{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T16:24:57Z","timestamp":1792167897571,"version":"4.4.0"},"reference-count":74,"publisher":"Springer Science and Business Media LLC","issue":"11","license":[{"start":{"date-parts":[[2020,9,14]],"date-time":"2020-09-14T00:00:00Z","timestamp":1600041600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2020,9,14]],"date-time":"2020-09-14T00:00:00Z","timestamp":1600041600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2020,11]]},"DOI":"10.1038\/s41594-020-0496-3","type":"journal-article","created":{"date-parts":[[2020,9,14]],"date-time":"2020-09-14T12:04:18Z","timestamp":1600085058000},"page":"1048-1056","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":115,"title":["Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly"],"prefix":"10.1038","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1584-3564","authenticated-orcid":false,"given":"Rodrigo","family":"Gallardo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew G.","family":"Iadanza","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8389-4120","authenticated-orcid":false,"given":"Yong","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6431-2191","authenticated-orcid":false,"given":"George R.","family":"Heath","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard","family":"Foster","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3079-8039","authenticated-orcid":false,"given":"Sheena E.","family":"Radford","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3640-5275","authenticated-orcid":false,"given":"Neil A.","family":"Ranson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2020,9,14]]},"reference":[{"key":"496_CR1","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41580-018-0060-8","volume":"19","author":"MG Iadanza","year":"2018","unstructured":"Iadanza, M. G., Jackson, M. P., Hewitt, E. W., Ranson, N. A. & Radford, S. E. A new era for understanding amyloid structures and disease. Nat. Rev. Mol. Cell Biol. 19, 755\u2013773 (2018).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"496_CR2","doi-asserted-by":"publisher","unstructured":"Otzen, D. & Riek, R. Functional amyloids. Cold Spring Harb. Perspect. Biol. https:\/\/doi.org\/10.1101\/cshperspect.a033860 (2019).","DOI":"10.1101\/cshperspect.a033860"},{"key":"496_CR3","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nature23002","volume":"547","author":"AWP Fitzpatrick","year":"2017","unstructured":"Fitzpatrick, A. W. P. et al. Cryo-EM structures of tau filaments from Alzheimer\u2019s disease. Nature 547, 185\u2013190 (2017).","journal-title":"Nature"},{"key":"496_CR4","doi-asserted-by":"crossref","first-page":"4760","DOI":"10.1038\/s41467-019-12683-8","volume":"10","author":"M Kollmer","year":"2019","unstructured":"Kollmer, M. et al. Cryo-EM structure and polymorphism of A\u03b2 amyloid fibrils purified from Alzheimer\u2019s brain tissue. Nat. Commun. 10, 4760 (2019).","journal-title":"Nat. Commun."},{"key":"496_CR5","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1038\/s41586-018-0454-y","volume":"561","author":"B Falcon","year":"2018","unstructured":"Falcon, B. et al. Structures of filaments from Pick\u2019s disease reveal a novel tau protein fold. Nature 561, 137\u2013140 (2018).","journal-title":"Nature"},{"key":"496_CR6","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1038\/s41586-019-1026-5","volume":"568","author":"B Falcon","year":"2019","unstructured":"Falcon, B. et al. Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Nature 568, 420\u2013423 (2019).","journal-title":"Nature"},{"key":"496_CR7","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/s41586-020-2043-0","volume":"580","author":"W Zhang","year":"2020","unstructured":"Zhang, W. et al. Novel tau filament fold in corticobasal degeneration. Nature 580, 283\u2013287 (2020).","journal-title":"Nature"},{"key":"496_CR8","doi-asserted-by":"publisher","unstructured":"Schweighauser, M. et al. Structures of \u03b1-synuclein filaments from multiple system atrophy. Nature https:\/\/doi.org\/10.1038\/s41586-020-2317-6 (2020).","DOI":"10.1038\/s41586-020-2317-6"},{"key":"496_CR9","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-09033-z","volume":"10","author":"F Liberta","year":"2019","unstructured":"Liberta, F. et al. Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids. Nat. Commun. 10, 1104 (2019).","journal-title":"Nat. Commun."},{"key":"496_CR10","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-09032-0","volume":"10","author":"L Radamaker","year":"2019","unstructured":"Radamaker, L. et al. Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis. Nat. Commun. 10, 1103 (2019).","journal-title":"Nat. Commun."},{"key":"496_CR11","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-09133-w","volume":"10","author":"P Swuec","year":"2019","unstructured":"Swuec, P. et al. Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient. Nat. Commun. 10, 1269 (2019).","journal-title":"Nat. Commun."},{"key":"496_CR12","volume":"10","author":"M Schmidt","year":"2019","unstructured":"Schmidt, M. et al. Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis. Nat. Commun. 10, 5008 (2019).","journal-title":"Nat. Commun."},{"key":"496_CR13","doi-asserted-by":"crossref","first-page":"1044","DOI":"10.1038\/s41594-019-0322-y","volume":"26","author":"DR Boyer","year":"2019","unstructured":"Boyer, D. R. et al. Structures of fibrils formed by \u03b1-synuclein hereditary disease mutant H50Q reveal new polymorphs. Nat. Struct. Mol. Biol. 26, 1044\u20131052 (2019).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"496_CR14","doi-asserted-by":"crossref","first-page":"3592","DOI":"10.1073\/pnas.1917914117","volume":"117","author":"DR Boyer","year":"2020","unstructured":"Boyer, D. R. et al. The \u03b1-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure. Proc. Natl Acad. Sci. USA 117, 3592\u20133602 (2020).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"496_CR15","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/0006-291X(86)90708-4","volume":"140","author":"P Westermark","year":"1986","unstructured":"Westermark, P., Wernstedt, C., Wilander, E. & Sletten, K. A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. Biochem. Biophys. Res. Commun. 140, 827\u2013831 (1986).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"496_CR16","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-018-03651-9","volume":"9","author":"M Birol","year":"2018","unstructured":"Birol, M., Kumar, S., Rhoades, E. & Miranker, A. D. Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid. Nat. Commun. 9, 1312 (2018).","journal-title":"Nat. Commun."},{"key":"496_CR17","doi-asserted-by":"crossref","first-page":"R121","DOI":"10.1530\/JME-17-0105","volume":"59","author":"D Raleigh","year":"2017","unstructured":"Raleigh, D., Zhang, X., Hastoy, B. & Clark, A. The \u03b2-cell assassin: IAPP cytotoxicity. J. Mol. Endocrinol. 59, R121\u2013R140 (2017).","journal-title":"J. Mol. Endocrinol."},{"key":"496_CR18","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.2337\/diab.45.9.1279","volume":"45","author":"S Sakagashira","year":"1996","unstructured":"Sakagashira, S. et al. Missense mutation of amylin gene (S20G) in Japanese NIDDM patients. Diabetes 45, 1279\u20131281 (1996).","journal-title":"Diabetes"},{"key":"496_CR19","doi-asserted-by":"crossref","first-page":"2166","DOI":"10.1007\/s00125-016-4045-x","volume":"59","author":"DT Meier","year":"2016","unstructured":"Meier, D. T. et al. The S20G substitution in hIAPP is more amyloidogenic and cytotoxic than wild-type hIAPP in mouse islets. Diabetologia 59, 2166\u20132171 (2016).","journal-title":"Diabetologia"},{"key":"496_CR20","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1016\/S0002-9440(10)64848-1","volume":"157","author":"S Sakagashira","year":"2000","unstructured":"Sakagashira, S. et al. S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin. Am. J. Pathol. 157, 2101\u20132109 (2000).","journal-title":"Am. J. Pathol."},{"key":"496_CR21","doi-asserted-by":"crossref","first-page":"5030","DOI":"10.1039\/C7SC00620A","volume":"8","author":"LM Young","year":"2017","unstructured":"Young, L. M., Tu, L. H., Raleigh, D. P., Ashcroft, A. E. & Radford, S. E. Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers. Chem. Sci. 8, 5030\u20135040 (2017).","journal-title":"Chem. Sci."},{"key":"496_CR22","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1006\/jmbi.2001.4593","volume":"308","author":"ET Jaikaran","year":"2001","unstructured":"Jaikaran, E. T. et al. Identification of a novel human islet amyloid polypeptide \u03b2-sheet domain and factors influencing fibrillogenesis. J. Mol. Biol. 308, 515\u2013525 (2001).","journal-title":"J. Mol. Biol."},{"key":"496_CR23","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1006\/jsbi.2000.4268","volume":"130","author":"C Goldsbury","year":"2000","unstructured":"Goldsbury, C. et al. Amyloid fibril formation from full-length and fragments of amylin. J. Struct. Biol. 130, 352\u2013362 (2000).","journal-title":"J. Struct. Biol."},{"key":"496_CR24","doi-asserted-by":"crossref","first-page":"5036","DOI":"10.1073\/pnas.87.13.5036","volume":"87","author":"P Westermark","year":"1990","unstructured":"Westermark, P., Engstrom, U., Johnson, K. H., Westermark, G. T. & Betsholtz, C. Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. Proc. Natl Acad. Sci. USA 87, 5036\u20135040 (1990).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"496_CR25","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1021\/ja00028a073","volume":"114","author":"TT Ashburn","year":"1992","unstructured":"Ashburn, T. T., Auger, M. & Lansbury, P. T. Jr. The structural basis of pancreatic amyloid formation: isotope-edited spectroscopy in the solid state. J. Am. Chem. Soc. 114, 790\u2013791 (1992).","journal-title":"J. Am. Chem. Soc."},{"key":"496_CR26","doi-asserted-by":"crossref","first-page":"5810","DOI":"10.1021\/acs.jpcb.5b09981","volume":"120","author":"AB Soriaga","year":"2016","unstructured":"Soriaga, A. B., Sangwan, S., Macdonald, R., Sawaya, M. R. & Eisenberg, D. Crystal structures of IAPP amyloidogenic segments reveal a novel packing motif of out-of-register beta sheets. J. Phys. Chem. B 120, 5810\u20135816 (2016).","journal-title":"J. Phys. Chem. B"},{"key":"496_CR27","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1110\/ps.036509.108","volume":"17","author":"JJ Wiltzius","year":"2008","unstructured":"Wiltzius, J. J. et al. Atomic structure of the cross-\u03b2 spine of islet amyloid polypeptide (amylin). Protein Sci. 17, 1467\u20131474 (2008).","journal-title":"Protein Sci."},{"key":"496_CR28","doi-asserted-by":"crossref","first-page":"9663","DOI":"10.1021\/jacs.6b05129","volume":"138","author":"MT Colvin","year":"2016","unstructured":"Colvin, M. T. et al. Atomic resolution structure of monomorphic A\u03b242 amyloid fibrils. J. Am. Chem. Soc. 138, 9663\u20139674 (2016).","journal-title":"J. Am. Chem. Soc."},{"key":"496_CR29","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1126\/science.aao2825","volume":"358","author":"L Gremer","year":"2017","unstructured":"Gremer, L. et al. Fibril structure of amyloid-\u03b2(1\u201342) by cryo-electron microscopy. Science 358, 116\u2013119 (2017).","journal-title":"Science"},{"key":"496_CR30","doi-asserted-by":"crossref","first-page":"E4976","DOI":"10.1073\/pnas.1600749113","volume":"113","author":"MA Walti","year":"2016","unstructured":"Walti, M. A. et al. Atomic-resolution structure of a disease-relevant A\u03b2(1\u201342) amyloid fibril. Proc. Natl Acad. Sci. USA 113, E4976\u2013E4984 (2016).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"496_CR31","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nsmb.2991","volume":"22","author":"Y Xiao","year":"2015","unstructured":"Xiao, Y. et al. A\u03b2(1\u201342) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer\u2019s disease. Nat. Struct. Mol. Biol. 22, 499\u2013505 (2015).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"496_CR32","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.sbi.2019.09.001","volume":"60","author":"R Gallardo","year":"2020","unstructured":"Gallardo, R., Ranson, N. A. & Radford, S. E. Amyloid structures: much more than just a cross-\u03b2 fold. Curr. Opin. Struct. Biol. 60, 7\u201316 (2020).","journal-title":"Curr. Opin. Struct. Biol."},{"key":"496_CR33","doi-asserted-by":"crossref","first-page":"e56467","DOI":"10.1371\/journal.pone.0056467","volume":"8","author":"AT Alexandrescu","year":"2013","unstructured":"Alexandrescu, A. T. Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR. PLoS ONE 8, e56467 (2013).","journal-title":"PLoS ONE"},{"key":"496_CR34","doi-asserted-by":"crossref","first-page":"48420","DOI":"10.1074\/jbc.M406853200","volume":"279","author":"SA Jayasinghe","year":"2004","unstructured":"Jayasinghe, S. A. & Langen, R. Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling. J. Biol. Chem. 279, 48420\u201348425 (2004).","journal-title":"J. Biol. Chem."},{"key":"496_CR35","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmb.2005.02.029","volume":"348","author":"AV Kajava","year":"2005","unstructured":"Kajava, A. V., Aebi, U. & Steven, A. C. The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. 348, 247\u2013252 (2005).","journal-title":"J. Mol. Biol."},{"key":"496_CR36","doi-asserted-by":"crossref","first-page":"e0161243","DOI":"10.1371\/journal.pone.0161243","volume":"11","author":"F Weirich","year":"2016","unstructured":"Weirich, F. et al. Structural characterization of fibrils from recombinant human islet amyloid polypeptide by solid-state NMR: the central FGAILS segment is part of the \u03b2-sheet core. PLoS ONE 11, e0161243 (2016).","journal-title":"PLoS ONE"},{"key":"496_CR37","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","volume":"372","author":"E Krissinel","year":"2007","unstructured":"Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774\u2013797 (2007).","journal-title":"J. Mol. Biol."},{"key":"496_CR38","doi-asserted-by":"crossref","unstructured":"Seino, S. & Study Group of Comprehensive Analysis of Genetic Factors in Diabetes Mellitus. S20G mutation of the amylin gene is associated with Type II diabetes in Japanese. Diabetologia 44, 906\u2013909 (2001).","DOI":"10.1007\/s001250100531"},{"key":"496_CR39","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/s41594-020-0442-4","volume":"27","author":"C R\u00f6der","year":"2020","unstructured":"R\u00f6der, C. et al. Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-\u03b2 fibrils. Nat. Struct. Mol. Biol. 27, 660\u2013667 (2020).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"496_CR40","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1006\/jsbi.1997.3858","volume":"119","author":"CS Goldsbury","year":"1997","unstructured":"Goldsbury, C. S. et al. Polymorphic fibrillar assembly of human amylin. J. Struct. Biol. 119, 17\u201327 (1997).","journal-title":"J. Struct. Biol."},{"key":"496_CR41","doi-asserted-by":"crossref","first-page":"5235","DOI":"10.1074\/jbc.M111.327817","volume":"287","author":"S Bedrood","year":"2012","unstructured":"Bedrood, S. et al. Fibril structure of human islet amyloid polypeptide. J. Biol. Chem. 287, 5235\u20135241 (2012).","journal-title":"J. Biol. Chem."},{"key":"496_CR42","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/s41594-020-0435-3","volume":"27","author":"Q Cao","year":"2020","unstructured":"Cao, Q., Boyer, D. R., Sawaya, M. R., Ge, P. & Eisenberg, D. S. Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils. Nat. Struct. Mol. Biol. 27, 653\u2013659 (2020).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"496_CR43","doi-asserted-by":"crossref","first-page":"13505","DOI":"10.1021\/bi701427q","volume":"46","author":"S Luca","year":"2007","unstructured":"Luca, S., Yau, W. M., Leapman, R. & Tycko, R. Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry 46, 13505\u201313522 (2007).","journal-title":"Biochemistry"},{"key":"496_CR44","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1006\/jmbi.2001.4608","volume":"308","author":"SB Padrick","year":"2001","unstructured":"Padrick, S. B. & Miranker, A. D. Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway. J. Mol. Biol. 308, 783\u2013794 (2001).","journal-title":"J. Mol. Biol."},{"key":"496_CR45","doi-asserted-by":"crossref","first-page":"2888","DOI":"10.1074\/jbc.M117.806109","volume":"293","author":"P Krotee","year":"2018","unstructured":"Krotee, P. et al. Common fibrillar spines of amyloid-\u03b2 and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors. J. Biol. Chem. 293, 2888\u20132902 (2018).","journal-title":"J. Biol. Chem."},{"key":"496_CR46","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1038\/nsmb.1643","volume":"16","author":"JJ Wiltzius","year":"2009","unstructured":"Wiltzius, J. J. et al. Molecular mechanisms for protein-encoded inheritance. Nat. Struct. Mol. Biol. 16, 973\u2013978 (2009).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"496_CR47","doi-asserted-by":"crossref","first-page":"8452","DOI":"10.1074\/jbc.RA118.006454","volume":"294","author":"E Godin","year":"2019","unstructured":"Godin, E., Nguyen, P. T., Zottig, X. & Bourgault, S. Identification of a hinge residue controlling islet amyloid polypeptide self-assembly and cytotoxicity. J. Biol. Chem. 294, 8452\u20138463 (2019).","journal-title":"J. Biol. Chem."},{"key":"496_CR48","doi-asserted-by":"crossref","first-page":"8099","DOI":"10.1039\/C6DT00628K","volume":"45","author":"M Rowinska-Zyrek","year":"2016","unstructured":"Rowinska-Zyrek, M. Coordination of Zn2+ and Cu2+ to the membrane disrupting fragment of amylin. Dalton Trans. 45, 8099\u20138106 (2016).","journal-title":"Dalton Trans."},{"key":"496_CR49","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/s41594-020-0403-y","volume":"27","author":"C Glynn","year":"2020","unstructured":"Glynn, C. et al. Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core. Nat. Struct. Mol. Biol. 27, 417\u2013423 (2020).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"496_CR50","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.str.2014.10.022","volume":"23","author":"NG Sgourakis","year":"2015","unstructured":"Sgourakis, N. G., Yau, W. M. & Qiang, W. Modeling an in-register, parallel \u201cIowa\u201d A\u03b2 fibril structure using solid-state NMR data from labeled samples with Rosetta. Structure 23, 216\u2013227 (2015).","journal-title":"Structure"},{"key":"496_CR51","doi-asserted-by":"crossref","first-page":"3609","DOI":"10.1038\/s41467-018-05971-2","volume":"9","author":"B Li","year":"2018","unstructured":"Li, B. et al. Cryo-EM of full-length \u03b1-synuclein reveals fibril polymorphs with a common structural kernel. Nat. Commun. 9, 3609 (2018).","journal-title":"Nat. Commun."},{"key":"496_CR52","doi-asserted-by":"crossref","first-page":"1230","DOI":"10.1126\/science.aba3526","volume":"367","author":"R Hervas","year":"2020","unstructured":"Hervas, R. et al. Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in Drosophila. Science 367, 1230\u20131234 (2020).","journal-title":"Science"},{"key":"496_CR53","doi-asserted-by":"crossref","first-page":"6557","DOI":"10.1073\/pnas.1002555107","volume":"107","author":"W Han","year":"2010","unstructured":"Han, W. & Li, C. Linking type 2 diabetes and Alzheimer\u2019s disease. Proc. Natl Acad. Sci. USA 107, 6557\u20136558 (2010).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"496_CR54","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/S1474-4422(05)70284-2","volume":"5","author":"GJ Biessels","year":"2006","unstructured":"Biessels, G. J., Staekenborg, S., Brunner, E., Brayne, C. & Scheltens, P. Risk of dementia in diabetes mellitus: a systematic review. Lancet Neurol. 5, 64\u201374 (2006).","journal-title":"Lancet Neurol."},{"key":"496_CR55","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1007\/978-981-13-3540-2_8","volume":"1128","author":"H Hanyu","year":"2019","unstructured":"Hanyu, H. Diabetes-related dementia. Adv. Exp. Med. Biol. 1128, 147\u2013160 (2019).","journal-title":"Adv. Exp. Med. Biol."},{"key":"496_CR56","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1021\/acschemneuro.5b00192","volume":"6","author":"R Hu","year":"2015","unstructured":"Hu, R., Zhang, M., Chen, H., Jiang, B. & Zheng, J. Cross-seeding interaction between \u03b2-amyloid and human islet amyloid polypeptide. ACS Chem. Neurosci. 6, 1759\u20131768 (2015).","journal-title":"ACS Chem. Neurosci."},{"key":"496_CR57","doi-asserted-by":"crossref","first-page":"3081","DOI":"10.1002\/anie.200904902","volume":"49","author":"E Andreetto","year":"2010","unstructured":"Andreetto, E. et al. Identification of hot regions of the A\u03b2\u2013IAPP interaction interface as high-affinity binding sites in both cross- and self-association. Angew. Chem. Int. Ed. Engl. 49, 3081\u20133085 (2010).","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"496_CR58","doi-asserted-by":"crossref","first-page":"17490","DOI":"10.1074\/jbc.M311300200","volume":"279","author":"B O\u2019Nuallain","year":"2004","unstructured":"O\u2019Nuallain, B., Williams, A. D., Westermark, P. & Wetzel, R. Seeding specificity in amyloid growth induced by heterologous fibrils. J. Biol. Chem. 279, 17490\u201317499 (2004).","journal-title":"J. Biol. Chem."},{"key":"496_CR59","doi-asserted-by":"crossref","first-page":"6990","DOI":"10.1039\/C5AN00865D","volume":"140","author":"LM Young","year":"2015","unstructured":"Young, L. M. et al. Insights into the consequences of co-polymerisation in the early stages of IAPP and A\u03b2 peptide assembly from mass spectrometry. Analyst 140, 6990\u20136999 (2015).","journal-title":"Analyst"},{"key":"496_CR60","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1038\/nn0901-887","volume":"4","author":"C Nilsberth","year":"2001","unstructured":"Nilsberth, C. et al. The \u2018Arctic\u2019 APP mutation (E693G) causes Alzheimer\u2019s disease by enhanced A\u03b2 protofibril formation. Nat. Neurosci. 4, 887\u2013893 (2001).","journal-title":"Nat. Neurosci."},{"key":"496_CR61","doi-asserted-by":"crossref","first-page":"18349","DOI":"10.1073\/pnas.0806270105","volume":"105","author":"AK Paravastu","year":"2008","unstructured":"Paravastu, A. K., Leapman, R. D., Yau, W. M. & Tycko, R. Molecular structural basis for polymorphism in Alzheimer\u2019s \u03b2-amyloid fibrils. Proc. Natl Acad. Sci. USA 105, 18349\u201318354 (2008).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"496_CR62","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","volume":"154","author":"JX Lu","year":"2013","unstructured":"Lu, J. X. et al. Molecular structure of \u03b2-amyloid fibrils in Alzheimer\u2019s disease brain tissue. Cell 154, 1257\u20131268 (2013).","journal-title":"Cell"},{"key":"496_CR63","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1101\/SQB.1962.027.001.005","volume":"27","author":"DL Caspar","year":"1962","unstructured":"Caspar, D. L. & Klug, A. Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27, 1\u201324 (1962).","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"496_CR64","doi-asserted-by":"crossref","first-page":"16284","DOI":"10.1021\/bi051432v","volume":"44","author":"A Abedini","year":"2005","unstructured":"Abedini, A. & Raleigh, D. P. The role of His-18 in amyloid formation by human islet amyloid polypeptide. Biochemistry 44, 16284\u201316291 (2005).","journal-title":"Biochemistry"},{"key":"496_CR65","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.biochi.2017.07.015","volume":"142","author":"L Khemtemourian","year":"2017","unstructured":"Khemtemourian, L., Guillemain, G., Foufelle, F. & Killian, J. A. Residue specific effects of human islet polypeptide amyloid on self-assembly and on cell toxicity. Biochimie 142, 22\u201330 (2017).","journal-title":"Biochimie"},{"key":"496_CR66","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nmeth.4193","volume":"14","author":"SQ Zheng","year":"2017","unstructured":"Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331\u2013332 (2017).","journal-title":"Nat. Methods"},{"key":"496_CR67","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jsb.2015.11.003","volume":"193","author":"K Zhang","year":"2016","unstructured":"Zhang, K. Gctf: real-time CTF determination and correction. J. Struct. Biol. 193, 1\u201312 (2016).","journal-title":"J. Struct. Biol."},{"key":"496_CR68","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.jsb.2017.02.003","volume":"198","author":"S He","year":"2017","unstructured":"He, S. & Scheres, S. H. W. Helical reconstruction in RELION. J. Struct. Biol. 198, 163\u2013176 (2017).","journal-title":"J. Struct. Biol."},{"key":"496_CR69","doi-asserted-by":"crossref","first-page":"e42166","DOI":"10.7554\/eLife.42166","volume":"7","author":"J Zivanov","year":"2018","unstructured":"Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. Elife 7, e42166 (2018).","journal-title":"Elife"},{"key":"496_CR70","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1107\/S2059798319016577","volume":"76","author":"SHW Scheres","year":"2020","unstructured":"Scheres, S. H. W. Amyloid structure determination in RELION-3.1. Acta Crystallogr. D Struct. Biol. 76, 94\u2013101 (2020).","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"496_CR71","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Struct. Biol. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"496_CR72","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","volume":"25","author":"EF Pettersen","year":"2004","unstructured":"Pettersen, E. F. et al. UCSF Chimera\u2014a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605\u20131612 (2004).","journal-title":"J. Comput. Chem."},{"key":"496_CR73","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","volume":"75","author":"D Liebschner","year":"2019","unstructured":"Liebschner, D. et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallogr. D Struct. Biol. 75, 861\u2013877 (2019).","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"496_CR74","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","volume":"66","author":"VB Chen","year":"2010","unstructured":"Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Struct. Biol. 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr. D Struct. Biol."}],"updated-by":[{"DOI":"10.1038\/s41594-020-00525-x","type":"correction","label":"Correction","source":"publisher","updated":{"date-parts":[[2020,10,9]],"date-time":"2020-10-09T00:00:00Z","timestamp":1602201600000}}],"container-title":["Nature Structural &amp; Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41594-020-0496-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41594-020-0496-3","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41594-020-0496-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,13]],"date-time":"2021-09-13T19:32:02Z","timestamp":1631561522000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41594-020-0496-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,9,14]]},"references-count":74,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2020,11]]}},"alternative-id":["496"],"URL":"https:\/\/doi.org\/10.1038\/s41594-020-0496-3","relation":{},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,9,14]]},"assertion":[{"value":"2 June 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 August 2020","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"14 September 2020","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 October 2020","order":4,"name":"change_date","label":"Change Date","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Correction","order":5,"name":"change_type","label":"Change Type","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"An amendment to this paper has been published and can be accessed via a link at the top of the paper.","order":6,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}