{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:41:07Z","timestamp":1759542067781,"version":"build-2065373602"},"reference-count":62,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,12,19]],"date-time":"2020-12-19T00:00:00Z","timestamp":1608336000000},"content-version":"am","delay-in-days":293,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2020,3]]},"DOI":"10.1016\/j.biochi.2019.12.005","type":"journal-article","created":{"date-parts":[[2019,12,12]],"date-time":"2019-12-12T12:52:55Z","timestamp":1576155175000},"page":"26-35","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"special_numbering":"C","title":["The flanking peptides issue from the maturation of the human islet amyloid polypeptide (hIAPP) slightly modulate hIAPP-fibril formation but not hIAPP-induced cell death"],"prefix":"10.1016","volume":"170","author":[{"given":"Shadai","family":"Salazar Vazquez","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bertrand","family":"Blondeau","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pierre","family":"Cattan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mathieu","family":"Armanet","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ghislaine","family":"Guillemain","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6754-5724","authenticated-orcid":false,"given":"Lucie","family":"Khemtemourian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2019.12.005_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.biochi.2019.12.005_bib2","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":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.biochi.2019.12.005_bib3","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1152\/physrev.00042.2009","article-title":"Islet amyloid polypeptide, islet amyloid, and diabetes mellitus","volume":"91","author":"Westermark","year":"2011","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.biochi.2019.12.005_bib4","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1084\/jem.5.5.527","article-title":"The relation of diabetes mellitus to lesions of the pancreas. Hyaline degeneration of the islands of langerhans","volume":"5","author":"Opie","year":"1901","journal-title":"J.\u00a0Exp. Med."},{"key":"10.1016\/j.biochi.2019.12.005_bib5","doi-asserted-by":"crossref","first-page":"8628","DOI":"10.1073\/pnas.84.23.8628","article-title":"Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients","volume":"84","author":"Cooper","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.biochi.2019.12.005_bib6","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","article-title":"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","volume":"84","author":"Westermark","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.biochi.2019.12.005_bib7","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1016\/S0006-291X(05)81133-7","article-title":"Amylin secretion from the perfused pancreas: dissociation from insulin and abnormal elevation in insulin-resistant diabetic rats","volume":"180","author":"Gedulin","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2019.12.005_bib8","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.\u00a0Clin. Endocrinol. Metab."},{"key":"10.1016\/j.biochi.2019.12.005_bib9","doi-asserted-by":"crossref","first-page":"634","DOI":"10.2337\/diab.39.5.634","article-title":"Evidence of cosecretion of islet amyloid polypeptide and insulin by -cells","volume":"39","author":"Kahn","year":"1990","journal-title":"Diabetes"},{"key":"10.1016\/j.biochi.2019.12.005_bib10","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1007\/BF00285291","article-title":"Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets","volume":"32","author":"Lukinius","year":"1989","journal-title":"Diabetologia"},{"key":"10.1016\/j.biochi.2019.12.005_bib11","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/0167-0115(93)90362-C","article-title":"Cosecretion of islet amyloid polypeptide (IAPP) and insulin from isolated rat pancreatic islets following stimulation or inhibition of beta-cell function","volume":"45","author":"Stridsberg","year":"1993","journal-title":"Regul. Pept."},{"key":"10.1016\/j.biochi.2019.12.005_bib12","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1083\/jcb.67.3.835","article-title":"Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma","volume":"67","author":"Blobel","year":"1975","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.biochi.2019.12.005_bib13","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/nature06384","article-title":"Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes","volume":"450","author":"Rapoport","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2019.12.005_bib14","doi-asserted-by":"crossref","first-page":"7079","DOI":"10.1021\/ja900285z","article-title":"Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy","volume":"131","author":"Soong","year":"2009","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.biochi.2019.12.005_bib15","doi-asserted-by":"crossref","first-page":"8478","DOI":"10.1021\/bi300574r","article-title":"Ionic strength effects on amyloid formation by amylin are a complicated interplay among debye screening, ion selectivity, and hofmeister effects","volume":"51","author":"Marek","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2019.12.005_bib16","doi-asserted-by":"crossref","first-page":"15598","DOI":"10.1021\/ja205007j","article-title":"Low pH acts as inhibitor of membrane damage induced by human islet amyloid polypeptide","volume":"133","author":"Khemt\u00e9mourian","year":"2011","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.biochi.2019.12.005_bib17","doi-asserted-by":"crossref","first-page":"8973","DOI":"10.1021\/ja1007867","article-title":"Role of zinc in human islet amyloid polypeptide aggregation","volume":"132","author":"Brender","year":"2010","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.biochi.2019.12.005_bib18","doi-asserted-by":"crossref","first-page":"5398","DOI":"10.1039\/C6SC00153J","article-title":"Structure and assembly mechanisms of toxic human islet amyloid polypeptide oligomers associated with copper","volume":"7","author":"Lee","year":"2016","journal-title":"Chem. Sci."},{"key":"10.1016\/j.biochi.2019.12.005_bib19","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.jmb.2011.05.015","article-title":"A\u00a0two-site mechanism for the inhibition of IAPP amyloidogenesis by zinc","volume":"410","author":"Salamekh","year":"2011","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2019.12.005_bib20","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.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2019.12.005_bib21","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.biochi.2019.12.005_bib22","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 (Fed. Eur. Biochem. Soc.) Lett."},{"key":"10.1016\/j.biochi.2019.12.005_bib23","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2019.12.005_bib24","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.biochi.2019.12.005_bib25","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2015\/849017","article-title":"The effects of lipid membranes, crowding and osmolytes on the aggregation, and fibrillation propensity of human IAPP","volume":"2015","author":"Gao","year":"2015","journal-title":"J.\u00a0Diabetes Res."},{"key":"10.1016\/j.biochi.2019.12.005_bib26","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.3390\/ijms19051443","article-title":"A\u00a0rationally designed Hsp 70 variant rescues the aggregation-associated toxicity of human IAPP in cultured pancreatic islet \u03b2-cells","volume":"19","author":"Bongiovanni","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.biochi.2019.12.005_bib27","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.jinorgbio.2007.09.010","article-title":"Copper(II) inhibits the formation of amylin amyloid in\u00a0vitro","volume":"102","author":"Ward","year":"2008","journal-title":"J.\u00a0Inorg. Biochem."},{"key":"10.1016\/j.biochi.2019.12.005_bib28","doi-asserted-by":"crossref","first-page":"6909","DOI":"10.1039\/c0cc02141e","article-title":"Copper-induced cytotoxicity: reactive oxygen species or islet amyloid polypeptide oligomer formation","volume":"46","author":"Yu","year":"2010","journal-title":"Chem. Commun."},{"key":"10.1016\/j.biochi.2019.12.005_bib29","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.1039\/C4MT00130C","article-title":"The role of copper(II) in the aggregation of human amylin","volume":"10","author":"Sinopoli","year":"2014","journal-title":"Metallomics"},{"key":"10.1016\/j.biochi.2019.12.005_bib30","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.jinorgbio.2014.07.002","article-title":"Cu(II) inhibits hIAPP fibrillation and promotes hIAPP-induced beta cell apoptosis through induction of ROS-mediated mitochondrial dysfunction","volume":"140","author":"Ma","year":"2014","journal-title":"J.\u00a0Inorg. Biochem."},{"key":"10.1016\/j.biochi.2019.12.005_bib31","doi-asserted-by":"crossref","first-page":"5398","DOI":"10.1039\/C6SC00153J","article-title":"Structure and assembly mechanisms of toxic human islet amyloid polypeptide oligomers associated with copper","volume":"8","author":"Lee","year":"2016","journal-title":"Chem. Sci."},{"key":"10.1016\/j.biochi.2019.12.005_bib32","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/0014-5793(95)01512-4","article-title":"Effects of beta cell granule components on human islet amyloid polypeptide fibril formation","volume":"379","author":"Westermark","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2019.12.005_bib33","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/j.jmb.2003.10.045","article-title":"The mechanism of insulin action on islet amyloid polypeptide fiber formation","volume":"335","author":"Larson","year":"2004","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2019.12.005_bib34","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1042\/bj20030852","article-title":"Pancreatic beta-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation","volume":"377","author":"Jaikaran","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2019.12.005_bib35","doi-asserted-by":"crossref","first-page":"12912","DOI":"10.1021\/ja504031d","article-title":"Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions","volume":"37","author":"Susa","year":"2014","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.biochi.2019.12.005_bib36","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.biochi.2017.07.015","article-title":"Residue specific effects of human islet polypeptide amyloid on self-assembly and on cell toxicity","volume":"142","author":"Khemtemourian","year":"2017","journal-title":"Biochimie"},{"key":"10.1016\/j.biochi.2019.12.005_bib37","doi-asserted-by":"crossref","first-page":"10918","DOI":"10.1021\/bi901076d","article-title":"Impaired processing of human pro-islet amyloid polypeptide is not a causative factor for fibril formation or membrane damage in\u00a0vitro","volume":"48","author":"Khemt\u00e9mourian","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2019.12.005_bib38","doi-asserted-by":"crossref","first-page":"E955","DOI":"10.1152\/ajpendo.00130.2014","article-title":"Physiological effects and therapeutic potential of proinsulin C-peptide","volume":"307","author":"Yosten","year":"2014","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.biochi.2019.12.005_bib39","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1007\/s00018-006-6204-6","article-title":"Proinsulin C-peptide elicits disaggregation of insulin resulting in enhanced physiological insulin effects","volume":"63","author":"Shafqat","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.biochi.2019.12.005_bib40","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1007\/BF02531316","article-title":"Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots","volume":"5","author":"Rouser","year":"1970","journal-title":"Lipids"},{"key":"10.1016\/j.biochi.2019.12.005_bib41","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0022-1759(84)90190-X","article-title":"Rapid colorimetric assay for cell viability: application to the quantitation of cytotoxic and growth inhibitory lymphokines","volume":"70","author":"Green","year":"1984","journal-title":"J.\u00a0Immunol. Methods"},{"key":"10.1016\/j.biochi.2019.12.005_bib42","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/1471-2105-8-65","article-title":"AGGRESCAN: a server for the prediction and evaluation of \u201chot spots\u201d of aggregation in polypeptides","volume":"8","author":"Conchillo-Sol\u00e9","year":"2007","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.biochi.2019.12.005_bib43","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1093\/bioinformatics\/btp691","article-title":"FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence","volume":"26","author":"Garbuzynskiy","year":"2010","journal-title":"Bioinformatics"},{"key":"10.1016\/j.biochi.2019.12.005_bib44","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1038\/nbt1012","article-title":"Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins","volume":"22","author":"Fernandez-Escamilla","year":"2004","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.biochi.2019.12.005_bib45","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. U.S.A."},{"key":"10.1016\/j.biochi.2019.12.005_bib46","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nmeth.1432","article-title":"Exploring the sequence determinants of amyloid structure using position-specific scoring matrices","volume":"7","author":"Maurer-Stroh","year":"2010","journal-title":"Nat. Methods"},{"key":"10.1016\/j.biochi.2019.12.005_bib47","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/S0076-6879(99)09020-5","article-title":"Quantification of beta-sheet amyloid fibril structures with thioflavin T","volume":"309","author":"LeVine","year":"1999","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.biochi.2019.12.005_bib48","doi-asserted-by":"crossref","first-page":"9561","DOI":"10.1039\/C7CP07516B","article-title":"Time dependence of NMR observables reveals salient differences in the accumulation of early aggregated species between human islet amyloid polypeptide and amyloid-\u03b2","volume":"20","author":"Hoffmann","year":"2018","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.biochi.2019.12.005_bib49","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.\u00a0Struct. Biol."},{"key":"10.1016\/j.biochi.2019.12.005_bib50","doi-asserted-by":"crossref","first-page":"2091","DOI":"10.1016\/j.bbamem.2013.05.014","article-title":"Evaluation of membrane models and their composition for islet amyloid polypeptide-membrane aggregation","volume":"1828","author":"Caillon","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2019.12.005_bib51","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1016\/j.bbamem.2018.02.022","article-title":"Amyloid growth and membrane damage: current themes and emerging perspectives from theory and experiments on A\u03b2 and hIAPP","volume":"1860","author":"Sciacca","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2019.12.005_bib52","doi-asserted-by":"crossref","first-page":"5125","DOI":"10.1021\/acs.jpclett.8b02241","article-title":"Phospholipids critical micellar concentrations trigger different mechanisms of intrinsically disordered proteins interaction with model membranes","volume":"17","author":"Scollo","year":"2018","journal-title":"J.\u00a0Phys. Chem. Lett."},{"key":"10.1016\/j.biochi.2019.12.005_bib53","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1021\/acs.biochem.6b01016","article-title":"Islet amyloid polypeptide membrane interactions: effects of membrane composition","volume":"56","author":"Zhang","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2019.12.005_bib54","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.biochi.2019.12.005_bib55","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1016\/j.bbamem.2018.02.018","article-title":"A\u00a0single mutation on the human amyloid polypeptide modulates fibril growth and affects the mechanism of amyloid-induced membrane damage","volume":"1860","author":"Hoffmann","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2019.12.005_bib56","doi-asserted-by":"crossref","first-page":"2368","DOI":"10.1021\/bi802097b","article-title":"Residual structure in islet amyloid polypeptide mediates its interactions with soluble insulin \u2020","volume":"48","author":"Wei","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2019.12.005_bib57","doi-asserted-by":"crossref","first-page":"3365","DOI":"10.1111\/j.1742-4658.2009.07061.x","article-title":"Insulin is a kinetic but not a thermodynamic inhibitor of amylin aggregation","volume":"276","author":"Cui","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.biochi.2019.12.005_bib58","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1039\/C4CP05563B","article-title":"On the lag phase in amyloid fibril formation","volume":"17","author":"Arosio","year":"2015","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.biochi.2019.12.005_bib59","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.ijbiomac.2019.06.050","article-title":"Human islet amyloid polypeptide (hIAPP) aggregation in type 2 diabetes: correlation between intrinsic physicochemical properties of hIAPP aggregates and their cytotoxicity","volume":"136","author":"Chaari","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.biochi.2019.12.005_bib60","doi-asserted-by":"crossref","first-page":"1941","DOI":"10.1021\/jacs.8b08537","article-title":"Misfolding of a human islet amyloid polypeptide at the lipid membrane populates through \u03b2-sheet conformers without involving \u03b1-helical intermediates","volume":"141","author":"Tan","year":"2019","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.biochi.2019.12.005_bib61","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1016\/j.bbamem.2018.02.020","article-title":"IAPP in type II diabetes: basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies","volume":"1860","author":"Asthana","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2019.12.005_bib62","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.bbadis.2018.11.021","article-title":"Nucleation of \u03b2-rich oligomers and \u03b2-barrels in the early aggregation of human islet amyloid polypeptide","volume":"1865","author":"Sun","year":"2019","journal-title":"Biochim. Biophys. Acta"}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908419303633?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908419303633?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:12:03Z","timestamp":1759540323000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908419303633"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3]]},"references-count":62,"alternative-id":["S0300908419303633"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2019.12.005","relation":{},"ISSN":["0300-9084"],"issn-type":[{"type":"print","value":"0300-9084"}],"subject":[],"published":{"date-parts":[[2020,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The flanking peptides issue from the maturation of the human islet amyloid polypeptide (hIAPP) slightly modulate hIAPP-fibril formation but not hIAPP-induced cell death","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2019.12.005","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM). All rights reserved.","name":"copyright","label":"Copyright"}]}}