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A new era for understanding amyloid structures and disease. Nat. Rev. Mol. Cell Biol. 19, 755\u2013773 (2018). https:\/\/doi.org\/10.1038\/s41580-018-0060-8","DOI":"10.1038\/s41580-018-0060-8"},{"key":"5","doi-asserted-by":"crossref","unstructured":"[5] Bemporad, F., Chiti, F. Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem. Biol. 19, 315\u2013327 (2012). https:\/\/doi.org\/10.1016\/j.chembiol.2012.02.003","DOI":"10.1016\/j.chembiol.2012.02.003"},{"key":"6","doi-asserted-by":"crossref","unstructured":"[6] Chatani, E., Yamamoto, N. Recent progress on understanding the mechanisms of amyloid nucleation. Biophys. Rev. 10, 527\u2013534 (2018). https:\/\/doi.org\/10.1007\/s12551-017-0353-8","DOI":"10.1007\/s12551-017-0353-8"},{"key":"7","doi-asserted-by":"crossref","unstructured":"[7] Masters, C.\u00a0L., Simms, G., Weinman, N.\u00a0A., Multhaup, G., Mcdonald, B.\u00a0L., Beyreuther, K. Amyloid plaque core protein in alzheimer-disease and down syndrome. Proc. Natl. Acad. Sci. U.S.A. 82, 4245\u20134249 (1985). https:\/\/doi.org\/10.1073\/pnas.82.12.4245","DOI":"10.1073\/pnas.82.12.4245"},{"key":"8","doi-asserted-by":"crossref","unstructured":"[8] Shi, Y., Kirwan, P., Smith, J., MacLean, G., Orkin, S.\u00a0H., Livesey, F.\u00a0J. A human stem cell model of early alzheimer\u2019s disease pathology in down syndrome. Sci. Transl. Med. 4, 124ra29 (2012). https:\/\/doi.org\/10.1126\/scitranslmed.3003771","DOI":"10.1126\/scitranslmed.3003771"},{"key":"9","doi-asserted-by":"crossref","unstructured":"[9] Chatani, E., Imamura, H., Yamamoto, N., Kato, M. Stepwise organization of the \u03b2-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils. J. Biol. Chem. 289, 10399\u201310410 (2014). https:\/\/doi.org\/10.1074\/jbc.M113.520874","DOI":"10.1074\/jbc.M113.520874"},{"key":"10","doi-asserted-by":"crossref","unstructured":"[10] Lee, J., Culyba, E.\u00a0K., Powers, E.\u00a0T., Kelly, J.\u00a0W. Amyloid-\u03b2 forms fibrils by nucleated conformational conversion of oligomers. Nat. Chem. Biol. 7, 602\u2013609 (2011). https:\/\/doi.org\/10.1038\/nchembio.624","DOI":"10.1038\/nchembio.624"},{"key":"11","doi-asserted-by":"crossref","unstructured":"[11] Bleiholder, C., Dupuis, N.\u00a0F., Wyttenbach, T., Bowers, M.\u00a0T. Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to \u03b2-sheet in amyloid fibril formation. Nat. Chem. 3, 172\u2013177 (2011). https:\/\/doi.org\/10.1038\/Nchem.945","DOI":"10.1038\/nchem.945"},{"key":"12","doi-asserted-by":"crossref","unstructured":"[12] Chimon, S., Shaibat, M.\u00a0A., Jones, C.\u00a0R., Calero, D.\u00a0C., Aizezi, B., Ishii, Y. Evidence of fibril-like \u03b2-sheet structures in a neurotoxic amyloid intermediate of alzheimer\u2019s \u03b2-amyloid. Nat. Struct. Mol. Biol. 14, 1157\u20131164 (2007). https:\/\/doi.org\/10.1038\/nsmb1345","DOI":"10.1038\/nsmb1345"},{"key":"13","doi-asserted-by":"crossref","unstructured":"[13] Nilsson, M.\u00a0R., Dobson, C.\u00a0M. Chemical modification of insulin in amyloid fibrils. Protein Sci. 12, 2637\u20132641 (2003). https:\/\/doi.org\/10.1110\/ps.0360403","DOI":"10.1110\/ps.0360403"},{"key":"14","doi-asserted-by":"crossref","unstructured":"[14] Weiss, M.\u00a0A. The structure and function of insulin: Decoding the tr transition. Vitam. Horm. 80, 33\u201349 (2009). https:\/\/doi.org\/10.1016\/S0083-6729(08)00602-X","DOI":"10.1016\/S0083-6729(08)00602-X"},{"key":"15","doi-asserted-by":"crossref","unstructured":"[15] Dische, F.\u00a0E., Wernstedt, C., Westermark, G.\u00a0T., Westermark, P., Pepys, M.\u00a0B., Rennie, J.\u00a0A., et al. Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient. Diabetologia 31, 158\u2013161 (1988). https:\/\/doi.org\/10.1007\/Bf00276849","DOI":"10.1007\/BF00276849"},{"key":"16","doi-asserted-by":"crossref","unstructured":"[16] Mori, W., Yuzu, K., Lobsiger, N., Nishioka, H., Sato, H., Nagase, T., et al. Degradation of insulin amyloid by antibiotic minocycline and formation of toxic intermediates. Sci. Rep. 11, 6857 (2021). https:\/\/doi.org\/10.1038\/s41598-021-86001-y","DOI":"10.1038\/s41598-021-86001-y"},{"key":"17","doi-asserted-by":"crossref","unstructured":"[17] Yuzu, K., Lindgren, M., Nystrom, S., Zhang, J., Mori, W., Kunitomi, R., et al. Insulin amyloid polymorphs: Implications for iatrogenic cytotoxicity. RSC Adv. 10, 37721\u201337727 (2020). https:\/\/doi.org\/10.1039\/d0ra07742a","DOI":"10.1039\/D0RA07742A"},{"key":"18","doi-asserted-by":"crossref","unstructured":"[18] Yamamoto, N., Tsuhara, S., Tamura, A., Chatani, E. 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Biol. 421, 499\u2013516 (2012). https:\/\/doi.org\/10.1016\/j.jmb.2012.01.004","DOI":"10.1016\/j.jmb.2012.01.004"},{"key":"26","doi-asserted-by":"crossref","unstructured":"[26] Tang, H.\u00a0D., Fu, Y., Zhan, S.\u00a0L., Luo, Y.\u00a0Z. \u03b1<sub>E<\/sub>C, the c-terminal extension of fibrinogen, has chaperone-like activity. Biochemistry 48, 3967\u20133976 (2009). https:\/\/doi.org\/10.1021\/bi900015n","DOI":"10.1021\/bi900015n"},{"key":"27","doi-asserted-by":"crossref","unstructured":"[27] Tang, H.\u00a0D., Fu, Y., Cui, Y.\u00a0J., He, Y.\u00a0B., Zeng, X., Ploplis, V.\u00a0A., et al. Fibrinogen has chaperone-like activity. Biochem. Biophys. Res. Commun. 378, 662\u2013667 (2009). https:\/\/doi.org\/10.1016\/j.bbrc.2008.11.112","DOI":"10.1016\/j.bbrc.2008.11.112"},{"key":"28","doi-asserted-by":"crossref","unstructured":"[28] Smith, S.\u00a0G., Walter, L.\u00a0G., Walker, M.\u00a0R. 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Structural development of amyloid precursors in insulin B chain and the inhibition effect by fibrinogen. bioRxiv (2021). https:\/\/doi.org\/10.1101\/2021.12.26.474222","DOI":"10.1101\/2021.12.26.474222"},{"key":"32","doi-asserted-by":"crossref","unstructured":"[32] Vestergaard, B., Groenning, M., Roessle, M., Kastrup, J.\u00a0S., van de Weert, M., Flink, J.\u00a0M., et al. A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils. PloS Biol. 5, 1089\u20131097 (2007). https:\/\/doi.org\/10.1371\/journal.pbio.0050134","DOI":"10.1371\/journal.pbio.0050134"},{"key":"33","doi-asserted-by":"crossref","unstructured":"[33] Oliveira, C.\u00a0L.\u00a0P., Behrens, M.\u00a0A., Pedersen, J.\u00a0S., Erlacher, K., Otzen, D., Pedersen, J.\u00a0S. A SAXS study of glucagon fibrillation. J. Mol. Biol. 387, 147\u2013161 (2009). https:\/\/doi.org\/10.1016\/j.jmb.2009.01.020","DOI":"10.1016\/j.jmb.2009.01.020"},{"key":"34","doi-asserted-by":"crossref","unstructured":"[34] Luo, J.\u00a0H., Warmlander, S.\u00a0K.\u00a0T.\u00a0S., Graslund, A., Abrahams, J.\u00a0P. Non-chaperone proteins can inhibit aggregation and cytotoxicity of alzheimer amyloid \u03b2 peptide. J. Biol. 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