{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T04:03:18Z","timestamp":1740110598241,"version":"3.37.3"},"reference-count":67,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"vor","delay-in-days":366,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100007259","name":"Stony Brook University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007259","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MCB1715525"],"award-info":[{"award-number":["MCB1715525"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM078114","GM122493"],"award-info":[{"award-number":["GM078114","GM122493"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"published-print":{"date-parts":[[2023,8]]},"DOI":"10.1016\/j.bbamem.2023.184161","type":"journal-article","created":{"date-parts":[[2023,4,28]],"date-time":"2023-04-28T15:14:46Z","timestamp":1682694886000},"page":"184161","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["Impact of Ca2+ on membrane catalyzed IAPP amyloid formation and IAPP induced vesicle leakage"],"prefix":"10.1016","volume":"1865","author":[{"given":"Ming-Hao","family":"Li","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaoxue","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Erwin","family":"London","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel P.","family":"Raleigh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamem.2023.184161_bb0005","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1124\/pr.115.010629","article-title":"Amylin: pharmacology, physiology, and clinical potential","volume":"67","author":"Hay","year":"2015","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.bbamem.2023.184161_bb0010","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.bbamem.2023.184161_bb0015","doi-asserted-by":"crossref","DOI":"10.1155\/2016\/2798269","article-title":"Islet amyloid polypeptide: structure, function, and pathophysiology","volume":"2016","author":"Akter","year":"2016","journal-title":"J. Diabetes Res."},{"key":"10.1016\/j.bbamem.2023.184161_bb0020","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.bbamem.2023.184161_bb0025","first-page":"R1475","article-title":"The role of amylin in the control of energy homeostasis","volume":"298","author":"Lutz","year":"2010","journal-title":"Am. J. Phys. Regul. Integr. Comp. Phys."},{"key":"10.1016\/j.bbamem.2023.184161_bb0030","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.bbamem.2023.184161_bb0035","doi-asserted-by":"crossref","first-page":"12977","DOI":"10.7554\/eLife.12977","article-title":"Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics","volume":"5","author":"Abedini","year":"2016","journal-title":"elife"},{"key":"10.1016\/j.bbamem.2023.184161_bb0040","doi-asserted-by":"crossref","first-page":"R121","DOI":"10.1530\/JME-17-0105","article-title":"The beta-cell assassin: IAPP cytotoxicity","volume":"59","author":"Raleigh","year":"2017","journal-title":"J. Mol. Endocrinol."},{"key":"10.1016\/j.bbamem.2023.184161_bb0045","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1016\/j.febslet.2013.01.017","article-title":"Mechanisms of islet amyloidosis toxicity in type 2 diabetes","volume":"587","author":"Abedini","year":"2013","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbamem.2023.184161_bb0050","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.bbamem.2023.184161_bb0055","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1007\/s00125-021-05569-2","article-title":"IAPP-induced beta cell stress recapitulates the islet transcriptome in type 2 diabetes","volume":"65","author":"Blencowe","year":"2022","journal-title":"Diabetologia"},{"key":"10.1016\/j.bbamem.2023.184161_bb0060","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.bbamem.2023.184161_bb0065","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.bbamem.2023.184161_bb0070","doi-asserted-by":"crossref","first-page":"1280","DOI":"10.1002\/cbic.201000039","article-title":"Interaction of hIAPP with model raft membranes and pancreatic beta-cells: cytotoxicity of hIAPP oligomers","volume":"11","author":"Weise","year":"2010","journal-title":"Chembiochem"},{"key":"10.1016\/j.bbamem.2023.184161_bb0075","doi-asserted-by":"crossref","first-page":"19279","DOI":"10.1073\/pnas.1305517110","article-title":"Islet amyloid polypeptide toxicity and membrane interactions","volume":"110","author":"Cao","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2023.184161_bb0080","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.chemphyslip.2009.03.008","article-title":"Membrane permeabilization by islet amyloid polypeptide","volume":"160","author":"Engel","year":"2009","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bbamem.2023.184161_bb0085","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1021\/ar200189b","article-title":"Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective","volume":"45","author":"Brender","year":"2012","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.bbamem.2023.184161_bb0090","doi-asserted-by":"crossref","first-page":"4336","DOI":"10.1021\/acschemneuro.0c00588","article-title":"Lipid-chaperone hypothesis: a common molecular mechanism of membrane disruption by intrinsically disordered proteins","volume":"11","author":"Sciacca","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bbamem.2023.184161_bb0095","doi-asserted-by":"crossref","first-page":"1845","DOI":"10.1021\/acs.chemrev.0c00981","article-title":"Proteostasis of islet amyloid polypeptide: a molecular perspective of risk factors and protective strategies for type II diabetes","volume":"121","author":"Milardi","year":"2021","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bbamem.2023.184161_bb0100","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/bs.apcsb.2021.08.001","article-title":"The role of membranes in function and dysfunction of intrinsically disordered amyloidogenic proteins","volume":"128","author":"Pathak","year":"2022","journal-title":"Adv. Protein Chem. Struct. Biol."},{"key":"10.1016\/j.bbamem.2023.184161_bb0105","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.bbamem.2023.184161_bb0110","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.jmb.2012.01.048","article-title":"The effect of abeta on IAPP aggregation in the presence of an isolated beta-cell membrane","volume":"421","author":"Seeliger","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2023.184161_bb0115","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.bbamem.2023.184161_bb0120","doi-asserted-by":"crossref","first-page":"8661","DOI":"10.1021\/acs.jpcb.7b05689","article-title":"Interplay between membrane composition and structural stability of membrane-bound hIAPP","volume":"121","author":"Dignon","year":"2017","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbamem.2023.184161_bb0125","doi-asserted-by":"crossref","DOI":"10.1016\/j.chemphyslip.2020.105010","article-title":"The human islet amyloid polypeptide in protein misfolding disorders: mechanisms of aggregation and interaction with biomembranes","volume":"234","author":"Saghir","year":"2021","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bbamem.2023.184161_bb0130","first-page":"2091","article-title":"Evaluation of membrane models and their composition for islet amyloid polypeptide-membrane aggregation","volume":"2013","author":"Caillon","year":"1828","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2023.184161_bb0135","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/0005-2760(86)90232-8","article-title":"Glucose-induced phospholipid hydrolysis in isolated pancreatic islets: quantitative effects on the phospholipid content of arachidonate and other fatty acids","volume":"879","author":"Turk","year":"1986","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2023.184161_bb0140","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1021\/acs.biochem.7b01190","article-title":"Sterol structure strongly modulates membrane-islet amyloid polypeptide interactions","volume":"57","author":"Zhang","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2023.184161_bb0145","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.bbamem.2023.184161_bb0150","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.849979","article-title":"Structural dissection of the first events following membrane binding of the islet amyloid polypeptide","volume":"9","author":"Khemtemourian","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.bbamem.2023.184161_bb0155","doi-asserted-by":"crossref","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. Diabetes Res."},{"key":"10.1016\/j.bbamem.2023.184161_bb0160","first-page":"414","article-title":"Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone","volume":"127","author":"Westermark","year":"1987","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbamem.2023.184161_bb0165","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1016\/j.molcel.2017.05.028","article-title":"Intracellular Ca(2+) sensing: its role in calcium homeostasis and signaling","volume":"66","author":"Bagur","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamem.2023.184161_bb0170","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1100\/tsw.2001.489","article-title":"Extracellular and intracellular regulation of calcium homeostasis","volume":"1","author":"Bronner","year":"2001","journal-title":"ScientificWorldJournal"},{"key":"10.1016\/j.bbamem.2023.184161_bb0175","doi-asserted-by":"crossref","first-page":"4914","DOI":"10.3390\/ijms22094914","article-title":"Calcium dyshomeostasis in Alzheimer's disease pathogenesis","volume":"22","author":"Cascella","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamem.2023.184161_bb0180","doi-asserted-by":"crossref","first-page":"2515","DOI":"10.3390\/ijms22052515","article-title":"Mitochondrial calcium signaling in pancreatic beta-cell","volume":"22","author":"Weiser","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamem.2023.184161_bb0185","doi-asserted-by":"crossref","DOI":"10.1210\/endocr\/bqz028","article-title":"The endoplasmic reticulum and calcium homeostasis in pancreatic beta cells","volume":"161","author":"Zhang","year":"2020","journal-title":"Endocrinology"},{"key":"10.1016\/j.bbamem.2023.184161_bb0190","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.bpj.2012.11.3811","article-title":"Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP","volume":"104","author":"Sciacca","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2023.184161_bb0195","doi-asserted-by":"crossref","first-page":"216","DOI":"10.3389\/fendo.2014.00216","article-title":"The role of calcium, lipid membranes and islet amyloid polypeptide in the onset of type 2 diabetes: innocent bystanders or partners in a crime?","volume":"5","author":"Milardi","year":"2014","journal-title":"Front. Endocrinol. (Lausanne)"},{"key":"10.1016\/j.bbamem.2023.184161_bb0200","first-page":"1625","article-title":"Amyloid growth and membrane damage: current themes and emerging perspectives from theory and experiments on abeta and hIAPP","volume":"2018","author":"Sciacca","year":"1860","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.bbamem.2023.184161_bb0205","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/BF01875709","article-title":"Calcium- and magnesium-induced fusion of mixed phosphatidylserine\/phosphatidylcholine vesicles: effect of ion binding","volume":"59","author":"Duzgunes","year":"1981","journal-title":"J. Membr. Biol."},{"key":"10.1016\/j.bbamem.2023.184161_bb0210","first-page":"E796","article-title":"Glucose-induced pulsatile insulin release from single islets at stable and oscillatory cytoplasmic Ca2+","volume":"274","author":"Bergsten","year":"1998","journal-title":"Am. J. Phys."},{"key":"10.1016\/j.bbamem.2023.184161_bb0215","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/0003-2697(80)90269-9","article-title":"Colorimetric determination of phospholipids with ammonium ferrothiocyanate","volume":"104","author":"Stewart","year":"1980","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamem.2023.184161_bb0220","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1021\/ol047480+","article-title":"Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide","volume":"7","author":"Abedini","year":"2005","journal-title":"Org. Lett."},{"key":"10.1016\/j.bbamem.2023.184161_bb0225","doi-asserted-by":"crossref","first-page":"4848","DOI":"10.1021\/ol101981b","article-title":"Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids","volume":"12","author":"Marek","year":"2010","journal-title":"Org. Lett."},{"key":"10.1016\/j.bbamem.2023.184161_bb0230","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.bbamem.2023.184161_bb0235","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/BF00762944","article-title":"Molecular mechanisms of calcium-induced membrane fusion","volume":"22","author":"Papahadjopoulos","year":"1990","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.bbamem.2023.184161_bb0240","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1085\/jgp.200709865","article-title":"Massive Ca-induced membrane fusion and phospholipid changes triggered by reverse Na\/Ca exchange in BHK fibroblasts","volume":"132","author":"Yaradanakul","year":"2008","journal-title":"J. Gen. Physiol."},{"key":"10.1016\/j.bbamem.2023.184161_bb0245","doi-asserted-by":"crossref","first-page":"12880","DOI":"10.1021\/acsnano.0c08614","article-title":"Calcium ions promote membrane fusion by forming negative-curvature inducing clusters on specific anionic lipids","volume":"15","author":"Allolio","year":"2021","journal-title":"ACS Nano"},{"key":"10.1016\/j.bbamem.2023.184161_bb0250","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0005-2736(76)90241-8","article-title":"Studies on membrane fusion. II. Induction of fusion in pure phospholipid membranes by calcium ions and other divalent metals","volume":"448","author":"Papahadjopoulos","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2023.184161_bb0255","doi-asserted-by":"crossref","first-page":"3976","DOI":"10.1529\/biophysj.107.123984","article-title":"Specific lipids supply critical negative spontaneous curvature\u2013an essential component of native Ca2+-triggered membrane fusion","volume":"94","author":"Churchward","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2023.184161_bb0260","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1016\/S0006-3495(86)83518-4","article-title":"Morphological responses to calcium-induced interaction of phosphatidylserine-containing vesicles","volume":"50","author":"Kachar","year":"1986","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2023.184161_bb0265","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. Am. Chem. Soc."},{"key":"10.1016\/j.bbamem.2023.184161_bb0270","doi-asserted-by":"crossref","first-page":"3339","DOI":"10.1039\/c3cc40383a","article-title":"Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide","volume":"49","author":"Brender","year":"2013","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/j.bbamem.2023.184161_bb0275","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.jmb.2011.05.015","article-title":"A two-site mechanism for the inhibition of IAPP amyloidogenesis by zinc","volume":"410","author":"Salamekh","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2023.184161_bb0280","doi-asserted-by":"crossref","DOI":"10.1016\/j.chemphyslip.2021.105083","article-title":"Investigation of the effects of two major secretory granules components, insulin and zinc, on human-IAPP amyloid aggregation and membrane damage","volume":"237","author":"Khemtemourian","year":"2021","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bbamem.2023.184161_bb0285","first-page":"529","article-title":"Zinc boosts EGCG's hIAPP amyloid inhibition both in solution and membrane","volume":"2019","author":"Lee","year":"1867","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.bbamem.2023.184161_bb0290","doi-asserted-by":"crossref","first-page":"7500","DOI":"10.1016\/S0021-9258(17)40995-1","article-title":"Rotational relaxation of the \"microviscosity\" probe diphenylhexatriene in paraffin oil and egg lecithin vesicles","volume":"252","author":"Dale","year":"1977","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2023.184161_bb0295","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/0009-3084(89)90049-2","article-title":"Membrane \u201cfluidity\u201d as detected by diphenylhexatriene probes","volume":"50","author":"Lentz","year":"1989","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bbamem.2023.184161_bb0300","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1021\/bi985065h","article-title":"Location of diphenylhexatriene (DPH) and its derivatives within membranes: comparison of different fluorescence quenching analyses of membrane depth","volume":"38","author":"Kaiser","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2023.184161_bb0305","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/0009-3084(93)90060-G","article-title":"Use of fluorescent probes to monitor molecular order and motions within liposome bilayers","volume":"64","author":"Lentz","year":"1993","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bbamem.2023.184161_bb0310","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/0003-2697(78)90412-8","article-title":"A convenient and sensitive fluorescence assay for phospholipid vesicles using diphenylhexatriene","volume":"88","author":"London","year":"1978","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamem.2023.184161_bb0315","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1016\/0003-2697(84)90026-5","article-title":"Fluorimetric determination of critical micelle concentration avoiding interference from detergent charge","volume":"139","author":"Chattopadhyay","year":"1984","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamem.2023.184161_bb0320","doi-asserted-by":"crossref","first-page":"4307","DOI":"10.1529\/biophysj.107.114967","article-title":"Effect of the structure of lipids favoring disordered domain formation on the stability of cholesterol-containing ordered domains (lipid rafts): identification of multiple raft-stabilization mechanisms","volume":"93","author":"Bakht","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2023.184161_bb0325","doi-asserted-by":"crossref","first-page":"2930","DOI":"10.1021\/bi00464a007","article-title":"Calcium-induced lipid phase separations and interactions of phosphatidylcholine\/anionic phospholipid vesicles. Fluorescence studies using carbazole-labeled and brominated phospholipids","volume":"29","author":"Silvius","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2023.184161_bb0330","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1007\/s00125-011-2143-3","article-title":"Exendin-4 increases islet amyloid deposition but offsets the resultant beta cell toxicity in human islet amyloid polypeptide transgenic mouse islets","volume":"54","author":"Aston-Mourney","year":"2011","journal-title":"Diabetologia"},{"key":"10.1016\/j.bbamem.2023.184161_bb6500","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1021\/bi00380a039","article-title":"Influence of the calcium-induced gel phase on the behavior of small molecules in phosphatidylserine and phosphatidylserine-phosphatidylcholine multilamellar vesicles","volume":"26","author":"Florine","year":"1987","journal-title":"Biochemistry"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273623000433?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273623000433?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,8,2]],"date-time":"2024-08-02T01:44:55Z","timestamp":1722563095000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0005273623000433"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,8]]},"references-count":67,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2023,8]]}},"alternative-id":["S0005273623000433"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamem.2023.184161","relation":{},"ISSN":["0005-2736"],"issn-type":[{"type":"print","value":"0005-2736"}],"subject":[],"published":{"date-parts":[[2023,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Impact of Ca2+ on membrane catalyzed IAPP amyloid formation and IAPP induced vesicle leakage","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Biomembranes","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamem.2023.184161","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"184161"}}