Life cycle of cytosolic prions

References

• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 44; http://dx.doi.org/10.1126/science.6801762; PMID: 6801762
   PubMed Web of Science ®Google Scholar
• Robakis NK, Sawh PR, Wolfe GC, Rubenstein R, Carp RI, Innis MA. Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues. Proc Natl Acad Sci U S A 1986; 83:6377 - 81; http://dx.doi.org/10.1073/pnas.83.17.6377; PMID: 3529083
   PubMed Web of Science ®Google Scholar
• Brown HR, Goller NL, Rudelli RD, Merz GS, Wolfe GC, Wisniewski HM, Robakis NK. The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells. Acta Neuropathol 1990; 80:1 - 6; http://dx.doi.org/10.1007/BF00294214; PMID: 1972856
   PubMed Web of Science ®Google Scholar
• Grassmann A, Wolf H, Hofmann J, Graham J, Vorberg I. Cellular aspects of prion replication in vitro. Viruses 2013; 5:374 - 405; http://dx.doi.org/10.3390/v5010374; PMID: 23340381
   PubMed Web of Science ®Google Scholar
• Wopfner F, Weidenhöfer G, Schneider R, von Brunn A, Gilch S, Schwarz TF, Werner T, Schätzl HM. Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein. J Mol Biol 1999; 289:1163 - 78; http://dx.doi.org/10.1006/jmbi.1999.2831; PMID: 10373359
   PubMed Web of Science ®Google Scholar
• Liu JJ, Lindquist S. Oligopeptide-repeat expansions modulate ‘protein-only’ inheritance in yeast. Nature 1999; 400:573 - 6; http://dx.doi.org/10.1038/22919; PMID: 10448860
   PubMed Web of Science ®Google Scholar
• Wickner RB, Edskes HK, Roberts BT, Baxa U, Pierce MM, Ross ED, Brachmann A. Prions: proteins as genes and infectious entities. Genes Dev 2004; 18:470 - 85; http://dx.doi.org/10.1101/gad.1177104; PMID: 15037545
   PubMed Web of Science ®Google Scholar
• Wickner RB. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 1994; 264:566 - 9; http://dx.doi.org/10.1126/science.7909170; PMID: 7909170
   PubMed Web of Science ®Google Scholar
• Wickner RB, Taylor KL, Edskes HK, Maddelein ML, Moriyama H, Roberts BT. Prions in Saccharomyces and Podospora spp.: protein-based inheritance. [table of contents.] Microbiol Mol Biol Rev 1999; 63:844 - 61; PMID: 10585968
   PubMed Web of Science ®Google Scholar
• Halfmann R, Jarosz DF, Jones SK, Chang A, Lancaster AK, Lindquist S. Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 2012; 482:363 - 8; http://dx.doi.org/10.1038/nature10875; PMID: 22337056
   PubMed Web of Science ®Google Scholar
• McGlinchey RP, Kryndushkin D, Wickner RB. Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A 2011; 108:5337 - 41; http://dx.doi.org/10.1073/pnas.1102762108; PMID: 21402947
   PubMed Web of Science ®Google Scholar
• Wickner RB, Edskes HK, Bateman D, Kelly AC, Gorkovskiy A. The yeast prions [PSI+] and [URE3] are molecular degenerative diseases. Prion 2011; 5:258 - 62; PMID: 22052353
   PubMed Web of Science ®Google Scholar
• Rogoza T, Goginashvili A, Rodionova S, Ivanov M, Viktorovskaya O, Rubel A, Volkov K, Mironova L. Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1. Proc Natl Acad Sci U S A 2010; 107:10573 - 7; http://dx.doi.org/10.1073/pnas.1005949107; PMID: 20498075
   PubMed Web of Science ®Google Scholar
• Orgel LE. Prion replication and secondary nucleation. Chem Biol 1996; 3:413 - 4; http://dx.doi.org/10.1016/S1074-5521(96)90087-3; PMID: 8807870
   PubMed Web of Science ®Google Scholar
• Hall D, Edskes H. Silent prions lying in wait: a two-hit model of prion/amyloid formation and infection. J Mol Biol 2004; 336:775 - 86; http://dx.doi.org/10.1016/j.jmb.2003.12.004; PMID: 15095987
   PubMed Web of Science ®Google Scholar
• Tanaka M, Collins SR, Toyama BH, Weissman JS. The physical basis of how prion conformations determine strain phenotypes. Nature 2006; 442:585 - 9; http://dx.doi.org/10.1038/nature04922; PMID: 16810177
   PubMed Web of Science ®Google Scholar
• Knowles TP, Waudby CA, Devlin GL, Cohen SI, Aguzzi A, Vendruscolo M, Terentjev EM, Welland ME, Dobson CM. An analytical solution to the kinetics of breakable filament assembly. Science 2009; 326:1533 - 7; http://dx.doi.org/10.1126/science.1178250; PMID: 20007899
   PubMed Web of Science ®Google Scholar
• 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; http://dx.doi.org/10.1126/science.7754373; PMID: 7754373
   PubMed Web of Science ®Google Scholar
• Wickner RB, Edskes HK, Bateman DA, Kelly AC, Gorkovskiy A, Dayani Y, Zhou A. Amyloids and yeast prion biology. Biochemistry 2013; 52:1514 - 27; http://dx.doi.org/10.1021/bi301686a; PMID: 23379365
   PubMed Web of Science ®Google Scholar
• Winkler J, Tyedmers J, Bukau B, Mogk A. Chaperone networks in protein disaggregation and prion propagation. J Struct Biol 2012; 179:152 - 60; http://dx.doi.org/10.1016/j.jsb.2012.05.002; PMID: 22580344
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Zhou P, Chernoff YO, Liebman SW. Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 1997; 147:507 - 19; PMID: 9335589
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 2001; 106:171 - 82; http://dx.doi.org/10.1016/S0092-8674(01)00427-5; PMID: 11511345
   PubMed Web of Science ®Google Scholar
• Osherovich LZ, Weissman JS. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 2001; 106:183 - 94; http://dx.doi.org/10.1016/S0092-8674(01)00440-8; PMID: 11511346
   PubMed Web of Science ®Google Scholar
• Uptain SM, Lindquist S. Prions as protein-based genetic elements. Annu Rev Microbiol 2002; 56:703 - 41; http://dx.doi.org/10.1146/annurev.micro.56.013002.100603; PMID: 12142498
   PubMed Web of Science ®Google Scholar
• Wickner RB, Fujimura T, Esteban R. Viruses and prions of Saccharomyces cerevisiae. Adv Virus Res 2013; 86:1 - 36; http://dx.doi.org/10.1016/B978-0-12-394315-6.00001-5; PMID: 23498901
   PubMed Web of Science ®Google Scholar
• Aguzzi A. Prions and the immune system: a journey through gut, spleen, and nerves. Adv Immunol 2003; 81:123 - 71; http://dx.doi.org/10.1016/S0065-2776(03)81004-0; PMID: 14711055
   PubMed Web of Science ®Google Scholar
• Kanu N, Imokawa Y, Drechsel DN, Williamson RA, Birkett CR, Bostock CJ, Brockes JP. Transfer of scrapie prion infectivity by cell contact in culture. Curr Biol 2002; 12:523 - 30; http://dx.doi.org/10.1016/S0960-9822(02)00722-4; PMID: 11937020
   PubMed Web of Science ®Google Scholar
• Gousset K, Schiff E, Langevin C, Marijanovic Z, Caputo A, Browman DT, Chenouard N, de Chaumont F, Martino A, Enninga J, et al. Prions hijack tunnelling nanotubes for intercellular spread. Nat Cell Biol 2009; 11:328 - 36; http://dx.doi.org/10.1038/ncb1841; PMID: 19198598
   PubMed Web of Science ®Google Scholar
• Gerdes HH, Carvalho RN. Intercellular transfer mediated by tunneling nanotubes. Curr Opin Cell Biol 2008; 20:470 - 5; http://dx.doi.org/10.1016/j.ceb.2008.03.005; PMID: 18456488
   PubMed Web of Science ®Google Scholar
• Leblanc P, Alais S, Porto-Carreiro I, Lehmann S, Grassi J, Raposo G, Darlix JL. Retrovirus infection strongly enhances scrapie infectivity release in cell culture. EMBO J 2006; 25:2674 - 85; http://dx.doi.org/10.1038/sj.emboj.7601162; PMID: 16724107
   PubMed Web of Science ®Google Scholar
• Vella LJ, Sharples RA, Lawson VA, Masters CL, Cappai R, Hill AF. Packaging of prions into exosomes is associated with a novel pathway of PrP processing. J Pathol 2007; 211:582 - 90; http://dx.doi.org/10.1002/path.2145; PMID: 17334982
   PubMed Web of Science ®Google Scholar
• Alais S, Simoes S, Baas D, Lehmann S, Raposo G, Darlix JL, Leblanc P. Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles. Biol Cell 2008; 100:603 - 15; http://dx.doi.org/10.1042/BC20080025; PMID: 18422484
   PubMed Web of Science ®Google Scholar
• Castro-Seoane R, Hummerich H, Sweeting T, Tattum MH, Linehan JM, Fernandez de Marco M, Brandner S, Collinge J, Klöhn PC. Plasmacytoid dendritic cells sequester high prion titres at early stages of prion infection. PLoS Pathog 2012; 8:e1002538; http://dx.doi.org/10.1371/journal.ppat.1002538; PMID: 22359509
   PubMedGoogle Scholar
• Caughey B, Baron GS, Chesebro B, Jeffrey M. Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions. Annu Rev Biochem 2009; 78:177 - 204; http://dx.doi.org/10.1146/annurev.biochem.78.082907.145410; PMID: 19231987
   PubMed Web of Science ®Google Scholar
• Krammer C, Kryndushkin D, Suhre MH, Kremmer E, Hofmann A, Pfeifer A, Scheibel T, Wickner RB, Schätzl HM, Vorberg I. The yeast Sup35NM domain propagates as a prion in mammalian cells. Proc Natl Acad Sci U S A 2009; 106:462 - 7; http://dx.doi.org/10.1073/pnas.0811571106; PMID: 19114662
   PubMed Web of Science ®Google Scholar
• Krammer C, Schätzl HM, Vorberg I. Prion-like propagation of cytosolic protein aggregates: insights from cell culture models. Prion 2009; 3:206 - 12; http://dx.doi.org/10.4161/pri.3.4.10013; PMID: 19901539
   PubMed Web of Science ®Google Scholar
• Doel SM, McCready SJ, Nierras CR, Cox BS. The dominant PNM2- mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 1994; 137:659 - 70; PMID: 8088511
   PubMed Web of Science ®Google Scholar
• Ter-Avanesyan MD, Dagkesamanskaya AR, Kushnirov VV, Smirnov VN. The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics 1994; 137:671 - 6; PMID: 8088512
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Chernoff YO, Kushnirov VV, Inge-Vechtomov SG, Liebman SW. Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 1996; 144:1375 - 86; PMID: 8978027
   PubMed Web of Science ®Google Scholar
• Liu JJ, Sondheimer N, Lindquist SL. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. [PSI+] Proc Natl Acad Sci U S A 2002; 99:Suppl 4 16446 - 53; http://dx.doi.org/10.1073/pnas.252652099; PMID: 12461168
   PubMed Web of Science ®Google Scholar
• Hofmann JP, Denner P, Nussbaum-Krammer C, Kuhn PH, Suhre MH, Scheibel T, Lichtenthaler SF, Schätzl HM, Bano D, Vorberg IM. Cell-to-cell propagation of infectious cytosolic protein aggregates. Proc Natl Acad Sci U S A 2013; 110:5951 - 6; http://dx.doi.org/10.1073/pnas.1217321110; PMID: 23509289
   PubMed Web of Science ®Google Scholar
• Sparrer HE, Santoso A, Szoka FC Jr., Weissman JS. Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein. Science 2000; 289:595 - 9; http://dx.doi.org/10.1126/science.289.5479.595; PMID: 10915616
   PubMed Web of Science ®Google Scholar
• 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; http://dx.doi.org/10.1038/nature02392; PMID: 15029196
   PubMed Web of Science ®Google Scholar
• Brachmann A, Baxa U, Wickner RB. Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J 2005; 24:3082 - 92; http://dx.doi.org/10.1038/sj.emboj.7600772; PMID: 16096644
   PubMed Web of Science ®Google Scholar
• King CY, Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 2004; 428:319 - 23; http://dx.doi.org/10.1038/nature02391; PMID: 15029195
   PubMed Web of Science ®Google Scholar
• Gauczynski S, Nikles D, El-Gogo S, Papy-Garcia D, Rey C, Alban S, Barritault D, Lasmezas CI, Weiss S. The 37-kDa/67-kDa laminin receptor acts as a receptor for infectious prions and is inhibited by polysulfated glycanes. J Infect Dis 2006; 194:702 - 9; http://dx.doi.org/10.1086/505914; PMID: 16897671
   PubMed Web of Science ®Google Scholar
• Wadia JS, Schaller M, Williamson RA, Dowdy SF. Pathologic prion protein infects cells by lipid-raft dependent macropinocytosis. PLoS One 2008; 3:e3314; http://dx.doi.org/10.1371/journal.pone.0003314; PMID: 19390657
   PubMed Web of Science ®Google Scholar
• Jen A, Parkyn CJ, Mootoosamy RC, Ford MJ, Warley A, Liu Q, Bu G, Baskakov IV, Moestrup S, McGuinness L, et al. Neuronal low-density lipoprotein receptor-related protein 1 binds and endocytoses prion fibrils via receptor cluster 4. J Cell Sci 2010; 123:246 - 55; http://dx.doi.org/10.1242/jcs.058099; PMID: 20048341
   PubMed Web of Science ®Google Scholar
• Münch C, O’Brien J, Bertolotti A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci U S A 2011; 108:3548 - 53; http://dx.doi.org/10.1073/pnas.1017275108; PMID: 21321227
   PubMed Web of Science ®Google Scholar
• Wu JW, Herman M, Liu L, Simoes S, Acker CM, Figueroa H, Steinberg JI, Margittai M, Kayed R, Zurzolo C, et al. Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J Biol Chem 2013; 288:1856 - 70; http://dx.doi.org/10.1074/jbc.M112.394528; PMID: 23188818
   PubMed Web of Science ®Google Scholar
• Holmes BB, Devos SL, Kfoury N, Li M, Jacks R, Yanamandra K, Ouidja MO, Brodsky FM, Marasa J, Bagchi DP, et al. Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc Natl Acad Sci U S A 2013; 110:E3138 - 47; http://dx.doi.org/10.1073/pnas.1301440110; PMID: 23898162
   PubMed Web of Science ®Google Scholar
• Bucciantini M, Nosi D, Forzan M, Russo E, Calamai M, Pieri L, Formigli L, Quercioli F, Soria S, Pavone F, et al. Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1. FASEB J 2012; 26:818 - 31; http://dx.doi.org/10.1096/fj.11-189381; PMID: 22071505
   PubMed Web of Science ®Google Scholar
• Race RE, Fadness LH, Chesebro B. Characterization of scrapie infection in mouse neuroblastoma cells. J Gen Virol 1987; 68:1391 - 9; http://dx.doi.org/10.1099/0022-1317-68-5-1391; PMID: 3106566
   PubMed Web of Science ®Google Scholar
• Butler DA, Scott MR, Bockman JM, Borchelt DR, Taraboulos A, Hsiao KK, Kingsbury DT, Prusiner SB. Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J Virol 1988; 62:1558 - 64; PMID: 3282080
   PubMed Web of Science ®Google Scholar
• Vorberg I, Raines A, Story B, Priola SA. Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents. J Infect Dis 2004; 189:431 - 9; http://dx.doi.org/10.1086/381166; PMID: 14745700
   PubMed Web of Science ®Google Scholar
• Ghaemmaghami S, Phuan PW, Perkins B, Ullman J, May BC, Cohen FE, Prusiner SB. Cell division modulates prion accumulation in cultured cells. Proc Natl Acad Sci U S A 2007; 104:17971 - 6; http://dx.doi.org/10.1073/pnas.0708372104; PMID: 17989223
   PubMed Web of Science ®Google Scholar
• Aguilaniu H, Gustafsson L, Rigoulet M, Nyström T. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 2003; 299:1751 - 3; http://dx.doi.org/10.1126/science.1080418; PMID: 12610228
   PubMed Web of Science ®Google Scholar
• Rujano MA, Bosveld F, Salomons FA, Dijk F, van Waarde MA, van der Want JJ, de Vos RA, Brunt ER, Sibon OC, Kampinga HH. Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes. PLoS Biol 2006; 4:e417; http://dx.doi.org/10.1371/journal.pbio.0040417; PMID: 17147470
   PubMed Web of Science ®Google Scholar
• Parsell DA, Kowal AS, Singer MA, Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 1994; 372:475 - 8; http://dx.doi.org/10.1038/372475a0; PMID: 7984243
   PubMed Web of Science ®Google Scholar
• Weibezahn J, Bukau B, Mogk A. Unscrambling an egg: protein disaggregation by AAA+ proteins. Microb Cell Fact 2004; 3:1; http://dx.doi.org/10.1186/1475-2859-3-1; PMID: 14728719
   PubMed Web of Science ®Google Scholar
• Chernoff YO, Newnam GP, Kumar J, Allen K, Zink AD. Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion. Mol Cell Biol 1999; 19:8103 - 12; PMID: 10567536
   PubMed Web of Science ®Google Scholar
• Kushnirov VV, Kryndushkin DS, Boguta M, Smirnov VN, Ter-Avanesyan MD. Chaperones that cure yeast artificial [PSI+] and their prion-specific effects. Curr Biol 2000; 10:1443 - 6; http://dx.doi.org/10.1016/S0960-9822(00)00802-2; PMID: 11102806
   PubMed Web of Science ®Google Scholar
• Cox B, Ness F, Tuite M. Analysis of the generation and segregation of propagons: entities that propagate the [PSI+] prion in yeast. Genetics 2003; 165:23 - 33; PMID: 14504215
   PubMed Web of Science ®Google Scholar
• Kryndushkin DS, Engel A, Edskes H, Wickner RB. Molecular chaperone Hsp104 can promote yeast prion generation. Genetics 2011; 188:339 - 48; http://dx.doi.org/10.1534/genetics.111.127779; PMID: 21467567
   PubMed Web of Science ®Google Scholar
• Wickner RB. Discovering protein-based inheritance through yeast genetics. J Biol Chem 2012; 287:14432 - 42; http://dx.doi.org/10.1074/jbc.X112.355636; PMID: 22396539
   PubMed Web of Science ®Google Scholar
• Castilla J, Saá P, Hetz C, Soto C. In vitro generation of infectious scrapie prions. Cell 2005; 121:195 - 206; http://dx.doi.org/10.1016/j.cell.2005.02.011; PMID: 15851027
   PubMed Web of Science ®Google Scholar
• Saá P, Castilla J, Soto C. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J Biol Chem 2006; 281:35245 - 52; http://dx.doi.org/10.1074/jbc.M603964200; PMID: 16982620
   PubMed Web of Science ®Google Scholar
• Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol Cell Biol 1999; 19:1325 - 33; PMID: 9891066
   PubMed Web of Science ®Google Scholar
• Murray AN, Solomon JP, Wang YJ, Balch WE, Kelly JW. Discovery and characterization of a mammalian amyloid disaggregation activity. Protein Sci 2010; 19:836 - 46; http://dx.doi.org/10.1002/pro.363; PMID: 20162625
   PubMed Web of Science ®Google Scholar
• Shorter J. The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 2011; 6:e26319; http://dx.doi.org/10.1371/journal.pone.0026319; PMID: 22022600
   PubMed Web of Science ®Google Scholar
• Rampelt H, Kirstein-Miles J, Nillegoda NB, Chi K, Scholz SR, Morimoto RI, Bukau B. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J 2012; 31:4221 - 35; http://dx.doi.org/10.1038/emboj.2012.264; PMID: 22990239
   PubMed Web of Science ®Google Scholar
• Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J 2006; 25:2510 - 8; http://dx.doi.org/10.1038/sj.emboj.7601139; PMID: 16688211
   PubMed Web of Science ®Google Scholar
• Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 2006; 25:2519 - 28; http://dx.doi.org/10.1038/sj.emboj.7601138; PMID: 16688212
   PubMed Web of Science ®Google Scholar
• Yasuda K, Nakai A, Hatayama T, Nagata K. Cloning and expression of murine high molecular mass heat shock proteins, HSP105. J Biol Chem 1995; 270:29718 - 23; http://dx.doi.org/10.1074/jbc.270.50.29718; PMID: 8530361
   PubMed Web of Science ®Google Scholar
• Vos MJ, Hageman J, Carra S, Kampinga HH. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 2008; 47:7001 - 11; http://dx.doi.org/10.1021/bi800639z; PMID: 18557634
   PubMed Web of Science ®Google Scholar
• Duennwald ML, Echeverria A, Shorter J. Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 2012; 10:e1001346; http://dx.doi.org/10.1371/journal.pbio.1001346; PMID: 22723742
   PubMed Web of Science ®Google Scholar
• Aguib Y, Heiseke A, Gilch S, Riemer C, Baier M, Schätzl HM, Ertmer A. Autophagy induction by trehalose counteracts cellular prion infection. Autophagy 2009; 5:361 - 9; http://dx.doi.org/10.4161/auto.5.3.7662; PMID: 19182537
   PubMed Web of Science ®Google Scholar
• Heiseke A, Aguib Y, Riemer C, Baier M, Schätzl HM. Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy. J Neurochem 2009; 109:25 - 34; http://dx.doi.org/10.1111/j.1471-4159.2009.05906.x; PMID: 19183256
   PubMed Web of Science ®Google Scholar
• Nussbaum-Krammer CI, Park KW, Li L, Melki R, Morimoto RI. Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans. PLoS Genet 2013; 9:e1003351; http://dx.doi.org/10.1371/journal.pgen.1003351; PMID: 23555277
   PubMed Web of Science ®Google Scholar
• Paquet S, Langevin C, Chapuis J, Jackson GS, Laude H, Vilette D. Efficient dissemination of prions through preferential transmission to nearby cells. J Gen Virol 2007; 88:706 - 13; http://dx.doi.org/10.1099/vir.0.82336-0; PMID: 17251590
   PubMed Web of Science ®Google Scholar
• Costanzo M, Abounit S, Marzo L, Danckaert A, Chamoun Z, Roux P, Zurzolo C. Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes. J Cell Sci 2013; 126:3678 - 85; http://dx.doi.org/10.1242/jcs.126086; PMID: 23781027
   PubMed Web of Science ®Google Scholar
• Saupe SJ. The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility. Semin Cell Dev Biol 2011; 22:460 - 8; http://dx.doi.org/10.1016/j.semcdb.2011.02.019; PMID: 21334447
   PubMed Web of Science ®Google Scholar
• Michelitsch MD, Weissman JS. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci U S A 2000; 97:11910 - 5; http://dx.doi.org/10.1073/pnas.97.22.11910; PMID: 11050225
   PubMed Web of Science ®Google Scholar
• Lashuel HA, Pappu RV. Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies. Chembiochem 2009; 10:1951 - 4; http://dx.doi.org/10.1002/cbic.200900373; PMID: 19598186
   PubMed Web of Science ®Google Scholar
• 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; http://dx.doi.org/10.1016/j.cell.2009.02.044; PMID: 19345193
   PubMed Web of Science ®Google Scholar
• Toombs JA, McCarty BR, Ross ED. Compositional determinants of prion formation in yeast. Mol Cell Biol 2010; 30:319 - 32; http://dx.doi.org/10.1128/MCB.01140-09; PMID: 19884345
   PubMed Web of Science ®Google Scholar
• Halfmann R, Alberti S, Krishnan R, Lyle N, O’Donnell CW, King OD, Berger B, Pappu RV, Lindquist S. Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Mol Cell 2011; 43:72 - 84; http://dx.doi.org/10.1016/j.molcel.2011.05.013; PMID: 21726811
   PubMed Web of Science ®Google Scholar
• Toombs JA, Petri M, Paul KR, Kan GY, Ben-Hur A, Ross ED. De novo design of synthetic prion domains. Proc Natl Acad Sci U S A 2012; 109:6519 - 24; http://dx.doi.org/10.1073/pnas.1119366109; PMID: 22474356
   PubMed Web of Science ®Google Scholar
• King OD, Gitler AD, Shorter J. The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res 2012; 1462:61 - 80; http://dx.doi.org/10.1016/j.brainres.2012.01.016; PMID: 22445064
   PubMed Web of Science ®Google Scholar
• Kim HJ, Kim NC, Wang YD, Scarborough EA, Moore J, Diaz Z, MacLea KS, Freibaum B, Li S, Molliex A, et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013; 495:467 - 73; http://dx.doi.org/10.1038/nature11922; PMID: 23455423
   PubMed Web of Science ®Google Scholar
• Suzuki G, Shimazu N, Tanaka M. A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress. Science 2012; 336:355 - 9; http://dx.doi.org/10.1126/science.1219491; PMID: 22517861
   PubMed Web of Science ®Google Scholar
• Coustou V, Deleu C, Saupe S, Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci U S A 1997; 94:9773 - 8; http://dx.doi.org/10.1073/pnas.94.18.9773; PMID: 9275200
   PubMed Web of Science ®Google Scholar
• Fowler DM, Koulov AV, Alory-Jost C, Marks MS, Balch WE, Kelly JW. Functional amyloid formation within mammalian tissue. PLoS Biol 2006; 4:e6; http://dx.doi.org/10.1371/journal.pbio.0040006; PMID: 16300414
   PubMed Web of Science ®Google Scholar
• Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, Rissman RA, Singru PS, Nilsson KP, Simon R, Schubert D, et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 2009; 325:328 - 32; http://dx.doi.org/10.1126/science.1173155; PMID: 19541956
   PubMed Web of Science ®Google Scholar
• Goedert M, Clavaguera F, Tolnay M. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci 2010; 33:317 - 25; http://dx.doi.org/10.1016/j.tins.2010.04.003; PMID: 20493564
   PubMed Web of Science ®Google Scholar
• Danzer KM, Krebs SK, Wolff M, Birk G, Hengerer B. Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J Neurochem 2009; 111:192 - 203; http://dx.doi.org/10.1111/j.1471-4159.2009.06324.x; PMID: 19686384
   PubMed Web of Science ®Google Scholar
• Ren PH, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, Kopito RR. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 2009; 11:219 - 25; http://dx.doi.org/10.1038/ncb1830; PMID: 19151706
   PubMed Web of Science ®Google Scholar
• Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 2009; 284:12845 - 52; http://dx.doi.org/10.1074/jbc.M808759200; PMID: 19282288
   PubMed Web of Science ®Google Scholar
• Guo JL, Lee VM. Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem 2011; 286:15317 - 31; http://dx.doi.org/10.1074/jbc.M110.209296; PMID: 21372138
   PubMed Web of Science ®Google Scholar
• Luk KC, Kehm VM, Zhang B, O’Brien P, Trojanowski JQ, Lee VM. Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. J Exp Med 2012; 209:975 - 86; http://dx.doi.org/10.1084/jem.20112457; PMID: 22508839
   PubMed Web of Science ®Google Scholar
• Desplats P, Lee HJ, Bae EJ, Patrick C, Rockenstein E, Crews L, Spencer B, Masliah E, Lee SJ. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci U S A 2009; 106:13010 - 5; http://dx.doi.org/10.1073/pnas.0903691106; PMID: 19651612
   PubMed Web of Science ®Google Scholar
• Clavaguera F, Bolmont T, Crowther RA, Abramowski D, Frank S, Probst A, Fraser G, Stalder AK, Beibel M, Staufenbiel M, et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat Cell Biol 2009; 11:909 - 13; http://dx.doi.org/10.1038/ncb1901; PMID: 19503072
   PubMed Web of Science ®Google Scholar
• Kfoury N, Holmes BB, Jiang H, Holtzman DM, Diamond MI. Trans-cellular propagation of Tau aggregation by fibrillar species. J Biol Chem 2012; 287:19440 - 51; http://dx.doi.org/10.1074/jbc.M112.346072; PMID: 22461630
   PubMed Web of Science ®Google Scholar
• Luk KC, Song C, O’Brien P, Stieber A, Branch JR, Brunden KR, Trojanowski JQ, Lee VM. Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc Natl Acad Sci U S A 2009; 106:20051 - 6; PMID: 19892735
   PubMed Web of Science ®Google Scholar
• Volpicelli-Daley LA, Luk KC, Patel TP, Tanik SA, Riddle DM, Stieber A, Meaney DF, Trojanowski JQ, Lee VM. Exogenous α-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron 2011; 72:57 - 71; http://dx.doi.org/10.1016/j.neuron.2011.08.033; PMID: 21982369
   PubMed Web of Science ®Google Scholar
• Nonaka T, Masuda-Suzukake M, Arai T, Hasegawa Y, Akatsu H, Obi T, Yoshida M, Murayama S, Mann DM, Akiyama H, et al. Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep 2013; 4:124 - 34; http://dx.doi.org/10.1016/j.celrep.2013.06.007; PMID: 23831027
   PubMed Web of Science ®Google Scholar
• Lee HJ, Suk JE, Patrick C, Bae EJ, Cho JH, Rho S, Hwang D, Masliah E, Lee SJ. Direct transfer of alpha-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies. J Biol Chem 2010; 285:9262 - 72; http://dx.doi.org/10.1074/jbc.M109.081125; PMID: 20071342
   PubMed Web of Science ®Google Scholar
• Wang F, Wang X, Yuan CG, Ma J. Generating a prion with bacterially expressed recombinant prion protein. Science 2010; 327:1132 - 5; http://dx.doi.org/10.1126/science.1183748; PMID: 20110469
   PubMed Web of Science ®Google Scholar