{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T02:05:59Z","timestamp":1791079559506,"version":"4.1.0"},"reference-count":55,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2012,2,1]],"date-time":"2012-02-01T00:00:00Z","timestamp":1328054400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2012,2,1]],"date-time":"2012-02-01T00:00:00Z","timestamp":1328054400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2013,7,16]],"date-time":"2013-07-16T00:00:00Z","timestamp":1373932800000},"content-version":"vor","delay-in-days":531,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/3.0\/"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2012,2]]},"DOI":"10.1016\/j.bpj.2011.12.047","type":"journal-article","created":{"date-parts":[[2012,2,7]],"date-time":"2012-02-07T11:36:59Z","timestamp":1328614619000},"page":"587-596","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":44,"title":["Effect of Sequence Variation on the Mechanical Response of Amyloid Fibrils Probed by Steered Molecular Dynamics Simulation"],"prefix":"10.1016","volume":"102","author":[{"given":"Hlengisizwe","family":"Ndlovu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alison\u00a0E.","family":"Ashcroft","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sheena\u00a0E.","family":"Radford","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah\u00a0A.","family":"Harris","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpj.2011.12.047_bib1","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bpj.2011.12.047_bib2","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nrd3050","article-title":"Protein aggregation diseases: pathogenicity and therapeutic perspectives","volume":"9","author":"Aguzzi","year":"2010","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bpj.2011.12.047_bib3","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1042\/bst0300552","article-title":"Amyloid-\u03b2 oligomers: their production, toxicity and therapeutic inhibition","volume":"30","author":"Walsh","year":"2002","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.bpj.2011.12.047_bib4","doi-asserted-by":"crossref","first-page":"29639","DOI":"10.1074\/jbc.R800016200","article-title":"Structural classification of toxic amyloid oligomers","volume":"283","author":"Glabe","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.12.047_bib5","doi-asserted-by":"crossref","first-page":"e20244","DOI":"10.1371\/journal.pone.0020244","article-title":"Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity","volume":"6","author":"Lee","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bpj.2011.12.047_bib6","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1038\/sj.emboj.7601953","article-title":"Lipids revert inert A\u03b2 amyloid fibrils to neurotoxic protofibrils that affect learning in mice","volume":"27","author":"Martins","year":"2008","journal-title":"EMBO\u00a0J."},{"key":"10.1016\/j.bpj.2011.12.047_bib7","doi-asserted-by":"crossref","first-page":"6033","DOI":"10.1073\/pnas.0708354105","article-title":"Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane","volume":"105","author":"Engel","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2011.12.047_bib8","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/nature04922","article-title":"The physical basis of how prion conformations determine strain phenotypes","volume":"442","author":"Tanaka","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2011.12.047_bib9","doi-asserted-by":"crossref","first-page":"e321","DOI":"10.1371\/journal.pbio.0020321","article-title":"Mechanism of prion propagation: amyloid growth occurs by monomer addition","volume":"2","author":"Collins","year":"2004","journal-title":"PLoS Biol."},{"key":"10.1016\/j.bpj.2011.12.047_bib10","doi-asserted-by":"crossref","first-page":"34272","DOI":"10.1074\/jbc.M109.049809","article-title":"Fibril fragmentation enhances amyloid cytotoxicity","volume":"284","author":"Xue","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.12.047_bib11","doi-asserted-by":"crossref","first-page":"20","DOI":"10.4161\/pri.4.1.11378","article-title":"Fibril fragmentation in amyloid assembly and cytotoxicity: when size matters","volume":"4","author":"Xue","year":"2010","journal-title":"Prion"},{"key":"10.1016\/j.bpj.2011.12.047_bib12","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1679\/aohc.72.199","article-title":"Mechanically functional amyloid fibril in the adhesive of a marine invertebrate as revealed by Raman spectroscopy and AFM","volume":"72","author":"Mostaert","year":"2009","journal-title":"Arch. Histol. Cytol."},{"key":"10.1016\/j.bpj.2011.12.047_bib13","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1007\/s10867-006-9023-y","article-title":"Nanoscale mechanical characterization of amyloid fibrils discovered in a natural adhesive","volume":"32","author":"Mostaert","year":"2006","journal-title":"J.\u00a0Biol. Phys."},{"key":"10.1016\/j.bpj.2011.12.047_bib14","doi-asserted-by":"crossref","first-page":"1630","DOI":"10.1021\/bm0600724","article-title":"Packing density and structural heterogeneity of insulin amyloid fibrils measured by AFM nanoindentation","volume":"7","author":"Guo","year":"2006","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.bpj.2011.12.047_bib15","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1021\/bm7010104","article-title":"Amyloid-like fibrils in elastin-related polypeptides: structural characterization and elastic properties","volume":"9","author":"del Mercato","year":"2008","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.bpj.2011.12.047_bib16","doi-asserted-by":"crossref","first-page":"15806","DOI":"10.1073\/pnas.0604035103","article-title":"Characterization of the nanoscale properties of individual amyloid fibrils","volume":"43","author":"Smith","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2011.12.047_bib17","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.1021\/nl0505896","article-title":"Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures","volume":"5","author":"Kol","year":"2005","journal-title":"Nano Lett."},{"key":"10.1016\/j.bpj.2011.12.047_bib18","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1021\/nl052205h","article-title":"Structural and mechanical study of a self-assembling protein nanotube","volume":"6","author":"Graveland-Bikker","year":"2006","journal-title":"Nano Lett."},{"key":"10.1016\/j.bpj.2011.12.047_bib19","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.bpj.2011.12.047_bib20","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.bpj.2010.11.052","article-title":"Structural and mechanical properties of TTR105-115 amyloid fibrils from compression experiments","volume":"100","author":"Meersman","year":"2011","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2011.12.047_bib21","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/j.jmb.2007.08.034","article-title":"Mechanical unbinding of A\u03b2 peptides from amyloid fibrils","volume":"373","author":"Raman","year":"2007","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.bpj.2011.12.047_bib22","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(1-40) amyloid fibrils under compressive and tensile loading","volume":"43","author":"Paparcone","year":"2010","journal-title":"J.\u00a0Biomech."},{"key":"10.1016\/j.bpj.2011.12.047_bib23","doi-asserted-by":"crossref","first-page":"3367","DOI":"10.1016\/j.biomaterials.2010.11.066","article-title":"Failure of A\u03b2(1-40) amyloid fibrils under tensile loading","volume":"32","author":"Paparcone","year":"2011","journal-title":"Biomaterials"},{"key":"10.1016\/j.bpj.2011.12.047_bib24","doi-asserted-by":"crossref","first-page":"8967","DOI":"10.1021\/bi100953t","article-title":"Mutations alter the geometry and mechanical properties of Alzheimer's A\u03b2(1-40) amyloid fibrils","volume":"49","author":"Paparcone","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.12.047_bib25","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 20-29 of amylin revealed by solid-state NMR and x-ray fiber diffraction","volume":"130","author":"Madine","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2011.12.047_bib26","doi-asserted-by":"crossref","first-page":"5036","DOI":"10.1073\/pnas.87.13.5036","article-title":"Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2011.12.047_bib27","doi-asserted-by":"crossref","first-page":"11012","DOI":"10.1021\/ja00076a078","article-title":"Interspecies sequence variations affect the kinetics and thermodynamics of amyloid formation: peptide models of pancreatic amyloid","volume":"115","author":"Ashburn","year":"1993","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2011.12.047_bib28","doi-asserted-by":"crossref","first-page":"1811","DOI":"10.1021\/bi981658g","article-title":"Effects of sequential proline substitutions on amyloid formation by human amylin 20\u201329","volume":"38","author":"Moriarty","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.12.047_bib29","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1006\/jmbi.2001.5244","article-title":"Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity","volume":"315","author":"Kapurniotu","year":"2002","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.bpj.2011.12.047_bib30","doi-asserted-by":"crossref","first-page":"15901","DOI":"10.1021\/bi048812l","article-title":"Role of aromatic interactions in amyloid formation by peptides derived from human amylin","volume":"43","author":"Tracz","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.12.047_bib31","doi-asserted-by":"crossref","first-page":"3255","DOI":"10.1021\/bi0621967","article-title":"Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology","volume":"46","author":"Marek","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.12.047_bib32","doi-asserted-by":"crossref","first-page":"4552","DOI":"10.1016\/j.bpj.2009.03.039","article-title":"Sequence and crowding effects in the aggregation of a 10-residue fragment derived from islet amyloid polypeptide","volume":"96","author":"Rivera","year":"2009","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2011.12.047_bib33","doi-asserted-by":"crossref","first-page":"125101","DOI":"10.1063\/1.3097982","article-title":"Structural diversity of the soluble trimers of human amylin (20\u201329) peptide revealed by MD simulation","volume":"130","author":"Mo","year":"2009","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.bpj.2011.12.047_bib34","doi-asserted-by":"crossref","first-page":"3000","DOI":"10.1529\/biophysj.104.047076","article-title":"Formation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in MD simulation","volume":"87","author":"Wu","year":"2004","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2011.12.047_bib35","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1016\/S0006-3495(03)74996-0","article-title":"Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAIL","volume":"84","author":"Zanuy","year":"2003","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2011.12.047_bib36","series-title":"Molecular Modeling of Nucleic Acids","first-page":"379","article-title":"Modeling unusual nucleic acid structures","author":"Macke","year":"1998"},{"key":"10.1016\/j.bpj.2011.12.047_bib37","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1002\/jcc.20290","article-title":"The AMBER biomolecular simulation programs","volume":"26","author":"Case","year":"2005","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.bpj.2011.12.047_bib38","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.\u00a0Comput. Chem."},{"key":"10.1016\/j.bpj.2011.12.047_bib39","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1002\/prot.21123","article-title":"Comparison of multiple AMBER force fields and development of improved protein backbone parameters","volume":"65","author":"Hornak","year":"2006","journal-title":"Proteins"},{"key":"10.1016\/j.bpj.2011.12.047_bib40","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1021\/jp973084f","article-title":"All-atom empirical potential for molecular modeling and dynamics studies of proteins","volume":"102","author":"MacKerell","year":"1998","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.bpj.2011.12.047_bib41","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.bpj.2011.12.047_bib42","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.bpj.2011.12.047_bib43","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.\u00a0Mol. Graph."},{"key":"10.1016\/j.bpj.2011.12.047_bib44","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S1093-3263(00)00133-9","article-title":"Steered molecular dynamics investigations of protein function","volume":"19","author":"Isralewitz","year":"2001","journal-title":"J.\u00a0Mol. Graph. Model."},{"key":"10.1016\/j.bpj.2011.12.047_bib45","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/S0959-440X(00)00194-9","article-title":"Steered molecular dynamics and mechanical functions of proteins","volume":"11","author":"Isralewitz","year":"2001","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bpj.2011.12.047_bib46","doi-asserted-by":"crossref","first-page":"12724","DOI":"10.1073\/pnas.0602995103","article-title":"Anisotropic deformation response of single protein molecules","volume":"103","author":"Dietz","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2011.12.047_bib47","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1038\/nsb968","article-title":"Pulling geometry defines the mechanical resistance of a \u03b2-sheet protein","volume":"10","author":"Brockwell","year":"2003","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bpj.2011.12.047_bib48","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1038\/nsb965","article-title":"The mechanical stability of ubiquitin is linkage dependent","volume":"10","author":"Carrion-Vazquez","year":"2003","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bpj.2011.12.047_bib49","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.2337\/diab.45.9.1279","article-title":"Mis-sense mutation of amylin gene (S20G) in Japanese NIDDM patients","volume":"5","author":"Sakagashira","year":"1996","journal-title":"Diabetes"},{"key":"10.1016\/j.bpj.2011.12.047_bib50","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1016\/S0002-9440(10)64848-1","article-title":"S20G mutant amylin exhibits increased in\u00a0vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin","volume":"157","author":"Sakagashira","year":"2000","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bpj.2011.12.047_bib51","series-title":"Monograph on the Physics and Chemistry of Materials","first-page":"159","article-title":"Theory of defects in solids: electronic structure of defects in insulators and semiconductors","author":"Stoneham","year":"1975"},{"key":"10.1016\/j.bpj.2011.12.047_bib52","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. Engl."},{"key":"10.1016\/j.bpj.2011.12.047_bib53","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1071\/CH06485","article-title":"Amyloid fibrils: from disease to design. New biomaterial applications for self-assembling cross-\u03b2 fibrils","volume":"60","author":"Gras","year":"2007","journal-title":"Aust. J. Chem."},{"key":"10.1016\/j.bpj.2011.12.047_bib54","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. USA"},{"key":"10.1016\/j.bpj.2011.12.047_bib55","doi-asserted-by":"crossref","first-page":"3135","DOI":"10.1021\/bm700561t","article-title":"Stability of tubular structures based on \u03b2-helical proteins: self-assembled versus polymerized nanoconstructs and wild-type versus mutated sequences","volume":"8","author":"Zanuy","year":"2007","journal-title":"Biomacromolecules"}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349512000367?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349512000367?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T16:18:07Z","timestamp":1757780287000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349512000367"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,2]]},"references-count":55,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2012,2]]}},"alternative-id":["S0006349512000367"],"URL":"https:\/\/doi.org\/10.1016\/j.bpj.2011.12.047","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2012,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Effect of Sequence Variation on the Mechanical Response of Amyloid Fibrils Probed by Steered Molecular Dynamics Simulation","name":"articletitle","label":"Article Title"},{"value":"Biophysical Journal","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpj.2011.12.047","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2012 Biophysical Society. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}