{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T06:13:24Z","timestamp":1793945604499,"version":"4.8.0"},"reference-count":67,"publisher":"Springer Science and Business Media LLC","issue":"9","license":[{"start":{"date-parts":[[2021,9,1]],"date-time":"2021-09-01T00:00:00Z","timestamp":1630454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2021,9,1]],"date-time":"2021-09-01T00:00:00Z","timestamp":1630454400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/100000049","name":"U.S. Department of Health & Human Services | NIH | National Institute on Aging","doi-asserted-by":"publisher","award":["061847"],"award-info":[{"award-number":["061847"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"U.S. Department of Health & Human Services | NIH | National Institute on Aging","doi-asserted-by":"publisher","award":["054022"],"award-info":[{"award-number":["054022"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"name":"National Science Foundation Graduate Research Fellowship Program"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2021,9]]},"DOI":"10.1038\/s41594-021-00646-x","type":"journal-article","created":{"date-parts":[[2021,9,13]],"date-time":"2021-09-13T12:03:30Z","timestamp":1631534610000},"page":"724-730","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":100,"title":["Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores"],"prefix":"10.1038","volume":"28","author":[{"given":"Qin","family":"Cao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4487-0230","authenticated-orcid":false,"given":"David R.","family":"Boyer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0874-9043","authenticated-orcid":false,"given":"Michael R.","family":"Sawaya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Romany","family":"Abskharon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1904-2150","authenticated-orcid":false,"given":"Lorena","family":"Saelices","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7055-8809","authenticated-orcid":false,"given":"Binh A.","family":"Nguyen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiahui","family":"Lu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin A.","family":"Murray","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fouad","family":"Kandeel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2432-5419","authenticated-orcid":false,"given":"David S.","family":"Eisenberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,9,9]]},"reference":[{"key":"646_CR1","doi-asserted-by":"publisher","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","volume":"148","author":"D Eisenberg","year":"2012","unstructured":"Eisenberg, D. & Jucker, M. The amyloid state of proteins in human diseases. Cell 148, 1188\u20131203 (2012).","journal-title":"Cell"},{"key":"646_CR2","doi-asserted-by":"publisher","first-page":"9662","DOI":"10.1073\/pnas.86.24.9662","volume":"86","author":"AN Roberts","year":"1989","unstructured":"Roberts, A. N. et al. Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus. Proc. Natl Acad. Sci. USA 86, 9662\u20139666 (1989).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"646_CR3","doi-asserted-by":"publisher","first-page":"81","DOI":"10.3109\/03009734.2011.573884","volume":"116","author":"P Westermark","year":"2011","unstructured":"Westermark, P. Amyloid in the islets of Langerhans: thoughts and some historical aspects. Ups. J. Med. Sci. 116, 81\u201389 (2011).","journal-title":"Ups. J. Med. Sci."},{"key":"646_CR4","doi-asserted-by":"publisher","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","volume":"84","author":"P Westermark","year":"1987","unstructured":"Westermark, P. et al. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc. Natl Acad. Sci. USA 84, 3881\u20133885 (1987).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"646_CR5","doi-asserted-by":"publisher","first-page":"7763","DOI":"10.1073\/pnas.85.20.7763","volume":"85","author":"GJ Cooper","year":"1988","unstructured":"Cooper, G. J. et al. Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle. Proc. Natl Acad. Sci. USA 85, 7763\u20137766 (1988).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"646_CR6","doi-asserted-by":"publisher","first-page":"411","DOI":"10.1056\/NEJM200008103430607","volume":"343","author":"JW H\u00f6ppener","year":"2000","unstructured":"H\u00f6ppener, J. W., Ahr\u00e9n, B. & Lips, C. J. Islet amyloid and type 2 diabetes mellitus. N. Engl. J. Med. 343, 411\u2013419 (2000).","journal-title":"N. Engl. J. Med."},{"key":"646_CR7","doi-asserted-by":"publisher","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":"646_CR8","doi-asserted-by":"publisher","first-page":"998","DOI":"10.1007\/BF03402051","volume":"6","author":"GT Westermark","year":"2000","unstructured":"Westermark, G. T., Gebre-Medhin, S., Steiner, D. F. & Westermark, P. Islet amyloid development in a mouse strain lacking endogenous islet amyloid polypeptide (IAPP) but expressing human IAPP. Mol. Med. 6, 998\u20131007 (2000).","journal-title":"Mol. Med."},{"key":"646_CR9","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1007\/s00125-004-1332-8","volume":"47","author":"J Fern\u00e1ndez-Alvarez","year":"2004","unstructured":"Fern\u00e1ndez-Alvarez, J. et al. Stable and functional regeneration of pancreatic \u03b2-cell population in nSTZ-rats treated with tungstate. Diabetologia 47, 470\u2013477 (2004).","journal-title":"Diabetologia"},{"key":"646_CR10","doi-asserted-by":"publisher","DOI":"10.1038\/srep21274","volume":"6","author":"EH Pilkington","year":"2016","unstructured":"Pilkington, E. H. et al. Pancreatic \u03b2-cell membrane fluidity and toxicity induced by human islet amyloid polypeptide species. Sci. Rep. 6, 21274 (2016).","journal-title":"Sci. Rep."},{"key":"646_CR11","doi-asserted-by":"publisher","first-page":"2591","DOI":"10.1084\/jem.20161134","volume":"214","author":"A Mukherjee","year":"2017","unstructured":"Mukherjee, A. et al. Induction of IAPP amyloid deposition and associated diabetic abnormalities by a prion-like mechanism. J. Exp. Med. 214, 2591\u20132610 (2017).","journal-title":"J. Exp. Med."},{"key":"646_CR12","doi-asserted-by":"publisher","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":"646_CR13","doi-asserted-by":"publisher","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":"646_CR14","doi-asserted-by":"publisher","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":"646_CR15","doi-asserted-by":"publisher","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":"646_CR16","doi-asserted-by":"publisher","first-page":"1048","DOI":"10.1038\/s41594-020-0496-3","volume":"27","author":"R Gallardo","year":"2020","unstructured":"Gallardo, R. et al. Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly. Nat. Struct. Mol. Biol. 27, 1048\u20131056 (2020).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"646_CR17","doi-asserted-by":"publisher","first-page":"e43584","DOI":"10.7554\/eLife.43584","volume":"8","author":"W Zhang","year":"2019","unstructured":"Zhang, W. et al. Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer\u2019s and Pick\u2019s diseases. eLife 8, e43584 (2019).","journal-title":"eLife"},{"key":"646_CR18","doi-asserted-by":"publisher","first-page":"464","DOI":"10.1038\/s41586-020-2317-6","volume":"585","author":"M Schweighauser","year":"2020","unstructured":"Schweighauser, M. et al. Structures of \u03b1-synuclein filaments from multiple system atrophy. Nature 585, 464\u2013469 (2020).","journal-title":"Nature"},{"key":"646_CR19","doi-asserted-by":"publisher","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":"646_CR20","doi-asserted-by":"publisher","first-page":"1799","DOI":"10.1039\/C2CC33432A","volume":"49","author":"M-S Chen","year":"2013","unstructured":"Chen, M.-S. et al. Characterizing the assembly behaviors of human amylin: a perspective derived from C-terminal variants. Chem. Commun. 49, 1799\u20131801 (2013).","journal-title":"Chem. Commun."},{"key":"646_CR21","doi-asserted-by":"publisher","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":"646_CR22","doi-asserted-by":"publisher","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":"646_CR23","doi-asserted-by":"publisher","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":"646_CR24","doi-asserted-by":"publisher","first-page":"282","DOI":"10.1016\/j.jmb.2011.12.032","volume":"421","author":"P Cao","year":"2012","unstructured":"Cao, P. et al. Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. J. Mol. Biol. 421, 282\u2013295 (2012).","journal-title":"J. Mol. Biol."},{"key":"646_CR25","doi-asserted-by":"publisher","first-page":"474","DOI":"10.2337\/diabetes.53.2.474","volume":"53","author":"J Janson","year":"2004","unstructured":"Janson, J. et al. Increased risk of type 2 diabetes in Alzheimer disease. Diabetes 53, 474\u2013481 (2004).","journal-title":"Diabetes"},{"key":"646_CR26","doi-asserted-by":"publisher","first-page":"1503","DOI":"10.1016\/j.neurobiolaging.2008.08.019","volume":"31","author":"J Miklossy","year":"2010","unstructured":"Miklossy, J. et al. Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes. Neurobiol. Aging 31, 1503\u20131515 (2010).","journal-title":"Neurobiol. Aging"},{"key":"646_CR27","doi-asserted-by":"publisher","first-page":"1256","DOI":"10.2337\/diabetes.51.4.1256","volume":"51","author":"R Peila","year":"2002","unstructured":"Peila, R., Rodriguez, B. L., Launer, L. J. & Honolulu-Asia Aging Study. Type 2 diabetes, APOE gene, and the risk for dementia and related pathologies: The Honolulu-Asia Aging Study. Diabetes 51, 1256\u20131262 (2002).","journal-title":"Diabetes"},{"key":"646_CR28","doi-asserted-by":"publisher","first-page":"834","DOI":"10.1016\/j.ajpath.2014.11.016","volume":"185","author":"ME Oskarsson","year":"2015","unstructured":"Oskarsson, M. E. et al. In vivo seeding and cross-seeding of localized amyloidosis: a molecular link between type 2 diabetes and Alzheimer disease. Am. J. Pathol. 185, 834\u2013846 (2015).","journal-title":"Am. J. Pathol."},{"key":"646_CR29","doi-asserted-by":"publisher","first-page":"1327","DOI":"10.1038\/mp.2016.230","volume":"22","author":"I Moreno-Gonzalez","year":"2017","unstructured":"Moreno-Gonzalez, I. et al. Molecular interaction between type 2 diabetes and Alzheimer\u2019s disease through cross-seeding of protein misfolding. Mol. Psychiatry 22, 1327\u20131334 (2017).","journal-title":"Mol. Psychiatry"},{"key":"646_CR30","doi-asserted-by":"publisher","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":"646_CR31","doi-asserted-by":"publisher","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":"646_CR32","doi-asserted-by":"publisher","first-page":"13095","DOI":"10.1002\/anie.201504973","volume":"54","author":"E Andreetto","year":"2015","unstructured":"Andreetto, E. et al. A hot-segment-based approach for the design of cross-amyloid interaction surface mimics as inhibitors of amyloid self-assembly. Angew. Chem. Int. Ed. 54, 13095\u201313100 (2015).","journal-title":"Angew. Chem. Int. Ed."},{"key":"646_CR33","doi-asserted-by":"publisher","first-page":"999","DOI":"10.1002\/2211-5463.13110","volume":"11","author":"S L\u00f6vestam","year":"2021","unstructured":"L\u00f6vestam, S. et al. Seeded assembly in vitro does not replicate the structures of \u03b1-synuclein filaments from multiple system atrophy. FEBS Open Bio 11, 999\u20131013 (2021).","journal-title":"FEBS Open Bio"},{"key":"646_CR34","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1038\/ncb748","volume":"4","author":"H Fujiwara","year":"2002","unstructured":"Fujiwara, H. et al. \u03b1-Synuclein is phosphorylated in synucleinopathy lesions. Nat. Cell Biol. 4, 160\u2013164 (2002).","journal-title":"Nat. Cell Biol."},{"key":"646_CR35","doi-asserted-by":"publisher","first-page":"10224","DOI":"10.1074\/jbc.REV120.011743","volume":"295","author":"ZA Sorrentino","year":"2020","unstructured":"Sorrentino, Z. A. & Giasson, B. I. The emerging role of \u03b1-synuclein truncation in aggregation and disease. J. Biol. Chem. 295, 10224\u201310244 (2020).","journal-title":"J. Biol. Chem."},{"key":"646_CR36","doi-asserted-by":"publisher","first-page":"1765","DOI":"10.1016\/j.bbamem.2018.02.020","volume":"1860","author":"S Asthana","year":"2018","unstructured":"Asthana, S., Mallick, B., Alexandrescu, A. T. & Jha, S. IAPP in type II diabetes: basic research on structure, molecular interactions and disease mechanisms suggests potential intervention strategies. Biochim. Biophys. Acta Biomembr. 1860, 1765\u20131782 (2018).","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"646_CR37","doi-asserted-by":"publisher","first-page":"2632","DOI":"10.1016\/j.ajpath.2011.02.036","volume":"178","author":"CA Jurgens","year":"2011","unstructured":"Jurgens, C. A. et al. \u03b2-cell loss and \u03b2-cell apoptosis in human type 2 diabetes are related to islet amyloid deposition. Am. J. Pathol. 178, 2632\u20132640 (2011).","journal-title":"Am. J. Pathol."},{"key":"646_CR38","doi-asserted-by":"publisher","first-page":"e19273","DOI":"10.7554\/eLife.19273","volume":"6","author":"P Krotee","year":"2017","unstructured":"Krotee, P. et al. Atomic structures of fibrillar segments of hIAPP suggest tightly mated \u03b2-sheets are important for cytotoxicity. eLife 6, e19273 (2017).","journal-title":"eLife"},{"key":"646_CR39","doi-asserted-by":"publisher","first-page":"699","DOI":"10.1007\/s00401-018-1914-z","volume":"136","author":"B Falcon","year":"2018","unstructured":"Falcon, B. et al. Tau filaments from multiple cases of sporadic and inherited Alzheimer\u2019s disease adopt a common fold. Acta Neuropathol. 136, 699\u2013708 (2018).","journal-title":"Acta Neuropathol."},{"key":"646_CR40","doi-asserted-by":"publisher","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":"646_CR41","doi-asserted-by":"publisher","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":"646_CR42","doi-asserted-by":"publisher","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":"646_CR43","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1177\/030098588502200505","volume":"22","author":"KH Johnson","year":"1985","unstructured":"Johnson, K. H. et al. Feline insular amyloid: immunohistochemical and immunochemical evidence that the amyloid is insulin-related. Vet. Pathol. 22, 463\u2013468 (1985).","journal-title":"Vet. Pathol."},{"key":"646_CR44","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1016\/j.jsb.2005.07.007","volume":"152","author":"DN Mastronarde","year":"2005","unstructured":"Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36\u201351 (2005).","journal-title":"J. Struct. Biol."},{"key":"646_CR45","doi-asserted-by":"publisher","first-page":"204","DOI":"10.1016\/j.jsb.2015.08.006","volume":"192","author":"T Grant","year":"2015","unstructured":"Grant, T. & Grigorieff, N. Automatic estimation and correction of anisotropic magnification distortion in electron microscopes. J. Struct. Biol. 192, 204\u2013208 (2015).","journal-title":"J. Struct. Biol."},{"key":"646_CR46","doi-asserted-by":"publisher","first-page":"216","DOI":"10.1016\/j.jsb.2015.08.008","volume":"192","author":"A Rohou","year":"2015","unstructured":"Rohou, A. & Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216\u2013221 (2015).","journal-title":"J. Struct. Biol."},{"key":"646_CR47","doi-asserted-by":"publisher","first-page":"e06980","DOI":"10.7554\/eLife.06980","volume":"4","author":"T Grant","year":"2015","unstructured":"Grant, T. & Grigorieff, N. Measuring the optimal exposure for single particle cryo-EM using a 2.6-\u00c5 reconstruction of rotavirus VP6. eLife 4, e06980 (2015).","journal-title":"eLife"},{"key":"646_CR48","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1016\/j.jsb.2006.05.009","volume":"157","author":"G Tang","year":"2007","unstructured":"Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38\u201346 (2007).","journal-title":"J. Struct. Biol."},{"key":"646_CR49","doi-asserted-by":"publisher","first-page":"613","DOI":"10.1107\/S2059798320007342","volume":"76","author":"T Wagner","year":"2020","unstructured":"Wagner, T. et al. Two particle-picking procedures for filamentous proteins: SPHIRE-crYOLO filament mode and SPHIRE-STRIPER. Acta Crystallogr. D Struct. Biol. 76, 613\u2013620 (2020).","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"646_CR50","doi-asserted-by":"publisher","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":"646_CR51","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","volume":"180","author":"SHW Scheres","year":"2012","unstructured":"Scheres, S. H. W. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519\u2013530 (2012).","journal-title":"J. Struct. Biol."},{"key":"646_CR52","doi-asserted-by":"publisher","first-page":"545","DOI":"10.1107\/S2059798318004655","volume":"74","author":"TC Terwilliger","year":"2018","unstructured":"Terwilliger, T. C., Sobolev, O. V., Afonine, P. V. & Adams, P. D. Automated map sharpening by maximization of detail and connectivity. Acta Crystallogr. D Struct. Biol. 74, 545\u2013559 (2018).","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"646_CR53","doi-asserted-by":"publisher","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. Biol. Crystallogr. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"646_CR54","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1107\/S2059798318006551","volume":"74","author":"PV Afonine","year":"2018","unstructured":"Afonine, P. V. et al. Real-space refinement in PHENIX for cryo-EM and crystallography. Acta Crystallogr. D Struct. Biol. 74, 531\u2013544 (2018).","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"646_CR55","doi-asserted-by":"publisher","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 Biol. Crystallogr. 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"646_CR56","unstructured":"The PyMOL Molecular Graphics System, Version 1.8 (Schr\u00f6dinger, 2015)."},{"key":"646_CR57","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-019-11183-z","volume":"10","author":"RA Warmack","year":"2019","unstructured":"Warmack, R. A. et al. Structure of amyloid-\u03b2 (20-34) with Alzheimer\u2019s-associated isomerization at Asp23 reveals a distinct protofilament interface. Nat. Commun. 10, 3357 (2019).","journal-title":"Nat. Commun."},{"key":"646_CR58","doi-asserted-by":"publisher","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","volume":"154","author":"J-X 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":"646_CR59","doi-asserted-by":"publisher","first-page":"331","DOI":"10.1002\/anie.201408598","volume":"54","author":"AK Schutz","year":"2015","unstructured":"Schutz, A. K. et al. Atomic-resolution three-dimensional structure of amyloid \u03b2 fibrils bearing the Osaka mutation. Angew. Chem. Int. Ed. 54, 331\u2013335 (2015).","journal-title":"Angew. Chem. Int. Ed."},{"key":"646_CR60","doi-asserted-by":"publisher","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":"646_CR61","doi-asserted-by":"publisher","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":"646_CR62","doi-asserted-by":"publisher","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":"646_CR63","doi-asserted-by":"publisher","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":"646_CR64","doi-asserted-by":"publisher","first-page":"17342","DOI":"10.1073\/pnas.0506723102","volume":"102","author":"T Luhrs","year":"2005","unstructured":"Luhrs, T. et al. 3D structure of Alzheimer\u2019s amyloid-\u03b2(1\u201342) fibrils. Proc. Natl Acad. Sci. USA 102, 17342\u201317347 (2005).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"646_CR65","doi-asserted-by":"publisher","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":"646_CR66","doi-asserted-by":"publisher","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 \u2018iowa\u2019 a\u03b2 fibril structure using solid-state NMR data from labeled samples with rosetta. Structure 23, 216\u2013227 (2015).","journal-title":"Structure"},{"key":"646_CR67","doi-asserted-by":"publisher","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."}],"container-title":["Nature Structural & Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41594-021-00646-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41594-021-00646-x","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41594-021-00646-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,13]],"date-time":"2021-09-13T12:11:17Z","timestamp":1631535077000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41594-021-00646-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,9]]},"references-count":67,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2021,9]]}},"alternative-id":["646"],"URL":"https:\/\/doi.org\/10.1038\/s41594-021-00646-x","relation":{},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,9]]},"assertion":[{"value":"9 April 2021","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 July 2021","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 September 2021","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"D.S.E. is an advisor and equity shareholder in ADRx, Inc. The remaining authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}