{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T00:29:25Z","timestamp":1761611365447,"version":"build-2065373602"},"reference-count":41,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2015,4,1]],"date-time":"2015-04-01T00:00:00Z","timestamp":1427846400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,4,1]],"date-time":"2015-04-01T00:00:00Z","timestamp":1427846400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100003621","name":"Ministry of Science, ICT and Future Planning","doi-asserted-by":"publisher","award":["2007-0056094","2012R1A1A2038373"],"award-info":[{"award-number":["2007-0056094","2012R1A1A2038373"]}],"id":[{"id":"10.13039\/501100003621","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002642","name":"Korea University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002642","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002701","name":"Ministry of Education","doi-asserted-by":"publisher","award":["2014H1A2A1021042"],"award-info":[{"award-number":["2014H1A2A1021042"]}],"id":[{"id":"10.13039\/501100002701","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Chemistry"],"published-print":{"date-parts":[[2015,4]]},"DOI":"10.1016\/j.bpc.2015.02.002","type":"journal-article","created":{"date-parts":[[2015,2,7]],"date-time":"2015-02-07T13:03:49Z","timestamp":1423314229000},"page":"1-8","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":17,"special_numbering":"C","title":["Relationship between structural composition and material properties of polymorphic hIAPP fibrils"],"prefix":"10.1016","volume":"199","author":[{"given":"Myeongsang","family":"Lee","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hyun Joon","family":"Chang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Donghoi","family":"Kim","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yongwoo","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Heesu","family":"Suh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Namjo","family":"Ahn","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gwonchan","family":"Yoon","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sungsoo","family":"Na","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpc.2015.02.002_bb0005","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1146\/annurev.med.57.121304.131243","article-title":"Amyloidosis","volume":"57","author":"Pepys","year":"2006","journal-title":"Annu. Rev. Med."},{"key":"10.1016\/j.bpc.2015.02.002_bb0010","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","article-title":"The amyloid state of proteins in human diseases","volume":"148","author":"Eisenberg","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.bpc.2015.02.002_bb0015","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1056\/NEJMra023144","article-title":"Molecular mechanisms of amyloidosis","volume":"349","author":"Merlini","year":"2003","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bpc.2015.02.002_bb0020","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nrn1007","article-title":"Unfolding the role of protein misfolding in neurodegenerative diseases","volume":"4","author":"Soto","year":"2003","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.bpc.2015.02.002_bb0025","doi-asserted-by":"crossref","first-page":"3252","DOI":"10.1073\/pnas.1011342108","article-title":"Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy","volume":"108","author":"Mizuno","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2015.02.002_bb0030","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-[bgr] spines reveal varied steric zippers","volume":"447","author":"Sawaya","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2015.02.002_bb0035","doi-asserted-by":"crossref","first-page":"4820","DOI":"10.1021\/cr900377t","article-title":"Polymorphism in Alzheimer A\u03b2 amyloid organization reflects conformational selection in a rugged energy landscape","volume":"110","author":"Miller","year":"2010","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bpc.2015.02.002_bb0040","doi-asserted-by":"crossref","first-page":"2152","DOI":"10.1002\/ange.200804198","article-title":"Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy","volume":"121","author":"Nielsen","year":"2009","journal-title":"Angew. Chem."},{"key":"10.1016\/j.bpc.2015.02.002_bb0045","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/nnano.2010.59","article-title":"Understanding amyloid aggregation by statistical analysis of atomic force microscopy images","volume":"5","author":"Adamcik","year":"2010","journal-title":"Nat. Nanotechnol."},{"key":"10.1016\/j.bpc.2015.02.002_bb0050","doi-asserted-by":"crossref","first-page":"11533","DOI":"10.1073\/pnas.0602345103","article-title":"Molecular dynamics analyses of cross-\u03b2-spine steric zipper models: \u03b2-Sheet twisting and aggregation","volume":"103","author":"Esposito","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2015.02.002_bb0055","doi-asserted-by":"crossref","first-page":"5154","DOI":"10.1021\/bi200147a","article-title":"Single-molecule atomic force microscopy force spectroscopy study of A\u03b2-40 interactions","volume":"50","author":"Kim","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2015.02.002_bb0060","doi-asserted-by":"crossref","first-page":"e59005","DOI":"10.1371\/journal.pone.0059005","article-title":"Cu2+ affects amyloid-\u03b2 (1\u201342) aggregation by increasing peptide-peptide binding forces","volume":"8","author":"Hane","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bpc.2015.02.002_bb0065","doi-asserted-by":"crossref","first-page":"14128","DOI":"10.1073\/pnas.1004704107","article-title":"Hollow core of Alzheimer's A\u03b242 amyloid observed by cryoEM is relevant at physiological pH","volume":"107","author":"Miller","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2015.02.002_bb0070","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1038\/nnano.2011.102","article-title":"Nanomechanics of functional and pathological amyloid materials","volume":"6","author":"Knowles","year":"2011","journal-title":"Nat. Nanotechnol."},{"key":"10.1016\/j.bpc.2015.02.002_bb0075","doi-asserted-by":"crossref","first-page":"4062","DOI":"10.1002\/anie.200703133","article-title":"Amyloids: not only pathological agents but also ordered nanomaterials","volume":"47","author":"Cherny","year":"2008","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.bpc.2015.02.002_bb0080","doi-asserted-by":"crossref","first-page":"5326","DOI":"10.1039\/C4CS00082J","article-title":"Amyloid-based nanosensors and nanodevices","volume":"43","author":"Hauser","year":"2014","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bpc.2015.02.002_bb0085","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1038\/nmeth.1218","article-title":"Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy","volume":"5","author":"Neuman","year":"2008","journal-title":"Nat. Methods"},{"key":"10.1016\/j.bpc.2015.02.002_bb0090","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1126\/science.1150057","article-title":"Role of intermolecular forces in defining material properties of protein nanofibrils","volume":"318","author":"Knowles","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.bpc.2015.02.002_bb0095","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1038\/nmat2387","article-title":"Deformation and failure of protein materials in physiologically extreme conditions and disease","volume":"8","author":"Buehler","year":"2009","journal-title":"Nat. Mater."},{"key":"10.1016\/j.bpc.2015.02.002_bb0100","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1073\/pnas.1321797111","article-title":"Designed amyloid fibers as materials for selective carbon dioxide capture","volume":"111","author":"Li","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2015.02.002_bb0105","doi-asserted-by":"crossref","first-page":"4527","DOI":"10.1073\/pnas.0431081100","article-title":"Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition","volume":"100","author":"Scheibel","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2015.02.002_bb0110","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1038\/nnano.2012.62","article-title":"Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties","volume":"7","author":"Li","year":"2012","journal-title":"Nat. Nanotechnol."},{"key":"10.1016\/j.bpc.2015.02.002_bb0115","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1038\/nnano.2012.248","article-title":"Peptide nanofibrils boost retroviral gene transfer and provide a rapid means for concentrating viruses","volume":"8","author":"Yolamanova","year":"2013","journal-title":"Nat. Nanotechnol."},{"key":"10.1016\/j.bpc.2015.02.002_bb0120","doi-asserted-by":"crossref","first-page":"5591","DOI":"10.1073\/pnas.042681399","article-title":"Amyloid fibers are water-filled nanotubes","volume":"99","author":"Perutz","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2015.02.002_bb0125","doi-asserted-by":"crossref","first-page":"105703","DOI":"10.1088\/0957-4484\/25\/10\/105703","article-title":"Tensile deformation and failure of amyloid and amyloid-like protein fibrils","volume":"25","author":"Max","year":"2014","journal-title":"Nanotechnology"},{"key":"10.1016\/j.bpc.2015.02.002_bb0130","first-page":"102","article-title":"Relationship between disease-specific structures of amyloid fibrils and their mechanical properties","author":"Yoon","year":"2013","journal-title":"Appl. Phys. Lett."},{"key":"10.1016\/j.bpc.2015.02.002_bb0135","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.bpj.2011.12.047","article-title":"Effect of sequence variation on the mechanical response of amyloid fibrils probed by steered molecular dynamics simulation","volume":"102","author":"Ndlovu","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpc.2015.02.002_bb0140","doi-asserted-by":"crossref","first-page":"e88502","DOI":"10.1371\/journal.pone.0088502","article-title":"Role of sequence and structural polymorphism on the mechanical properties of amyloid fibrils","volume":"9","author":"Yoon","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.bpc.2015.02.002_bb0145","doi-asserted-by":"crossref","first-page":"3454","DOI":"10.1002\/adfm.201002493","article-title":"Mechanical characterization of amyloid fibrils using coarse-grained normal mode analysis","volume":"21","author":"Yoon","year":"2011","journal-title":"Adv. Funct. Mater."},{"key":"10.1016\/j.bpc.2015.02.002_bb0150","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.cplett.2014.03.043","article-title":"The bond survival time variation of polymorphic amyloid fibrils in the mechanical insight","volume":"600","author":"Lee","year":"2014","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.bpc.2015.02.002_bb0155","doi-asserted-by":"crossref","first-page":"18493","DOI":"10.1039\/C4CP02494J","article-title":"The mechanical response of hIAPP nanowires based on different bending direction simulations","volume":"16","author":"Kim","year":"2014","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.bpc.2015.02.002_bb0160","doi-asserted-by":"crossref","first-page":"429","DOI":"10.3762\/bjnano.4.50","article-title":"Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects","volume":"4","author":"Ndlovu","year":"2013","journal-title":"Beilstein J. Nanotechnol."},{"key":"10.1016\/j.bpc.2015.02.002_bb0165","doi-asserted-by":"crossref","first-page":"14990","DOI":"10.1021\/ja802483d","article-title":"Structural insights into the polymorphism of amyloid-like fibrils formed by region 20\u201329 of amylin revealed by solid-state NMR and X-ray fiber diffraction","volume":"130","author":"Madine","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bpc.2015.02.002_bb0170","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips","year":"2005","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bpc.2015.02.002_bb0175","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"10.1016\/j.bpc.2015.02.002_bb0180","doi-asserted-by":"crossref","first-page":"15806","DOI":"10.1073\/pnas.0604035103","article-title":"Characterization of the nanoscale properties of individual amyloid fibrils","volume":"103","author":"Smith","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2015.02.002_bb0185","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1016\/j.bpj.2009.12.4317","article-title":"Alzheimer's A\u03b2(1\u201340) amyloid fibrils feature size-dependent mechanical properties","volume":"98","author":"Xu","year":"2010","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpc.2015.02.002_bb0190","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1016\/j.jbiomech.2009.11.026","article-title":"Atomistic simulation of nanomechanical properties of Alzheimer's A\u03b2(1\u201340) amyloid fibrils under compressive and tensile loading","volume":"43","author":"Paparcone","year":"2010","journal-title":"J. Biomech."},{"key":"10.1016\/j.bpc.2015.02.002_bb0195","doi-asserted-by":"crossref","first-page":"3295","DOI":"10.1242\/jeb.202.23.3295","article-title":"The mechanical design of spider silks: from fibroin sequence to mechanical function","volume":"202","author":"Gosline","year":"1999","journal-title":"J. Exp. Biol."},{"key":"10.1016\/j.bpc.2015.02.002_bb0200","doi-asserted-by":"crossref","first-page":"2626","DOI":"10.1021\/nl101341w","article-title":"Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils","volume":"10","author":"Nova","year":"2010","journal-title":"Nano Lett."},{"key":"10.1016\/j.bpc.2015.02.002_bb0205","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1002\/pat.1994.220050801","article-title":"Mechanical and thermal properties of dragline silk from the spider Nephila clavipes","volume":"5","author":"Cunniff","year":"1994","journal-title":"Polym. Adv. Technol."}],"container-title":["Biophysical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462215000101?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462215000101?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T07:52:42Z","timestamp":1759564362000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301462215000101"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,4]]},"references-count":41,"alternative-id":["S0301462215000101"],"URL":"https:\/\/doi.org\/10.1016\/j.bpc.2015.02.002","relation":{},"ISSN":["0301-4622"],"issn-type":[{"type":"print","value":"0301-4622"}],"subject":[],"published":{"date-parts":[[2015,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Relationship between structural composition and material properties of polymorphic hIAPP fibrils","name":"articletitle","label":"Article Title"},{"value":"Biophysical Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpc.2015.02.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}