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The quick aggregation of hIAPP leads to the formation of toxic species, such as oligomers and fibers, that damage mammalian cells (both human and rat pancreatic cells). Whether this toxicity is necessary for the progression of type 2 diabetes or merely a side effect of the disease remains unclear. If hIAPP aggregation into toxic amyloid is on\u2010path for developing type 2 diabetes in humans, islet amyloid polypeptide (IAPP) aggregation would likely need to play a similar role within other organisms known to develop the disease. In this work, we compared the aggregation potential and cellular toxicity of full\u2010length IAPP from several diabetic and nondiabetic organisms whose aggregation propensities had not yet been determined for full\u2010length IAPP.<\/jats:p>","DOI":"10.1002\/psc.3199","type":"journal-article","created":{"date-parts":[[2019,6,24]],"date-time":"2019-06-24T01:29:23Z","timestamp":1561339763000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Amyloidogenicity of naturally occurring full\u2010length animal IAPP variants"],"prefix":"10.1002","volume":"25","author":[{"given":"Larry M.","family":"Palato","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry Loyola Marymount University  Los Angeles CA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shannon","family":"Pilcher","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry Loyola 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