{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T12:36:08Z","timestamp":1790253368514,"version":"4.1.0"},"reference-count":61,"publisher":"Elsevier BV","issue":"21","license":[{"start":{"date-parts":[[2019,5,1]],"date-time":"2019-05-01T00:00:00Z","timestamp":1556668800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,31]],"date-time":"2020-08-31T00:00:00Z","timestamp":1598832000000},"content-version":"vor","delay-in-days":488,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (NSERC)","doi-asserted-by":"publisher","award":["06209"],"award-info":[{"award-number":["06209"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2019,5]]},"DOI":"10.1074\/jbc.ra118.006454","type":"journal-article","created":{"date-parts":[[2019,4,11]],"date-time":"2019-04-11T22:45:17Z","timestamp":1555022717000},"page":"8452-8463","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":43,"title":["Identification of a hinge residue controlling islet amyloid polypeptide self-assembly and cytotoxicity"],"prefix":"10.1016","volume":"294","author":[{"given":"Elizabeth","family":"Godin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phuong Trang","family":"Nguyen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ximena","family":"Zottig","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5563-8787","authenticated-orcid":false,"given":"Steve","family":"Bourgault","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA118.006454_bib1","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.RA118.006454_bib2","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1038\/nature02265","article-title":"Therapeutic approaches to protein-misfolding diseases","volume":"426","author":"Cohen","year":"2003","journal-title":"Nature"},{"key":"10.1074\/jbc.RA118.006454_bib3","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1084\/jem.5.4.397","article-title":"On the relation of chronic interstitial pancreatitis to the islands of langerhans and to diabetes melutus","volume":"5","author":"Opie","year":"1901","journal-title":"J. Exp. Med"},{"key":"10.1074\/jbc.RA118.006454_bib4","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":"10.1074\/jbc.RA118.006454_bib5","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. Engl. J. Med"},{"key":"10.1074\/jbc.RA118.006454_bib6","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":"10.1074\/jbc.RA118.006454_bib7","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":"10.1074\/jbc.RA118.006454_bib8","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":"10.1074\/jbc.RA118.006454_bib9","doi-asserted-by":"crossref","DOI":"10.1155\/2015\/515307","article-title":"Mechanistic contributions of biological cofactors in islet amyloid polypeptide amyloidogenesis","volume":"2015","author":"Nguyen","year":"2015","journal-title":"J. Diabetes Res"},{"key":"10.1074\/jbc.RA118.006454_bib10","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":"10.1074\/jbc.RA118.006454_bib11","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1016\/j.febslet.2013.01.046","article-title":"Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity","volume":"587","author":"Cao","year":"2013","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.RA118.006454_bib12","doi-asserted-by":"crossref","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":"10.1074\/jbc.RA118.006454_bib13","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.19273","article-title":"Atomic structures of fibrillar segments of hIAPP suggest tightly mated beta-sheets are important for cytotoxicity","volume":"6","author":"Krotee","year":"2017","journal-title":"Elife"},{"key":"10.1074\/jbc.RA118.006454_bib14","doi-asserted-by":"crossref","first-page":"699","DOI":"10.2337\/db15-1264","article-title":"Monitoring C-peptide storage and secretion in islet beta-cells in vitro and in vivo","volume":"65","author":"Zhu","year":"2016","journal-title":"Diabetes"},{"key":"10.1074\/jbc.RA118.006454_bib15","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1110\/ps.062486907","article-title":"Direct detection of transient \u03b1-helical states in islet amyloid polypeptide","volume":"16","author":"Williamson","year":"2007","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.RA118.006454_bib16","doi-asserted-by":"crossref","first-page":"11982","DOI":"10.1074\/jbc.M809085200","article-title":"Dynamic \u03b1-helix structure of micelle-bound human amylin","volume":"284","author":"Patil","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.006454_bib17","doi-asserted-by":"crossref","first-page":"2337","DOI":"10.1016\/j.bbamem.2011.06.012","article-title":"Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment","volume":"1808","author":"Nanga","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA118.006454_bib18","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.31226","article-title":"Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate","volume":"6","author":"Rodriguez Camargo","year":"2017","journal-title":"Elife"},{"key":"10.1074\/jbc.RA118.006454_bib19","doi-asserted-by":"crossref","first-page":"13505","DOI":"10.1021\/bi701427q","article-title":"Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR","volume":"46","author":"Luca","year":"2007","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA118.006454_bib20","doi-asserted-by":"crossref","first-page":"5235","DOI":"10.1074\/jbc.M111.327817","article-title":"Fibril structure of human islet amyloid polypeptide","volume":"287","author":"Bedrood","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.006454_bib21","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1093\/protein\/gzp036","article-title":"A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides","volume":"22","author":"Abedini","year":"2009","journal-title":"Protein Eng. Des. Sel"},{"key":"10.1074\/jbc.RA118.006454_bib22","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.jmb.2009.07.077","article-title":"Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide","volume":"393","author":"Williamson","year":"2009","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA118.006454_bib23","doi-asserted-by":"crossref","first-page":"14383","DOI":"10.1002\/anie.201507092","article-title":"Delineating the role of helical intermediates in natively unfolded polypeptide amyloid assembly and cytotoxicity","volume":"54","author":"De Carufel","year":"2015","journal-title":"Angew. Chem. Int. Ed. Engl"},{"key":"10.1074\/jbc.RA118.006454_bib24","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1039\/C7SC03789A","article-title":"Site-specific detection of protein secondary structure using 2D IR dihedral indexing: a proposed assembly mechanism of oligomeric hIAPP","volume":"9","author":"Maj","year":"2018","journal-title":"Chem. Sci"},{"key":"10.1074\/jbc.RA118.006454_bib25","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1093\/protein\/gzm076","article-title":"Amide inequivalence in the fibrillar assembly of islet amyloid polypeptide","volume":"21","author":"Koo","year":"2008","journal-title":"Protein Eng. Des. Sel"},{"key":"10.1074\/jbc.RA118.006454_bib26","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1110\/ps.041051205","article-title":"Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid","volume":"14","author":"Koo","year":"2005","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.RA118.006454_bib27","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1021\/bi3014278","article-title":"Role of aromatic interactions in amyloid formation by islet amyloid polypeptide","volume":"52","author":"Tu","year":"2013","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA118.006454_bib28","doi-asserted-by":"crossref","first-page":"11300","DOI":"10.1021\/ja072157y","article-title":"A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor","volume":"129","author":"Abedini","year":"2007","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA118.006454_bib29","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":"10.1074\/jbc.RA118.006454_bib30","doi-asserted-by":"crossref","first-page":"3808","DOI":"10.1021\/acs.biochem.7b00209","article-title":"Role of site-specific asparagine deamidation in islet amyloid polypeptide amyloidogenesis: key contributions of residues 14 and 21","volume":"56","author":"Nguyen","year":"2017","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA118.006454_bib31","doi-asserted-by":"crossref","first-page":"7783","DOI":"10.1021\/bi100337p","article-title":"Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity","volume":"49","author":"Fox","year":"2010","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA118.006454_bib32","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1016\/S0002-9440(10)64848-1","article-title":"S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin","volume":"157","author":"Sakagashira","year":"2000","journal-title":"Am. J. Pathol"},{"key":"10.1074\/jbc.RA118.006454_bib33","doi-asserted-by":"crossref","first-page":"3308","DOI":"10.1021\/jm900291j","article-title":"Molecular and conformational determinants of pituitary adenylate cyclase-activating polypeptide (PACAP) for activation of the PAC1 receptor","volume":"52","author":"Bourgault","year":"2009","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.RA118.006454_bib34","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1038\/nrd939","article-title":"Designing peptide receptor agonists and antagonists","volume":"1","author":"Hruby","year":"2002","journal-title":"Nat. Rev. Drug. Discov"},{"key":"10.1074\/jbc.RA118.006454_bib35","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1002\/1097-0282(2001)60:5<351::AID-BIP10174>3.0.CO;2-U","article-title":"Controls exerted by the Aib residue: helix formation and helix reversal","volume":"60","author":"Karle","year":"2001","journal-title":"Biopolymers"},{"key":"10.1074\/jbc.RA118.006454_bib36","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. U.S.A"},{"key":"10.1074\/jbc.RA118.006454_bib37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/13506129509031881","article-title":"Thioflavine T interaction with amyloid \u03b2-sheet structures","volume":"2","author":"LeVine","year":"1995","journal-title":"Amyloid"},{"key":"10.1074\/jbc.RA118.006454_bib38","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1080\/19336896.2015.1132138","article-title":"Proline and lysine residues provide modulatory switches in amyloid formation: insights from prion protein","volume":"10","author":"Kraus","year":"2016","journal-title":"Prion"},{"key":"10.1074\/jbc.RA118.006454_bib39","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.jmb.2005.10.052","article-title":"Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP?","volume":"355","author":"Abedini","year":"2006","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA118.006454_bib40","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.ab.2017.06.007","article-title":"Thioflavin T fluorescence to analyse amyloid formation kinetics: measurement frequency as a factor explaining irreproducibility","volume":"532","author":"Sebastiao","year":"2017","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.RA118.006454_bib41","doi-asserted-by":"crossref","first-page":"11358","DOI":"10.1021\/acsnano.7b05895","article-title":"Mechanistic origin of the combined effect of surfaces and mechanical agitation on amyloid formation","volume":"11","author":"Grigolato","year":"2017","journal-title":"ACS Nano"},{"key":"10.1074\/jbc.RA118.006454_bib42","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1002\/bip.22243","article-title":"New insights into the roles of sulfated glycosaminoglycans in islet amyloid polypeptide amyloidogenesis and cytotoxicity","volume":"100","author":"De Carufel","year":"2013","journal-title":"Biopolymers"},{"key":"10.1074\/jbc.RA118.006454_bib43","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1021\/ar000214l","article-title":"Rapid photochemical cross-linking\u2013a new tool for studies of metastable, amyloidogenic protein assemblies","volume":"37","author":"Bitan","year":"2004","journal-title":"Acc. Chem. Res"},{"key":"10.1074\/jbc.RA118.006454_bib44","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":"10.1074\/jbc.RA118.006454_bib45","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":"10.1074\/jbc.RA118.006454_bib46","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-018-03651-9","article-title":"Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid","volume":"9","author":"Birol","year":"2018","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.RA118.006454_bib47","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1146\/annurev.biophys.050708.133622","article-title":"The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes","volume":"38","author":"Hebda","year":"2009","journal-title":"Annu. Rev. Biophys"},{"key":"10.1074\/jbc.RA118.006454_bib48","doi-asserted-by":"crossref","first-page":"52810","DOI":"10.1074\/jbc.M308244200","article-title":"Fibrillogenic amylin evokes islet beta-cell apoptosis through linked activation of a caspase cascade and JNK1","volume":"278","author":"Zhang","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.006454_bib49","doi-asserted-by":"crossref","first-page":"19285","DOI":"10.1073\/pnas.1314481110","article-title":"Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient beta-sheet","volume":"110","author":"Buchanan","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA118.006454_bib50","doi-asserted-by":"crossref","first-page":"16748","DOI":"10.1021\/jacs.7b08830","article-title":"A free energy barrier caused by the refolding of an oligomeric intermediate controls the lag time of amyloid formation by hIAPP","volume":"139","author":"Serrano","year":"2017","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA118.006454_bib51","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1021\/jp511758w","article-title":"Probing the sources of the apparent irreproducibility of amyloid formation: drastic changes in kinetics and a switch in mechanism due to micellelike oligomer formation at critical concentrations of IAPP","volume":"119","author":"Brender","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"10.1074\/jbc.RA118.006454_bib52","doi-asserted-by":"crossref","first-page":"13530","DOI":"10.1021\/ja050767x","article-title":"Elongation of ordered peptide aggregate of an amyloidogenic hexapeptide NFGAIL observed in molecular dynamics simulations with explicit solvent","volume":"127","author":"Wu","year":"2005","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA118.006454_bib53","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1002\/prot.24007","article-title":"Role of amino acid hydrophobicity, aromaticity, and molecular volume on IAPP(20\u201329) amyloid self-assembly","volume":"80","author":"Doran","year":"2012","journal-title":"Proteins"},{"key":"10.1074\/jbc.RA118.006454_bib54","doi-asserted-by":"crossref","first-page":"2016","DOI":"10.2337\/db07-0197","article-title":"High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated beta-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes","volume":"56","author":"Huang","year":"2007","journal-title":"Diabetes"},{"key":"10.1074\/jbc.RA118.006454_bib55","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1021\/ja406831n","article-title":"Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors","volume":"136","author":"Young","year":"2014","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA118.006454_bib56","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":"10.1074\/jbc.RA118.006454_bib57","doi-asserted-by":"crossref","first-page":"6424","DOI":"10.1021\/ja710484d","article-title":"Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide","volume":"130","author":"Brender","year":"2008","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA118.006454_bib58","doi-asserted-by":"crossref","first-page":"12689","DOI":"10.1021\/bi8014357","article-title":"Structures of rat and human islet amyloid polypeptide IAPP(1\u201319) in micelles by NMR spectroscopy","volume":"47","author":"Nanga","year":"2008","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA118.006454_bib59","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.1021\/cb500505m","article-title":"Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity","volume":"9","author":"Mannini","year":"2014","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/jbc.RA118.006454_bib60","doi-asserted-by":"crossref","first-page":"3859","DOI":"10.1021\/ja411577t","article-title":"The role of stable \u03b1-synuclein oligomers in the molecular events underlying amyloid formation","volume":"136","author":"Lorenzen","year":"2014","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA118.006454_bib61","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"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820363353?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820363353?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA118.006454","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T07:54:46Z","timestamp":1641282886000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820363353"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,5]]},"references-count":61,"journal-issue":{"issue":"21","published-print":{"date-parts":[[2019,5]]}},"alternative-id":["S0021925820363353"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra118.006454","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2019,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Identification of a hinge residue controlling islet amyloid polypeptide self-assembly and cytotoxicity","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA118.006454","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Godin et al.","name":"copyright","label":"Copyright"}]}}