The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease

Brain Research

Volumn 1462, Issue , 2012, Pages 61-80

  King, Oliver D ^a   Gitler, Aaron D ^b   Shorter, James ^c  

^a BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Amyotrophic lateral sclerosis; EWSR1; FUS; Neurodegeneration; Prion; RNA binding protein; TAF15; TDP 43

Indexed keywords

ASPARAGINE; FUSED IN SARCOMA PROTEIN; GLUTAMINE; GLYCINE; PRION PROTEIN; PROTEIN EWSR1; PROTEIN TAF15; RNA BINDING PROTEIN; TAR DNA BINDING PROTEIN; TYROSINE; UBIQUITIN; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; AMINO ACID SUBSTITUTION; AMYOTROPHIC LATERAL SCLEROSIS; BRAIN NERVE CELL; CARCINOGENESIS; CELL INCLUSION; CLASSIFICATION ALGORITHM; DEGENERATIVE DISEASE; DISORDERS OF AMINO ACID AND PROTEIN METABOLISM; FRONTOTEMPORAL DEMENTIA; GENE MUTATION; GENE REARRANGEMENT; HEREDITY; HUMAN; HUMAN GENOME; HUNTINGTON CHOREA; LEUKEMIA; MOTONEURON; NEUROPATHOLOGY; NEUROTOXICITY; NONHUMAN; PHENOTYPIC VARIATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN RNA BINDING; REVIEW; SARCOMA;

ALGORITHMS; AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; CALMODULIN-BINDING PROTEINS; DNA-BINDING PROTEINS; FRONTOTEMPORAL LOBAR DEGENERATION; HUMANS; NEURODEGENERATIVE DISEASES; PRIONS; RNA-BINDING PROTEIN FUS; RNA-BINDING PROTEINS; TATA-BINDING PROTEIN ASSOCIATED FACTORS;

EID: 84862151933     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2012.01.016     Document Type: Review

References (201)

1. A. Aguzzi Cell biology: beyond the prion principle Nature 459 2009 924 925
2. A. Aguzzi, and L. Rajendran The transcellular spread of cytosolic amyloids, prions, and prionoids Neuron 64 2009 783 790
3. S. Alberti, R. Halfmann, O. King, A. Kapila, and S. Lindquist A systematic survey identifies prions and illuminates sequence features of prionogenic proteins Cell 137 2009 146 158
4. S. Al-Sarraj, A. King, C. Troakes, B. Smith, S. Maekawa, I. Bodi, B. Rogelj, A. Al-Chalabi, T. Hortobagyi, and C.E. Shaw p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS Acta Neuropathol. 122 2011 691 702
5. T. Arai, M. Hasegawa, H. Akiyama, K. Ikeda, T. Nonaka, H. Mori, D. Mann, K. Tsuchiya, M. Yoshida, Y. Hashizume, and T. Oda TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis Biochem. Biophys. Res. Commun. 351 2006 602 611 (Pubitemid 44708852)
6. P.E. Ash, Y.J. Zhang, C.M. Roberts, T. Saldi, H. Hutter, E. Buratti, L. Petrucelli, and C.D. Link Neurotoxic effects of TDP-43 overexpression in C. elegans Hum. Mol. Genet. 19 2010 3206 3218
7. C. Attwooll, M. Tariq, M. Harris, J.D. Coyne, N. Telford, and J.M. Varley Identification of a novel fusion gene involving hTAFII68 and CHN from a t(9;17)(q22;q11.2) translocation in an extraskeletal myxoid chondrosarcoma Oncogene 18 1999 7599 7601 (Pubitemid 30035062)
8. S.J. Barmada, G. Skibinski, E. Korb, E.J. Rao, J.Y. Wu, and S. Finkbeiner Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis J. Neurosci. 30 2010 639 649
9. D. Baumer, D. Hilton, S.M. Paine, M.R. Turner, J. Lowe, K. Talbot, and O. Ansorge Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations Neurology 75 2010 611 618
10. U. Baxa, V. Speransky, A.C. Steven, and R.B. Wickner Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein Proc. Natl. Acad. Sci. U. S. A. 99 2002 5253 5260 (Pubitemid 34411535)
11. J.E. Bell, S.M. Gentleman, J.W. Ironside, L. McCardle, P.L. Lantos, L. Doey, J. Lowe, J. Fergusson, P. Luthert, S. McQuaid, and I.V. Allen Prion protein immunocytochemistry - UK five centre consensus report Neuropathol. Appl. Neurobiol. 23 1997 26 35 (Pubitemid 27081214)
12. A. Belly, F. Moreau-Gachelin, R. Sadoul, and Y. Goldberg Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads Neurosci. Lett. 379 2005 152 157 (Pubitemid 40544525)
13. V.V. Belzil, P.N. Valdmanis, P.A. Dion, H. Daoud, E. Kabashi, A. Noreau, J. Gauthier, P. Hince, A. Desjarlais, J.P. Bouchard, L. Lacomblez, F. Salachas, P.F. Pradat, W. Camu, V. Meininger, N. Dupre, and G.A. Rouleau Mutations in FUS cause FALS and SALS in French and French Canadian populations Neurology 73 2009 1176 1179
14. A. Bertolotti, Y. Lutz, D.J. Heard, P. Chambon, and L. Tora hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II EMBO J. 15 1996 5022 5031 (Pubitemid 26315812)
15. J. Bieschke, E. Cohen, A. Murray, A. Dillin, and J.W. Kelly A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis Protein Sci. 18 2009 2231 2241
16. I.P. Blair, K.L. Williams, S.T. Warraich, J.C. Durnall, A.D. Thoeng, J. Manavis, P.C. Blumbergs, S. Vucic, M.C. Kiernan, and G.A. Nicholson FUS mutations in amyotrophic lateral sclerosis: clinical, pathological, neurophysiological and genetic analysis J. Neurol. Neurosurg. Psychiatry 81 2010 639 645
17. D.A. Bosco, N. Lemay, H.K. Ko, H. Zhou, C. Burke, T.J. Kwiatkowski Jr., P. Sapp, D. McKenna-Yasek, R.H. Brown Jr., and L.J. Hayward Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules Hum. Mol. Genet. 19 2010 4160 4175
18. A. Brachmann, U. Baxa, and R.B. Wickner Prion generation in vitro: amyloid of Ure2p is infectious EMBO J. 24 2005 3082 3092 (Pubitemid 41486344)
19. O. Broustal, A. Camuzat, L. Guillot-Noel, N. Guy, S. Millecamps, D. Deffond, L. Lacomblez, V. Golfier, D. Hannequin, F. Salachas, W. Camu, M. Didic, B. Dubois, V. Meininger, I. Le Ber, and A. Brice FUS mutations in frontotemporal lobar degeneration with amyotrophic lateral sclerosis J. Alzheimers Dis. 22 2010 765 769
20. P. Brundin, R. Melki, and R. Kopito Prion-like transmission of protein aggregates in neurodegenerative diseases Nat. Rev. Mol. Cell Biol. 11 2010 301 307
21. J.R. Buchan, D. Muhlrad, and R. Parker P bodies promote stress granule assembly in Saccharomyces cerevisiae J. Cell Biol. 183 2008 441 455
22. H. Budka, A. Aguzzi, P. Brown, J.M. Brucher, O. Bugiani, F. Gullotta, M. Haltia, J.J. Hauw, J.W. Ironside, and K. Jellinger Neuropathological diagnostic criteria for Creutzfeldt-Jakob disease (CJD) and other human spongiform encephalopathies (prion diseases) Brain Pathol. 5 1995 459 466
23. E. Buratti, and F.E. Baralle Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease Front. Biosci. 13 2008 867 878 (Pubitemid 351594732)
24. E. Buratti, and F.E. Baralle The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation RNA Biol. 7 2010 420 429
25. A. Caccamo, S. Majumder, and S. Oddo Cognitive decline typical of frontotemporal lobar degeneration in transgenic mice expressing the 25-kDa C-terminal fragment of TDP-43 Am. J. Pathol. 180 2012 293 302
26. A.K. Chen, R.Y. Lin, E.Z. Hsieh, P.H. Tu, R.P. Chen, T.Y. Liao, W. Chen, C.H. Wang, and J.J. Huang Induction of amyloid fibrils by the C-terminal fragments of TDP-43 in amyotrophic lateral sclerosis J. Am. Chem. Soc. 132 2010 1186 1187
27. A.S. Chen-Plotkin, V.M. Lee, and J.Q. Trojanowski TAR DNA-binding protein 43 in neurodegenerative disease Nat. Rev. Neurol. 6 2010 211 220
28. P. Chien, J.S. Weissman, and A.H. DePace Emerging principles of conformation-based prion inheritance Annu. Rev. Biochem. 73 2004 617 656 (Pubitemid 39050382)
29. A. Chio, G. Benzi, M. Dossena, R. Mutani, and G. Mora Severely increased risk of amyotrophic lateral sclerosis among Italian professional football players Brain 128 2005 472 476 (Pubitemid 40380183)
30. F. Clavaguera, T. Bolmont, R.A. Crowther, D. Abramowski, S. Frank, A. Probst, G. Fraser, A.K. Stalder, M. Beibel, M. Staufenbiel, M. Jucker, M. Goedert, and M. Tolnay Transmission and spreading of tauopathy in transgenic mouse brain Nat. Cell Biol. 11 2009 909 913
31. E. Cohen, J. Bieschke, R.M. Perciavalle, J.W. Kelly, and A. Dillin Opposing activities protect against age-onset proteotoxicity Science 313 2006 1604 1610 (Pubitemid 44414028)
32. D.W. Colby, and S.B. Prusiner De novo generation of prion strains Nat. Rev. Microbiol. 9 2011 771 777
33. D.W. Colby, K. Giles, G. Legname, H. Wille, I.V. Baskakov, S.J. DeArmond, and S.B. Prusiner Design and construction of diverse mammalian prion strains Proc. Natl. Acad. Sci. U. S. A. 106 2009 20417 20422
34. D.W. Colby, R. Wain, I.V. Baskakov, G. Legname, C.G. Palmer, H.O. Nguyen, A. Lemus, F.E. Cohen, S.J. DeArmond, and S.B. Prusiner Protease-sensitive synthetic prions PLoS Pathog. 6 2010 e1000736
35. J. Collinge, and A.R. Clarke A general model of prion strains and their pathogenicity Science 318 2007 930 936 (Pubitemid 350098981)
36. L. Corrado, R. Del Bo, B. Castellotti, A. Ratti, C. Cereda, S. Penco, G. Soraru, Y. Carlomagno, S. Ghezzi, V. Pensato, C. Colombrita, S. Gagliardi, L. Cozzi, V. Orsetti, M. Mancuso, G. Siciliano, L. Mazzini, G.P. Comi, C. Gellera, M. Ceroni, S. D'Alfonso, and V. Silani Mutations of FUS gene in sporadic amyotrophic lateral sclerosis J. Med. Genet. 47 2010 190 194
37. J. Couthouis, M.P. Hart, J. Shorter, M. Dejesus-Hernandez, R. Erion, R. Oristano, A.X. Liu, D. Ramos, N. Jethava, D. Hosangadi, J. Epstein, A. Chiang, Z. Diaz, T. Nakaya, F. Ibrahim, H.J. Kim, J.A. Solski, K.L. Williams, J. Mojsilovic-Petrovic, C. Ingre, K. Boylan, N.R. Graff-Radford, D.W. Dickson, D. Clay-Falcone, L. Elman, L. McCluskey, R. Greene, R.G. Kalb, V.M. Lee, J.Q. Trojanowski, A. Ludolph, W. Robberecht, P.M. Andersen, G.A. Nicholson, I.P. Blair, O.D. King, N.M. Bonini, V. Van Deerlin, R. Rademakers, Z. Mourelatos, and A.D. Gitler Feature article: a yeast functional screen predicts new candidate ALS disease genes Proc. Natl. Acad. Sci. U. S. A. 108 2011 20881 20890
38. P.A. Cox, R. Richer, J.S. Metcalf, S.A. Banack, G.A. Codd, and W.G. Bradley Cyanobacteria and BMAA exposure from desert dust: a possible link to sporadic ALS among Gulf War veterans Amyotroph. Lateral Scler. 10 Suppl. 2 2009 109 117
39. E.T. Crow, Z. Du, and L. Li A small, glutamine-free domain propagates the [SWI(+)] prion in budding yeast Mol. Cell. Biol. 31 2011 3436 3444
40. A. Crozat, P. Aman, N. Mandahl, and D. Ron Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma Nature 363 1993 640 644 (Pubitemid 23227627)
41. M. Cushman, B.S. Johnson, O.D. King, A.D. Gitler, and J. Shorter Prion-like disorders: blurring the divide between transmissibility and infectivity J. Cell Sci. 123 2010 1191 1201
42. S. Da Cruz, and D.W. Cleveland Understanding the role of TDP-43 and FUS/TLS in ALS and beyond Curr. Opin. Neurobiol. 21 2011 904 919
43. M. DeJesus-Hernandez, J. Kocerha, N. Finch, R. Crook, M. Baker, P. Desaro, A. Johnston, N. Rutherford, A. Wojtas, K. Kennelly, Z.K. Wszolek, N. Graff-Radford, K. Boylan, and R. Rademakers De novo truncating FUS gene mutation as a cause of sporadic amyotrophic lateral sclerosis Hum. Mutat. 31 2010 E1377 E1389
44. M. DeJesus-Hernandez, I.R. Mackenzie, B.F. Boeve, A.L. Boxer, M. Baker, N.J. Rutherford, A.M. Nicholson, N.A. Finch, H. Flynn, J. Adamson, N. Kouri, A. Wojtas, P. Sengdy, G.Y. Hsiung, A. Karydas, W.W. Seeley, K.A. Josephs, G. Coppola, D.H. Geschwind, Z.K. Wszolek, H. Feldman, D.S. Knopman, R.C. Petersen, B.L. Miller, D.W. Dickson, K.B. Boylan, N.R. Graff-Radford, and R. Rademakers Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS Neuron 72 2011 245 256
45. O. Delattre, J. Zucman, B. Plougastel, C. Desmaze, T. Melot, M. Peter, H. Kovar, I. Joubert, P. de Jong, and G. Rouleau Gene fusion with an ETS DNA-binding domain caused by chromosome translocation in human tumours Nature 359 1992 162 165
46. N.R. Deleault, R.W. Lucassen, and S. Supattapone RNA molecules stimulate prion protein conversion Nature 425 2003 717 720 (Pubitemid 37314314)
47. M.E. DeSantis, and J. Shorter The elusive middle domain of Hsp104 and ClpB: location and function Biochim. Biophys. Acta 1823 2012 29 39
48. P. Desplats, H.J. Lee, E.J. Bae, C. Patrick, E. Rockenstein, L. Crews, B. Spencer, E. Masliah, and S.J. Lee Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein Proc. Natl. Acad. Sci. U. S. A. 106 2009 13010 13015
49. H. Doi, S. Koyano, Y. Suzuki, N. Nukina, and Y. Kuroiwa The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases Neurosci. Res. 66 2010 131 133
50. D. Dormann, and C. Haass TDP-43 and FUS: a nuclear affair Trends Neurosci. 2011 doi: 10.1016/j.tins.2011.05.02
51. D. Dormann, R. Rodde, D. Edbauer, E. Bentmann, I. Fischer, A. Hruscha, M.E. Than, I.R. Mackenzie, A. Capell, B. Schmid, M. Neumann, and C. Haass ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import EMBO J. 29 2010 2841 2857
52. C. Drepper, T. Herrmann, C. Wessig, M. Beck, and M. Sendtner C-terminal FUS/TLS mutations in familial and sporadic ALS in Germany Neurobiol. Aging 32 548 2011 e1 e4
53. Z. Du, K.W. Park, H. Yu, Q. Fan, and L. Li Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae Nat. Genet. 40 2008 460 465 (Pubitemid 351450881)
54. M.L. Duennwald, and J. Shorter Countering amyloid polymorphism and drug resistance with minimal drug cocktails Prion 4 2010 244 251
55. C.J. Dunning, J.F. Reyes, J.A. Steiner, and P. Brundin Can Parkinson's disease pathology be propagated from one neuron to another? Prog Neurobiol. 2011 doi: 10.1016/j.pneurobio.2011.11.003
56. S.S. Eaglestone, B.S. Cox, and M.F. Tuite Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism EMBO J. 18 1999 1974 1981 (Pubitemid 29158540)
57. Y.S. Eisele, U. Obermuller, G. Heilbronner, F. Baumann, S.A. Kaeser, H. Wolburg, L.C. Walker, M. Staufenbiel, M. Heikenwalder, and M. Jucker Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis Science 330 2010 980 982
58. A.C. Elden, H.J. Kim, M.P. Hart, A.S. Chen-Plotkin, B.S. Johnson, X. Fang, M. Armakola, F. Geser, R. Greene, M.M. Lu, A. Padmanabhan, D. Clay-Falcone, L. McCluskey, L. Elman, D. Juhr, P.J. Gruber, U. Rub, G. Auburger, J.Q. Trojanowski, V.M. Lee, V.M. Van Deerlin, N.M. Bonini, and A.D. Gitler Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS Nature 466 2010 1069 1075
59. G.R. Fink A transforming principle Cell 120 2005 153 154 (Pubitemid 40174755)
60. F. Fiumara, L. Fioriti, E.R. Kandel, and W.A. Hendrickson Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins Cell 143 2010 1121 1135
61. R.A. Fuentealba, M. Udan, S. Bell, I. Wegorzewska, J. Shao, M.I. Diamond, C.C. Weihl, and R.H. Baloh Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43 J. Biol. Chem. 285 2010 26304 26314
62. R. Fujii, and T. Takumi TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines J. Cell Sci. 118 2005 5755 5765 (Pubitemid 43079269)
63. R. Fujii, S. Okabe, T. Urushido, K. Inoue, A. Yoshimura, T. Tachibana, T. Nishikawa, G.G. Hicks, and T. Takumi The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology Curr. Biol. 15 2005 587 593 (Pubitemid 40413401)
64. Y. Furukawa, K. Kaneko, S. Watanabe, K. Yamanaka, and N. Nukina A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions J. Biol. Chem. 286 2011 18664 18672
65. K. Fushimi, C. Long, N. Jayaram, X. Chen, L. Li, and J.Y. Wu Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy Protein Cell 2 2011 141 149
66. D.M. Gendoo, and P.M. Harrison Origins and evolution of the HET-s prion-forming protein: searching for other amyloid-forming solenoids PLoS One 6 2011 e27342
67. S. Ghaemmaghami, M. Ahn, P. Lessard, K. Giles, G. Legname, S.J. DeArmond, and S.B. Prusiner Continuous quinacrine treatment results in the formation of drug-resistant prions PLoS Pathog. 5 2009 e1000673
68. I. Gijselinck, T. Van Langenhove, J. van der Zee, K. Sleegers, S. Philtjens, G. Kleinberger, J. Janssens, K. Bettens, C. Van Cauwenberghe, S. Pereson, S. Engelborghs, A. Sieben, P. De Jonghe, R. Vandenberghe, P. Santens, J. De Bleecker, G. Maes, V. Baumer, L. Dillen, G. Joris, I. Cuijt, E. Corsmit, E. Elinck, J. Van Dongen, S. Vermeulen, M. Van den Broeck, C. Vaerenberg, M. Mattheijssens, K. Peeters, W. Robberecht, P. Cras, J.J. Martin, P.P. De Deyn, M. Cruts, and C. Van Broeckhoven A C9orf72 promoter repeat expansion in a Flanders-Belgian cohort with disorders of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum: a gene identification study Lancet Neurol. 11 2012 54 65
69. N. Gilks, N. Kedersha, M. Ayodele, L. Shen, G. Stoecklin, L.M. Dember, and P. Anderson Stress granule assembly is mediated by prion-like aggregation of TIA-1 Mol. Biol. Cell 15 2004 5383 5398 (Pubitemid 39564732)
70. A.D. Gitler Beer and bread to brains and beyond: can yeast cells teach us about neurodegenerative disease? Neurosignals 16 2008 52 62 (Pubitemid 350308321)
71. A.D. Gitler, and J. Shorter RNA-binding proteins with prion-like domains in ALS and FTLD-U Prion 5 2011 179 187
72. M. Goedert, F. Clavaguera, and M. Tolnay The propagation of prion-like protein inclusions in neurodegenerative diseases Trends Neurosci. 33 2010 317 325
73. L. Goldschmidt, P.K. Teng, R. Riek, and D. Eisenberg Identifying the amylome, proteins capable of forming amyloid-like fibrils Proc. Natl. Acad. Sci. U. S. A. 107 2010 3487 3492
74. Z. Guo, and D. Eisenberg Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I Proc. Natl. Acad. Sci. U. S. A. 103 2006 8042 8047 (Pubitemid 43801049)
75. W. Guo, Y. Chen, X. Zhou, A. Kar, P. Ray, X. Chen, E.J. Rao, M. Yang, H. Ye, L. Zhu, J. Liu, M. Xu, Y. Yang, C. Wang, D. Zhang, E.H. Bigio, M. Mesulam, Y. Shen, Q. Xu, K. Fushimi, and J.Y. Wu An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity Nat. Struct. Mol. Biol. 18 2011 822 830
76. S. Haider, B. Ballester, D. Smedley, J. Zhang, P. Rice, and A. Kasprzyk BioMart Central Portal - unified access to biological data Nucleic Acids Res. 37 2009 W23 W27
77. R. Halfmann, and S. Lindquist Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits Science 330 2010 629 632
78. R. Halfmann, S. Alberti, and S. Lindquist Prions, protein homeostasis, and phenotypic diversity Trends Cell Biol. 20 2010 125 133
79. R. Halfmann, S. Alberti, R. Krishnan, N. Lyle, C.W. O'Donnell, O.D. King, B. Berger, R.V. Pappu, and S. Lindquist Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins Mol. Cell 43 2011 72 84
80. P.M. Harrison, and M. Gerstein A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes Genome Biol. 4 2003 R40
81. S.U. Heinrich, and S. Lindquist Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB) Proc. Natl. Acad. Sci. U. S. A. 108 2011 2999 3004
82. C. Hewitt, J. Kirby, J.R. Highley, J.A. Hartley, R. Hibberd, H.C. Hollinger, T.L. Williams, P.G. Ince, C.J. McDermott, and P.J. Shaw Novel FUS/TLS mutations and pathology in familial and sporadic amyotrophic lateral sclerosis Arch. Neurol. 67 2010 455 461
83. J.I. Hoell, E. Larsson, S. Runge, J.D. Nusbaum, S. Duggimpudi, T.A. Farazi, M. Hafner, A. Borkhardt, C. Sander, and T. Tuschl RNA targets of wild-type and mutant FET family proteins Nat. Struct. Mol. Biol. 18 2011 1428 1431
84. E.J. Huang, J. Zhang, F. Geser, J.Q. Trojanowski, J.B. Strober, D.W. Dickson, R.H. Brown Jr., B.E. Shapiro, and C. Lomen-Hoerth Extensive FUS-immunoreactive pathology in juvenile amyotrophic lateral sclerosis with basophilic inclusions Brain Pathol. 20 2010 1069 1076
85. C.K. Iwahashi, D.H. Yasui, H.J. An, C.M. Greco, F. Tassone, K. Nannen, B. Babineau, C.B. Lebrilla, R.J. Hagerman, and P.J. Hagerman Protein composition of the intranuclear inclusions of FXTAS Brain 129 2006 256 271 (Pubitemid 43063776)
86. B.S. Johnson, J.M. McCaffery, S. Lindquist, and A.D. Gitler A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity Proc. Natl. Acad. Sci. U. S. A. 105 2008 6439 6444 (Pubitemid 351758364)
87. B.S. Johnson, D. Snead, J.J. Lee, J.M. McCaffery, J. Shorter, and A.D. Gitler TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity J. Biol. Chem. 284 2009 20329 20339
88. J.O. Johnson, J. Mandrioli, M. Benatar, Y. Abramzon, V.M. Van Deerlin, J.Q. Trojanowski, J.R. Gibbs, M. Brunetti, S. Gronka, J. Wuu, J. Ding, L. McCluskey, M. Martinez-Lage, D. Falcone, D.G. Hernandez, S. Arepalli, S. Chong, J.C. Schymick, J. Rothstein, F. Landi, Y.D. Wang, A. Calvo, G. Mora, M. Sabatelli, M.R. Monsurro, S. Battistini, F. Salvi, R. Spataro, P. Sola, G. Borghero, G. Galassi, S.W. Scholz, J.P. Taylor, G. Restagno, A. Chio, and B.J. Traynor Exome sequencing reveals VCP mutations as a cause of familial ALS Neuron 68 2010 857 864
89. S. Ju, D.F. Tardiff, H. Han, K. Divya, Q. Zhong, D.A. Bosco, L.J. Hayward, R.H. Brown Jr., S.L. Lindquist, D. Ringe, and G.A. Petsko A yeast model of FUS/TLS-dependent cytotoxicity PLoS Biol. 9 2011 e1001052
90. E. Kabashi, L. Lin, M.L. Tradewell, P.A. Dion, V. Bercier, P. Bourgouin, D. Rochefort, S. Bel Hadj, H.D. Durham, C. Vande Velde, G.A. Rouleau, and P. Drapeau Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo Hum. Mol. Genet. 19 2010 671 683
91. C.S. Kasyapa, P. Kunapuli, and J.K. Cowell Mass spectroscopy identifies the splicing-associated proteins, PSF, hnRNP H3, hnRNP A2/B1, and TLS/FUS as interacting partners of the ZNF198 protein associated with rearrangement in myeloproliferative disease Exp. Cell Res. 309 2005 78 85 (Pubitemid 41191225)
92. R. Kayed, E. Head, J.L. Thompson, T.M. McIntire, S.C. Milton, C.W. Cotman, and C.G. Glabe Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 486 489 (Pubitemid 36444329)
93. K. Keleman, S. Kruttner, M. Alenius, and B.J. Dickson Function of the Drosophila CPEB protein Orb2 in long-term courtship memory Nat. Neurosci. 10 2007 1587 1593 (Pubitemid 350175870)
94. D.J. Kenan, C.C. Query, and J.D. Keene RNA recognition: towards identifying determinants of specificity Trends Biochem. Sci. 16 1991 214 220 (Pubitemid 121004438)
95. C.Y. King, and R. Diaz-Avalos Protein-only transmission of three yeast prion strains Nature 428 2004 319 323 (Pubitemid 38418802)
96. D. Kryndushkin, R.B. Wickner, and F. Shewmaker FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis Protein Cell 2 2011 223 236
97. T.J. Kwiatkowski Jr., D.A. Bosco, A.L. Leclerc, E. Tamrazian, C.R. Vanderburg, C. Russ, A. Davis, J. Gilchrist, E.J. Kasarskis, T. Munsat, P. Valdmanis, G.A. Rouleau, B.A. Hosler, P. Cortelli, P.J. de Jong, Y. Yoshinaga, J.L. Haines, M.A. Pericak-Vance, J. Yan, N. Ticozzi, T. Siddique, D. McKenna-Yasek, P.C. Sapp, H.R. Horvitz, J.E. Landers, and R.H. Brown Jr. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis Science 323 2009 1205 1208
98. L.K. Kwong, K. Uryu, J.Q. Trojanowski, and V.M. Lee TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis Neurosignals 16 2008 41 51 (Pubitemid 350308320)
99. C. Lagier-Tourenne, and D.W. Cleveland Rethinking ALS: the FUS about TDP-43 Cell 136 2009 1001 1004
100. A.K. Lancaster, J.P. Bardill, H.L. True, and J. Masel 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 2010 393 400
101. H.A. Lashuel, D. Hartley, B.M. Petre, T. Walz, and P.T. Lansbury Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations Nature 418 2002 291 (Pubitemid 34790672)
102. S. Lee, and D. Eisenberg Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process Nat. Struct. Biol. 10 2003 725 730 (Pubitemid 37052411)
103. B.J. Lee, A.E. Cansizoglu, K.E. Suel, T.H. Louis, Z. Zhang, and Y.M. Chook Rules for nuclear localization sequence recognition by karyopherin beta 2 Cell 126 2006 543 558 (Pubitemid 44163605)
104. E.B. Lee, V.M. Lee, and J.Q. Trojanowski Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration Nat. Rev. Neurosci. 13 2011 38 50
105. G. Legname, I.V. Baskakov, H.O. Nguyen, D. Riesner, F.E. Cohen, S.J. DeArmond, and S.B. Prusiner Synthetic mammalian prions Science 305 2004 673 676 (Pubitemid 39006757)
106. L. Li, and S. Lindquist Creating a protein-based element of inheritance Science 287 2000 661 664 (Pubitemid 30070915)
107. J. Li, S. Browning, S.P. Mahal, A.M. Oelschlegel, and C. Weissmann Darwinian evolution of prions in cell culture Science 327 2010 869 872
108. Y. Li, P. Ray, E.J. Rao, C. Shi, W. Guo, X. Chen, E.A. Woodruff III, K. Fushimi, and J.Y. Wu A Drosophila model for TDP-43 proteinopathy Proc. Natl. Acad. Sci. U. S. A. 107 2010 3169 3174
109. J. Li, S.P. Mahal, C.A. Demczyk, and C. Weissmann Mutability of prions EMBO Rep. 12 2011 1243 1250
110. Y. Liu, and D. Eisenberg 3D domain swapping: as domains continue to swap Protein Sci. 11 2002 1285 1299 (Pubitemid 34547201)
111. L. Liu-Yesucevitz, A. Bilgutay, Y.J. Zhang, T. Vanderweyde, A. Citro, T. Mehta, N. Zaarur, A. McKee, R. Bowser, M. Sherman, L. Petrucelli, and B. Wolozin Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue PLoS One 5 2010 e13250
112. L. Liu-Yesucevitz, G.J. Bassell, A.D. Gitler, A.C. Hart, E. Klann, J.D. Richter, S.T. Warren, and B. Wolozin Local RNA translation at the synapse and in disease J. Neurosci. 31 2011 16086 16093
113. I.R. Mackenzie, R. Rademakers, and M. Neumann TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia Lancet Neurol. 9 2010 995 1007
114. K.S. Maclea, and E.D. Ross Strategies for identifying new prions in yeast Prion 5 2011
115. E. Majounie, Y. Abramzon, A.E. Renton, R. Perry, S.S. Bassett, O. Pletnikova, J.C. Troncoso, J. Hardy, A.B. Singleton, and B.J. Traynor Repeat expansion in C9ORF72 in Alzheimer's disease N Engl J. Med. 366 2012 283 284
116. J. Masel, and A. Bergman The evolution of the evolvability properties of the yeast prion [PSI +] Evolution 57 2003 1498 1512 (Pubitemid 36953639)
117. J. Masel, and C.K. Griswold The strength of selection against the yeast prion [PSI +] Genetics 181 2009 1057 1063
118. D.C. Masison, and R.B. Wickner Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells Science 270 1995 93 95
119. D.C. Masison, M.L. Maddelein, and R.B. Wickner The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation Proc. Natl. Acad. Sci. U. S. A. 94 1997 12503 12508 (Pubitemid 27492558)
120. R.P. McGlinchey, D. Kryndushkin, and R.B. Wickner Suicidal [PSI +] is a lethal yeast prion Proc. Natl. Acad. Sci. U. S. A. 108 2011 5337 5341
121. M. Meyer-Luehmann, J. Coomaraswamy, T. Bolmont, S. Kaeser, C. Schaefer, E. Kilger, A. Neuenschwander, D. Abramowski, P. Frey, A.L. Jaton, J.M. Vigouret, P. Paganetti, D.M. Walsh, P.M. Mathews, J. Ghiso, M. Staufenbiel, L.C. Walker, and M. Jucker Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host Science 313 2006 1781 1784 (Pubitemid 44454153)
122. M.D. Michelitsch, and J.S. Weissman 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. 97 2000 11910 11915
123. D.G. Munoz, M. Neumann, H. Kusaka, O. Yokota, K. Ishihara, S. Terada, S. Kuroda, and I.R. Mackenzie FUS pathology in basophilic inclusion body disease Acta Neuropathol. 118 2009 617 627
124. M.E. Murray, M. Dejesus-Hernandez, N.J. Rutherford, M. Baker, R. Duara, N.R. Graff-Radford, Z.K. Wszolek, T.J. Ferman, K.A. Josephs, K.B. Boylan, R. Rademakers, and D.W. Dickson Clinical and neuropathologic heterogeneity of c9FTD/ALS associated with hexanucleotide repeat expansion in C9ORF72 Acta Neuropathol. 122 2011 673 690
125. T. Nakayashiki, C.P. Kurtzman, H.K. Edskes, and R.B. Wickner Yeast prions [URE3] and [PSI +] are diseases Proc. Natl. Acad. Sci. U. S. A. 102 2005 10575 10580 (Pubitemid 41061596)
126. O. Namy, A. Galopier, C. Martini, S. Matsufuji, C. Fabret, and J.P. Rousset Epigenetic control of polyamines by the prion [PSI +] Nat. Cell Biol. 10 2008 1069 1075
127. R. Nelson, and D. Eisenberg Structural models of amyloid-like fibrils Adv. Protein Chem. 73 2006 235 282 (Pubitemid 44960406)
128. M. Neumann, D.M. Sampathu, L.K. Kwong, A.C. Truax, M.C. Micsenyi, T.T. Chou, J. Bruce, T. Schuck, M. Grossman, C.M. Clark, L.F. McCluskey, B.L. Miller, E. Masliah, I.R. Mackenzie, H. Feldman, W. Feiden, H.A. Kretzschmar, J.Q. Trojanowski, and V.M. Lee Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis Science 314 2006 130 133 (Pubitemid 44547757)
129. M. Neumann, R. Rademakers, S. Roeber, M. Baker, H.A. Kretzschmar, and I.R. Mackenzie A new subtype of frontotemporal lobar degeneration with FUS pathology Brain 132 2009 2922 2931
130. M. Neumann, E. Bentmann, D. Dormann, A. Jawaid, M. DeJesus-Hernandez, O. Ansorge, S. Roeber, H.A. Kretzschmar, D.G. Munoz, H. Kusaka, O. Yokota, L.C. Ang, J. Bilbao, R. Rademakers, C. Haass, and I.R. Mackenzie FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations Brain 134 2011 2595 2609
131. N.L. Ogihara, G. Ghirlanda, J.W. Bryson, M. Gingery, W.F. DeGrado, and D. Eisenberg Design of three-dimensional domain-swapped dimers and fibrous oligomers Proc. Natl. Acad. Sci. U. S. A. 98 2001 1404 1409 (Pubitemid 32165511)
132. L.Z. Osherovich, and J.S. Weissman Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion Cell 106 2001 183 194 (Pubitemid 32772629)
133. B.K. Patel, and S.W. Liebman Prion-proof for [PIN +]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN +] J. Mol. Biol. 365 2007 773 782 (Pubitemid 44960370)
134. B.K. Patel, J. Gavin-Smyth, and S.W. Liebman The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion Nat. Cell Biol. 11 2009 344 349
135. G.S. Pesiridis, K. Tripathy, S. Tanik, J.Q. Trojanowski, and V.M. Lee A Two-hit hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport J. Biol. Chem. 286 2011 18845 18855
136. J.R. Piro, F. Wang, D.J. Walsh, J.R. Rees, J. Ma, and S. Supattapone Seeding specificity and ultrastructural characteristics of infectious recombinant prions Biochemistry 50 2011 7111 7116
137. M. Polymenidou, and D.W. Cleveland The seeds of neurodegeneration: prion-like spreading in ALS Cell 147 2011 498 508
138. M. Polymenidou, C. Lagier-Tourenne, K.R. Hutt, S.C. Huelga, J. Moran, T.Y. Liang, S.C. Ling, E. Sun, E. Wancewicz, C. Mazur, H. Kordasiewicz, Y. Sedaghat, J.P. Donohue, L. Shiue, C.F. Bennett, G.W. Yeo, and D.W. Cleveland Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43 Nat. Neurosci. 14 2011 459 468
139. J. Prilusky, C.E. Felder, T. Zeev-Ben-Mordehai, E.H. Rydberg, O. Man, J.S. Beckmann, I. Silman, and J.L. Sussman FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded Bioinformatics 21 2005 3435 3438 (Pubitemid 41222454)
140. S.B. Prusiner Some speculations about prions, amyloid, and Alzheimer's disease N. Engl. J. Med. 310 1984 661 663 (Pubitemid 14194391)
141. R. Rademakers, H. Stewart, M. Dejesus-Hernandez, C. Krieger, N. Graff-Radford, M. Fabros, H. Briemberg, N. Cashman, A. Eisen, and I.R. Mackenzie Fus gene mutations in familial and sporadic amyotrophic lateral sclerosis Muscle Nerve 42 2010 170 176
142. J.M. Ravits, and A.R. La Spada ALS motor phenotype heterogeneity, focality, and spread: deconstructing motor neuron degeneration Neurology 73 2009 805 811
143. A.E. Renton, E. Majounie, A. Waite, J. Simon-Sanchez, S. Rollinson, J.R. Gibbs, J.C. Schymick, H. Laaksovirta, J.C. van Swieten, L. Myllykangas, H. Kalimo, A. Paetau, Y. Abramzon, A.M. Remes, A. Kaganovich, S.W. Scholz, J. Duckworth, J. Ding, D.W. Harmer, D.G. Hernandez, J.O. Johnson, K. Mok, M. Ryten, D. Trabzuni, R.J. Guerreiro, R.W. Orrell, J. Neal, A. Murray, J. Pearson, I.E. Jansen, D. Sondervan, H. Seelaar, D. Blake, K. Young, N. Halliwell, J.B. Callister, G. Toulson, A. Richardson, A. Gerhard, J. Snowden, D. Mann, D. Neary, M.A. Nalls, T. Peuralinna, L. Jansson, V.M. Isoviita, A.L. Kaivorinne, M. Holtta-Vuori, E. Ikonen, R. Sulkava, M. Benatar, J. Wuu, A. Chio, G. Restagno, G. Borghero, M. Sabatelli, D. Heckerman, E. Rogaeva, L. Zinman, J.D. Rothstein, M. Sendtner, C. Drepper, E.E. Eichler, C. Alkan, Z. Abdullaev, S.D. Pack, A. Dutra, E. Pak, J. Hardy, A. Singleton, N.M. Williams, P. Heutink, S. Pickering-Brown, H.R. Morris, P.J. Tienari, and B.J. Traynor A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD Neuron 72 2011 257 268
144. G.P. Ritson, S.K. Custer, B.D. Freibaum, J.B. Guinto, D. Geffel, J. Moore, W. Tang, M.J. Winton, M. Neumann, J.Q. Trojanowski, V.M. Lee, M.S. Forman, and J.P. Taylor TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97 J. Neurosci. 30 2010 7729 7739
145. B.E. Roberts, M.L. Duennwald, H. Wang, C. Chung, N.P. Lopreiato, E.A. Sweeny, M.N. Knight, and J. Shorter A synergistic small-molecule combination directly eradicates diverse prion strain structures Nat. Chem. Biol. 5 2009 936 946
146. T. Rogoza, A. Goginashvili, S. Rodionova, M. Ivanov, O. Viktorovskaya, A. Rubel, K. Volkov, and L. Mironova 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. 107 2010 10573 10577
147. E.D. Ross, U. Baxa, and R.B. Wickner Scrambled prion domains form prions and amyloid Mol. Cell. Biol. 24 2004 7206 7213 (Pubitemid 39014446)
148. E.D. Ross, H.K. Edskes, M.J. Terry, and R.B. Wickner Primary sequence independence for prion formation Proc. Natl. Acad. Sci. U. S. A. 102 2005 12825 12830 (Pubitemid 41279450)
149. A. Saini, and V.S. Chauhan Delineation of the core aggregation sequences of TDP-43 C-terminal fragment Chembiochem 12 2011 2495 2501
150. A.B. Salnikova, D.S. Kryndushkin, V.N. Smirnov, V.V. Kushnirov, and M.D. Ter-Avanesyan Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids J. Biol. Chem. 280 2005 8808 8812 (Pubitemid 40409569)
151. A. Santoso, P. Chien, L.Z. Osherovich, and J.S. Weissman Molecular basis of a yeast prion species barrier Cell 100 2000 277 288 (Pubitemid 30064915)
152. S.J. Saupe A short history of small s: a prion of the fungus Podospora anserina Prion 1 2007 110 115
153. M.R. Sawaya, S. Sambashivan, R. Nelson, M.I. Ivanova, S.A. Sievers, M.I. Apostol, M.J. Thompson, M. Balbirnie, J.J. Wiltzius, H.T. McFarlane, A.O. Madsen, C. Riekel, and D. Eisenberg Atomic structures of amyloid cross-beta spines reveal varied steric zippers Nature 447 2007 453 457 (Pubitemid 46816731)
154. T.R. Serio, A.G. Cashikar, A.S. Kowal, G.J. Sawicki, J.J. Moslehi, L. Serpell, M.F. Arnsdorf, and S.L. Lindquist Nucleated conformational conversion and the replication of conformational information by a prion determinant Science 289 2000 1317 1321 (Pubitemid 30656041)
155. J. Shorter Hsp104: a weapon to combat diverse neurodegenerative disorders Neurosignals 16 2008 63 74 (Pubitemid 350308322)
156. J. Shorter Emergence and natural selection of drug-resistant prions Mol. Biosyst. 6 2010 1115 1130
157. J. Shorter The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system PLoS One 6 2011 e26319
158. J. Shorter, and S. Lindquist Prions as adaptive conduits of memory and inheritance Nat. Rev. Genet. 6 2005 435 450 (Pubitemid 40733889)
159. J. Shorter, and S. Lindquist Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities Mol. Cell 23 2006 425 438 (Pubitemid 44128844)
160. K. Si, S. Lindquist, and E.R. Kandel A neuronal isoform of the Aplysia CPEB has prion-like properties Cell 115 2003 879 891 (Pubitemid 38058499)
161. K. Si, Y.B. Choi, E. White-Grindley, A. Majumdar, and E.R. Kandel Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation Cell 140 2010 421 435
162. O.A. Sofola, P. Jin, Y. Qin, R. Duan, H. Liu, M. de Haro, D.L. Nelson, and J. Botas RNA-binding proteins hnRNP A2/B1 and CUGBP1 suppress fragile X CGG premutation repeat-induced neurodegeneration in a Drosophila model of FXTAS Neuron 55 2007 565 571 (Pubitemid 47223640)
163. N. Sondheimer, and S. Lindquist Rnq1: an epigenetic modifier of protein function in yeast Mol. Cell 5 2000 163 172 (Pubitemid 30105445)
164. J. Sreedharan, I.P. Blair, V.B. Tripathi, X. Hu, C. Vance, B. Rogelj, S. Ackerley, J.C. Durnall, K.L. Williams, E. Buratti, F. Baralle, J. de Belleroche, J.D. Mitchell, P.N. Leigh, A. Al-Chalabi, C.C. Miller, G. Nicholson, and C.E. Shaw TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis Science 319 2008 1668 1672 (Pubitemid 351432505)
165. K.E. Suel, H. Gu, and Y.M. Chook Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals PLoS Biol. 6 2008 e137
166. Z. Sun, Z. Diaz, X. Fang, M.P. Hart, A. Chesi, J. Shorter, and A.D. Gitler Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS PLoS Biol. 9 2011 e1000614
167. E.A. Sweeny, and J. Shorter Prion proteostasis: Hsp104 meets its supporting cast Prion 2 2008 135 140
168. A.Y. Tan, and J.L. Manley The TET family of proteins: functions and roles in disease J. Mol. Cell Biol. 1 2009 82 92
169. M. Tanaka, P. Chien, N. Naber, R. Cooke, and J.S. Weissman Conformational variations in an infectious protein determine prion strain differences Nature 428 2004 323 328 (Pubitemid 38418803)
170. V. Taneja, M.L. Maddelein, N. Talarek, S.J. Saupe, and S.W. Liebman A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast Mol. Cell 27 2007 67 77 (Pubitemid 46991382)
171. K.L. Taylor, N. Cheng, R.W. Williams, A.C. Steven, and R.B. Wickner Prion domain initiation of amyloid formation in vitro from native Ure2p Science 283 1999 1339 1343
172. M.D. Ter-Avanesyan, V.V. Kushnirov, A.R. Dagkesamanskaya, S.A. Didichenko, Y.O. Chernoff, S.G. Inge-Vechtomov, and V.N. Smirnov Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein Mol. Microbiol. 7 1993 683 692 (Pubitemid 23090350)
173. M.D. Ter-Avanesyan, A.R. Dagkesamanskaya, V.V. Kushnirov, and V.N. Smirnov The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi +] in the yeast Saccharomyces cerevisiae Genetics 137 1994 671 676 (Pubitemid 24196460)
174. N. Ticozzi, C. Vance, A.L. Leclerc, P. Keagle, J.D. Glass, D. McKenna-Yasek, P.C. Sapp, V. Silani, D.A. Bosco, C.E. Shaw, R.H. Brown Jr., and J.E. Landers Mutational analysis reveals the FUS homolog TAF15 as a candidate gene for familial amyotrophic lateral sclerosis Am. J. Med. Genet. B Neuropsychiatr. Genet. 156B 2011 285 290
175. J.R. Tollervey, T. Curk, B. Rogelj, M. Briese, M. Cereda, M. Kayikci, J. Konig, T. Hortobagyi, A.L. Nishimura, V. Zupunski, R. Patani, S. Chandran, G. Rot, B. Zupan, C.E. Shaw, and J. Ule Characterizing the RNA targets and position-dependent splicing regulation by TDP-43 Nat. Neurosci. 14 2011 452 458
176. J.A. Toombs, B.R. McCarty, and E.D. Ross Compositional determinants of prion formation in yeast Mol. Cell. Biol. 30 2010 319 332
177. H.L. True, and S.L. Lindquist A yeast prion provides a mechanism for genetic variation and phenotypic diversity Nature 407 2000 477 483
178. H.L. True, I. Berlin, and S.L. Lindquist Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits Nature 431 2004 184 187 (Pubitemid 39243470)
179. M.F. Tuite, and T.R. Serio The prion hypothesis: from biological anomaly to basic regulatory mechanism Nat. Rev. Mol. Cell Biol. 11 2010 823 833
180. J. Tyedmers, S. Treusch, J. Dong, J.M. McCaffery, B. Bevis, and S. Lindquist Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation Proc. Natl. Acad. Sci. U. S. A. 107 2010 8633 8638
181. M. Udan, and R.H. Baloh Implications of the prion-related Q/N domains in TDP-43 and FUS Prion 5 2011 1 5
182. H. Urwin, K.A. Josephs, J.D. Rohrer, I.R. Mackenzie, M. Neumann, A. Authier, H. Seelaar, J.C. Van Swieten, J.M. Brown, P. Johannsen, J.E. Nielsen, I.E. Holm, D.W. Dickson, R. Rademakers, N.R. Graff-Radford, J.E. Parisi, R.C. Petersen, K.J. Hatanpaa, C.L. White III, M.F. Weiner, F. Geser, V.M. Van Deerlin, J.Q. Trojanowski, B.L. Miller, W.W. Seeley, J. van der Zee, S. Kumar-Singh, S. Engelborghs, P.P. De Deyn, C. Van Broeckhoven, E.H. Bigio, H.X. Deng, G.M. Halliday, J.J. Kril, D.G. Munoz, D.M. Mann, S.M. Pickering-Brown, V. Doodeman, G. Adamson, S. Ghazi-Noori, E.M. Fisher, J.L. Holton, T. Revesz, M.N. Rossor, J. Collinge, S. Mead, and A.M. Isaacs FUS pathology defines the majority of tau- and TDP-43-negative frontotemporal lobar degeneration Acta Neuropathol. 120 2010 33 41
183. C. Vance, B. Rogelj, T. Hortobagyi, K.J. De Vos, A.L. Nishimura, J. Sreedharan, X. Hu, B. Smith, D. Ruddy, P. Wright, J. Ganesalingam, K.L. Williams, V. Tripathi, S. Al-Saraj, A. Al-Chalabi, P.N. Leigh, I.P. Blair, G. Nicholson, J. de Belleroche, J.M. Gallo, C.C. Miller, and C.E. Shaw Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6 Science 323 2009 1208 1211
184. S. Vashist, M. Cushman, and J. Shorter Applying Hsp104 to protein-misfolding disorders Biochem. Cell Biol. 88 2010 1 13
185. A. Voigt, D. Herholz, F.C. Fiesel, K. Kaur, D. Muller, P. Karsten, S.S. Weber, P.J. Kahle, T. Marquardt, and J.B. Schulz TDP-43-mediated neuron loss in vivo requires RNA-binding activity PLoS One 5 2010 e12247
186. L.C. Walker, H. Levine III, M.P. Mattson, and M. Jucker Inducible proteopathies Trends Neurosci. 29 2006 438 443 (Pubitemid 44118445)
187. H. Wang, M.L. Duennwald, B.E. Roberts, L.M. Rozeboom, Y.L. Zhang, A.D. Steele, R. Krishnan, L.J. Su, D. Griffin, S. Mukhopadhyay, E.J. Hennessy, P. Weigele, B.J. Blanchard, J. King, A.A. Deniz, S.L. Buchwald, V.M. Ingram, S. Lindquist, and J. Shorter Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs Proc. Natl. Acad. Sci. U. S. A. 105 2008 7159 7164 (Pubitemid 351754448)
188. I.F. Wang, L.S. Wu, H.Y. Chang, and C.K. Shen TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor J. Neurochem. 105 2008 797 806
189. F. Wang, X. Wang, C.G. Yuan, and J. Ma Generating a prion with bacterially expressed recombinant prion protein Science 327 2010 1132 1135
190. F. Wang, X. Wang, and J. Ma Conversion of bacterially expressed recombinant prion protein Methods 53 2011 208 213
191. F. Wang, Z. Zhang, X. Wang, J. Li, L. Zha, C.G. Yuan, C. Weissmann, and J. Ma Genetic informational RNA is not required for recombinant prion infectivity J. Virol. 86 2011 1874 1876
192. J.W. Wang, J.R. Brent, A. Tomlinson, N.A. Shneider, and B.D. McCabe The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span J. Clin. Invest. 121 2011 4118 4126
193. C. Weissmann, J. Li, S.P. Mahal, and S. Browning Prions on the move EMBO Rep. 12 2011 1109 1117
194. R.B. Wickner, K.L. Taylor, H.K. Edskes, and M.L. Maddelein Prions: portable prion domains Curr. Biol. 10 2000 R335 R337
195. R.B. Wickner, H.K. Edskes, F. Shewmaker, and T. Nakayashiki Prions of fungi: inherited structures and biological roles Nat. Rev. Microbiol. 5 2007 611 618 (Pubitemid 47074116)
196. R.B. Wickner, H.K. Edskes, D. Bateman, A.C. Kelly, and A. Gorkovskiy The yeast prions [PSI +] and [URE3] are molecular degenerative diseases Prion 5 2011
197. J.J. Wiltzius, M. Landau, R. Nelson, M.R. Sawaya, M.I. Apostol, L. Goldschmidt, A.B. Soriaga, D. Cascio, K. Rajashankar, and D. Eisenberg Molecular mechanisms for protein-encoded inheritance Nat. Struct. Mol. Biol. 16 2009 973 978
198. J. Woulfe, D.A. Gray, and I.R. Mackenzie FUS-immunoreactive intranuclear inclusions in neurodegenerative disease Brain Pathol. 20 2010 589 597
199. C. Yang, W. Tan, C. Whittle, L. Qiu, L. Cao, S. Akbarian, and Z. Xu The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanism PLoS One 5 2010 e15878
200. Y.J. Zhang, Y.F. Xu, C. Cook, T.F. Gendron, P. Roettges, C.D. Link, W.L. Lin, J. Tong, M. Castanedes-Casey, P. Ash, J. Gass, V. Rangachari, E. Buratti, F. Baralle, T.E. Golde, D.W. Dickson, and L. Petrucelli Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity Proc. Natl. Acad. Sci. U. S. A. 106 2009 7607 7612
201. H. Zinszner, J. Sok, D. Immanuel, Y. Yin, and D. Ron TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling J. Cell Sci. 110 Pt 15 1997 1741 1750 (Pubitemid 27352853)