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M. Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade. Annu. Rev. Biochem. 86, 27\u201368 (2017). https:\/\/doi.org\/10.1146\/annurev-biochem-061516-045115","DOI":"10.1146\/annurev-biochem-061516-045115"},{"key":"2","doi-asserted-by":"crossref","unstructured":"[2] Maddelein, M. L., Dos Reis S., Duvezin-Caubet, S., Coulary-Salin, B., Saupe, S. J. Amyloid aggregates of the HET-s prion protein are infectious. Proc. Natl. Acad. Sci. U.S.A. 99, 7402\u20137407 (2002). https:\/\/doi.org\/10.1073\/pnas.072199199","DOI":"10.1073\/pnas.072199199"},{"key":"3","doi-asserted-by":"crossref","unstructured":"[3] Chapman, M. R., Robinson, L. S., Pinkner, J. S., Roth, R., Heuser, J., Hammar, M., et al. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295, 851\u2013855 (2002). https:\/\/doi.org\/10.1126\/science.1067484","DOI":"10.1126\/science.1067484"},{"key":"4","doi-asserted-by":"crossref","unstructured":"[4] Maji, S. K., Perrin, M. H., Sawaya, M. R., Jessberger, S., Vadodaria, K., Rissman, R. A., et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325, 328\u2013332 (2009). https:\/\/doi.org\/10.1126\/science.1173155","DOI":"10.1126\/science.1173155"},{"key":"5","doi-asserted-by":"crossref","unstructured":"[5] Adler-Abramovich, L., Vaks, L., Carny, O., Trudler, D., Magno, A., Caflisch, A., et al. Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria. Nat. Chem. Biol. 8, 701\u2013706 (2012). https:\/\/doi.org\/10.1038\/nchembio.1002","DOI":"10.1038\/nchembio.1002"},{"key":"6","doi-asserted-by":"crossref","unstructured":"[6] M\u00e9nard-Moyon, C., Venkatesh, V., Krishna, K. V., Bonachera, F., Verma, S., Bianco, A. Self-assembly of tyrosine into controlled supramolecular nanostructures. Chemistry 21, 11681\u201311686 (2015). https:\/\/doi.org\/10.1002\/chem.201502076","DOI":"10.1002\/chem.201502076"},{"key":"7","doi-asserted-by":"crossref","unstructured":"[7] Linse S. Monomer-dependent secondary nucleation in amyloid formation. Biophys. Rev. 9, 329\u2013338 (2017). https:\/\/doi.org\/10.1007\/s12551-017-0289-z","DOI":"10.1007\/s12551-017-0289-z"},{"key":"8","doi-asserted-by":"crossref","unstructured":"[8] Meisl, G., Rajah, L., Cohen, S. A. I., Pfammatter, M., \u0160ari\u0107, A., Hellstrand, E., et al. Scaling behaviour and rate-determining steps in filamentous self-assembly. Chem. Sci. 8, 7087\u20137097 (2017). https:\/\/doi.org\/10.1039\/c7sc01965c","DOI":"10.1039\/C7SC01965C"},{"key":"9","doi-asserted-by":"crossref","unstructured":"[9] Morris, A. M., Watzky, M. A., Finke, R. G. Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature. Biochim. Biophys. Acta. 1794, 375\u2013397 (2009). https:\/\/doi.org\/10.1016\/j.bbapap.2008.10.016","DOI":"10.1016\/j.bbapap.2008.10.016"},{"key":"10","doi-asserted-by":"crossref","unstructured":"[10] Michaels, T. C. T., Qian, D., \u0160ari\u0107, A., Vendruscolo, M., Linse, S., Knowles, T. P. J. Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379\u2013397 (2023). https:\/\/doi.org\/10.1038\/s42254-023-00598-9","DOI":"10.1038\/s42254-023-00598-9"},{"key":"11","doi-asserted-by":"crossref","unstructured":"[11] Tanaka, M., Collins, S. R., Toyama, B. H., Weissman, J. S. The physical basis of how prion conformations determine strain phenotypes. Nature 442, 585\u2013589 (2006). https:\/\/doi.org\/10.1038\/nature04922","DOI":"10.1038\/nature04922"},{"key":"12","doi-asserted-by":"crossref","unstructured":"[12] Meisl, G., Kirkegaard, J. B., Arosio, P., Michaels, T. C., Vendruscolo, M., Dobson, C. M., et al. Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat. Protoc. 11, 252\u2013272 (2016). https:\/\/doi.org\/10.1038\/nprot.2016.010","DOI":"10.1038\/nprot.2016.010"},{"key":"13","doi-asserted-by":"crossref","unstructured":"[13] Morris, A. M., Finke, R. G. Alpha-synuclein aggregation variable temperature and variable pH kinetic data: A re-analysis using the Finke-Watzky 2-step model of nucleation and autocatalytic growth. Biophys. Chem. 140, 9\u201315 (2009). https:\/\/doi.org\/10.1016\/j.bpc.2008.11.003","DOI":"10.1016\/j.bpc.2008.11.003"},{"key":"14","doi-asserted-by":"crossref","unstructured":"[14] Tsolis, A. C., Papandreou, N. C., Iconomidou, V. A., Hamodrakas, S. J. A consensus method for the prediction of \u2018aggregation-prone\u2019 peptides in globular proteins. PLoS One 8, e54175 (2013). https:\/\/doi.org\/10.1371\/journal.pone.0054175","DOI":"10.1371\/journal.pone.0054175"},{"key":"15","doi-asserted-by":"crossref","unstructured":"[15] Mizuguchi-Fukase, C., Ohgita, T., Saito, H. Kinetic and thermodynamic analyses of aggregation and fibril formation of amyloidogenic proteins. SEIBUTSU BUTSURI 62, 224\u2013227 (2022). https:\/\/doi.org\/10.2142\/biophys.62.224","DOI":"10.2142\/biophys.62.224"},{"key":"16","doi-asserted-by":"crossref","unstructured":"[16] Ohgita, T., Namba, N., Kono, H., Shimanouchi, T., Saito, H. Mechanisms of enhanced aggregation and fibril formation of Parkinson\u2019s disease-related variants of \u03b1-synuclein. Sci. Rep. 12, 6770 (2022). https:\/\/doi.org\/10.1038\/s41598-022-10789-6","DOI":"10.1038\/s41598-022-10789-6"},{"key":"17","doi-asserted-by":"crossref","unstructured":"[17] Ohgita, T., Kono, H., Morita, I., Oyama, H., Shimanouchi, T., Kobayashi, N., et al. Intramolecular interaction kinetically regulates fibril formation by human and mouse \u03b1-synuclein. Sci. Rep. 13, 10885 (2023). https:\/\/doi.org\/10.1038\/s41598-023-38070-4","DOI":"10.1038\/s41598-023-38070-4"},{"key":"18","doi-asserted-by":"crossref","unstructured":"[18] Mizuguchi, C., Nakagawa, M., Namba, N., Sakai, M., Kurimitsu, N., Suzuki, A., et al. Mechanisms of aggregation and fibril formation of the amyloidogenic N-terminal fragment of apolipoprotein A-I. J. Biol. Chem. 294, 13515\u201313524 (2019). https:\/\/doi.org\/10.1074\/jbc.RA119.008000","DOI":"10.1074\/jbc.RA119.008000"},{"key":"19","doi-asserted-by":"crossref","unstructured":"[19] Namba, N., Ohgita, T., Tamagaki-Asahina, H., Nishitsuji, K., Shimanouchi, T., Sato, T., et al. Amyloidogenic 60\u201371 deletion\/VarThr insertion mutation of apolipoprotein A-I generates a new aggregation-prone segment that promotes nucleation through entropic effects. Sci. Rep. 13, 18514 (2023). https:\/\/doi.org\/10.1038\/s41598-023-45803-y","DOI":"10.1038\/s41598-023-45803-y"},{"key":"20","doi-asserted-by":"crossref","unstructured":"[20] Fouke, K. E., Wegman, M. E., Weber, S. A., Brady, E. B., Rom\u00e1n-Vendrell, C., Morgan, J. R. Synuclein regulates synaptic vesicle clustering and docking at a vertebrate synapse. Front. Cell Dev. Biol. 9, 774650 (2021). https:\/\/doi.org\/10.3389\/fcell.2021.774650","DOI":"10.3389\/fcell.2021.774650"},{"key":"21","doi-asserted-by":"crossref","unstructured":"[21] Man, W. K., Tahirbegi, B., Vrettas, M. D., Preet, S., Ying, L., Vendruscolo, M., et al. The docking of synaptic vesicles on the presynaptic membrane induced by \u03b1-synuclein is modulated by lipid composition. Nat. Commun. 12, 927 (2021). https:\/\/doi.org\/10.1038\/s41467-021-21027-4","DOI":"10.1038\/s41467-021-21027-4"},{"key":"22","doi-asserted-by":"crossref","unstructured":"[22] Wang, C., Zhao, C., Li, D., Tian, Z., Lai, Y., Diao, J., et al. Versatile structures of \u03b1-synuclein. Front. Mol. Neurosci. 9, 48 (2016). https:\/\/doi.org\/10.3389\/fnmol.2016.00048","DOI":"10.3389\/fnmol.2016.00048"},{"key":"23","doi-asserted-by":"crossref","unstructured":"[23] Alam, P., Bousset, L., Melki, R., Otzen, D. E. \u03b1-Synuclein oligomers and fibrils: A spectrum of species, a spectrum of toxicities. J. Neurochem. 150, 522\u2013534 (2019). https:\/\/doi.org\/10.1111\/jnc.14808","DOI":"10.1111\/jnc.14808"},{"key":"24","doi-asserted-by":"crossref","unstructured":"[24] Goedert, M., Jakes, R., Spillantini, M. G. The synucleinopathies: Twenty years on. J. Parkinsons Dis. 7, S51\u2013S69 (2017). https:\/\/doi.org\/10.3233\/JPD-179005","DOI":"10.3233\/JPD-179005"},{"key":"25","doi-asserted-by":"crossref","unstructured":"[25] Flagmeier, P., Meisl, G., Vendruscolo, M., Knowles, T. P. J., Dobson, C. M., Buell, A. K., et al. Mutations associated with familial Parkinson\u2019s disease alter the initiation and amplification steps of alpha-synuclein aggregation. Proc. Natl. Acad. Sci. U.S.A. 113, 10328\u201310333 (2016). https:\/\/doi.org\/10.1073\/pnas.1604645113","DOI":"10.1073\/pnas.1604645113"},{"key":"26","doi-asserted-by":"crossref","unstructured":"[26] Zhang, Z., Kang, S. S., Liu, X., Ahn, E. H., Zhang, Z., He, L., et al. Asparagine endopeptidase cleaves alpha-synuclein and mediates pathologic activities in Parkinson\u2019s disease. Nat. Struct. Mol. Biol. 24, 632\u2013642 (2017). https:\/\/doi.org\/10.1038\/nsmb.3433","DOI":"10.1038\/nsmb.3433"},{"key":"27","doi-asserted-by":"crossref","unstructured":"[27] McGlinchey, R. P., Lacy, S. M., Huffer, K. E., Tayebi, N., Sidransky, E., Lee, J. C. C-terminal \u03b1-synuclein truncations are linked to cysteine cathepsin activity in Parkinson\u2019s disease. J. Biol. Chem. 294, 9973\u20139984 (2019). https:\/\/doi.org\/10.1074\/jbc.RA119.008930","DOI":"10.1074\/jbc.RA119.008930"},{"key":"28","doi-asserted-by":"crossref","unstructured":"[28] Sonustun, B., Altay, M. F., Strand, C., Ebanks, K., Hondhamuni, G., Warner, T. T., et al. Pathological relevance of post-translationally modified alpha-synuclein (pSer87, pSer129, nTyr39) in idiopathic Parkinson\u2019s disease and multiple system atrophy. Cells 11, 906 (2022). https:\/\/doi.org\/10.3390\/cells11050906","DOI":"10.3390\/cells11050906"},{"key":"29","doi-asserted-by":"crossref","unstructured":"[29] Paleologou, K. E., Oueslati, A., Shakked, G., Rospigliosi, C. C., Kim, H. Y., Lamberto, G. R., et al. Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions. J. Neurosci. 30, 3184\u20133198 (2010). https:\/\/doi.org\/10.1523\/JNEUROSCI.5922-09.2010","DOI":"10.1523\/JNEUROSCI.5922-09.2010"},{"key":"30","doi-asserted-by":"crossref","unstructured":"[30] Stephens, A. D., Zacharopoulou, M., Moons, R., Fusco, G., Seetaloo, N., Chiki, A., et al. Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity. Nat. Commun. 11, 2820 (2020). https:\/\/doi.org\/10.1038\/s41467-020-16564-3","DOI":"10.1038\/s41467-020-16564-3"},{"key":"31","doi-asserted-by":"crossref","unstructured":"[31] Ranjan, P., Kumar, A. Perturbation in long-range contacts modulates the kinetics of amyloid formation in \u03b1-synuclein familial mutants. ACS Chem. Neurosci. 8, 2235\u20132246 (2017). https:\/\/doi.org\/10.1021\/acschemneuro.7b00149","DOI":"10.1021\/acschemneuro.7b00149"},{"key":"32","doi-asserted-by":"crossref","unstructured":"[32] Cohen, S. I. A., Cukalevski, R., Michaels, T. C. T., Saric, A., Tornquist, M., Vendruscolo, M., et al. Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-beta peptide. Nat. Chem. 10, 523\u2013531 (2018). https:\/\/doi.org\/10.1038\/s41557-018-0023-x","DOI":"10.1038\/s41557-018-0023-x"},{"key":"33","doi-asserted-by":"crossref","unstructured":"[33] Saric, A., Buell, A. K., Meisl, G., Michaels, T. C. T., Dobson, C. M., Linse, S., et al. Physical determinants of the self-replication of protein fibrils. Nat. Phys. 12, 874\u2013880 (2016). https:\/\/doi.org\/10.1038\/nphys3828","DOI":"10.1038\/nphys3828"},{"key":"34","doi-asserted-by":"crossref","unstructured":"[34] Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., et al. Mutation in the alpha-synuclein gene identified in families with Parkinson\u2019s disease. Science 276, 2045\u20132047 (1997). https:\/\/doi.org\/10.1126\/science.276.5321.2045","DOI":"10.1126\/science.276.5321.2045"},{"key":"35","doi-asserted-by":"crossref","unstructured":"[35] Prymaczok, N. C., Riek, R., Gerez, J. More than a rumor spreads in Parkinson\u2019s disease. Front. Hum. Neurosci. 10, 608 (2016). https:\/\/doi.org\/10.3389\/fnhum.2016.00608","DOI":"10.3389\/fnhum.2016.00608"},{"key":"36","doi-asserted-by":"crossref","unstructured":"[36] Terada, M., Suzuki, G., Nonaka, T., Kametani, F., Tamaoka, A., Hasegawa, M. The effect of truncation on prion-like properties of \u03b1-synuclein. J. Biol. Chem. 293, 13910\u201313920 (2018). https:\/\/doi.org\/10.1074\/jbc.RA118.001862","DOI":"10.1074\/jbc.RA118.001862"},{"key":"37","doi-asserted-by":"crossref","unstructured":"[37] Sorrentino, Z. A., Vijayaraghavan, N., Gorion, K. M., Riffe, C. J., Strang, K. H., Caldwell, J., et al. Physiological C-terminal truncation of \u03b1-synuclein potentiates the prion-like formation of pathological inclusions. J. Biol. Chem. 293, 18914\u201318932 (2018). https:\/\/doi.org\/10.1074\/jbc.RA118.005603","DOI":"10.1074\/jbc.RA118.005603"},{"key":"38","doi-asserted-by":"crossref","unstructured":"[38] Landeck, N., Strathearn, K. E., Ysselstein, D., Buck, K., Dutta, S., Banerjee, S., et al. Two C-terminal sequence variations determine differential neurotoxicity between human and mouse alpha-synuclein. Mol. Neurodegener. 15, 49 (2020). https:\/\/doi.org\/10.1186\/s13024-020-00380-w","DOI":"10.1186\/s13024-020-00380-w"},{"key":"39","doi-asserted-by":"crossref","unstructured":"[39] Sahin, C., Kj\u00e6r, L., Christensen, M. S., N. Pedersen, J., Christiansen, G., P\u00e9rez, A. W., et al. \u03b1-Synucleins from animal species show low fibrillation propensities and weak oligomer membrane disruption. Biochemistry 57, 5145\u20135158 (2018). https:\/\/doi.org\/10.1021\/acs.biochem.8b00627","DOI":"10.1021\/acs.biochem.8b00627"},{"key":"40","doi-asserted-by":"crossref","unstructured":"[40] Frankel, R., Sparr, E., Linse, S. On the aggregation of apolipoprotein A-I. Int. J. Mol. Sci. 23, 8780 (2022). https:\/\/doi.org\/10.3390\/ijms23158780","DOI":"10.3390\/ijms23158780"},{"key":"41","doi-asserted-by":"crossref","unstructured":"[41] Eriksson, M., Sch\u00f6nland, S., Yumlu, S., Hegenbartet, U., von Hutten, H., Gioeva, Z., et al. Hereditary apolipoprotein AI-associated amyloidosis in surgical pathology specimens: Identification of three novel mutations in the APOA1 gene. J. Mol. Diagn. 11, 257\u2013262 (2009). https:\/\/doi.org\/10.2353\/jmoldx.2009.080161","DOI":"10.2353\/jmoldx.2009.080161"},{"key":"42","doi-asserted-by":"crossref","unstructured":"[42] Gursky O. Novel clinical manifestations and treatment of hereditary apoA-I amyloidosis: When a good protein turns bad. Kidney Int. 98, 62\u201364 (2020). https:\/\/doi.org\/10.1016\/j.kint.2020.03.030","DOI":"10.1016\/j.kint.2020.03.030"},{"key":"43","doi-asserted-by":"crossref","unstructured":"[43] Colombat, M., Aldigier, J. C., Rothschild, P. R., Javaugue, V., Desport, E., Frouget, T., et al. New clinical forms of hereditary apoA-I amyloidosis entail both glomerular and retinal amyloidosis. Kidney Int. 98, 195\u2013208 (2020). https:\/\/doi.org\/10.1016\/j.kint.2020.03.033","DOI":"10.1016\/j.kint.2020.03.033"},{"key":"44","doi-asserted-by":"crossref","unstructured":"[44] Del Giudice, R., Lindvall, M., Nilsson, O., Monti, D. M., Lagerstedt, J. O. The apparent organ-specificity of amyloidogenic apoA-I variants is linked to tissue-specific extracellular matrix components. Int. J. Mol. Sci. 24, 318 (2022). https:\/\/doi.org\/10.3390\/ijms24010318","DOI":"10.3390\/ijms24010318"},{"key":"45","doi-asserted-by":"crossref","unstructured":"[45] Gillmore, J. D., Stangou, A. J., Lachmann, H. J., Goodman, H. J., Wechalekar, A. D., Acheson, J., et al. Organ transplantation in hereditary apolipoprotein AI amyloidosis. Am. J. Transplant. 6, 2342\u20132347 (2006). https:\/\/doi.org\/10.1111\/j.1600-6143.2006.01507.x","DOI":"10.1111\/j.1600-6143.2006.01507.x"},{"key":"46","doi-asserted-by":"crossref","unstructured":"[46] Bains, G., Patel, A. B., Narayanaswami, V. Pyrene: A probe to study protein conformation and conformational changes. Molecules 16, 7909\u20137935 (2011). https:\/\/doi.org\/10.3390\/molecules16097909","DOI":"10.3390\/molecules16097909"},{"key":"47","doi-asserted-by":"crossref","unstructured":"[47] Sidhu, A., Vaneyck, J., Blum, C., Segers-Nolten, I., Subramaniam, V. Polymorph-specific distribution of binding sites determines thioflavin-T fluorescence intensity in \u03b1-synuclein fibrils. Amyloid 25, 189\u2013196 (2018). https:\/\/doi.org\/10.1080\/13506129.2018.1517736","DOI":"10.1080\/13506129.2018.1517736"},{"key":"48","doi-asserted-by":"crossref","unstructured":"[48] Stankovi\u0107, I. M., Niu, S., Hall, M. B., Zari\u0107, S. D. Role of aromatic amino acids in amyloid self-assembly. Int. J. Biol. Macromol. 156, 949\u2013959 (2020). https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.03.064","DOI":"10.1016\/j.ijbiomac.2020.03.064"},{"key":"49","doi-asserted-by":"crossref","unstructured":"[49] Doherty, C. P. A., Ulamec, S. M., Maya-Martinez, R., Good, S. C., Makepeace, J., Khan, G. N., et al. A short motif in the N-terminal region of alpha-synuclein is critical for both aggregation and function. Nat. Struct. Mol. Biol. 27, 249\u2013259 (2020). https:\/\/doi.org\/10.1038\/s41594-020-0384-x","DOI":"10.1038\/s41594-020-0384-x"},{"key":"50","doi-asserted-by":"crossref","unstructured":"[50] Ohgita, T., Furutani, Y., Nakano, M., Hattori, M., Suzuki, A., Nakagawa, M., et al. Novel conformation-selective monoclonal antibodies against apoA-I amyloid fibrils. FEBS J. 288, 1496\u20131513 (2021). https:\/\/doi.org\/10.1111\/febs.15487","DOI":"10.1111\/febs.15487"},{"key":"51","doi-asserted-by":"crossref","unstructured":"[51] Tuttle, M. D., Comellas, G., Nieuwkoop, A. J., Covell, D. J., Berthold, D. A., Kloepper, K. D., et al. Solid-state NMR structure of a pathogenic fibril of full-length human \u03b1-synuclein. Nat. Struct. Mol. Biol. 23, 409\u2013415 (2016). https:\/\/doi.org\/10.1038\/nsmb.3194","DOI":"10.1038\/nsmb.3194"},{"key":"52","doi-asserted-by":"crossref","unstructured":"[52] Mirecka, E. A., Shaykhalishahi, H., Gauhar, A., Akg\u00fcl, S., Lecher, J., Willbold, D., et al. Sequestration of a \u03b2-hairpin for control of \u03b1-synuclein aggregation. Angew Chem. Int. Ed. Engl. 53, 4227\u20134230 (2014). https:\/\/doi.org\/10.1002\/anie.201309001","DOI":"10.1002\/anie.201309001"},{"key":"53","doi-asserted-by":"crossref","unstructured":"[53] Szeg\u0151, \u00c9. M., Bo\u00df, F., Komnig, D., G\u00e4rtner, C., H\u00f6fs, L., Shaykhalishahi, H., et al. A \u03b2-wrapin targeting the N-terminus of \u03b1-synuclein monomers reduces fibril-induced aggregation in neurons. Front. Neurosci. 15, 696440 (2021). https:\/\/doi.org\/10.3389\/fnins.2021.696440","DOI":"10.3389\/fnins.2021.696440"},{"key":"54","doi-asserted-by":"crossref","unstructured":"[54] Kyte, J., Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105\u2013132 (1982). https:\/\/doi.org\/10.1016\/0022-2836(82)90515-0","DOI":"10.1016\/0022-2836(82)90515-0"},{"key":"55","doi-asserted-by":"crossref","unstructured":"[55] Auer, S., Ricchiuto, P., Kashchiev, D. Two-step nucleation of amyloid fibrils: Omnipresent or not? J. Mol. Biol. 422, 723\u2013730 (2012). https:\/\/doi.org\/10.1016\/j.jmb.2012.06.022","DOI":"10.1016\/j.jmb.2012.06.022"},{"key":"56","doi-asserted-by":"crossref","unstructured":"[56] Goto, Y., Noji, M., Nakajima K., Yamaguchi, K. Supersaturation-dependent formation of amyloid fibrils. Molecules 27, 4588 (2022). https:\/\/doi.org\/10.3390\/molecules27144588","DOI":"10.3390\/molecules27144588"},{"key":"57","doi-asserted-by":"crossref","unstructured":"[57] Bigi, A., Cascella, R., Chiti, F., Cecchi, C. Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases. Bioessays 44, e2200086 (2022). https:\/\/doi.org\/10.1002\/bies.202200086","DOI":"10.1002\/bies.202200086"},{"key":"58","doi-asserted-by":"crossref","unstructured":"[58] Ghosh, S., Ali, R., Verma, S. A\u03b2-oligomers: A potential therapeutic target for Alzheimer\u2019s disease. Int. J. Biol. 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