{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T19:39:43Z","timestamp":1791229183517,"version":"4.1.0"},"reference-count":30,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2006,2,1]],"date-time":"2006-02-01T00:00:00Z","timestamp":1138752000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2006,2]]},"DOI":"10.1016\/j.jmb.2005.12.020","type":"journal-article","created":{"date-parts":[[2005,12,22]],"date-time":"2005-12-22T18:18:40Z","timestamp":1135275520000},"page":"783-789","source":"Crossref","is-referenced-by-count":172,"title":["Islet Amyloid Polypeptide Inserts into Phospholipid Monolayers as Monomer"],"prefix":"10.1016","volume":"356","author":[{"given":"Maarten F.M.","family":"Engel","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"HaciAli","family":"Yigittop","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald C.","family":"Elgersma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk T.S.","family":"Rijkers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rob M.J.","family":"Liskamp","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ben","family":"de Kruijff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo W.M.","family":"H\u00f6ppener","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J.","family":"Antoinette Killian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2005.12.020_bib1","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1056\/NEJM200008103430607","article-title":"Islet amyloid and type 2 diabetes mellitus","volume":"343","author":"H\u00f6ppener","year":"2000","journal-title":"New Engl. J. Med."},{"key":"10.1016\/j.jmb.2005.12.020_bib2","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.1210\/jc.2004-0405","article-title":"Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes","volume":"89","author":"Hull","year":"2004","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.jmb.2005.12.020_bib3","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":"10.1016\/j.jmb.2005.12.020_bib4","doi-asserted-by":"crossref","first-page":"491","DOI":"10.2337\/diabetes.48.3.491","article-title":"The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles","volume":"48","author":"Janson","year":"1999","journal-title":"Diabetes"},{"key":"10.1016\/j.jmb.2005.12.020_bib5","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":"10.1016\/j.jmb.2005.12.020_bib6","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":"10.1016\/j.jmb.2005.12.020_bib7","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":"10.1016\/j.jmb.2005.12.020_bib8","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":"10.1016\/j.jmb.2005.12.020_bib9","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":"10.1016\/j.jmb.2005.12.020_bib10","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":"10.1016\/j.jmb.2005.12.020_bib11","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":"10.1016\/j.jmb.2005.12.020_bib12","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 Letters"},{"key":"10.1016\/j.jmb.2005.12.020_bib13","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 Letters"},{"key":"10.1016\/j.jmb.2005.12.020_bib14","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":"10.1016\/j.jmb.2005.12.020_bib15","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 Letters"},{"key":"10.1016\/j.jmb.2005.12.020_bib16","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/0005-2736(73)90126-0","article-title":"The specific interaction of myelin basic protein with lipids at the air-water interface","volume":"311","author":"Demel","year":"1973","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2005.12.020_bib17","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1007\/BF02538912","article-title":"Lipid composition of glucose-stimulated pancreatic islets and insulin-secreting tumor cells","volume":"29","author":"Rustenbeck","year":"1994","journal-title":"Lipids"},{"key":"10.1016\/j.jmb.2005.12.020_bib18","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":"10.1016\/j.jmb.2005.12.020_bib19","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.jmb.2005.12.020_bib20","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":"10.1016\/j.jmb.2005.12.020_bib21","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1006\/jsbi.2000.4268","article-title":"Amyloid fibril formation from full-length and fragments of amylin","volume":"130","author":"Goldsbury","year":"2000","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jmb.2005.12.020_bib22","doi-asserted-by":"crossref","first-page":"5738","DOI":"10.1073\/pnas.86.15.5738","article-title":"Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone","volume":"86","author":"Nishi","year":"1989","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.12.020_bib23","doi-asserted-by":"crossref","first-page":"12113","DOI":"10.1021\/bi050840w","article-title":"Lipid membranes modulate the structure of islet amyloid polypeptide","volume":"44","author":"Jayasinghe","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.12.020_bib24","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.peptides.2004.01.001","article-title":"Aggregation of liposomes induced by the toxic peptides Alzheimer's A\u03b2s, human amylin and prion (106-126): facilitation by membrane-bound GM1 ganglioside","volume":"25","author":"Kurganov","year":"2004","journal-title":"Peptides"},{"key":"10.1016\/j.jmb.2005.12.020_bib25","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":"10.1016\/j.jmb.2005.12.020_bib26","doi-asserted-by":"crossref","first-page":"10302","DOI":"10.1021\/bi049002c","article-title":"Formation of amyloid fibers triggered by phosphatidylserine-containing membranes","volume":"43","author":"Zhao","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.12.020_bib27","doi-asserted-by":"crossref","first-page":"6297","DOI":"10.1073\/pnas.0407035102","article-title":"Raft lipids as common components of human extracellular amyloid fibrils","volume":"102","author":"Gellermann","year":"2005","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.12.020_bib28","doi-asserted-by":"crossref","first-page":"4285","DOI":"10.1002\/1521-3765(20020916)8:18<4285::AID-CHEM4285>3.0.CO;2-0","article-title":"Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides","volume":"8","author":"Rijkers","year":"2002","journal-title":"Chem. Eur. J."},{"key":"10.1016\/j.jmb.2005.12.020_bib29","doi-asserted-by":"crossref","first-page":"6657","DOI":"10.1021\/ja00017a044","article-title":"Disulfide bond formation in peptides by dimethyl-sulfoxide\u2014scope and applications","volume":"113","author":"Tam","year":"1991","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2005.12.020_bib30","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1007\/978-1-4615-1863-1_3","article-title":"Monomolecular layers in the study of biomembranes","volume":"23","author":"Demel","year":"1994","journal-title":"Subcell. Biochem."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283605015809?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283605015809?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,1,19]],"date-time":"2019-01-19T06:56:20Z","timestamp":1547880980000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283605015809"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,2]]},"references-count":30,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2006,2]]}},"alternative-id":["S0022283605015809"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2005.12.020","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2006,2]]}}}