{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T11:41:20Z","timestamp":1791114080891,"version":"4.1.0"},"reference-count":67,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2007,11,1]],"date-time":"2007-11-01T00:00:00Z","timestamp":1193875200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2007,11,1]],"date-time":"2007-11-01T00:00:00Z","timestamp":1193875200000},"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":2084,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007215","name":"Verband der Chemischen Industrie","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007215","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2007,11]]},"DOI":"10.1529\/biophysj.107.110635","type":"journal-article","created":{"date-parts":[[2007,7,27]],"date-time":"2007-07-27T20:54:25Z","timestamp":1185569665000},"page":"3132-3141","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":178,"title":["Mechanism of Islet Amyloid Polypeptide Fibrillation at Lipid Interfaces Studied by Infrared Reflection Absorption Spectroscopy"],"prefix":"10.1016","volume":"93","author":[{"given":"D.H.J.","family":"Lopes","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Meister","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Gohlke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Hauser","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Blume","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R.","family":"Winter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1529\/biophysj.107.110635_bib1","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.copbio.2005.05.005","article-title":"Protein fibers as performance proteins: new technologies and applications","volume":"16","author":"Scheibel","year":"2005","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1529\/biophysj.107.110635_bib2","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/S0959-440X(98)80016-X","article-title":"The alternative conformations of amyloidogenic proteins and their multi-step assembly pathway","volume":"8","author":"Kelly","year":"1998","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1529\/biophysj.107.110635_bib3","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1098\/rstb.2000.0758","article-title":"The structural basis of protein folding and its links with human disease","volume":"356","author":"Dobson","year":"2001","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"10.1529\/biophysj.107.110635_bib4","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1038\/35081564","article-title":"Alpha-synuclein and neurodegenerative diseases","volume":"2","author":"Goedert","year":"2001","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1529\/biophysj.107.110635_bib5","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1023\/A:1021832302524","article-title":"\u03b2-amyloid production, aggregation, and clearance as targets for therapy in Alzheimer's disease","volume":"22","author":"De Felice","year":"2002","journal-title":"Cell. Mol. Neurobiol."},{"key":"10.1529\/biophysj.107.110635_bib6","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1073\/pnas.0509386103","article-title":"A\u03b2 and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease","volume":"103","author":"Guo","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1529\/biophysj.107.110635_bib7","doi-asserted-by":"crossref","first-page":"1774","DOI":"10.1529\/biophysj.105.070136","article-title":"Structure of core domain of fibril-forming PHF\/tau fragments","volume":"90","author":"Inouye","year":"2006","journal-title":"Biophys. J."},{"key":"10.1529\/biophysj.107.110635_bib8","doi-asserted-by":"crossref","first-page":"4074","DOI":"10.1073\/pnas.0511295103","article-title":"The 3D profile method for identifying fibril-forming segments of proteins","volume":"103","author":"Thompson","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1529\/biophysj.107.110635_bib9","doi-asserted-by":"crossref","first-page":"4638","DOI":"10.1021\/bi052226q","article-title":"Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides","volume":"45","author":"Rojas Quijano","year":"2006","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.107.110635_bib10","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1073\/pnas.0406847102","article-title":"Molecular basis for amyloid fibril formation and stability","volume":"102","author":"Makin","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1529\/biophysj.107.110635_bib11","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.sbi.2003.12.002","article-title":"Progress towards a molecular-level structural understanding of amyloid fibrils","volume":"14","author":"Tycko","year":"2004","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1529\/biophysj.107.110635_bib12","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1529\/biophysj.106.085928","article-title":"Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin","volume":"91","author":"Cordeiro","year":"2006","journal-title":"Biophys. J."},{"key":"10.1529\/biophysj.107.110635_bib13","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.jmb.2005.11.075","article-title":"Solvation-assisted pressure tuning of insulin fibrillation: from novel aggregation pathways to biotechnological applications","volume":"356","author":"Grudzielanek","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib14","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/0167-4889(89)90220-6","article-title":"Amylin and the amylin gene: structure, function and relationship to islet amyloid and to diabetes mellitus","volume":"1014","author":"Cooper","year":"1989","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1529\/biophysj.107.110635_bib15","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/340272b0","article-title":"Amylin hormone","volume":"340","author":"Cooper","year":"1989","journal-title":"Nature"},{"key":"10.1529\/biophysj.107.110635_bib16","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/0006-291X(89)92529-1","article-title":"Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets","volume":"160","author":"Ohsawa","year":"1989","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1529\/biophysj.107.110635_bib17","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1016\/0006-291X(90)90636-2","article-title":"Islet amyloid polypeptide (IAPP;amylin) influences the endocrine but not the exocrine rat pancreas","volume":"167","author":"Fehmann","year":"1990","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1529\/biophysj.107.110635_bib18","first-page":"522","article-title":"Islet amyloid polypeptide: mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus","volume":"66","author":"Johnson","year":"1992","journal-title":"Lab. Invest."},{"key":"10.1529\/biophysj.107.110635_bib19","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/j.jmb.2005.12.020","article-title":"Islet amyloid polypeptide inserts into phospholipid monolayers as monomer","volume":"356","author":"Engel","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib20","doi-asserted-by":"crossref","first-page":"10427","DOI":"10.1073\/pnas.0502066102","article-title":"Amyloid ion channels: a common structural link for protein-misfolding disease","volume":"102","author":"Quist","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1529\/biophysj.107.110635_bib21","doi-asserted-by":"crossref","first-page":"12206","DOI":"10.1074\/jbc.M312452200","article-title":"Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation","volume":"279","author":"Green","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1529\/biophysj.107.110635_bib22","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1006\/jmbi.1999.2646","article-title":"Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro","volume":"287","author":"Kayed","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib23","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.febslet.2004.09.075","article-title":"Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers","volume":"577","author":"Sparr","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1529\/biophysj.107.110635_bib24","doi-asserted-by":"crossref","first-page":"10971","DOI":"10.1021\/bi034889i","article-title":"The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies","volume":"42","author":"Porat","year":"2003","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.107.110635_bib25","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/S0014-5793(01)02972-6","article-title":"Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation","volume":"507","author":"Harroun","year":"2001","journal-title":"FEBS Lett."},{"issue":"Suppl. 1","key":"10.1529\/biophysj.107.110635_bib26","first-page":"A30","article-title":"High islet amyloid polypeptide secretion results in transient hyperglycemia without beta-cell death","volume":"47","author":"Janson","year":"1998","journal-title":"Diabetes"},{"key":"10.1529\/biophysj.107.110635_bib27","doi-asserted-by":"crossref","first-page":"1988","DOI":"10.1074\/jbc.271.4.1988","article-title":"Pore formation by the cytotoxic islet amyloid peptide amylin","volume":"271","author":"Mirzabekov","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1529\/biophysj.107.110635_bib28","doi-asserted-by":"crossref","first-page":"9496","DOI":"10.1021\/bi060579z","article-title":"Conserved and cooperative assembly of membrane-bound \u03b1-helical states of islet amyloid polypeptide","volume":"45","author":"Knight","year":"2006","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.107.110635_bib29","doi-asserted-by":"crossref","first-page":"12113","DOI":"10.1021\/bi050840w","article-title":"Lipid membranes modulate the structure of islet amyloid polyp","volume":"44","author":"Jayasinghe","year":"2005","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.107.110635_bib30","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/BF01219652","article-title":"The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus","volume":"15","author":"Westermark","year":"1978","journal-title":"Diabetologia"},{"key":"10.1529\/biophysj.107.110635_bib31","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1016\/S0046-8177(81)80197-9","article-title":"The relation of islet amyloid to the clinical type of diabetes","volume":"12","author":"Maloy","year":"1981","journal-title":"Hum. Pathol."},{"key":"10.1529\/biophysj.107.110635_bib32","first-page":"495","article-title":"Pancreatic islet amyloid in type 2 diabetes mellitus: a clinical and historical review","volume":"99","author":"Hayden","year":"2002","journal-title":"Mo. Med."},{"key":"10.1529\/biophysj.107.110635_bib33","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1016\/j.jmb.2004.07.052","article-title":"Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide","volume":"342","author":"Green","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib34","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1016\/j.febslet.2004.12.085","article-title":"Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin","volume":"579","author":"Balali-Mood","year":"2005","journal-title":"FEBS Lett."},{"key":"10.1529\/biophysj.107.110635_bib35","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/j.jmb.2004.06.086","article-title":"Phospholipid catalysis of diabetic amyloid assembly","volume":"341","author":"Knight","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib36","doi-asserted-by":"crossref","first-page":"17294","DOI":"10.1074\/jbc.M500997200","article-title":"Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers","volume":"280","author":"Demuro","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1529\/biophysj.107.110635_bib37","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed","year":"2003","journal-title":"Science"},{"key":"10.1529\/biophysj.107.110635_bib38","doi-asserted-by":"crossref","first-page":"46363","DOI":"10.1074\/jbc.C400260200","article-title":"Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases","volume":"279","author":"Kayed","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1529\/biophysj.107.110635_bib39","doi-asserted-by":"crossref","first-page":"11338","DOI":"10.1021\/bi020314u","article-title":"Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes","volume":"41","author":"Anguiano","year":"2002","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.107.110635_bib40","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1055\/s-2001-17297","article-title":"Rodent obesity models: an overview","volume":"109","author":"Tschop","year":"2001","journal-title":"Exp. Clin. Endocrinol. Diabetes"},{"key":"10.1529\/biophysj.107.110635_bib41","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1007\/s001250051175","article-title":"Extensive islet amyloid formation is induced by development of type II diabetes mellitus and contributes to its progression: pathogenesis of diabetes in a mouse model","volume":"42","author":"Hoppener","year":"1999","journal-title":"Diabetologia"},{"key":"10.1529\/biophysj.107.110635_bib42","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.2337\/diabetes.53.6.1509","article-title":"Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2 diabetes","volume":"53","author":"Butler","year":"2004","journal-title":"Diabetes"},{"key":"10.1529\/biophysj.107.110635_bib43","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/S0006-3495(94)80495-3","article-title":"External reflection FTIR of peptide monolayer films in situ at the air\/water interface: experimental design, spectra-structure correlations, and effects of hydrogen-deuterium exchange","volume":"67","author":"Flach","year":"1994","journal-title":"Biophys. J."},{"key":"10.1529\/biophysj.107.110635_bib44","doi-asserted-by":"crossref","first-page":"3478","DOI":"10.1039\/b506558p","article-title":"Protein-lipid interactions at the air\/water interface","volume":"7","author":"Lad","year":"2005","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1529\/biophysj.107.110635_bib45","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/s00249-004-0446-8","article-title":"Monolayer-multilayer transitions in a lung surfactant model: IR reflection-absorption spectroscopy and atomic force microscopy","volume":"34","author":"Wang","year":"2005","journal-title":"Eur. Biophys. J."},{"key":"10.1529\/biophysj.107.110635_bib46","doi-asserted-by":"crossref","first-page":"3730","DOI":"10.1021\/la0304316","article-title":"Orientation of peptides in aqueous monolayer films. Infrared reflection-absorption spectroscopy studies of a synthetic amphipathic \u03b2-sheet","volume":"20","author":"Xu","year":"2004","journal-title":"Langmuir"},{"key":"10.1529\/biophysj.107.110635_bib47","doi-asserted-by":"crossref","first-page":"3750","DOI":"10.1529\/biophysj.103.035964","article-title":"Infrared reflection absorption spectroscopy of amphipathic model peptides at the air\/water interface","volume":"86","author":"Kerth","year":"2004","journal-title":"Biophys. J."},{"key":"10.1529\/biophysj.107.110635_bib48","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.1002\/cbic.200500116","article-title":"Adsorption of amyloid beta (1\u201340) peptide at phospholipid monolayers","volume":"6","author":"Maltseva","year":"2005","journal-title":"ChemBioChem."},{"key":"10.1529\/biophysj.107.110635_bib49","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1529\/biophysj.106.084624","article-title":"Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS)","volume":"91","author":"Meister","year":"2006","journal-title":"Biophys. J."},{"key":"10.1529\/biophysj.107.110635_bib50","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0005-2736(75)90045-0","article-title":"Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers","volume":"406","author":"Demel","year":"1975","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1529\/biophysj.107.110635_bib51","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0014-5793(00)01287-4","article-title":"Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils","volume":"470","author":"Higham","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1529\/biophysj.107.110635_bib52","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0925-4439(01)00078-3","article-title":"Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology","volume":"1537","author":"Jaikaran","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1529\/biophysj.107.110635_bib53","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmb.2005.02.029","article-title":"The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin","volume":"348","author":"Kajava","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib54","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1038\/368756a0","article-title":"Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus","volume":"368","author":"Lorenzo","year":"1994","journal-title":"Nature"},{"key":"10.1529\/biophysj.107.110635_bib55","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1093\/protein\/1.4.289","article-title":"An algorithm for protein secondary structure prediction based on class prediction","volume":"1","author":"Deleage","year":"1987","journal-title":"Protein Eng."},{"key":"10.1529\/biophysj.107.110635_bib56","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/0167-4838(88)90206-3","article-title":"Improvements in a secondary structure prediction method based on a search for local sequence homologies and its use as a model building tool","volume":"955","author":"Levin","year":"1988","journal-title":"Biochim. Biochim. Acta"},{"key":"10.1529\/biophysj.107.110635_bib57","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1093\/protein\/7.2.157","article-title":"SOPM: a self-optimized method for protein secondary structure prediction","volume":"7","author":"Geourjon","year":"1994","journal-title":"Protein Eng."},{"key":"10.1529\/biophysj.107.110635_bib58","doi-asserted-by":"crossref","first-page":"242","DOI":"10.3109\/13506120108993820","article-title":"Enhanced in vitro production of amyloid-like fibrils from mutant (S20G) islet amyloid polypeptide","volume":"8","author":"Ma","year":"2001","journal-title":"Amyloid"},{"key":"10.1529\/biophysj.107.110635_bib59","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1529\/biophysj.104.048843","article-title":"Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy","volume":"88","author":"Jansen","year":"2005","journal-title":"Biophys. J."},{"key":"10.1529\/biophysj.107.110635_bib60","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1006\/jmbi.2001.4593","article-title":"Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis","volume":"308","author":"Jaikaran","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib61","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1110\/ps.062486907","article-title":"Direct detection of transient alpha-helical states in islet amyloid polypeptide","volume":"16","author":"Williamson","year":"2007","journal-title":"Protein Sci."},{"key":"10.1529\/biophysj.107.110635_bib62","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1006\/jmbi.1998.2348","article-title":"Solution structures of micelle-bound amyloid beta-(1\u201340) and beta-(1\u201342) peptides of Alzheimer's disease","volume":"285","author":"Shao","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib63","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1006\/jmbi.2001.4970","article-title":"Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis","volume":"312","author":"Kirkitadze","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib64","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1021\/bi020429y","article-title":"The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation","volume":"42","author":"Kessler","year":"2003","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.107.110635_bib65","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":"10.1529\/biophysj.107.110635_bib66","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmb.2005.02.029","article-title":"The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin","volume":"348","author":"Kajava","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.107.110635_bib67","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1006\/jmbi.1998.2299","article-title":"Watching amyloid fibrils grow by time-lapse atomic force microscopy","volume":"285","author":"Goldsbury","year":"1999","journal-title":"J. Mol. Biol."}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349507715679?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349507715679?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T16:23:03Z","timestamp":1762100583000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349507715679"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,11]]},"references-count":67,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2007,11]]}},"alternative-id":["S0006349507715679"],"URL":"https:\/\/doi.org\/10.1529\/biophysj.107.110635","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2007,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mechanism of Islet Amyloid Polypeptide Fibrillation at Lipid Interfaces Studied by Infrared Reflection Absorption Spectroscopy","name":"articletitle","label":"Article Title"},{"value":"Biophysical Journal","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1529\/biophysj.107.110635","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2007 The Biophysical Society. Published by Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}