1. Iadanza, M. G., Jackson, M. P., Hewitt, E. W., Ranson, N. A., and Radford, S. E.(2018) A new era for understanding amyloid structures and disease. Nat. Rev. Mol. Cell Biol. 19, 755-773
2. Hartl, F. U. (2017) Protein Misfolding Diseases. Annu. Rev. Biochem. 86, 21-26
3. Ono, K. (2018) Alzheimer's disease as oligomeropathy. Neurochem. Int. 119, 57-70
4. Chuang, E., Hori, A. M., Hesketh, C. D., and Shorter, J. (2018) Amyloid assembly and disassembly. J. Cell Sci. 131, jcs189928
5. Otzen, D., and Riek, R. (2019) Functional amyloids. Cold Spring Harb. Perspect. Biol. 11, a033860
6. Benilova, I., Karran, E., and De Strooper, B. (2012) The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nat. Neurosci. 15, 349-357
7. Bitan, G., Fradinger, E. A., Spring, S. M., and Teplow, D. B. (2005) Neurotoxic protein oligomers--what you see is not always what you get. Amyloid 12, 88-95
8. Roychaudhuri, R., Yang, M., Hoshi, M. M., and Teplow, D. B. (2009) Amyloid β-protein assembly and Alzheimer disease. J. Biol. Chem. 284, 4749-4753
9. Murakami, K., Izuo, N., and Bitan, G. (2022) Aptamers targeting amyloidogenic proteins and their emerging role in neurodegenerative diseases. J. Biol. Chem. 298, 101478
10. Jarrett, J. T., and Lansbury, P. T., Jr. (1993) Seeding ""one-dimensional crystallization"" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058
11. Esler, W. P., Stimson, E. R., Jennings, J. M., Vinters, H. V., Ghilardi, J. R., Lee, J. P., Mantyh, P. W., and Maggio, J. E. (2000) Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry 39, 6288-6295
12. Zekry, D., Hauw, J. J., and Gold, G. (2002) Mixed dementia: epidemiology, diagnosis, and treatment. J. Am. Geriatr. Soc. 50, 1431-1438
13. Irwin, D. J., Lee, V. M., and Trojanowski, J. Q. (2013) Parkinson's disease dementia: convergence of α-synuclein, tau and amyloid-β pathologies. Nat. Rev. Neurosci. 14, 626-636
14. Moussaud, S., Jones, D. R., Moussaud-Lamodiere, E. L., Delenclos, M., Ross, O. A., and McLean, P. J. (2014) α-Synuclein and tau: teammates in neurodegeneration? Mol. Neurodegener. 9, 43
15. Colom-Cadena, M., Gelpi, E., Charif, S., Belbin, O., Blesa, R., Marti, M. J., Clarimon, J., and Lleo, A. (2013) Confluence of α-synuclein, tau, and β-amyloid pathologies in dementia with Lewy bodies. J. Neuropathol. Exp. Neurol. 72, 1203-1212
16. Spires-Jones, T. L., Attems, J., and Thal, D. R. (2017) Interactions of pathological proteins in neurodegenerative diseases. Acta Neuropathol. 134, 187-205
17. Silva, J. L., and Cordeiro, Y. (2016) The ""Jekyll and Hyde"" actions of nucleic acids on the prion-like aggregation of proteins. J. Biol. Chem. 291, 15482-15490
18. Conlon, E. G., and Manley, J. L. (2017) RNA-binding proteins in neurodegeneration: mechanisms in aggregate. Genes Dev. 31, 1509-1528
19. Lu, J. X., Qiang, W., Yau, W. M., Schwieters, C. D., Meredith, S. C., and Tycko, R. (2013) Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue. Cell 154, 1257-1268
20. Paravastu, A. K., Leapman, R. D., Yau, W. M., and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. Proc. Natl. Acad. Sci. U. S. A. 105, 18349-18354
21. Qiang, W., Yau, W. M., Lu, J. X., Collinge, J., and Tycko, R. (2017) Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes. Nature 541, 217-221
22. Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., and Ishii, Y. (2015) Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease. Nat. Struc. Mol. Biol. 22, 499-505
23. Colvin, M. T., Silvers, R., Ni, Q. Z., Can, T. V., Sergeyev, I., Rosay, M., Donovan, K. J., Michael, B., Wall, J., Linse, S., and Griffin, R. G. (2016) Atomic resolution structure of monomorphic Aβ42 amyloid fibrils. J. Am. Chem. Soc. 138, 9663-9674
24. Walti, M. A., Ravotti, F., Arai, H., Glabe, C. G., Wall, J. S., Bockmann, A., Guntert, P., Meier, B. H., and Riek, R. (2016) Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril. Proc. Natl. Acad. Sci. U. S. A. 113, E4976-4984
25. Kollmer, M., Close, W., Funk, L., Rasmussen, J., Bsoul, A., Schierhorn, A., Schmidt, M., Sigurdson, C. J., Jucker, M., and Fandrich, M. (2019) Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer's brain tissue. Nat. Commun. 10, 4760
26. Meinhardt, J., Sachse, C., Hortschansky, P., Grigorieff, N., and Fandrich, M. (2009) Aβ(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J. Mol. Biol. 386, 869-877
27. Schmidt, M., Sachse, C., Richter, W., Xu, C., Fandrich, M., and Grigorieff, N. (2009) Comparison of Alzheimer Aβ(1-40) and Aβ(1-42) amyloid fibrils reveals similar protofilament structures. Proc. Natl. Acad. Sci. U. S. A. 106, 19813-19818
28. Yang, Y., Arseni, D., Zhang, W., Huang, M., Lovestam, S., Schweighauser, M., Kotecha, A., Murzin, A. G., Peak-Chew, S. Y., Macdonald, J., Lavenir, I., Garringer, H. J., Gelpi, E., Newell, K. L., Kovacs, G. G., Vidal, R., Ghetti, B., Ryskeldi-Falcon, B., Scheres, S. H. W., and Goedert, M. (2022) Cryo-EM structures of amyloid-β42 filaments from human brains. Science 375, 167-172
29. Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., and Scheres, S. H. W. (2017) Cryo-EM structures of tau filaments from Alzheimer's disease. Nature 547, 185-190
30. Arseni, D., Hasegawa, M., Murzin, A. G., Kametani, F., Arai, M., Yoshida, M., and Ryskeldi-Falcon, B. (2022) Structure of pathological TDP-43 filaments from ALS with FTLD. Nature 601, 139-143
31. Berriman, J., Serpell, L. C., Oberg, K. A., Fink, A. L., Goedert, M., and Crowther, R. A. (2003) Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-β structure. Proc. Natl. Acad. Sci. U. S. A. 100, 9034-9038
32. Cao, Q., Boyer, D. R., Sawaya, M. R., Ge, P., and Eisenberg, D. S. (2019) Cryo-EM structures of four polymorphic TDP-43 amyloid cores. Nat. Struct. Mol. Biol. 26, 619-627
33. Li, Q., Babinchak, W. M., and Surewicz, W. K. (2021) Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43. Nat. Commun. 12, 1620
34. Goedert, M. (2015) NEURODEGENERATION. Alzheimer's and Parkinson's diseases: The prion concept in relation to assembled Aβ, tau, and α-synuclein. Science 349, 1255555
35. Jucker, M., and Walker, L. C. (2013) Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501, 45-51
36. Guo, J. P., Arai, T., Miklossy, J., and McGeer, P. L. (2006) Aβ and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 103, 1953-1958
37. Gotz, J., Chen, F., van Dorpe, J., and Nitsch, R. M. (2001) Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ42 fibrils. Science 293, 1491-1495
38. Lewis, J., Dickson, D. W., Lin, W. L., Chisholm, L., Corral, A., Jones, G., Yen, S. H., Sahara, N., Skipper, L., Yager, D., Eckman, C., Hardy, J., Hutton, M., and McGowan, E. (2001) Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293, 1487-1491
39. Hamilton, R. L. (2000) Lewy bodies in Alzheimer's disease: a neuropathological review of 145 cases using α-synuclein immunohistochemistry. Brain Pathol. 10, 378-384
40. Uchikado, H., Lin, W. L., DeLucia, M. W., and Dickson, D. W. (2006) Alzheimer disease with amygdala Lewy bodies: a distinct form of α-synucleinopathy. J. Neuropathol. Exp. Neurol. 65, 685-697
41. Toledo, J. B., Brettschneider, J., Grossman, M., Arnold, S. E., Hu, W. T., Xie, S. X., Lee, V. M., Shaw, L. M., and Trojanowski, J. Q. (2012) CSF biomarkers cutoffs: the importance of coincident neuropathological diseases. Acta Neuropathol. 124, 23-35
42. Armstrong, R. A., Cairns, N. J., and Lantos, P. L. (1997) β-Amyloid (Aβ) deposition in the medial temporal lobe of patients with dementia with Lewy bodies. Neurosci. Lett. 227, 193-196
43. Irwin, D. J., Grossman, M., Weintraub, D., Hurtig, H. I., Duda, J. E., Xie, S. X., Lee, E. B., Van Deerlin, V. M., Lopez, O. L., Kofler, J. K., Nelson, P. T., Jicha, G. A., Woltjer, R., Quinn, J. F., Kaye, J., Leverenz, J. B., Tsuang, D., Longfellow, K., Yearout, D., Kukull, W., Keene, C. D., Montine, T. J., Zabetian, C. P., and Trojanowski, J. Q. (2017) Neuropathological and genetic correlates of survival and dementia onset in synucleinopathies: a retrospective analysis. Lancet Neurol. 16, 55-65
44. Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M., and Mucke, L. (2001) β-Amyloid peptides enhance α-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease. Proc. Natl. Acad. Sci. U. S. A. 98, 12245-12250
45. Mandal, P. K., Pettegrew, J. W., Masliah, E., Hamilton, R. L., and Mandal, R. (2006) Interaction between Aβ peptide and α synuclein: molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease. Neurochem. Res. 31, 1153-1162
46. Ono, K. (2017) The oligomer hypothesis in α-synucleinopathy. Neurochem. Res. 42, 3362-3371
47. Tsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., Yuan, J. X., and Masliah, E. (2008) Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases. PLoS One 3, e3135
48. Ono, K., Takahashi, R., Ikeda, T., and Yamada, M. (2012) Cross-seeding effects of amyloid β-protein and α-synuclein. J. Neurochem. 122, 883-890
49. Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., and Lee, V. M. (2013) Distinct α-synuclein strains differentially promote tau inclusions in neurons. Cell 154, 103-117
50. Bassil, F., Brown, H. J., Pattabhiraman, S., Iwasyk, J. E., Maghames, C. M., Meymand, E. S., Cox, T. O., Riddle, D. M., Zhang, B., Trojanowski, J. Q., and Lee, V. M. (2020) Amyloid-β (Aβ) Plaques promote seeding and spreading of α-synuclein and tau in a mouse model of Lewy body disorders with Aβ pathology. Neuron 105, 260-275 e266
51. Zhao, J., Luo, Y., Jang, H., Yu, X., Wei, G., Nussinov, R., and Zheng, J. (2012) Probing ion channel activity of human islet amyloid polypeptide (amylin). Biochim. Biophys. Acta 1818, 3121-3130
52. Subedi, S., Sasidharan, S., Nag, N., Saudagar, P., and Tripathi, T. (2022) Amyloid cross-seeding: mechanism, implication, and inhibition. Molecules 27, 1776
53. Leibson, C. L., Rocca, W. A., Hanson, V. A., Cha, R., Kokmen, E., O'Brien, P. C., and Palumbo, P. J. (1997) Risk of dementia among persons with diabetes mellitus: a population-based cohort study. Am. J. Epidemiol. 145, 301-308
54. Ott, A., Stolk, R. P., van Harskamp, F., Pols, H. A., Hofman, A., and Breteler, M. M. (1999) Diabetes mellitus and the risk of dementia: The Rotterdam study. Neurology 53, 1937-1942
55. Bharadwaj, P., Solomon, T., Sahoo, B. R., Ignasiak, K., Gaskin, S., Rowles, J., Verdile, G., Howard, M. J., Bond, C. S., Ramamoorthy, A., Martins, R. N., and Newsholme, P. (2020) Amylin and β amyloid proteins interact to form amorphous heterocomplexes with enhanced toxicity in neuronal cells. Sci. Rep. 10, 10356
56. Oskarsson, M. E., Paulsson, J. F., Schultz, S. W., Ingelsson, M., Westermark, P., and Westermark, G. T. (2015) In vivo seeding and cross-seeding of localized amyloidosis: a molecular link between type 2 diabetes and Alzheimer disease. Am. J. Pathol. 185, 834-846
57. Martinez-Valbuena, I., Amat-Villegas, I., Valenti-Azcarate, R., Carmona-Abellan, M. D. M., Marcilla, I., Tunon, M. T., and Luquin, M. R. (2018) Interaction of amyloidogenic proteins in pancreatic β cells from subjects with synucleinopathies. Acta Neuropathol. 135, 877-886
58. Mucibabic, M., Steneberg, P., Lidh, E., Straseviciene, J., Ziolkowska, A., Dahl, U., Lindahl, E., and Edlund, H. (2020) α-Synuclein promotes IAPP fibril formation in vitro and β-cell amyloid formation in vivo in mice. Sci. Rep. 10, 20438
59. Tang, Y., Zhang, D., Liu, Y., Zhang, Y., Zhou, Y., Chang, Y., Zheng, B., Xu, A., and Zheng, J. (2022) A new strategy to reconcile amyloid cross-seeding and amyloid prevention in a binary system of α-synuclein fragmental peptide and hIAPP. Protein Sci. 31, 485-497
60. Colon, W., and Kelly, J. W. (1992) Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31, 8654-8660
61. Gharibyan, A. L., Wasana Jayaweera, S., Lehmann, M., Anan, I., and Olofsson, A. (2022) Endogenous human proteins interfering with amyloid formation. Biomolecules 12, 446
62. Stein, T. D., Anders, N. J., DeCarli, C., Chan, S. L., Mattson, M. P., and Johnson, J. A. (2004) Neutralization of transthyretin reverses the neuroprotective effects of secreted amyloid precursor protein (APP) in APPSW mice resulting in tau phosphorylation and loss of hippocampal neurons: support for the amyloid hypothesis. J. Neurosci. 24, 7707-7717
63. Choi, S. H., Leight, S. N., Lee, V. M., Li, T., Wong, P. C., Johnson, J. A., Saraiva, M. J., and Sisodia, S. S. (2007) Accelerated Aβ deposition in APPswe/PS1deltaE9 mice with hemizygous deletions of TTR (transthyretin). J. Neurosci. 27, 7006-7010
64. Nilsson, L., Pamren, A., Islam, T., Brannstrom, K., Golchin, S. A., Pettersson, N., Iakovleva, I., Sandblad, L., Gharibyan, A. L., and Olofsson, A. (2018) Transthyretin interferes with Aβ amyloid formation by redirecting oligomeric nuclei into non-amyloid aggregates. J. Mol. Biol. 430, 2722-2733
65. Ghadami, S. A., Chia, S., Ruggeri, F. S., Meisl, G., Bemporad, F., Habchi, J., Cascella, R., Dobson, C. M., Vendruscolo, M., Knowles, T. P. J., and Chiti, F. (2020) Transthyretin inhibits primary and secondary nucleations of amyloid-β peptide aggregation and reduces the toxicity of its oligomers. Biomacromolecules 21, 1112-1125
66. Wasana Jayaweera, S., Surano, S., Pettersson, N., Oskarsson, E., Lettius, L., Gharibyan, A. L., Anan, I., and Olofsson, A. (2021) Mechanisms of transthyretin inhibition of IAPP amyloid formation. Biomolecules 11, 411
67. Mazzei, G., Ikegami, R., Abolhassani, N., Haruyama, N., Sakumi, K., Saito, T., Saido, T. C., and Nakabeppu, Y. (2021) A high-fat diet exacerbates the Alzheimer's disease pathology in the hippocampus of the AppNL-F/NL-F knock-in mouse model. Aging Cell 20, e13429
68. Hedlund, J., Johansson, J., and Persson, B. (2009) BRICHOS - a superfamily of multidomain proteins with diverse functions. BMC Res. Notes 2, 180
69. Dolfe, L., Tambaro, S., Tigro, H., Del Campo, M., Hoozemans, J. J. M., Wiehager, B., Graff, C., Winblad, B., Ankarcrona, M., Kaldmae, M., Teunissen, C. E., Ronnback, A., Johansson, J., and Presto, J. (2018) The Bri2 and Bri3 BRICHOS domains interact differently with Aβ42 and Alzheimer amyloid plaques. J. Alzheimers Dis. Rep. 2, 27-39
70. Hermansson, E., Schultz, S., Crowther, D., Linse, S., Winblad, B., Westermark, G., Johansson, J., and Presto, J. (2014) The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogaster. Dis. Model. Mech. 7, 659-665
71. Poska, H., Haslbeck, M., Kurudenkandy, F. R., Hermansson, E., Chen, G., Kostallas, G., Abelein, A., Biverstal, H., Crux, S., Fisahn, A., Presto, J., and Johansson, J. (2016) Dementia-related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Aβ42 toxicity in Drosophila. Biochem. J. 473, 3683-3704
72. Cohen, S. I. A., Arosio, P., Presto, J., Kurudenkandy, F. R., Biverstal, H., Dolfe, L., Dunning, C., Yang, X., Frohm, B., Vendruscolo, M., Johansson, J., Dobson, C. M., Fisahn, A., Knowles, T. P. J., and Linse, S. (2015) A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers. Nat. Struct. Mol. Biol. 22, 207-213
73. Chen, G., Abelein, A., Nilsson, H. E., Leppert, A., Andrade-Talavera, Y., Tambaro, S., Hemmingsson, L., Roshan, F., Landreh, M., Biverstal, H., Koeck, P. J. B., Presto, J., Hebert, H., Fisahn, A., and Johansson, J. (2017) Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state. Nat. Commun. 8, 2081
74. Poska, H., Leppert, A., Tigro, H., Zhong, X., Kaldmae, M., Nilsson, H. E., Hebert, H., Chen, G., and Johansson, J. (2020) Recombinant Bri3 BRICHOS domain is a molecular chaperone with effect against amyloid formation and non-fibrillar protein aggregation. Sci. Rep. 10, 9817
75. Oskarsson, M. E., Hermansson, E., Wang, Y., Welsh, N., Presto, J., Johansson, J., and Westermark, G. T. (2018) BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human β cells. Proc. Natl. Acad. Sci. U. S. A. 115, E2752-E2761
76. Ginsberg, S. D., Galvin, J. E., Chiu, T. S., Lee, V. M., Masliah, E., and Trojanowski, J. Q. (1998) RNA sequestration to pathological lesions of neurodegenerative diseases. Acta Neuropathol. 96, 487-494
77. Ginsberg, S. D., Crino, P. B., Hemby, S. E., Weingarten, J. A., Lee, V. M., Eberwine, J. H., and Trojanowski, J. Q. (1999) Predominance of neuronal mRNAs in individual Alzheimer's disease senile plaques. Ann. Neurol. 45, 174-181
78. Marcinkiewicz, M. (2002) βAPP and furin mRNA concentrates in immature senile plaques in the brain of Alzheimer patients. J. Neuropathol. Exp. Neurol. 61, 815-829
79. Silva, J. L., Lima, L. M., Foguel, D., and Cordeiro, Y. (2008) Intriguing nucleic-acid-binding features of mammalian prion protein. Trends Biochem. Sci. 33, 132-140
80. Silva, J. L., Gomes, M. P., Vieira, T. C., and Cordeiro, Y. (2010) PrP interactions with nucleic acids and glycosaminoglycans in function and disease. Front. Biosci. (Landmark Ed) 15, 132-150
81. Deleault, N. R., Piro, J. R., Walsh, D. J., Wang, F., Ma, J., Geoghegan, J. C., and Supattapone, S. (2012) Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids. Proc. Natl. Acad. Sci. U. S. A. 109, 8546-8551
82. Calamai, M., Taddei, N., Stefani, M., Ramponi, G., and Chiti, F. (2003) Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins. Biochemistry 42, 15078-15083
83. Shu, Y., Pi, F., Sharma, A., Rajabi, M., Haque, F., Shu, D., Leggas, M., Evers, B. M., and Guo, P. (2014) Stable RNA nanoparticles as potential new generation drugs for cancer therapy. Adv. Drug Deliv. Rev. 66, 74-89
84. Prusiner, S. B., Scott, M. R., DeArmond, S. J., and Cohen, F. E. (1998) Prion protein biology. Cell 93, 337-348
85. Collinge, J. (2001) Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24, 519-550
86. Aguzzi, A., and Polymenidou, M. (2004) Mammalian prion biology: one century of evolving concepts. Cell 116, 313-327
87. Louka, A., Zacco, E., Temussi, P. A., Tartaglia, G. G., and Pastore, A. (2020) RNA as the stone guest of protein aggregation. Nucleic Acids Res. 48, 11880-11889
88. McLennan, N. F., Brennan, P. M., McNeill, A., Davies, I., Fotheringham, A., Rennison, K. A., Ritchie, D., Brannan, F., Head, M. W., Ironside, J. W., Williams, A., and Bell, J. E. (2004) Prion protein accumulation and neuroprotection in hypoxic brain damage. Am. J. Pathol. 165, 227-235
89. Mitteregger, G., Vosko, M., Krebs, B., Xiang, W., Kohlmannsperger, V., Nolting, S., Hamann, G. F., and Kretzschmar, H. A. (2007) The role of the octarepeat region in neuroprotective function of the cellular prion protein. Brain Pathol. 17, 174-183
90. Sengupta, I., and Udgaonkar, J. B. (2018) Structural mechanisms of oligomer and amyloid fibril formation by the prion protein. Chem. Commun. (Camb.) 54, 6230-6242
91. Nandi, P. K. (1997) Interaction of prion peptide HuPrP106-126 with nucleic acid. Arch. Virol. 142, 2537-2545
92. Nandi, P. K. (1998) Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution. Arch. Virol. 143, 1251-1263
93. Nandi, P. K., and Leclerc, E. (1999) Polymerization of murine recombinant prion protein in nucleic acid solution. Arch. Virol. 144, 1751-1763
94. Cordeiro, Y., Machado, F., Juliano, L., Juliano, M. A., Brentani, R. R., Foguel, D., and Silva, J. L. (2001) DNA converts cellular prion protein into the β-sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem. 276, 49400-49409
95. Macedo, B., Millen, T. A., Braga, C. A., Gomes, M. P., Ferreira, P. S., Kraineva, J., Winter, R., Silva, J. L., and Cordeiro, Y. (2012) Nonspecific prion protein-nucleic acid interactions lead to different aggregates and cytotoxic species. Biochemistry 51, 5402-5413
96. Cavaliere, P., Pagano, B., Granata, V., Prigent, S., Rezaei, H., Giancola, C., and Zagari, A. (2013) Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation. Nucleic Acids Res. 41, 327-339
97. Davis, J. T. (2004) G-quartets 40 years later: from 5'-GMP to molecular biology and supramolecular chemistry. Angew. Chem. Int. Ed. Engl. 43, 668-698
98. Lima, L. M., Cordeiro, Y., Tinoco, L. W., Marques, A. F., Oliveira, C. L., Sampath, S., Kodali, R., Choi, G., Foguel, D., Torriani, I., Caughey, B., and Silva, J. L. (2006) Structural insights into the interaction between prion protein and nucleic acid. Biochemistry 45, 9180-9187
99. Gomes, M. P., Millen, T. A., Ferreira, P. S., e Silva, N. L., Vieira, T. C., Almeida, M. S., Silva, J. L., and Cordeiro, Y. (2008) Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cells. J. Biol. Chem. 283, 19616-19625
100. Deleault, N. R., Lucassen, R. W., and Supattapone, S. (2003) RNA molecules stimulate prion protein conversion. Nature 425, 717-720
101. Saborio, G. P., Permanne, B., and Soto, C. (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411, 810-813
102. Olsthoorn, R. C. (2014) G-quadruplexes within prion mRNA: the missing link in prion disease? Nucleic Acids Res. 42, 9327-9333
103. Staple, D. W., and Butcher, S. E. (2005) Pseudoknots: RNA structures with diverse functions. PLoS Biol. 3, e213
104. Bera, A., and Biring, S. (2018) A quantitative characterization of interaction between prion protein with nucleic acids. Biochem. Biophys. Rep. 14, 114-124
105. Strom, A., Wang, G. S., Picketts, D. J., Reimer, R., Stuke, A. W., and Scott, F. W. (2011) Cellular prion protein localizes to the nucleus of endocrine and neuronal cells and interacts with structural chromatin components. Eur. J. Cell Biol. 90, 414-419
106. Mange, A., Crozet, C., Lehmann, S., and Beranger, F. (2004) Scrapie-like prion protein is translocated to the nuclei of infected cells independently of proteasome inhibition and interacts with chromatin. J. Cell Sci. 117, 2411-2416
107. Marijanovic, Z., Caputo, A., Campana, V., and Zurzolo, C. (2009) Identification of an intracellular site of prion conversion. PLoS Pathog. 5, e1000426
108. Beaudoin, S., Vanderperre, B., Grenier, C., Tremblay, I., Leduc, F., and Roucou, X. (2009) A large ribonucleoprotein particle induced by cytoplasmic PrP shares striking similarities with the chromatoid body, an RNA granule predicted to function in posttranscriptional gene regulation. Biochim. Biophys. Acta 1793, 335-345
109. Baron, G. S., Magalhaes, A. C., Prado, M. A., and Caughey, B. (2006) Mouse-adapted scrapie infection of SN56 cells: greater efficiency with microsome-associated versus purified PrP-res. J. Virol. 80, 2106-2117
110. Rouvinski, A., Karniely, S., Kounin, M., Moussa, S., Goldberg, M. D., Warburg, G., Lyakhovetsky, R., Papy-Garcia, D., Kutzsche, J., Korth, C., Carlson, G. A., Godsave, S. F., Peters, P. J., Luhr, K., Kristensson, K., and Taraboulos, A. (2014) Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. J. Cell Biol. 204, 423-441
111. Brown, D. R., Clive, C., and Haswell, S. J. (2001) Antioxidant activity related to copper binding of native prion protein. J. Neurochem. 76, 69-76
112. Brown, D. R. (2003) Prion protein expression modulates neuronal copper content. J. Neurochem. 87, 377-385
113. Liu, M., Yu, S., Yang, J., Yin, X., and Zhao, D. (2007) RNA and CuCl2 induced conformational changes of the recombinant ovine prion protein. Mol. Cell. Biochem. 294, 197-203
114. Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., McCluskey, L. F., Miller, B. L., Masliah, E., Mackenzie, I. R., Feldman, H., Feiden, W., Kretzschmar, H. A., Trojanowski, J. Q., and Lee, V. M. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130-133
115. Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., and Oda, T. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 351, 602-611
116. Sephton, C. F., Cenik, B., Cenik, B. K., Herz, J., and Yu, G. (2012) TDP-43 in central nervous system development and function: clues to TDP-43-associated neurodegeneration. Biol. Chem. 393, 589-594
117. Donde, A., Sun, M., Ling, J. P., Braunstein, K. E., Pang, B., Wen, X., Cheng, X., Chen, L., and Wong, P. C. (2019) Splicing repression is a major function of TDP-43 in motor neurons. Acta Neuropathol. 138, 813-826
118. Prasad, A., Bharathi, V., Sivalingam, V., Girdhar, A., and Patel, B. K. (2019) Molecular mechanisms of TDP-43 misfolding and pathology in amyotrophic lateral sclerosis. Front. Mol. Neurosci. 12, 25
119. Mori, K., Lammich, S., Mackenzie, I. R., Forne, I., Zilow, S., Kretzschmar, H., Edbauer, D., Janssens, J., Kleinberger, G., Cruts, M., Herms, J., Neumann, M., Van Broeckhoven, C., Arzberger, T., and Haass, C. (2013) hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations. Acta Neuropathol. 125, 413-423
120. Bruijn, L. I., Becher, M. W., Lee, M. K., Anderson, K. L., Jenkins, N. A., Copeland, N. G., Sisodia, S. S., Rothstein, J. D., Borchelt, D. R., Price, D. L., and Cleveland, D. W. (1997) ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 18, 327-338
121. Lukavsky, P. J., Daujotyte, D., Tollervey, J. R., Ule, J., Stuani, C., Buratti, E., Baralle, F. E., Damberger, F. F., and Allain, F. H. (2013) Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43. Nat. Struct. Mol. Biol. 20, 1443-1449
122. Kuo, P. H., Chiang, C. H., Wang, Y. T., Doudeva, L. G., and Yuan, H. S. (2014) The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids. Nucleic Acids Res. 42, 4712-4722
123. Kabashi, E., Valdmanis, P. N., Dion, P., Spiegelman, D., McConkey, B. J., Vande Velde, C., Bouchard, J. P., Lacomblez, L., Pochigaeva, K., Salachas, F., Pradat, P. F., Camu, W., Meininger, V., Dupre, N., and Rouleau, G. A. (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat. Genet. 40, 572-574
124. Molliex, A., Temirov, J., Lee, J., Coughlin, M., Kanagaraj, A. P., Kim, H. J., Mittag, T., and Taylor, J. P. (2015) Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell 163, 123-133
125. Berning, B. A., and Walker, A. K. (2019) The pathobiology of TDP-43 C-terminal fragments in ALS and FTLD. Front. Neurosci. 13, 335
126. Nonaka, T., and Hasegawa, M. (2020) Prion-like properties of assembled TDP-43. Curr. Opin. Neurobiol. 61, 23-28
127. Feiler, M. S., Strobel, B., Freischmidt, A., Helferich, A. M., Kappel, J., Brewer, B. M., Li, D., Thal, D. R., Walther, P., Ludolph, A. C., Danzer, K. M., and Weishaupt, J. H. (2015) TDP-43 is intercellularly transmitted across axon terminals. J. Cell Biol. 211, 897-911
128. Ayala, Y. M., Pantano, S., D'Ambrogio, A., Buratti, E., Brindisi, A., Marchetti, C., Romano, M., and Baralle, F. E. (2005) Human, Drosophila, and C.elegans TDP43: nucleic acid binding properties and splicing regulatory function. J. Mol. Biol. 348, 575-588
129. Brown, A. L., Wilkins, O. G., Keuss, M. J., Hill, S. E., Zanovello, M., Lee, W. C., Bampton, A., Lee, F. C. Y., Masino, L., Qi, Y. A., Bryce-Smith, S., Gatt, A., Hallegger, M., Fagegaltier, D., Phatnani, H., Consortium, N. A., Newcombe, J., Gustavsson, E. K., Seddighi, S., Reyes, J. F., Coon, S. L., Ramos, D., Schiavo, G., Fisher, E. M. C., Raj, T., Secrier, M., Lashley, T., Ule, J., Buratti, E., Humphrey, J., Ward, M. E., and Fratta, P. (2022) TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of UNC13A. Nature 603, 131-137
130. Bhardwaj, A., Myers, M. P., Buratti, E., and Baralle, F. E. (2013) Characterizing TDP-43 interaction with its RNA targets. Nucleic Acids Res. 41, 5062-5074
131. Rengifo-Gonzalez, J. C., El Hage, K., Clement, M. J., Steiner, E., Joshi, V., Craveur, P., Durand, D., Pastre, D., and Bouhss, A. (2021) The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation. Elife 10, e67605
132. Kitamura, A., Shibasaki, A., Takeda, K., Suno, R., and Kinjo, M. (2018) Analysis of the substrate recognition state of TDP-43 to single-stranded DNA using fluorescence correlation spectroscopy. Biochem. Biophys. Rep. 14, 58-63
133. Conicella, A. E., Dignon, G. L., Zerze, G. H., Schmidt, H. B., D'Ordine, A. M., Kim, Y. C., Rohatgi, R., Ayala, Y. M., Mittal, J., and Fawzi, N. L. (2020) TDP-43 α-helical structure tunes liquid-liquid phase separation and function. Proc. Natl. Acad. Sci. U. S. A. 117, 5883-5894
134. Hyman, A. A., Weber, C. A., and Julicher, F. (2014) Liquid-liquid phase separation in biology. Annu. Rev. Cell Dev. Biol. 30, 39-58
135. Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J., Shorter, J., Wolozin, B., Van Den Bosch, L., Tompa, P., and Fuxreiter, M. (2018) Protein phase separation: A new phase in cell biology. Trends Cell Biol. 28, 420-435
136. Fonda, B. D., Jami, K. M., Boulos, N. R., and Murray, D. T. (2021) Identification of the rigid core for aged liquid droplets of an RNA-binding protein low complexity domain. J. Am. Chem. Soc. 143, 6657-6668
137. Wang, A., Conicella, A. E., Schmidt, H. B., Martin, E. W., Rhoads, S. N., Reeb, A. N., Nourse, A., Ramirez Montero, D., Ryan, V. H., Rohatgi, R., Shewmaker, F., Naik, M. T., Mittag, T., Ayala, Y. M., and Fawzi, N. L. (2018) A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing. EMBO J. 37, e97452
138. Khalfallah, Y., Kuta, R., Grasmuck, C., Prat, A., Durham, H. D., and Vande Velde, C. (2018) TDP-43 regulation of stress granule dynamics in neurodegenerative disease-relevant cell types. Sci. Rep. 8, 7551
139. Chang, C. K., Wu, T. H., Wu, C. Y., Chiang, M. H., Toh, E. K., Hsu, Y. C., Lin, K. F., Liao, Y. H., Huang, T. H., and Huang, J. J. (2012) The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity. Biochem. Biophys. Res. Commun. 425, 219-224
140. Ayala, Y. M., Zago, P., D'Ambrogio, A., Xu, Y. F., Petrucelli, L., Buratti, E., and Baralle, F. E. (2008) Structural determinants of the cellular localization and shuttling of TDP-43. J. Cell Sci. 121, 3778-3785
141. Winton, M. J., Igaz, L. M., Wong, M. M., Kwong, L. K., Trojanowski, J. Q., and Lee, V. M. (2008) Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J. Biol. Chem. 283, 13302-13309
142. Crozat, A., Aman, P., Mandahl, N., and Ron, D. (1993) Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma. Nature 363, 640-644
143. Calvio, C., Neubauer, G., Mann, M., and Lamond, A. I. (1995) Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry. RNA 1, 724-733
144. Kwiatkowski, T. J., Jr., Bosco, D. A., Leclerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J., Kasarskis, E. J., Munsat, T., Valdmanis, P., Rouleau, G. A., Hosler, B. A., Cortelli, P., de Jong, P. J., Yoshinaga, Y., Haines, J. L., Pericak-Vance, M. A., Yan, J., Ticozzi, N., Siddique, T., McKenna-Yasek, D., Sapp, P. C., Horvitz, H. R., Landers, J. E., and Brown, R. H., Jr. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Scien
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