메뉴 건너뛰기




Volumn 6, Issue 3, 2012, Pages 191-200

Patterns of [PSI+] aggregation allow insights into cellular organization of yeast prion aggregates

Author keywords

PSI+ ; Aggregate organization; Hsp104; IPOD (insoluble protein deposit); Mature prion; Prion fiber severing; Prion induction; Propagon

Indexed keywords

ACTIN; AMYLOID; MONOMER; PROTEIN;

EID: 84863665504     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.18986     Document Type: Review
Times cited : (9)

References (134)
  • 1
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • PMID:7909170
    • Wickner RB. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 1994; 264:566-9; PMID:7909170; http:// dx.doi.org/10.1126/science.7909170.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 2
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • PMID:6801762
    • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136-44; PMID:6801762; http://dx.doi.org/10.1126/science. 6801762.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 3
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • PMID:19345193
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146-58; PMID:19345193; http://dx.doi. org/10.1016/j.cell.2009.02. 044.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 4
    • 77249122579 scopus 로고    scopus 로고
    • Prions, protein homeostasis and phenotypic diversity
    • PMID:20071174
    • Halfmann R, Alberti S, Lindquist S. Prions, protein homeostasis and phenotypic diversity. Trends Cell Biol 2010; 20:125-33; PMID:20071174; http://dx.doi. org/10.1016/j.tcb.2009.12.003.
    • (2010) Trends Cell Biol , vol.20 , pp. 125-133
    • Halfmann, R.1    Alberti, S.2    Lindquist, S.3
  • 5
    • 78649417132 scopus 로고    scopus 로고
    • The prion hypothesis: From biological anomaly to basic regulatory mechanism
    • PMID:21081963
    • Tuite MF, Serio TR. The prion hypothesis: from biological anomaly to basic regulatory mechanism. Nat Rev Mol Cell Biol 2010; 11:823-33; PMID:21081963; http://dx.doi.org/10.1038/nrm3007.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 823-833
    • Tuite, M.F.1    Serio, T.R.2
  • 6
    • 80053569315 scopus 로고    scopus 로고
    • Newly identified prions in budding yeast, and their possible functions
    • PMID:21397710
    • Crow ET, Li L. Newly identified prions in budding yeast, and their possible functions. Semin Cell Dev Biol 2011; 22:452-9; PMID:21397710; http://dx.doi. org/10.1016/j.semcdb.2011.03.003.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 452-459
    • Crow, E.T.1    Li, L.2
  • 8
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • PMID:11028992
    • True HL, Lindquist SL. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 2000; 407:477-83; PMID:11028992; http:// dx.doi.org/10.1038/35035005.
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 9
    • 4544235083 scopus 로고    scopus 로고
    • Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits
    • PMID:15311209
    • True HL, Berlin I, Lindquist SL. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 2004; 431:184- 7; PMID:15311209; http://dx.doi.org/10.1038/ nature02885.
    • (2004) Nature , vol.431 , pp. 184-187
    • True, H.L.1    Berlin, I.2    Lindquist, S.L.3
  • 11
    • 33947390044 scopus 로고    scopus 로고
    • Evolution of budding yeast prion-determinant sequences across diverse fungi
    • PMID:17320905
    • Harrison LB, Yu Z, Stajich JE, Dietrich FS, Harrison PM. Evolution of budding yeast prion-determinant sequences across diverse fungi. J Mol Biol 2007; 368:273-82; PMID:17320905; http://dx.doi. org/10.1016/j.jmb.2007.01.070.
    • (2007) J Mol Biol , vol.368 , pp. 273-282
    • Harrison, L.B.1    Yu, Z.2    Stajich, J.E.3    Dietrich, F.S.4    Harrison, P.M.5
  • 12
    • 0019604156 scopus 로고
    • Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae
    • PMID:7037537
    • Tuite MF, Mundy CR, Cox BS. Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. Genetics 1981; 98:691-711; PMID:7037537.
    • (1981) Genetics , vol.98 , pp. 691-711
    • Tuite, M.F.1    Mundy, C.R.2    Cox, B.S.3
  • 13
    • 0033118934 scopus 로고    scopus 로고
    • Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
    • PMID:10202160
    • Eaglestone SS, Cox BS, Tuite MF. Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J 1999; 18:1974- 81; PMID:10202160; http://dx.doi.org/10.1093/ emboj/18.7.1974.
    • (1999) EMBO J , vol.18 , pp. 1974-1981
    • Eaglestone, S.S.1    Cox, B.S.2    Tuite, M.F.3
  • 14
    • 56849099636 scopus 로고    scopus 로고
    • Prion switching in response to environmental stress
    • PMID:19067491
    • Tyedmers J, Madariaga ML, Lindquist S. Prion switching in response to environmental stress. PLoS Biol 2008; 6:294; PMID:19067491; http://dx.doi. org/10.1371/journal.pbio.0060294.
    • (2008) PLoS Biol , vol.6 , pp. 294
    • Tyedmers, J.1    Madariaga, M.L.2    Lindquist, S.3
  • 18
    • 78049361927 scopus 로고    scopus 로고
    • Epigenetics in the extreme: Prions and the inheritance of environmentally acquired traits
    • PMID:21030648
    • Halfmann R, Lindquist S. Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits. Science 2010; 330:629-32; PMID:21030648; http://dx.doi.org/10.1126/science.1191081.
    • (2010) Science , vol.330 , pp. 629-632
    • Halfmann, R.1    Lindquist, S.2
  • 19
    • 43249090675 scopus 로고    scopus 로고
    • Prion-prion interactions
    • PMID:19164893
    • Derkatch IL, Liebman SW. Prion-prion interactions. Prion 2007; 1:161-9; PMID:19164893; http://dx.doi. org/10.4161/pri.1.3.4837.
    • (2007) Prion , vol.1 , pp. 161-169
    • Derkatch, I.L.1    Liebman, S.W.2
  • 20
    • 80054752823 scopus 로고    scopus 로고
    • Fungal prions: Structure, function and propagation
    • PMID:21717344
    • Tuite MF, Marchante R, Kushnirov V. Fungal prions: structure, function and propagation. Top Curr Chem 2011; 305:257-98; PMID:21717344; http://dx.doi. org/10.1007/128-2011-172.
    • (2011) Top Curr Chem , vol.305 , pp. 257-298
    • Tuite, M.F.1    Marchante, R.2    Kushnirov, V.3
  • 23
    • 0034808029 scopus 로고    scopus 로고
    • Induction of distinct [URE3] yeast prion strains
    • PMID:11564886
    • Schlumpberger M, Prusiner SB, Herskowitz I. Induction of distinct [URE3] yeast prion strains. Mol Cell Biol 2001; 21:7035-46; PMID:11564886; http:// dx.doi.org/10.1128/MCB.21.20.7035-46.2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 7035-7046
    • Schlumpberger, M.1    Prusiner, S.B.2    Herskowitz, I.3
  • 25
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • PMID:15029195
    • King CY, Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 2004; 428:319- 23; PMID:15029195; http://dx.doi.org/10.1038/ nature02391.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 26
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • PMID:15029196
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. Conformational variations in an infectious protein determine prion strain differences. Nature 2004; 428:323-8; PMID:15029196; http://dx.doi. org/10.1038/nature02392.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 27
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • PMID:15944694
    • Krishnan R, Lindquist SL. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 2005; 435:765-72; PMID:15944694; http:// dx.doi.org/10.1038/nature03679.
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 28
    • 77954223665 scopus 로고    scopus 로고
    • +] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation
    • PMID:20442412
    • +] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation. J Biol Chem 2010; 285:20748-55; PMID:20442412; http://dx.doi. org/10.1074/jbc.M110.115303.
    • (2010) J Biol Chem , vol.285 , pp. 20748-20755
    • Kalastavadi, T.1    True, H.L.2
  • 29
    • 0035890264 scopus 로고    scopus 로고
    • Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion
    • PMID:11707395
    • Uptain SM, Sawicki GJ, Caughey B, Lindquist S. Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion. EMBO J 2001; 20:6236-45; PMID:11707395; http://dx.doi. org/10.1093/emboj/20.22. 6236.
    • (2001) EMBO J , vol.20 , pp. 6236-6245
    • Uptain, S.M.1    Sawicki, G.J.2    Caughey, B.3    Lindquist, S.4
  • 30
    • 22544450457 scopus 로고    scopus 로고
    • Strain-specific morphologies of yeast prion amyloid fibrils
    • PMID:16006506
    • Diaz-Avalos R, King CY, Wall J, Simon M, Caspar DL. Strain-specific morphologies of yeast prion amyloid fibrils. Proc Natl Acad Sci USA 2005; 102:10165- 70; PMID:16006506; http://dx.doi.org/10.1073/ pnas.0504599102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10165-10170
    • Diaz-Avalos, R.1    King, C.Y.2    Wall, J.3    Simon, M.4    Caspar, D.L.5
  • 31
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • PMID:16810177
    • Tanaka M, Collins SR, Toyama BH, Weissman JS. The physical basis of how prion conformations determine strain phenotypes. Nature 2006; 442:585-9; PMID:16810177; http://dx.doi.org/10.1038/ nature04922.
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 32
    • 0141455115 scopus 로고    scopus 로고
    • +] prion in yeast
    • PMID:14504215
    • +] prion in yeast. Genetics 2003; 165:23-33; PMID:14504215.
    • (2003) Genetics , vol.165 , pp. 23-33
    • Cox, B.1    Ness, F.2    Tuite, M.3
  • 33
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • PMID:15931169
    • Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 2005; 6:435- 50; PMID:15931169; http://dx.doi.org/10. 1038/ nrg1616.
    • (2005) Nat Rev Genet , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 34
    • 0036277603 scopus 로고    scopus 로고
    • Analysis of prion factors in yeast
    • PMID:12073366
    • Chernoff YO, Uptain SM, Lindquist SL. Analysis of prion factors in yeast. Methods Enzymol 2002; 351:499-538; PMID:12073366; http://dx.doi. org/10.1016/S0076-6879(02)51867-X.
    • (2002) Methods Enzymol , vol.351 , pp. 499-538
    • Chernoff, Y.O.1    Uptain, S.M.2    Lindquist, S.L.3
  • 35
    • 0242636317 scopus 로고    scopus 로고
    • Propagation of yeast prions
    • PMID:14625537
    • Tuite MF, Cox BS. Propagation of yeast prions. Nat Rev Mol Cell Biol 2003; 4:878-90; PMID:14625537; http://dx.doi.org/10.1038/nrm1247.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 878-890
    • Tuite, M.F.1    Cox, B.S.2
  • 36
    • 34447530804 scopus 로고    scopus 로고
    • Prions of fungi: Inherited structures and biological roles
    • PMID:17632572
    • Wickner RB, Edskes HK, Shewmaker F, Nakayashiki T. Prions of fungi: inherited structures and biological roles. Nat Rev Microbiol 2007; 5:611-8; PMID:17632572; http://dx.doi.org/10.1038/nrmicro1708.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 611-618
    • Wickner, R.B.1    Edskes, H.K.2    Shewmaker, F.3    Nakayashiki, T.4
  • 37
    • 77956041261 scopus 로고    scopus 로고
    • Biochemical, cell biological and genetic assays to analyze amyloid and prion aggregation in yeast
    • PMID:20946833
    • Alberti S, Halfmann R, Lindquist S. Biochemical, cell biological and genetic assays to analyze amyloid and prion aggregation in yeast. Methods Enzymol 2010; 470:709-34; PMID:20946833; http://dx.doi. org/10.1016/S0076- 6879(10)70030-6.
    • (2010) Methods Enzymol , vol.470 , pp. 709-734
    • Alberti, S.1    Halfmann, R.2    Lindquist, S.3
  • 38
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • PMID:8662547
    • Patino MM, Liu JJ, Glover JR, Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 1996; 273:622-6; PMID:8662547; http://dx.doi.org/10.1126/science. 273.5275.622.
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.J.2    Glover, J.R.3    Lindquist, S.4
  • 39
    • 0029888121 scopus 로고    scopus 로고
    • +] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
    • PMID:8670813
    • +] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 1996; 15:3127-34; PMID:8670813.
    • (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
  • 40
    • 0033574042 scopus 로고    scopus 로고
    • The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
    • PMID:9990052
    • Edskes HK, Gray VT, Wickner RB. The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc Natl Acad Sci USA 1999; 96:1498-503; PMID:9990052; http:// dx.doi.org/10.1073/pnas.96.4. 1498.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1498-1503
    • Edskes, H.K.1    Gray, V.T.2    Wickner, R.B.3
  • 41
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • PMID:10678178
    • Sondheimer N, Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 2000; 5:163- 72; PMID:10678178; http://dx.doi.org/ 10.1016/ S1097-2765(00)80412-8.
    • (2000) Mol Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 43
    • 33749632462 scopus 로고    scopus 로고
    • Analysis of amyloid aggregates using agarose gel electrophoresis
    • PMID:17046650
    • Bagriantsev SN, Kushnirov VV, Liebman SW. Analysis of amyloid aggregates using agarose gel electrophoresis. Methods Enzymol 2006; 412:33-48; PMID:17046650; http://dx.doi.org/10.1016/S0076-6879(06)12003-0.
    • (2006) Methods Enzymol , vol.412 , pp. 33-48
    • Bagriantsev, S.N.1    Kushnirov, V.V.2    Liebman, S.W.3
  • 44
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • PMID:9267034
    • Scherzinger E, Lurz R, Turmaine M, Mangiarini L, Hollenbach B, Hasenbank R, et al. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 1997; 90:549-58; PMID:9267034; http://dx.doi. org/10.1016/S0092-8674(00)80514-0.
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1    Lurz, R.2    Turmaine, M.3    Mangiarini, L.4    Hollenbach, B.5    Hasenbank, R.6
  • 45
    • 0034960225 scopus 로고    scopus 로고
    • Mechanism of prion loss after Hsp104 inactivation in yeast
    • PMID:11416143
    • Wegrzyn RD, Bapat K, Newnam GP, Zink AD, Chernoff YO. Mechanism of prion loss after Hsp104 inactivation in yeast. Mol Cell Biol 2001; 21:4656- 69; PMID:11416143; http://dx.doi.org/10.1128/ MCB.21.14.4656-69.2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 4656-4669
    • Wegrzyn, R.D.1    Bapat, K.2    Newnam, G.P.3    Zink, A.D.4    Chernoff, Y.O.5
  • 46
    • 0035179616 scopus 로고    scopus 로고
    • The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)]
    • PMID:11123686
    • Zhou P, Derkatch IL, Liebman SW. The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)]. Mol Microbiol 2001; 39:37-46; PMID:11123686; http://dx.doi. org/10.1046/j.1365-2958.2001.02224.x.
    • (2001) Mol Microbiol , vol.39 , pp. 37-46
    • Zhou, P.1    Derkatch, I.L.2    Liebman, S.W.3
  • 47
    • 0041825135 scopus 로고    scopus 로고
    • Analysis of yeast prion aggregates with amyloid-staining compound in vivo
    • PMID:12951439
    • Kimura Y, Koitabashi S, Fujita T. Analysis of yeast prion aggregates with amyloid-staining compound in vivo. Cell Struct Funct 2003; 28:187-93; PMID:12951439; http://dx.doi.org/10.1247/csf.28.187.
    • (2003) Cell Struct Funct , vol.28 , pp. 187-193
    • Kimura, Y.1    Koitabashi, S.2    Fujita, T.3
  • 48
    • 41349087784 scopus 로고    scopus 로고
    • Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae
    • PMID:18362884
    • Du Z, Park KW, Yu H, Fan Q, Li L. Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat Genet 2008; 40:460-5; PMID:18362884; http://dx.doi.org/10.1038/ng.112.
    • (2008) Nat Genet , vol.40 , pp. 460-465
    • Du, Z.1    Park, K.W.2    Yu, H.3    Fan, Q.4    Li, L.5
  • 49
    • 61849091420 scopus 로고    scopus 로고
    • The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion
    • PMID:19219034
    • Patel BK, Gavin-Smyth J, Liebman SW. The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat Cell Biol 2009; 11:344- 9; PMID:19219034; http://dx.doi.org/10.1038/ ncb1843.
    • (2009) Nat Cell Biol , vol.11 , pp. 344-349
    • Patel, B.K.1    Gavin-Smyth, J.2    Liebman, S.W.3
  • 51
    • 33747470607 scopus 로고    scopus 로고
    • Dynamics of yeast prion aggregates in single living cells
    • PMID:16923127
    • Kawai-Noma S, Ayano S, Pack CG, Kinjo M, Yoshida M, Yasuda K, et al. Dynamics of yeast prion aggregates in single living cells. Genes Cells 2006; 11:1085-96; PMID:16923127; http://dx.doi.org/10.1111/j.1365- 2443.2006.01004.x.
    • (2006) Genes Cells , vol.11 , pp. 1085-1096
    • Kawai-Noma, S.1    Ayano, S.2    Pack, C.G.3    Kinjo, M.4    Yoshida, M.5    Yasuda, K.6
  • 53
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • PMID:10037606
    • Taylor KL, Cheng N, Williams RW, Steven AC, Wickner RB. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 1999; 283:1339-43; PMID:10037606; http://dx.doi. org/10.1126/science.283.5406.1339.
    • (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
  • 54
    • 33847291919 scopus 로고    scopus 로고
    • Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM
    • PMID:17121829
    • Vitrenko YA, Gracheva EO, Richmond JE, Liebman SW. Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM. J Biol Chem 2007; 282:1779-87; PMID:17121829; http://dx.doi.org/10. 1074/jbc.M609269200.
    • (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
  • 55
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • PMID:9192614
    • King CY, Tittmann P, Gross H, Gebert R, Aebi M, Wüthrich K. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc Natl Acad Sci USA 1997; 94:6618- 22; PMID:9192614; http://dx.doi.org/10.1073/ pnas.94.13.6618.
    • (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    Wüthrich, K.6
  • 56
    • 0035844884 scopus 로고    scopus 로고
    • Prion filament networks in [URE3] cells of Saccharomyces cerevisiae
    • PMID:11402074
    • Speransky VV, Taylor KL, Edskes HK, Wickner RB, Steven AC. Prion filament networks in [URE3] cells of Saccharomyces cerevisiae. J Cell Biol 2001; 153:1327- 36; PMID:11402074; http://dx.doi.org/10.1083/ jcb.153.6.1327.
    • (2001) J Cell Biol , vol.153 , pp. 1327-1336
    • Speransky, V.V.1    Taylor, K.L.2    Edskes, H.K.3    Wickner, R.B.4    Steven, A.C.5
  • 57
    • 77955005998 scopus 로고    scopus 로고
    • In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells
    • PMID:20643880
    • Kawai-Noma S, Pack CG, Kojidani T, Asakawa H, Hiraoka Y, Kinjo M, et al. In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells. J Cell Biol 2010; 190:223-31; PMID:20643880; http:// dx.doi.org/10.1083/jcb. 201002149.
    • (2010) J Cell Biol , vol.190 , pp. 223-231
    • Kawai-Noma, S.1    Pack, C.G.2    Kojidani, T.3    Asakawa, H.4    Hiraoka, Y.5    Kinjo, M.6
  • 58
    • 77952711519 scopus 로고    scopus 로고
    • Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation
    • PMID:20421488
    • Tyedmers J, Treusch S, Dong J, McCaffery JM, Bevis B, Lindquist S. Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proc Natl Acad Sci USA 2010; 107:8633-8; PMID:20421488; http://dx.doi.org/10.1073/pnas.1003895107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 8633-8638
    • Tyedmers, J.1    Treusch, S.2    Dong, J.3    McCaffery, J.M.4    Bevis, B.5    Lindquist, S.6
  • 59
    • 33644555537 scopus 로고    scopus 로고
    • Molecular chaperones and the assembly of the prion Sup35p, an in vitro study
    • PMID:16467849
    • Krzewska J, Melki R. Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J 2006; 25:822-33; PMID:16467849; http:// dx.doi.org/10.1038/sj.emboj.7600985.
    • (2006) EMBO J , vol.25 , pp. 822-833
    • Krzewska, J.1    Melki, R.2
  • 60
    • 78651083450 scopus 로고    scopus 로고
    • +] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone
    • PMID:21219467
    • +] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone. Mol Microbiol 2011; 79:523-32; PMID:21219467; http://dx.doi.org/10.1111/j.1365- 2958.2010.07466.x.
    • (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
  • 61
    • 27144451227 scopus 로고    scopus 로고
    • Prion generation in vitro: Amyloid of Ure2p is infectious
    • PMID:16096644
    • Brachmann A, Baxa U, Wickner RB. Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J 2005; 24:3082-92; PMID:16096644; http://dx.doi. org/10.1038/sj.emboj.7600772.
    • (2005) EMBO J , vol.24 , pp. 3082-3092
    • Brachmann, A.1    Baxa, U.2    Wickner, R.B.3
  • 62
    • 33845605514 scopus 로고    scopus 로고
    • +]
    • PMID:17097676
    • +]. J Mol Biol 2007; 365:773-82; PMID:17097676; http://dx.doi. org/10.1016/j.jmb.2006.10.069.
    • (2007) J Mol Biol , vol.365 , pp. 773-782
    • Patel, B.K.1    Liebman, S.W.2
  • 63
    • 77956654770 scopus 로고    scopus 로고
    • Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function
    • PMID:20679490
    • Du Z, Crow ET, Kang HS, Li L. Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function. Mol Cell Biol 2010; 30:4644- 55; PMID:20679490; http://dx.doi.org/10.1128/ MCB.00225-10.
    • (2010) Mol Cell Biol , vol.30 , pp. 4644-4655
    • Du, Z.1    Crow, E.T.2    Kang, H.S.3    Li, L.4
  • 65
    • 30644474711 scopus 로고    scopus 로고
    • Modulation of prion formation, aggregation and toxicity by the actin cytoskeleton in yeast
    • PMID:16382152
    • Ganusova EE, Ozolins LN, Bhagat S, Newnam GP, Wegrzyn RD, Sherman MY, et al. Modulation of prion formation, aggregation and toxicity by the actin cytoskeleton in yeast. Mol Cell Biol 2006; 26:617- 29; PMID:16382152; http://dx.doi.org/10.1128/ MCB.26.2.617-29.2006.
    • (2006) Mol Cell Biol , vol.26 , pp. 617-629
    • Ganusova, E.E.1    Ozolins, L.N.2    Bhagat, S.3    Newnam, G.P.4    Wegrzyn, R.D.5    Sherman, M.Y.6
  • 67
    • 24644467295 scopus 로고    scopus 로고
    • Prion protein remodelling confers an immediate phenotypic switch
    • PMID:16148935
    • Satpute-Krishnan P, Serio TR. Prion protein remodelling confers an immediate phenotypic switch. Nature 2005; 437:262-5; PMID:16148935; http://dx.doi. org/10.1038/nature03981.
    • (2005) Nature , vol.437 , pp. 262-265
    • Satpute-Krishnan, P.1    Serio, T.R.2
  • 68
    • 13844313010 scopus 로고    scopus 로고
    • Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication
    • PMID:15701791
    • Song Y, Wu YX, Jung G, Tutar Y, Eisenberg E, Greene LE, et al. Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication. Eukaryot Cell 2005; 4:289-97; PMID:15701791; http://dx.doi. org/10.1128/EC.4.2.289-97. 2005.
    • (2005) Eukaryot Cell , vol.4 , pp. 289-297
    • Song, Y.1    Wu, Y.X.2    Jung, G.3    Tutar, Y.4    Eisenberg, E.5    Greene, L.E.6
  • 69
    • 24644476403 scopus 로고    scopus 로고
    • Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division
    • PMID:16123122
    • Wu YX, Greene LE, Masison DC, Eisenberg E. Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division. Proc Natl Acad Sci USA 2005; 102:12789-94; PMID:16123122; http://dx.doi.org/10.1073/pnas. 0506384102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12789-12794
    • Wu, Y.X.1    Greene, L.E.2    Masison, D.C.3    Eisenberg, E.4
  • 70
    • 33846973006 scopus 로고    scopus 로고
    • Hsp104- Dependent remodeling of prion complexes mediates protein-only inheritance
    • PMID:17253904
    • Satpute-Krishnan P, Langseth SX, Serio TR. Hsp104- dependent remodeling of prion complexes mediates protein-only inheritance. PLoS Biol 2007; 5:24; PMID:17253904; http://dx.doi.org/10.1371/journal. pbio.0050024.
    • (2007) PLoS Biol , vol.5 , pp. 24
    • Satpute-Krishnan, P.1    Langseth, S.X.2    Serio, T.R.3
  • 71
    • 67650102361 scopus 로고    scopus 로고
    • Application of GFP-labeling to study prions in yeast
    • PMID:19519522
    • Greene LE, Park YN, Masison DC, Eisenberg E. Application of GFP-labeling to study prions in yeast. Protein Pept Lett 2009; 16:635-41; PMID:19519522; http://dx.doi.org/10.2174/092986609788490221.
    • (2009) Protein Pept Lett , vol.16 , pp. 635-641
    • Greene, L.E.1    Park, Y.N.2    Masison, D.C.3    Eisenberg, E.4
  • 72
    • 31044445005 scopus 로고    scopus 로고
    • Prion variant maintained only at high levels of the Hsp104 disaggregase
    • PMID:16307272
    • Borchsenius AS, Müller S, Newnam GP, Inge-Vechtomov SG, Chernoff YO. Prion variant maintained only at high levels of the Hsp104 disaggregase. Curr Genet 2006; 49:21-9; PMID:16307272; http:// dx.doi.org/10.1007/s00294-005-0035- 0.
    • (2006) Curr Genet , vol.49 , pp. 21-29
    • Borchsenius, A.S.1    Müller, S.2    Newnam, G.P.3    Inge-Vechtomov, S.G.4    Chernoff, Y.O.5
  • 73
    • 78049408567 scopus 로고    scopus 로고
    • A size threshold limits prion transmission and establishes phenotypic diversity
    • PMID:21030659
    • Derdowski A, Sindi SS, Klaips CL, DiSalvo S, Serio TR. A size threshold limits prion transmission and establishes phenotypic diversity. Science 2010; 330:680- 3; PMID:21030659; http://dx.doi.org/10.1126/science. 1197785.
    • (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
  • 74
    • 0036310663 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast
    • PMID:12101251
    • Ness F, Ferreira P, Cox BS, Tuite MF. Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol Cell Biol 2002; 22:5593-605; PMID:12101251; http://dx.doi. org/10.1128/MCB.22.15.5593-605.2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 5593-5605
    • Ness, F.1    Ferreira, P.2    Cox, B.S.3    Tuite, M.F.4
  • 75
    • 67349190990 scopus 로고    scopus 로고
    • Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates
    • PMID:19422835
    • Mathur V, Hong JY, Liebman SW. Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates. J Mol Biol 2009; 390:155-67; PMID:19422835; http://dx.doi.org/10.1016/j.jmb.2009.04.063.
    • (2009) J Mol Biol , vol.390 , pp. 155-167
    • Mathur, V.1    Hong, J.Y.2    Liebman, S.W.3
  • 76
    • 0035803490 scopus 로고    scopus 로고
    • Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'
    • PMID:11726504
    • Borchsenius AS, Wegrzyn RD, Newnam GP, Inge-Vechtomov SG, Chernoff YO. Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'. EMBO J 2001; 20:6683- 91; PMID:11726504; http://dx.doi.org/10. 1093/ emboj/20.23.6683.
    • (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
  • 77
    • 69849100344 scopus 로고    scopus 로고
    • Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine- HCl-treated [PSI] cells
    • PMID:19674118
    • Kawai-Noma S, Pack CG, Tsuji T, Kinjo M, Taguchi H. Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine- HCl-treated [PSI] cells. Genes Cells 2009; 14:1045-54; PMID:19674118; http://dx.doi.org/10.1111/j.1365- 2443.2009.01333.x.
    • (2009) Genes Cells , vol.14 , pp. 1045-1054
    • Kawai-Noma, S.1    Pack, C.G.2    Tsuji, T.3    Kinjo, M.4    Taguchi, H.5
  • 78
    • 67650135519 scopus 로고    scopus 로고
    • Hsp104 and prion propagation
    • PMID:19519517
    • Romanova NV, Chernoff YO. Hsp104 and prion propagation. Protein Pept Lett 2009; 16:598-605; PMID:19519517; http://dx.doi. org/10.2174/092986609788490078.
    • (2009) Protein Pept Lett , vol.16 , pp. 598-605
    • Romanova, N.V.1    Chernoff, Y.O.2
  • 79
    • 79953860164 scopus 로고    scopus 로고
    • Destabilization and recovery of a yeast prion after mild heat shock
    • PMID:21392508
    • Newnam GP, Birchmore JL, Chernoff YO. Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol 2011; 408:432-48; PMID:21392508; http://dx.doi.org/10.1016/j. jmb.2011.02.034.
    • (2011) J Mol Biol , vol.408 , pp. 432-448
    • Newnam, G.P.1    Birchmore, J.L.2    Chernoff, Y.O.3
  • 80
    • 0346100706 scopus 로고    scopus 로고
    • Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants
    • PMID:14704158
    • Bradley ME, Liebman SW. Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants. Genetics 2003; 165:1675-85; PMID:14704158.
    • (2003) Genetics , vol.165 , pp. 1675-1685
    • Bradley, M.E.1    Liebman, S.W.2
  • 81
    • 0019411527 scopus 로고
    • Reversion analysis of [psi- ] mutations in Saccharomyces cerevisiae
    • PMID:7021322
    • Lund PM, Cox BS. Reversion analysis of [psi- ] mutations in Saccharomyces cerevisiae. Genet Res 1981; 37:173-82; PMID:7021322; http://dx.doi. org/10.1017/S0016672300020140.
    • (1981) Genet Res , vol.37 , pp. 173-182
    • Lund, P.M.1    Cox, B.S.2
  • 82
    • 0033527045 scopus 로고    scopus 로고
    • Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast
    • PMID:10448860
    • Liu JJ, Lindquist S. Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature 1999; 400:573-6; PMID:10448860; http://dx.doi. org/10.1038/22919.
    • (1999) Nature , vol.400 , pp. 573-576
    • Liu, J.J.1    Lindquist, S.2
  • 83
    • 0027483882 scopus 로고
    • Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae
    • PMID:8221937
    • Chernoff YO, Derkach IL, Inge-Vechtomov SG. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr Genet 1993; 24:268-70; PMID:8221937; http:// dx.doi.org/10.1007/BF00351802.
    • (1993) Curr Genet , vol.24 , pp. 268-270
    • Chernoff, Y.O.1    Derkach, I.L.2    Inge-Vechtomov, S.G.3
  • 84
    • 0027513128 scopus 로고
    • Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein
    • PMID:8469113
    • Ter-Avanesyan MD, Kushnirov VV, Dagkesamanskaya AR, Didichenko SA, Chernoff YO, Inge-Vechtomov SG, et al. Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol Microbiol 1993; 7:683-92; PMID:8469113; http:// dx.doi.org/10.1111/j.1365-2958.1993.tb01159.x.
    • (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    Inge-Vechtomov, S.G.6
  • 86
    • 79960467038 scopus 로고    scopus 로고
    • Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton
    • PMID:21777813
    • Chernova TA, Romanyuk AV, Karpova TS, Shanks JR, Ali M, Moffatt N, et al. Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Mol Cell 2011; 43:242-52; PMID:21777813; http:// dx.doi.org/10.1016/j.molcel.2011.07.001.
    • (2011) Mol Cell , vol.43 , pp. 242-252
    • Chernova, T.A.1    Romanyuk, A.V.2    Karpova, T.S.3    Shanks, J.R.4    Ali, M.5    Moffatt, N.6
  • 88
    • 70350147706 scopus 로고    scopus 로고
    • Sequestration of essential proteins causes prion associated toxicity in yeast
    • PMID:19682262
    • Vishveshwara N, Bradley ME, Liebman SW. Sequestration of essential proteins causes prion associated toxicity in yeast. Mol Microbiol 2009; 73:1101-14; PMID:19682262; http://dx.doi.org/10.1111/j.1365- 2958.2009.06836.x.
    • (2009) Mol Microbiol , vol.73 , pp. 1101-1114
    • Vishveshwara, N.1    Bradley, M.E.2    Liebman, S.W.3
  • 89
    • 0034595216 scopus 로고    scopus 로고
    • Dependence and independence of [PSI(+)] and [PIN(+)]: A two-prion system in yeast?
    • PMID:10790361
    • Derkatch IL, Bradley ME, Masse SV, Zadorsky SP, Polozkov GV, Inge-Vechtomov SG, et al. Dependence and independence of [PSI(+)] and [PIN(+)]: a two-prion system in yeast? EMBO J 2000; 19:1942- 52; PMID:10790361; http://dx.doi.org/10.1093/ emboj/19.9.1942.
    • (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    Inge-Vechtomov, S.G.6
  • 90
    • 0034601056 scopus 로고    scopus 로고
    • The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele
    • PMID:10880435
    • Fernandez-Bellot E, Guillemet E, Cullin C. The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele. EMBO J 2000; 19:3215- 22; PMID:10880435; http://dx.doi.org/10.1093/ emboj/19.13.3215.
    • (2000) EMBO J , vol.19 , pp. 3215-3222
    • Fernandez-Bellot, E.1    Guillemet, E.2    Cullin, C.3
  • 91
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: The story of [PIN(+)]
    • PMID:11511345
    • Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 2001; 106:171-82; PMID:11511345; http://dx.doi.org/10.1016/S0092-8674(01)00427-5.
    • (2001) Cell , vol.106 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 92
    • 0035958547 scopus 로고    scopus 로고
    • Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion
    • PMID:11511346
    • Osherovich LZ, Weissman JS. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 2001; 106:183-94; PMID:11511346; http://dx.doi.org/10.1016/S0092- 8674(01)00440-8.
    • (2001) Cell , vol.106 , pp. 183-194
    • Osherovich, L.Z.1    Weissman, J.S.2
  • 93
    • 15744371668 scopus 로고    scopus 로고
    • Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids
    • PMID:15618222
    • Salnikova AB, Kryndushkin DS, Smirnov VN, Kushnirov VV, Ter-Avanesyan MD. Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 2005; 280:8808-12; PMID:15618222; http://dx.doi. org/10.1074/jbc.M410150200.
    • (2005) J Biol Chem , vol.280 , pp. 8808-8812
    • Salnikova, A.B.1    Kryndushkin, D.S.2    Smirnov, V.N.3    Kushnirov, V.V.4    Ter-Avanesyan, M.D.5
  • 94
    • 34250866206 scopus 로고    scopus 로고
    • A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast
    • PMID:17612491
    • Taneja V, Maddelein ML, Talarek N, Saupe SJ, Liebman SW. A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast. Mol Cell 2007; 27:67-77; PMID:17612491; http:// dx.doi.org/10.1016/j.molcel.2007. 05.027.
    • (2007) Mol Cell , vol.27 , pp. 67-77
    • Taneja, V.1    Maddelein, M.L.2    Talarek, N.3    Saupe, S.J.4    Liebman, S.W.5
  • 95
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • PMID:18756251
    • Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008; 454:1088-95; PMID:18756251; http://dx.doi.org/10.1038/ nature07195.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 96
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • PMID:19653858
    • He C, Klionsky DJ. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 2009; 43:67-93; PMID:19653858; http://dx.doi. org/10.1146/annurev-genet-102808-114910.
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 97
    • 67649467294 scopus 로고    scopus 로고
    • Dynamics and diversity in autophagy mechanisms: Lessons from yeast
    • PMID:19491929
    • Nakatogawa H, Suzuki K, Kamada Y, Ohsumi Y. Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat Rev Mol Cell Biol 2009; 10:458- 67; PMID:19491929; http://dx.doi.org/10.1038/ nrm2708.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 458-467
    • Nakatogawa, H.1    Suzuki, K.2    Kamada, Y.3    Ohsumi, Y.4
  • 98
    • 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
    • PMID:15326312
    • Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, Liebman SW. 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 2004; 101:12934-9; PMID:15326312; http://dx.doi. org/10.1073/pnas. 0404968101.
    • (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    Liebman, S.W.6
  • 99
    • 4444377399 scopus 로고    scopus 로고
    • The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions
    • PMID:15298677
    • Kimura Y, Koitabashi S, Kakizuka A, Fujita T. The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions. Genes Cells 2004; 9:685-96; PMID:15298677; http://dx.doi.org/10.1111/j.1356- 9597.2004.00759.x.
    • (2004) Genes Cells , vol.9 , pp. 685-696
    • Kimura, Y.1    Koitabashi, S.2    Kakizuka, A.3    Fujita, T.4
  • 100
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • PMID:20944667
    • Tyedmers J, Mogk A, Bukau B. Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 2010; 11:777-88; PMID:20944667; http://dx.doi. org/10.1038/nrm2993.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 101
    • 0242585476 scopus 로고    scopus 로고
    • Asymmetric inheritance of oxidatively damaged proteins during cytokinesis
    • PMID:12610228
    • Aguilaniu H, Gustafsson L, Rigoulet M, Nyström T. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 2003; 299:1751- 3; PMID:12610228; http://dx.doi.org/10.1126/science. 1080418.
    • (2003) Science , vol.299 , pp. 1751-1753
    • Aguilaniu, H.1    Gustafsson, L.2    Rigoulet, M.3    Nyström, T.4
  • 102
    • 74549184412 scopus 로고    scopus 로고
    • The polarisome is required for segregation and retrograde transport of protein aggregates
    • PMID:20141839
    • Liu B, Larsson L, Caballero A, Hao X, Oling D, Grantham J, et al. The polarisome is required for segregation and retrograde transport of protein aggregates. Cell 2010; 140:257-67; PMID:20141839; http:// dx.doi.org/10.1016/j. cell.2009.12.031.
    • (2010) Cell , vol.140 , pp. 257-267
    • Liu, B.1    Larsson, L.2    Caballero, A.3    Hao, X.4    Oling, D.5    Grantham, J.6
  • 103
    • 77649293067 scopus 로고    scopus 로고
    • Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing
    • PMID:20094032
    • Winkler J, Seybert A, König L, Pruggnaller S, Haselmann U, Sourjik V, et al. Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing. EMBO J 2010; 29:910- 23; PMID:20094032; http://dx.doi.org/10.1038/ emboj.2009.412.
    • (2010) EMBO J , vol.29 , pp. 910-923
    • Winkler, J.1    Seybert, A.2    König, L.3    Pruggnaller, S.4    Haselmann, U.5    Sourjik, V.6
  • 104
    • 67649326107 scopus 로고    scopus 로고
    • + chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins
    • PMID:19398583
    • + chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins. Mol Cell Biol 2009; 29:3738- 45; PMID:19398583; http://dx.doi.org/10.1128/ MCB.00201-09.
    • (2009) Mol Cell Biol , vol.29 , pp. 3738-3745
    • Tessarz, P.1    Schwarz, M.2    Mogk, A.3    Bukau, B.4
  • 105
    • 34447526217 scopus 로고    scopus 로고
    • Stress and prions: Lessons from the yeast model
    • PMID:17509571
    • Chernoff YO. Stress and prions: lessons from the yeast model. FEBS Lett 2007; 581:3695-701; PMID:17509571; http://dx.doi.org/10.1016/j.febslet. 2007.04.075.
    • (2007) FEBS Lett , vol.581 , pp. 3695-3701
    • Chernoff, Y.O.1
  • 106
    • 39149142505 scopus 로고    scopus 로고
    • Insights into the mechanism of prion propagation
    • PMID:18243685
    • Perrett S, Jones GW. Insights into the mechanism of prion propagation. Curr Opin Struct Biol 2008; 18:52- 9; PMID:18243685; http://dx.doi.org/10.1016/ j. sbi.2007.12.005.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 52-59
    • Perrett, S.1    Jones, G.W.2
  • 107
    • 53849127165 scopus 로고    scopus 로고
    • Cellular factors important for the de novo formation of yeast prions
    • PMID:18793193
    • Tuite M, Stojanovski K, Ness F, Merritt G, Koloteva- Levine N. Cellular factors important for the de novo formation of yeast prions. Biochem Soc Trans 2008; 36:1083-7; PMID:18793193; http://dx.doi. org/10.1042/BST0361083.
    • (2008) Biochem Soc Trans , vol.36 , pp. 1083-1087
    • Tuite, M.1    Stojanovski, K.2    Ness, F.3    Merritt, G.K.-.L.N.4
  • 108
    • 24644439320 scopus 로고    scopus 로고
    • Chaperoning prions: The cellular machinery for propagating an infectious protein?
    • PMID:16015602
    • Jones GW, Tuite MF. Chaperoning prions: the cellular machinery for propagating an infectious protein? Bioessays 2005; 27:823-32; PMID:16015602; http:// dx.doi.org/10.1002/bies.20267.
    • (2005) Bioessays , vol.27 , pp. 823-832
    • Jones, G.W.1    Tuite, M.F.2
  • 109
    • 79957996872 scopus 로고    scopus 로고
    • Prion formation and polyglutamine aggregation are controlled by two classes of genes
    • PMID:21625618
    • Manogaran AL, Hong JY, Hufana J, Tyedmers J, Lindquist S, Liebman SW. Prion formation and polyglutamine aggregation are controlled by two classes of genes. PLoS Genet 2011; 7:1001386; PMID:21625618; http://dx.doi.org/10.1371/ journal. pgen.1001386.
    • (2011) PLoS Genet , vol.7 , pp. 1001386
    • Manogaran, A.L.1    Hong, J.Y.2    Hufana, J.3    Tyedmers, J.4    Lindquist, S.5    Liebman, S.W.6
  • 110
    • 0347993105 scopus 로고    scopus 로고
    • Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool
    • PMID:14559899
    • Chernova TA, Allen KD, Wesoloski LM, Shanks JR, Chernoff YO, Wilkinson KD. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. J Biol Chem 2003; 278:52102-15; PMID:14559899; http://dx.doi. org/10.1074/jbc.M310283200.
    • (2003) J Biol Chem , vol.278 , pp. 52102-52115
    • Chernova, T.A.1    Allen, K.D.2    Wesoloski, L.M.3    Shanks, J.R.4    Chernoff, Y.O.5    Wilkinson, K.D.6
  • 111
    • 34047271439 scopus 로고    scopus 로고
    • Effects of ubiquitin system alterations on the formation and loss of a yeast prion
    • PMID:17142456
    • Allen KD, Chernova TA, Tennant EP, Wilkinson KD, Chernoff YO. Effects of ubiquitin system alterations on the formation and loss of a yeast prion. J Biol Chem 2007; 282:3004-13; PMID:17142456; http://dx.doi. org/10.1074/jbc. M609597200.
    • (2007) J Biol Chem , vol.282 , pp. 3004-3013
    • Allen, K.D.1    Chernova, T.A.2    Tennant, E.P.3    Wilkinson, K.D.4    Chernoff, Y.O.5
  • 112
    • 80052692601 scopus 로고    scopus 로고
    • Qualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion Sup35p
    • PMID:21931608
    • Redeker V, Hughes C, Savistchenko J, Vissers JP, Melki R. Qualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion Sup35p. PLoS One 2011; 6:23659; PMID:21931608; http:// dx.doi.org/10.1371/journal.pone.0023659.
    • (2011) PLoS One , vol.6 , pp. 23659
    • Redeker, V.1    Hughes, C.2    Savistchenko, J.3    Vissers, J.P.4    Melki, R.5
  • 113
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. [psi+]
    • PMID:7754373
    • Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. [psi+]. Science 1995; 268:880-4; PMID:7754373; http://dx.doi.org/10. 1126/science.7754373.
    • (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
  • 114
    • 63049114323 scopus 로고    scopus 로고
    • Prion proteostasis: Hsp104 meets its supporting cast
    • PMID:19242125
    • Sweeny EA, Shorter J. Prion proteostasis: Hsp104 meets its supporting cast. Prion 2008; 2:135-40; PMID:19242125; http://dx.doi.org/10.4161/ pri.2.4.7952.
    • (2008) Prion , vol.2 , pp. 135-140
    • Sweeny, E.A.1    Shorter, J.2
  • 115
    • 75349113019 scopus 로고    scopus 로고
    • Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation
    • PMID:20130680
    • Haslberger T, Bukau B, Mogk A. Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochem Cell Biol 2010; 88:63-75; PMID:20130680; http://dx.doi. org/10.1139/O09-118.
    • (2010) Biochem Cell Biol , vol.88 , pp. 63-75
    • Haslberger, T.1    Bukau, B.2    Mogk, A.3
  • 116
    • 0034932879 scopus 로고    scopus 로고
    • +] prion by guanidine hydrochloride is the result of Hsp104 inactivation
    • PMID:11442834
    • +] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol Microbiol 2001; 40:1357-69; PMID:11442834; http://dx.doi.org/10.1046/j.1365-2958.2001.02478.x.
    • (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
  • 117
    • 0034974996 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits Hsp104 activity in vivo: A possible explanation for its effect in curing yeast prions
    • PMID:11375656
    • Jung G, Masison DC. Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr Microbiol 2001; 43:7-10; PMID:11375656; http://dx.doi.org/10.1007/ s002840010251.
    • (2001) Curr Microbiol , vol.43 , pp. 7-10
    • Jung, G.1    Masison, D.C.2
  • 118
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • PMID:9674429
    • Glover JR, Lindquist S. Hsp104, Hsp70 and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998; 94:73-82; PMID:9674429; http://dx.doi.org/10.1016/S0092-8674(00)81223-4.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 119
    • 8844251486 scopus 로고    scopus 로고
    • Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
    • PMID:15550247
    • Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, et al. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 2004; 119:653- 65; PMID:15550247; http://dx.doi.org/10.1016/j. cell.2004.11.027.
    • (2004) Cell , vol.119 , pp. 653-665
    • Weibezahn, J.1    Tessarz, P.2    Schlieker, C.3    Zahn, R.4    Maglica, Z.5    Lee, S.6
  • 120
    • 7244247277 scopus 로고    scopus 로고
    • Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation
    • PMID:15302880
    • Zietkiewicz S, Krzewska J, Liberek K. Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem 2004; 279:44376-83; PMID:15302880; http://dx.doi. org/10.1074/jbc.M402405200.
    • (2004) J Biol Chem , vol.279 , pp. 44376-44383
    • Zietkiewicz, S.1    Krzewska, J.2    Liberek, K.3
  • 121
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • PMID:15155912
    • Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 2004; 304:1793-7; PMID:15155912; http:// dx.doi.org/10.1126/science.1098007.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 122
    • 33746405081 scopus 로고    scopus 로고
    • Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities
    • PMID:16885031
    • Shorter J, Lindquist S. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell 2006; 23:425-38; PMID:16885031; http://dx.doi.org/10.1016/j.molcel. 2006.05.042.
    • (2006) Mol Cell , vol.23 , pp. 425-438
    • Shorter, J.1    Lindquist, S.2
  • 123
    • 10044227566 scopus 로고    scopus 로고
    • Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it
    • PMID:15448141
    • Inoue Y, Taguchi H, Kishimoto A, Yoshida M. Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it. J Biol Chem 2004; 279:52319- 23; PMID:15448141; http://dx.doi.org/10.1074/jbc. M408159200.
    • (2004) J Biol Chem , vol.279 , pp. 52319-52323
    • Inoue, Y.1    Taguchi, H.2    Kishimoto, A.3    Yoshida, M.4
  • 124
    • 55949109442 scopus 로고    scopus 로고
    • In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
    • PMID:19026788
    • Tipton KA, Verges KJ, Weissman JS. In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. Mol Cell 2008; 32:584-91; PMID:19026788; http://dx.doi. org/10.1016/j.molcel.2008.11.003.
    • (2008) Mol Cell , vol.32 , pp. 584-591
    • Tipton, K.A.1    Verges, K.J.2    Weissman, J.S.3
  • 125
    • 55949105643 scopus 로고    scopus 로고
    • Specificity of the J-protein Sis1 in the propagation of 3 yeast prions
    • PMID:18955697
    • Higurashi T, Hines JK, Sahi C, Aron R, Craig EA. Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci USA 2008; 105:16596-601; PMID:18955697; http://dx.doi. org/10.1073/pnas.0808934105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16596-16601
    • Higurashi, T.1    Hines, J.K.2    Sahi, C.3    Aron, R.4    Craig, E.A.5
  • 126
    • 67649361913 scopus 로고    scopus 로고
    • Influence of Hsp70s and their regulators on yeast prion propagation
    • PMID:19556854
    • Masison DC, Kirkland PA, Sharma D. Influence of Hsp70s and their regulators on yeast prion propagation. Prion 2009; 3:65-73; PMID:19556854; http:// dx.doi.org/10.4161/pri.3.2.9134.
    • (2009) Prion , vol.3 , pp. 65-73
    • Masison, D.C.1    Kirkland, P.A.2    Sharma, D.3
  • 127
    • 67649363859 scopus 로고    scopus 로고
    • Prion propagation by Hsp40 molecular chaperones
    • PMID:19535913
    • Summers DW, Douglas PM, Cyr DM. Prion propagation by Hsp40 molecular chaperones. Prion 2009; 3:59-64; PMID:19535913; http://dx.doi.org/10.4161/ pri.3.2.9062.
    • (2009) Prion , vol.3 , pp. 59-64
    • Summers, D.W.1    Douglas, P.M.2    Cyr, D.M.3
  • 128
    • 34548101963 scopus 로고    scopus 로고
    • J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation
    • PMID:17673909
    • Aron R, Higurashi T, Sahi C, Craig EA. J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. EMBO J 2007; 26:3794-803; PMID:17673909; http://dx.doi. org/10.1038/sj.emboj.7601811.
    • (2007) EMBO J , vol.26 , pp. 3794-3803
    • Aron, R.1    Higurashi, T.2    Sahi, C.3    Craig, E.A.4
  • 129
    • 0034481527 scopus 로고    scopus 로고
    • An antiprion effect of the anticytoskeletal drug latrunculin A in yeast
    • PMID:11243411
    • Bailleul-Winslett PA, Newnam GP, Wegrzyn RD, Chernoff YO. An antiprion effect of the anticytoskeletal drug latrunculin A in yeast. Gene Expr 2000; 9:145-56; PMID:11243411.
    • (2000) Gene Expr , vol.9 , pp. 145-156
    • Bailleul-Winslett, P.A.1    Newnam, G.P.2    Wegrzyn, R.D.3    Chernoff, Y.O.4
  • 130
    • 0032832981 scopus 로고    scopus 로고
    • Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae
    • PMID:10471702
    • Bailleul PA, Newnam GP, Steenbergen JN, Chernoff YO. Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Genetics 1999; 153:81-94; PMID:10471702.
    • (1999) Genetics , vol.153 , pp. 81-94
    • Bailleul, P.A.1    Newnam, G.P.2    Steenbergen, J.N.3    Chernoff, Y.O.4
  • 131
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • PMID:10958771
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000; 289:1317-21; PMID:10958771; http://dx.doi. org/10.1126/science.289.5483.1317.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 132
    • 0034602804 scopus 로고    scopus 로고
    • Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae
    • PMID:10618402
    • Eaglestone SS, Ruddock LW, Cox BS, Tuite MF. Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae. Proc Natl Acad Sci USA 2000; 97:240-4; PMID:10618402; http://dx.doi. org/10.1073/pnas.97.1.240.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 240-244
    • Eaglestone, S.S.1    Ruddock, L.W.2    Cox, B.S.3    Tuite, M.F.4
  • 133
    • 61849132199 scopus 로고    scopus 로고
    • The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae
    • PMID:19262693
    • Byrne LJ, Cole DJ, Cox BS, Ridout MS, Morgan BJ, Tuite MF. The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae. PLoS One 2009; 4:4670; PMID:19262693; http:// dx.doi.org/10.1371/ journal.pone.0004670.
    • (2009) PLoS One , vol.4 , pp. 4670
    • Byrne, L.J.1    Cole, D.J.2    Cox, B.S.3    Ridout, M.S.4    Morgan, B.J.5    Tuite, M.F.6
  • 134
    • 59649096550 scopus 로고    scopus 로고
    • Abnormal proteins can form aggresome in yeast: Aggresome-targeting signals and components of the machinery
    • PMID:18854435
    • Wang Y, Meriin AB, Zaarur N, Romanova NV, Chernoff YO, Costello CE, et al. Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery. FASEB J 2009; 23:451-63; PMID:18854435; http://dx.doi. org/10.1096/fj.08-117614.
    • (2009) FASEB J , vol.23 , pp. 451-463
    • Wang, Y.1    Meriin, A.B.2    Zaarur, N.3    Romanova, N.V.4    Chernoff, Y.O.5    Costello, C.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.