    • Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
    • Kryndushkin DS, Alexandrov IM, Ter-Avanesyan MD, Kushnirov VV, (2003) Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 278: 49636-49643.
    • (2003) J Biol Chem , vol.278 , pp. 49636-49643
    • Kryndushkin, D.S.1    Alexandrov, I.M.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 31
    • 34447639732 scopus 로고    scopus 로고
    • Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes
    • Legname G, Nguyen H-OB, Peretz D, Cohen FE, DeArmond SJ, et al. (2006) Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci USA 103: 19105-19110.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 19105-19110
    • Legname, G.1    Nguyen, H.-O.B.2    Peretz, D.3    Cohen, F.E.4    DeArmond, S.J.5
  • 33
    • 84886439402 scopus 로고    scopus 로고
    • Spontaneous Variants of the [RNQ+] Prion in Yeast Demonstrate the Extensive Conformational Diversity Possible with Prion Proteins
    • Huang VJ, Stein KC, True HL, (2013) Spontaneous Variants of the [RNQ+] Prion in Yeast Demonstrate the Extensive Conformational Diversity Possible with Prion Proteins. PLoS ONE 8: e79582.
    • (2013) PLoS ONE , vol.8
    • Huang, V.J.1    Stein, K.C.2    True, H.L.3
  • 34
    • 77954223665 scopus 로고    scopus 로고
    • Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation
    • Kalastavadi T, True HL, (2010) Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation. J Biol Chem 285: 20748-20755.
    • (2010) J Biol Chem , vol.285 , pp. 20748-20755
    • Kalastavadi, T.1    True, H.L.2
  • 35
    • 0035086136 scopus 로고    scopus 로고
    • Strain-specified relative conformational stability of the scrapie prion protein
    • Peretz D, Scott MR, Groth D, Williamson RA, Burton DR, et al. (2001) Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci 10: 854-863.
    • (2001) Protein Sci , vol.10 , pp. 854-863
    • Peretz, D.1    Scott, M.R.2    Groth, D.3    Williamson, R.A.4    Burton, D.R.5
  • 36
    • 79953286302 scopus 로고    scopus 로고
    • The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease
    • Ayers JI, Schutt CR, Shikiya RA, Aguzzi A, Kincaid AE, et al. (2011) The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease. PLoS Pathog 7: e1001317.
    • (2011) PLoS Pathog , vol.7
    • Ayers, J.I.1    Schutt, C.R.2    Shikiya, R.A.3    Aguzzi, A.4    Kincaid, A.E.5
  • 37
    • 84893499249 scopus 로고    scopus 로고
    • Conformational Stability of Mammalian Prion Protein Amyloid Fibrils Is Dictated by a Packing Polymorphism within the Core Region
    • Cobb NJ, Apostol MI, Chen S, Smirnovas V, Surewicz WK, (2014) Conformational Stability of Mammalian Prion Protein Amyloid Fibrils Is Dictated by a Packing Polymorphism within the Core Region. J Biol Chem 289: 2643-2650.
    • (2014) J Biol Chem , vol.289 , pp. 2643-2650
    • Cobb, N.J.1    Apostol, M.I.2    Chen, S.3    Smirnovas, V.4    Surewicz, W.K.5
  • 38
    • 0034595216 scopus 로고    scopus 로고
    • Dependence and independence of [PSI(+)] and [PIN(+)]: a two-prion system in yeast?
    • Derkatch IL, Bradley ME, Masse SV, Zadorsky SP, Polozkov GV, et al. (2000) Dependence and independence of [PSI(+)] and [PIN(+)]: a two-prion system in yeast? EMBO J 19: 1942-1952.
    • (2000) EMBO J , vol.19 , pp. 1942-1952
    • Derkatch, I.L.1    Bradley, M.E.2    Masse, S.V.3    Zadorsky, S.P.4    Polozkov, G.V.5
  • 39
    • 0030833388 scopus 로고    scopus 로고
    • Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae
    • Derkatch IL, Bradley ME, Zhou P, Chernoff YO, Liebman SW, (1997) Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147: 507-519.
    • (1997) Genetics , vol.147 , pp. 507-519
    • Derkatch, I.L.1    Bradley, M.E.2    Zhou, P.3    Chernoff, Y.O.4    Liebman, S.W.5
  • 40
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: the story of [PIN(+)]
    • Derkatch IL, Bradley ME, Hong JY, Liebman SW, (2001) Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106: 171-182.
    • (2001) Cell , vol.106 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 41
    • 0035958547 scopus 로고    scopus 로고
    • Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion
    • Osherovich LZ, Weissman JS, (2001) Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 106: 183-194.
    • (2001) Cell , vol.106 , pp. 183-194
    • Osherovich, L.Z.1    Weissman, J.S.2
  • 42
    • 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
  • 43
    • 83755178155 scopus 로고    scopus 로고
    • The [RNQ+] prion: a model of both functional and pathological amyloid
    • Stein KC, True HL, (2011) The [RNQ+] prion: a model of both functional and pathological amyloid. Prion 5: 291-298.
    • (2011) Prion , vol.5 , pp. 291-298
    • Stein, K.C.1    True, H.L.2
  • 45
    • 0346100706 scopus 로고    scopus 로고
    • Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants
    • Bradley ME, Liebman SW, (2003) Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants. Genetics 165: 1675-1685.
    • (2003) Genetics , vol.165 , pp. 1675-1685
    • Bradley, M.E.1    Liebman, S.W.2
  • 46
    • 84897108228 scopus 로고    scopus 로고
    • Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities
    • Westergard L, True HL, (2014) Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities. Mol Microbiol 92: 183-193.
    • (2014) Mol Microbiol , vol.92 , pp. 183-193
    • Westergard, L.1    True, H.L.2
  • 47
    • 4444312783 scopus 로고    scopus 로고
    • Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro
    • Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, et al. (2004) Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci USA 101: 12934-12939.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12934-12939
    • Derkatch, I.L.1    Uptain, S.M.2    Outeiro, T.F.3    Krishnan, R.4    Lindquist, S.L.5
  • 48
    • 33847291919 scopus 로고    scopus 로고
    • Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM
    • Vitrenko YA, Gracheva EO, Richmond JE, Liebman SW, (2007) Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM. J Biol Chem 282: 1779-1787.
    • (2007) J Biol Chem , vol.282 , pp. 1779-1787
    • Vitrenko, Y.A.1    Gracheva, E.O.2    Richmond, J.E.3    Liebman, S.W.4
  • 49
    • 64649107312 scopus 로고    scopus 로고
    • Heterologous prion interactions are altered by mutations in the prion protein Rnq1p
    • Bardill JP, True HL, (2009) Heterologous prion interactions are altered by mutations in the prion protein Rnq1p. J Mol Biol 388: 583-596.
    • (2009) J Mol Biol , vol.388 , pp. 583-596
    • Bardill, J.P.1    True, H.L.2
  • 50
    • 34247211144 scopus 로고    scopus 로고
    • Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP
    • 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.
    • (2007) Curr Genet , vol.51 , pp. 309-319
    • Vitrenko, Y.A.1    Pavon, M.E.2    Stone, S.I.3    Liebman, S.W.4
  • 51
    • 10944273371 scopus 로고    scopus 로고
    • Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast
    • Bagriantsev S, Liebman SW, (2004) Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast. J Biol Chem 279: 51042-51048.
    • (2004) J Biol Chem , vol.279 , pp. 51042-51048
    • Bagriantsev, S.1    Liebman, S.W.2
  • 52
    • 84881661468 scopus 로고    scopus 로고
    • Exploring the Basis of [PIN+] Variant Differences in [PSI+] Induction
    • Sharma J, Liebman SW, (2013) Exploring the Basis of [PIN+] Variant Differences in [PSI+] Induction. J Mol Biol 425: 3046-3059.
    • (2013) J Mol Biol , vol.425 , pp. 3046-3059
    • Sharma, J.1    Liebman, S.W.2
  • 53
    • 55949109442 scopus 로고    scopus 로고
    • In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
    • Tipton KA, Verges KJ, Weissman JS, (2008) In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. Mol Cell 32: 584-591.
    • (2008) Mol Cell , vol.32 , pp. 584-591
    • Tipton, K.A.1    Verges, K.J.2    Weissman, J.S.3
  • 54
    • 0035873740 scopus 로고    scopus 로고
    • The role of Sis1 in the maintenance of the [RNQ+] prion
    • Sondheimer N, Lopez N, Craig EA, Lindquist S, (2001) The role of Sis1 in the maintenance of the [RNQ+] prion. EMBO J 20: 2435-2442.
    • (2001) EMBO J , vol.20 , pp. 2435-2442
    • Sondheimer, N.1    Lopez, N.2    Craig, E.A.3    Lindquist, S.4
  • 55
    • 34548101963 scopus 로고    scopus 로고
    • J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation
    • Aron R, Higurashi T, Sahi C, Craig EA, (2007) J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. EMBO J 26: 3794-3803.
    • (2007) EMBO J , vol.26 , pp. 3794-3803
    • Aron, R.1    Higurashi, T.2    Sahi, C.3    Craig, E.A.4
  • 56
    • 48749104090 scopus 로고    scopus 로고
    • Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition
    • Bagriantsev SN, Gracheva EO, Richmond JE, Liebman SW, (2008) Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. Mol Biol Cell 19: 2433-2443.
    • (2008) Mol Biol Cell , vol.19 , pp. 2433-2443
    • Bagriantsev, S.N.1    Gracheva, E.O.2    Richmond, J.E.3    Liebman, S.W.4
  • 57
    • 0034160086 scopus 로고    scopus 로고
    • Protein-only inheritance in yeast: something to get [PSI+]-ched about
    • Serio TR, Lindquist SL, (2000) Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends Cell Biol 10: 98-105.
    • (2000) Trends Cell Biol , vol.10 , pp. 98-105
    • Serio, T.R.1    Lindquist, S.L.2
  • 58
    • 0035890264 scopus 로고    scopus 로고
    • Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion
    • Uptain SM, Sawicki GJ, Caughey B, Lindquist S, (2001) Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion. EMBO J 20: 6236-6245.
    • (2001) EMBO J , vol.20 , pp. 6236-6245
    • Uptain, S.M.1    Sawicki, G.J.2    Caughey, B.3    Lindquist, S.4
  • 59
    • 0028840417 scopus 로고
    • The end in sight: terminating translation in eukaryotes
    • Stansfield I, Jones KM, Tuite MF, (1995) The end in sight: terminating translation in eukaryotes. Trends Biochem Sci 20: 489-491.
    • (1995) Trends Biochem Sci , vol.20 , pp. 489-491
    • Stansfield, I.1    Jones, K.M.2    Tuite, M.F.3
  • 60
    • 83755195619 scopus 로고    scopus 로고
    • Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies
    • Kabani M, Melki R, (2011) Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies. Prion 5: 277-284.
    • (2011) Prion , vol.5 , pp. 277-284
    • Kabani, M.1    Melki, R.2
  • 61
    • 85046915495 scopus 로고    scopus 로고
    • Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 in Saccharomyces cerevisiae
    • Shibata S, Kurahashi H, Nakamura Y, (2009) Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 in Saccharomyces cerevisiae. Prion 3: 250-258.
    • (2009) Prion , vol.3 , pp. 250-258
    • Shibata, S.1    Kurahashi, H.2    Nakamura, Y.3
  • 62
    • 79955083629 scopus 로고    scopus 로고
    • [PSI(+)] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast
    • Kurahashi H, Pack C-G, Shibata S, Oishi K, Sako Y, et al. (2011) [PSI(+)] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast. Genes Cells 16: 576-589.
    • (2011) Genes Cells , vol.16 , pp. 576-589
    • Kurahashi, H.1    Pack, C.-G.2    Shibata, S.3    Oishi, K.4    Sako, Y.5
  • 63
    • 33745616512 scopus 로고    scopus 로고
    • Biochemical and genetic methods for characterization of [PIN+] prions in yeast
    • Liebman SW, Bagriantsev SN, Derkatch IL, (2006) Biochemical and genetic methods for characterization of [PIN+] prions in yeast. METHODS 39: 23-34.
    • (2006) METHODS , vol.39 , pp. 23-34
    • Liebman, S.W.1    Bagriantsev, S.N.2    Derkatch, I.L.3
  • 64
    • 77649265357 scopus 로고    scopus 로고
    • Exploring the sequence determinants of amyloid structure using position-specific scoring matrices
    • Maurer-Stroh S, Debulpaep M, Kuemmerer N, López de la Paz M, Martins IC, et al. (2010) Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nat Chem Biol 7: 237-242.
    • (2010) Nat Chem Biol , vol.7 , pp. 237-242
    • Maurer-Stroh, S.1    Debulpaep, M.2    Kuemmerer, N.3    López de la Paz, M.4    Martins, I.C.5
  • 65
    • 45749102914 scopus 로고    scopus 로고
    • The Zyggregator method for predicting protein aggregation propensities
    • Tartaglia GG, Vendruscolo M, (2008) The Zyggregator method for predicting protein aggregation propensities. Chem Soc Rev 37: 1395-1401.
    • (2008) Chem Soc Rev , vol.37 , pp. 1395-1401
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 66
    • 33845978790 scopus 로고    scopus 로고
    • Insight into the structure of amyloid fibrils from the analysis of globular proteins
    • Trovato A, Chiti F, Maritan A, Seno F, (2006) Insight into the structure of amyloid fibrils from the analysis of globular proteins. PLoS Comput Biol 2: e170.
    • (2006) PLoS Comput Biol , vol.2
    • Trovato, A.1    Chiti, F.2    Maritan, A.3    Seno, F.4
  • 67
    • 33947517558 scopus 로고    scopus 로고
    • AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
    • Conchillo-Solé O, de Groot NS, Avilés FX, Vendrell J, Daura X, et al. (2007) AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics 8: 65.
    • (2007) BMC Bioinformatics , vol.8 , pp. 65
    • Conchillo-Solé, O.1    de Groot, N.S.2    Avilés, F.X.3    Vendrell, J.4    Daura, X.5
  • 68
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A-M, Rousseau F, Schymkowitz J, Serrano L, (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotech 22: 1302-1306.
    • (2004) Nat Biotech , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 70
    • 76749102953 scopus 로고    scopus 로고
    • Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1
    • Kadnar ML, Articov G, Derkatch IL, (2010) Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1. PLoS Genet 6: e1000824.
    • (2010) PLoS Genet , vol.6
    • Kadnar, M.L.1    Articov, G.2    Derkatch, I.L.3
  • 71
    • 67649852558 scopus 로고    scopus 로고
    • Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins
    • Pechmann S, Levy ED, Tartaglia GG, Vendruscolo M, (2009) Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins. Proc Natl Acad Sci USA 106: 10159-10164.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10159-10164
    • Pechmann, S.1    Levy, E.D.2    Tartaglia, G.G.3    Vendruscolo, M.4
  • 73
    • 70349780021 scopus 로고    scopus 로고
    • Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion
    • Bardill JP, Dulle JE, Fisher JR, True HL, (2009) Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion. Prion 3: 151-160.
    • (2009) Prion , vol.3 , pp. 151-160
    • Bardill, J.P.1    Dulle, J.E.2    Fisher, J.R.3    True, H.L.4
  • 74
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
    • Rüdiger S, Schneider-Mergener J, Bukau B, (2001) Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 20: 1042-1050.
    • (2001) EMBO J , vol.20 , pp. 1042-1050
    • Rüdiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 75
    • 84864661889 scopus 로고    scopus 로고
    • Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome
    • Srinivasan SR, Gillies AT, Chang L, Thompson AD, Gestwicki JE, (2012) Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome. Mol Biosyst 8: 2323.
    • (2012) Mol Biosyst , vol.8 , pp. 2323
    • Srinivasan, S.R.1    Gillies, A.T.2    Chang, L.3    Thompson, A.D.4    Gestwicki, J.E.5
  • 76
    • 70349996473 scopus 로고    scopus 로고
    • ANCHOR: web server for predicting protein binding regions in disordered proteins
    • Dosztányi Z, Mészáros B, Simon I, (2009) ANCHOR: web server for predicting protein binding regions in disordered proteins. Bioinformatics 25: 2745-2746.
    • (2009) Bioinformatics , vol.25 , pp. 2745-2746
    • Dosztányi, Z.1    Mészáros, B.2    Simon, I.3
  • 77
    • 67049119327 scopus 로고    scopus 로고
    • Prediction of protein binding regions in disordered proteins
    • Mészáros B, Simon I, Dosztányi Z, (2009) Prediction of protein binding regions in disordered proteins. PLoS Comput Biol 5: e1000376.
    • (2009) PLoS Comput Biol , vol.5
    • Mészáros, B.1    Simon, I.2    Dosztányi, Z.3
  • 78
    • 79958193848 scopus 로고    scopus 로고
    • Molecular chaperone Hsp104 can promote yeast prion generation
    • Kryndushkin DS, Engel A, Edskes H, Wickner RB, (2011) Molecular chaperone Hsp104 can promote yeast prion generation. Genetics 188: 339-348.
    • (2011) Genetics , vol.188 , pp. 339-348
    • Kryndushkin, D.S.1    Engel, A.2    Edskes, H.3    Wickner, R.B.4
  • 79
    • 77749271373 scopus 로고    scopus 로고
    • The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system
    • Lancaster AK, Bardill JP, True HL, Masel J, (2010) The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system. Genetics 184: 393-400.
    • (2010) Genetics , vol.184 , pp. 393-400
    • Lancaster, A.K.1    Bardill, J.P.2    True, H.L.3    Masel, J.4
  • 80
    • 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
  • 81
    • 17444417025 scopus 로고    scopus 로고
    • Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]
    • Allen KD, Wegrzyn RD, Chernova TA, Müller S, Newnam GP, et al. (2005) Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 169: 1227-1242.
    • (2005) Genetics , vol.169 , pp. 1227-1242
    • Allen, K.D.1    Wegrzyn, R.D.2    Chernova, T.A.3    Müller, S.4    Newnam, G.P.5
  • 82
    • 77952964383 scopus 로고    scopus 로고
    • Prion strain mutation determined by prion protein conformational compatibility and primary structure
    • Angers RC, Kang H-E, Napier D, Browning S, Seward T, et al. (2010) Prion strain mutation determined by prion protein conformational compatibility and primary structure. Science 328: 1154-1158.
    • (2010) Science , vol.328 , pp. 1154-1158
    • Angers, R.C.1    Kang, H.-E.2    Napier, D.3    Browning, S.4    Seward, T.5
  • 83
    • 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. Nat Chem Biol 6: 225-230.
    • (2010) Nat Chem Biol , vol.6 , pp. 225-230
    • Ohhashi, Y.1    Ito, K.2    Toyama, B.H.3    Weissman, J.S.4    Tanaka, M.5
  • 84
    • 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 J-J, 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. , pp. 16446-16453
    • Liu, J.-J.1    Sondheimer, N.2    Lindquist, S.L.3
  • 85
    • 0032974451 scopus 로고    scopus 로고
    • Two prion-inducing regions of Ure2p are nonoverlapping
    • Maddelein ML, Wickner RB, (1999) Two prion-inducing regions of Ure2p are nonoverlapping. Mol Cell Biol 19: 4516-4524.
    • (1999) Mol Cell Biol , vol.19 , pp. 4516-4524
    • Maddelein, M.L.1    Wickner, R.B.2
  • 86
    • 77954616668 scopus 로고    scopus 로고
    • Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences
    • Lakhani VV, Ding F, Dokholyan NV, (2010) Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences. PLoS Comput Biol 6: e1000772.
    • (2010) PLoS Comput Biol , vol.6
    • Lakhani, V.V.1    Ding, F.2    Dokholyan, N.V.3
  • 87
    • 35648936428 scopus 로고    scopus 로고
    • Flanking polyproline sequences inhibit beta-sheet structure in polyglutamine segments by inducing PPII-like helix structure
    • Darnell G, Orgel JPRO, Pahl R, Meredith SC, (2007) Flanking polyproline sequences inhibit beta-sheet structure in polyglutamine segments by inducing PPII-like helix structure. J Mol Biol 374: 688-704.
    • (2007) J Mol Biol , vol.374 , pp. 688-704
    • Darnell, G.1    Orgel, J.P.R.O.2    Pahl, R.3    Meredith, S.C.4
  • 88
    • 0034977531 scopus 로고    scopus 로고
    • Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway
    • Padrick SB, Miranker AD, (2001) Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway. J Mol Biol 308: 783-794.
    • (2001) J Mol Biol , vol.308 , pp. 783-794
    • Padrick, S.B.1    Miranker, A.D.2
  • 90
    • 33847266871 scopus 로고    scopus 로고
    • Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain
    • Krzewska J, Tanaka M, Burston SG, Melki R, (2007) Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain. J Biol Chem 282: 1679-1686.
    • (2007) J Biol Chem , vol.282 , pp. 1679-1686
    • Krzewska, J.1    Tanaka, M.2    Burston, S.G.3    Melki, R.4
  • 91
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
    • Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu JJ, et al. (1997) Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89: 811-819.
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1    Kowal, A.S.2    Schirmer, E.C.3    Patino, M.M.4    Liu, J.J.5
  • 92
    • 78651083450 scopus 로고    scopus 로고
    • In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone
    • Baxa U, Keller PW, Cheng N, Wall JS, Steven AC, (2011) In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone. Mol Microbiol 79: 523-532.
    • (2011) Mol Microbiol , vol.79 , pp. 523-532
    • Baxa, U.1    Keller, P.W.2    Cheng, N.3    Wall, J.S.4    Steven, A.C.5
  • 93
    • 84894486685 scopus 로고    scopus 로고
    • Distinct Prion Strains Are Defined by Amyloid Core Structure and Chaperone Binding Site Dynamics
    • Frederick KK, Debelouchina GT, Kayatekin C, Dorminy T, Jacavone AC, et al. (2014) Distinct Prion Strains Are Defined by Amyloid Core Structure and Chaperone Binding Site Dynamics. Chem Biol 21: 295-305.
    • (2014) Chem Biol , vol.21 , pp. 295-305
    • Frederick, K.K.1    Debelouchina, G.T.2    Kayatekin, C.3    Dorminy, T.4    Jacavone, A.C.5
  • 94
    • 33644817188 scopus 로고    scopus 로고
    • Prion domains: sequences, structures and interactions
    • Ross ED, Minton A, Wickner RB, (2005) Prion domains: sequences, structures and interactions. Nat Cell Biol 7: 1039-1044.
    • (2005) Nat Cell Biol , vol.7 , pp. 1039-1044
    • Ross, E.D.1    Minton, A.2    Wickner, R.B.3
  • 95
    • 79960104526 scopus 로고    scopus 로고
    • [PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain
    • Toombs JA, Liss NM, Cobble KR, Ben-Musa Z, Ross ED, (2011) [PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain. PLoS ONE 6: e21953.
    • (2011) PLoS ONE , vol.6
    • Toombs, J.A.1    Liss, N.M.2    Cobble, K.R.3    Ben-Musa, Z.4    Ross, E.D.5
  • 96
    • 84855274299 scopus 로고    scopus 로고
    • Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104)
    • Helsen CW, Glover JR, (2012) Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104). J Biol Chem 287: 542-556.
    • (2012) J Biol Chem , vol.287 , pp. 542-556
    • Helsen, C.W.1    Glover, J.R.2
  • 98
    • 0035803490 scopus 로고    scopus 로고
    • Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds
    • Borchsenius AS, Wegrzyn RD, Newnam GP, Inge-Vechtomov SG, Chernoff YO, (2001) Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'. EMBO J 20: 6683-6691.
    • (2001) EMBO J , vol.20 , pp. 6683-6691
    • Borchsenius, A.S.1    Wegrzyn, R.D.2    Newnam, G.P.3    Inge-Vechtomov, S.G.4    Chernoff, Y.O.5
  • 100
    • 83755183712 scopus 로고    scopus 로고
    • Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements
    • Hines JK, Higurashi T, Srinivasan M, Craig EA, (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5: 238-244.
    • (2011) Prion , vol.5 , pp. 238-244
    • Hines, J.K.1    Higurashi, T.2    Srinivasan, M.3    Craig, E.A.4
  • 101
    • 84899910555 scopus 로고    scopus 로고
    • Extracellular environment modulates the formation and propagation of particular amyloid structures
    • doi:10.1111/mmi.12579
    • Westergard L, True HL, (2014) Extracellular environment modulates the formation and propagation of particular amyloid structures. Mol Microbiol doi:10.1111/mmi.12579.
    • (2014) Mol Microbiol
    • Westergard, L.1    True, H.L.2
  • 102
    • 84896906645 scopus 로고    scopus 로고
    • Elucidating the role of cofactors in mammalian prion propagation
    • Supattapone S, (2013) Elucidating the role of cofactors in mammalian prion propagation. Prion 8: 102-107.
    • (2013) Prion , vol.8 , pp. 102-107
    • Supattapone, S.1
  • 103
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, et al. (2002) A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 99: 16742-16747.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Balbach, J.J.3    Antzutkin, O.N.4    Leapman, R.D.5
  • 104
    • 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


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