{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T10:30:47Z","timestamp":1792665047403,"version":"4.5.0"},"reference-count":162,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2015,7,1]],"date-time":"2015-07-01T00:00:00Z","timestamp":1435708800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["clinicalkey.jp","clinicalkey.com","cell.com","clinicalkey.es","clinicalkey.com.au","clinicalkey.fr","bmn.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Trends in Molecular Medicine"],"published-print":{"date-parts":[[2015,7]]},"DOI":"10.1016\/j.molmed.2015.04.005","type":"journal-article","created":{"date-parts":[[2015,5,18]],"date-time":"2015-05-18T09:03:33Z","timestamp":1431939813000},"page":"439-449","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":339,"title":["Type 2 diabetes as a protein misfolding disease"],"prefix":"10.1016","volume":"21","author":[{"given":"Abhisek","family":"Mukherjee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diego","family":"Morales-Scheihing","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter C.","family":"Butler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudio","family":"Soto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.molmed.2015.04.005_bib0800","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nrn1007","article-title":"Unfolding the role of protein misfolding in neurodegenerative diseases","volume":"4","author":"Soto","year":"2003","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.molmed.2015.04.005_bib0805","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1126\/science.282.5391.1075","article-title":"Genetic classification of primary neurodegenerative disease","volume":"282","author":"Hardy","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.molmed.2015.04.005_bib0810","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.2174\/138161212799315768","article-title":"Natural animal models of neurodegenerative protein misfolding diseases","volume":"18","author":"Moreno-Gonzalez","year":"2012","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.molmed.2015.04.005_bib0815","doi-asserted-by":"crossref","first-page":"102","DOI":"10.2337\/diabetes.52.1.102","article-title":"Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes","volume":"52","author":"Butler","year":"2003","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib0820","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1016\/S0140-6736(13)62154-6","article-title":"Pathophysiology and treatment of type 2 diabetes: perspectives on the past, present, and future","volume":"383","author":"Kahn","year":"2014","journal-title":"Lancet"},{"key":"10.1016\/j.molmed.2015.04.005_bib0825","doi-asserted-by":"crossref","first-page":"4154","DOI":"10.1210\/en.2003-0410","article-title":"Saturated fatty acids synergize with elevated glucose to cause pancreatic beta-cell death","volume":"144","author":"El-Assaad","year":"2003","journal-title":"Endocrinology"},{"key":"10.1016\/j.molmed.2015.04.005_bib0830","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1210\/endo.143.2.8623","article-title":"Minireview: secondary beta-cell failure in type 2 diabetes \u2013 a convergence of glucotoxicity and lipotoxicity","volume":"143","author":"Poitout","year":"2002","journal-title":"Endocrinology"},{"key":"10.1016\/j.molmed.2015.04.005_bib0835","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/s11892-009-0090-x","article-title":"Cholesterol in beta-cell dysfunction: the emerging connection between HDL cholesterol and type 2 diabetes","volume":"10","author":"Brunham","year":"2010","journal-title":"Curr. Diab. Rep."},{"key":"10.1016\/j.molmed.2015.04.005_bib0840","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1038\/nri2925","article-title":"Type 2 diabetes as an inflammatory disease","volume":"11","author":"Donath","year":"2011","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.molmed.2015.04.005_bib0845","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1210\/er.2007-0037","article-title":"Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis","volume":"29","author":"Haataja","year":"2008","journal-title":"Endocr. Rev."},{"key":"10.1016\/j.molmed.2015.04.005_bib0850","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.molmed.2015.04.005_bib0855","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.molmed.2015.04.005_bib0860","doi-asserted-by":"crossref","first-page":"7763","DOI":"10.1073\/pnas.85.20.7763","article-title":"Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle","volume":"85","author":"Cooper","year":"1988","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.molmed.2015.04.005_bib0865","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":"10.1016\/j.molmed.2015.04.005_bib0870","first-page":"814","article-title":"[On occurrence of island amyloidosis of the pancreas in diabetes mellitus]","volume":"22","author":"Ludwig","year":"1967","journal-title":"Z. Gesamte Inn. Med."},{"key":"10.1016\/j.molmed.2015.04.005_bib0875","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1517\/03009734000000014","article-title":"Quantitative studies on amyloid in the islets of Langerhans","volume":"77","author":"Westermark","year":"1972","journal-title":"Ups. J. Med. Sci."},{"key":"10.1016\/j.molmed.2015.04.005_bib0880","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/BF01219652","article-title":"The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus","volume":"15","author":"Westermark","year":"1978","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib0885","first-page":"151","article-title":"Islet amyloid, increased A-cells, reduced B-cells and exocrine fibrosis: quantitative changes in the pancreas in type 2 diabetes","volume":"9","author":"Clark","year":"1988","journal-title":"Diabetes Res."},{"key":"10.1016\/j.molmed.2015.04.005_bib0890","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/0014-4827(89)90407-2","article-title":"Islet amyloid polypeptide (IAPP):cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus","volume":"183","author":"Betsholtz","year":"1989","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.molmed.2015.04.005_bib0895","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1056\/NEJM198908243210806","article-title":"Islet amyloid, islet-amyloid polypeptide, and diabetes mellitus","volume":"321","author":"Johnson","year":"1989","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.molmed.2015.04.005_bib0900","doi-asserted-by":"crossref","first-page":"2632","DOI":"10.1016\/j.ajpath.2011.02.036","article-title":"Beta-cell loss and beta-cell apoptosis in human type 2 diabetes are related to islet amyloid deposition","volume":"178","author":"Jurgens","year":"2011","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.molmed.2015.04.005_bib0905","doi-asserted-by":"crossref","first-page":"2837","DOI":"10.1093\/brain\/awm238","article-title":"Beta-amyloid imaging and memory in non-demented individuals: evidence for preclinical Alzheimer's disease","volume":"130","author":"Pike","year":"2007","journal-title":"Brain"},{"key":"10.1016\/j.molmed.2015.04.005_bib0910","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.nicl.2013.02.006","article-title":"Amyloid imaging in cognitively normal individuals, at-risk populations and preclinical Alzheimer's disease","volume":"2","author":"Chetelat","year":"2013","journal-title":"Neuroimage Clin."},{"key":"10.1016\/j.molmed.2015.04.005_bib0915","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1007\/s11892-005-0007-2","article-title":"Is aggregated IAPP a cause of beta-cell failure in transplanted human pancreatic islets?","volume":"5","author":"Westermark","year":"2005","journal-title":"Curr. Diab. Rep."},{"key":"10.1016\/j.molmed.2015.04.005_bib0920","doi-asserted-by":"crossref","first-page":"242","DOI":"10.3109\/13506120108993820","article-title":"Enhanced in vitro production of amyloid-like fibrils from mutant (S20G) islet amyloid polypeptide","volume":"8","author":"Ma","year":"2001","journal-title":"Amyloid"},{"key":"10.1016\/j.molmed.2015.04.005_bib0925","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":"10.1016\/j.molmed.2015.04.005_bib0930","doi-asserted-by":"crossref","first-page":"906","DOI":"10.1007\/s001250100531","article-title":"S20G mutation of the amylin gene is associated with type II diabetes in Japanese. Study Group of Comprehensive Analysis of Genetic Factors in Diabetes Mellitus","volume":"44","author":"Seino","year":"2001","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib0935","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1046\/j.1365-2265.2001.01244.x","article-title":"The islet amyloid polypeptide (amylin) gene S20G mutation in Chinese subjects: evidence for associations with type 2 diabetes and cholesterol levels","volume":"54","author":"Lee","year":"2001","journal-title":"Clin. Endocrinol. (Oxf.)"},{"key":"10.1016\/j.molmed.2015.04.005_bib0940","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1007\/BF00452067","article-title":"Longitudinal studies on the development of diabetes in individual Macaca nigra","volume":"29","author":"Howard","year":"1986","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib0945","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1007\/BF00402271","article-title":"Diabetes mellitus in Macaca mulatta monkeys is characterised by islet amyloidosis and reduction in beta-cell population","volume":"36","author":"de Koning","year":"1993","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib0950","doi-asserted-by":"crossref","first-page":"255","DOI":"10.3109\/13506129809007298","article-title":"Quantitative immunohistochemical analysis of islet amyloid polypeptide (IAPP) in normal, impaired glucose tolerant, and diabetic cats","volume":"5","author":"Ma","year":"1998","journal-title":"Amyloid"},{"key":"10.1016\/j.molmed.2015.04.005_bib0955","doi-asserted-by":"crossref","first-page":"13992","DOI":"10.1073\/pnas.0906471106","article-title":"Pancreatic islet amyloidosis, beta-cell apoptosis, and alpha-cell proliferation are determinants of islet remodeling in type-2 diabetic baboons","volume":"106","author":"Guardado-Mendoza","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.molmed.2015.04.005_bib0960","doi-asserted-by":"crossref","first-page":"7283","DOI":"10.1073\/pnas.93.14.7283","article-title":"Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide","volume":"93","author":"Janson","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.molmed.2015.04.005_bib0965","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.molmed.2015.04.005_bib0970","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1038\/nature13910","article-title":"IAPP-driven metabolic reprogramming induces regression of p53-deficient tumours in vivo","volume":"517","author":"Venkatanarayan","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.molmed.2015.04.005_bib0975","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.tibs.2006.01.002","article-title":"Amyloids, prions and the inherent infectious nature of misfolded protein aggregates","volume":"31","author":"Soto","year":"2006","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.molmed.2015.04.005_bib0980","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/0092-8674(93)90635-4","article-title":"Seeding \u201cone-dimensional crystallization\u201d of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?","volume":"73","author":"Jarrett","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.molmed.2015.04.005_bib0985","first-page":"609","article-title":"Human islet amyloid polypeptide expression in COS-1 cells. A model of intracellular amyloidogenesis","volume":"147","author":"O\u2019Brien","year":"1995","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.molmed.2015.04.005_bib0990","doi-asserted-by":"crossref","first-page":"861","DOI":"10.2353\/ajpath.2010.090532","article-title":"Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway","volume":"176","author":"Gurlo","year":"2010","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.molmed.2015.04.005_bib0995","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":"10.1016\/j.molmed.2015.04.005_bib1000","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1093\/ilar.47.3.186","article-title":"Animal models of type 2 diabetes: clinical presentation and pathophysiological relevance to the human condition","volume":"47","author":"Cefalu","year":"2006","journal-title":"ILAR J."},{"key":"10.1016\/j.molmed.2015.04.005_bib1005","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1093\/ilar.47.3.234","article-title":"Feline models of type 2 diabetes mellitus","volume":"47","author":"Henson","year":"2006","journal-title":"ILAR J."},{"key":"10.1016\/j.molmed.2015.04.005_bib1010","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1007\/0-387-23226-5_18","article-title":"Amyloid inhibitors and beta-sheet breakers","volume":"38","author":"Soto","year":"2005","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1015","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/0014-5793(89)81467-X","article-title":"Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species","volume":"251","author":"Betsholtz","year":"1989","journal-title":"FEBS Lett."},{"key":"10.1016\/j.molmed.2015.04.005_bib1020","first-page":"245","article-title":"The use of animal models in the study of diabetes mellitus","volume":"23","author":"Chatzigeorgiou","year":"2009","journal-title":"In Vivo"},{"key":"10.1016\/j.molmed.2015.04.005_bib1025","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1093\/ilar.47.3.225","article-title":"Islet amyloid polypeptide (IAPP) transgenic rodents as models for type 2 diabetes","volume":"47","author":"Matveyenko","year":"2006","journal-title":"ILAR J."},{"key":"10.1016\/j.molmed.2015.04.005_bib1030","doi-asserted-by":"crossref","first-page":"5083","DOI":"10.1096\/fj.14-251744","article-title":"The pathogenic mechanism of diabetes varies with the degree of overexpression and oligomerization of human amylin in the pancreatic islet beta cells","volume":"28","author":"Zhang","year":"2014","journal-title":"FASEB J."},{"key":"10.1016\/j.molmed.2015.04.005_bib1035","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1111\/j.1471-4159.2006.04426.x","article-title":"A beta oligomers \u2013 a decade of discovery","volume":"101","author":"Walsh","year":"2007","journal-title":"J. Neurochem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1040","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1016\/j.neurobiolaging.2005.04.017","article-title":"Common mechanisms of amyloid oligomer pathogenesis in degenerative disease","volume":"27","author":"Glabe","year":"2006","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.molmed.2015.04.005_bib1045","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","article-title":"Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders","volume":"26","author":"Caughey","year":"2003","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.molmed.2015.04.005_bib1050","doi-asserted-by":"crossref","first-page":"1046","DOI":"10.1007\/s00125-010-1671-6","article-title":"Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence?","volume":"53","author":"Zraika","year":"2010","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib1055","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1001\/archneurol.2007.56","article-title":"Protein misfolding and neurodegeneration","volume":"65","author":"Soto","year":"2008","journal-title":"Arch. Neurol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1060","doi-asserted-by":"crossref","first-page":"e17","DOI":"10.1371\/journal.pbio.0060017","article-title":"Amyloid as a depot for the formulation of long-acting drugs","volume":"6","author":"Maji","year":"2008","journal-title":"PLoS Biol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1065","doi-asserted-by":"crossref","first-page":"11665","DOI":"10.1074\/jbc.M111.282533","article-title":"Microcin amyloid fibrils are a reservoir of toxic oligomeric species","volume":"287","author":"Shahnawaz","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1070","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1126\/science.1213151","article-title":"Atomic view of a toxic amyloid small oligomer","volume":"335","author":"Laganowsky","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.molmed.2015.04.005_bib1075","doi-asserted-by":"crossref","first-page":"141","DOI":"10.2337\/diabetes.53.1.141","article-title":"Role of beta-cell prohormone convertase (PC)1\/3 in processing of pro-islet amyloid polypeptide","volume":"53","author":"Marzban","year":"2004","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1080","doi-asserted-by":"crossref","first-page":"1808","DOI":"10.1210\/en.2004-1175","article-title":"Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in \u03b2-cells","volume":"146","author":"Marzban","year":"2005","journal-title":"Endocrinology"},{"key":"10.1016\/j.molmed.2015.04.005_bib1085","doi-asserted-by":"crossref","first-page":"534","DOI":"10.2337\/diabetes.50.3.534","article-title":"The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site","volume":"50","author":"Wang","year":"2001","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1090","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.molmed.2015.04.005_bib1095","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.molmed.2015.04.005_bib1100","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1006\/bbrc.1997.7014","article-title":"B cell granule peptides affect human islet amyloid polypeptide (IAPP) fibril formation in vitro","volume":"236","author":"Janciauskiene","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.molmed.2015.04.005_bib1105","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1042\/bj3310809","article-title":"A novel assay in vitro of human islet amyloid polypeptide amyloidogenesis and effects of insulin secretory vesicle peptides on amyloid formation","volume":"331","author":"Kudva","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.molmed.2015.04.005_bib1110","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1055\/s-2007-1003759","article-title":"Glucose stimulates and potentiates islet amyloid polypeptide secretion by the B-cell","volume":"23","author":"Kahn","year":"1991","journal-title":"Horm. Metab. Res."},{"key":"10.1016\/j.molmed.2015.04.005_bib1115","first-page":"E1008","article-title":"Islet amyloid polypeptide and insulin gene expression are regulated in parallel by glucose in vivo in rats","volume":"271","author":"Mulder","year":"1996","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1120","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.2337\/diab.45.8.1094","article-title":"Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and beta-cell dysfunction","volume":"45","author":"Couce","year":"1996","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1125","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1016\/0006-291X(91)92094-Z","article-title":"Identification of the metal associated with the insulin degrading enzyme","volume":"181","author":"Ebrahim","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.molmed.2015.04.005_bib1130","doi-asserted-by":"crossref","first-page":"36621","DOI":"10.1074\/jbc.M006170200","article-title":"Degradation of amylin by insulin-degrading enzyme","volume":"275","author":"Bennett","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1135","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1038\/nature05616","article-title":"A genome-wide association study identifies novel risk loci for type 2 diabetes","volume":"445","author":"Sladek","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.molmed.2015.04.005_bib1140","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1126\/science.1142364","article-title":"Replication of genome-wide association signals in UK samples reveals risk loci for type 2 diabetes","volume":"316","author":"Zeggini","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.molmed.2015.04.005_bib1145","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.2337\/diabetes.52.9.2315","article-title":"An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures","volume":"52","author":"Bennett","year":"2003","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1150","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/nature13297","article-title":"Anti-diabetic activity of insulin-degrading enzyme inhibitors mediated by multiple hormones","volume":"511","author":"Maianti","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.molmed.2015.04.005_bib1155","doi-asserted-by":"crossref","first-page":"304","DOI":"10.2337\/db06-0430","article-title":"Identification of the amyloid-degrading enzyme neprilysin in mouse islets and potential role in islet amyloidogenesis","volume":"56","author":"Zraika","year":"2007","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1160","doi-asserted-by":"crossref","first-page":"2989","DOI":"10.1007\/s00125-012-2678-y","article-title":"Degradation of islet amyloid polypeptide by neprilysin","volume":"55","author":"Guan","year":"2012","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib1165","doi-asserted-by":"crossref","first-page":"18177","DOI":"10.1074\/jbc.M109.082032","article-title":"Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation","volume":"285","author":"Zraika","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1170","doi-asserted-by":"crossref","first-page":"19702","DOI":"10.1074\/jbc.270.34.19702","article-title":"Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro","volume":"270","author":"Gregori","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1175","doi-asserted-by":"crossref","first-page":"12924","DOI":"10.1074\/jbc.M306390200","article-title":"Proteasomal inhibition by alpha-synuclein filaments and oligomers","volume":"279","author":"Lindersson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1180","doi-asserted-by":"crossref","first-page":"11753","DOI":"10.1074\/jbc.M208641200","article-title":"Aggregated and monomeric alpha-synuclein bind to the S6\u2032 proteasomal protein and inhibit proteasomal function","volume":"278","author":"Snyder","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1185","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.molcel.2007.04.001","article-title":"Disease-associated prion protein oligomers inhibit the 26S proteasome","volume":"26","author":"Kristiansen","year":"2007","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molmed.2015.04.005_bib1190","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1146\/annurev.pharmtox.051208.165340","article-title":"Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology","volume":"49","author":"Schwartz","year":"2009","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1195","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.2337\/db05-0450","article-title":"Evidence for a role of the ubiquitin\u2013proteasome pathway in pancreatic islets","volume":"55","author":"Lopez-Avalos","year":"2006","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1200","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1126\/science.1087753","article-title":"Molecular pathways of neurodegeneration in Parkinson's disease","volume":"302","author":"Dawson","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.molmed.2015.04.005_bib1205","doi-asserted-by":"crossref","first-page":"13256","DOI":"10.1074\/jbc.M314124200","article-title":"Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases","volume":"279","author":"Choi","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1210","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/j.cell.2006.06.046","article-title":"Ubiquitin hydrolase Uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory","volume":"126","author":"Gong","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.molmed.2015.04.005_bib1215","doi-asserted-by":"crossref","first-page":"227","DOI":"10.2337\/db10-0522","article-title":"Beta-cell dysfunctional ERAD\/ubiquitin\/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency","volume":"60","author":"Costes","year":"2011","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1220","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1007\/s00125-011-2323-1","article-title":"Ubiquitin C-terminal hydrolase L1 is required for pancreatic beta cell survival and function in lipotoxic conditions","volume":"55","author":"Chu","year":"2012","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib1225","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.4161\/auto.28478","article-title":"UCHL1 deficiency exacerbates human islet amyloid polypeptide toxicity in beta-cells: evidence of interplay between the ubiquitin\/proteasome system and autophagy","volume":"10","author":"Costes","year":"2014","journal-title":"Autophagy"},{"key":"10.1016\/j.molmed.2015.04.005_bib1230","doi-asserted-by":"crossref","first-page":"1785","DOI":"10.1126\/science.1073619","article-title":"Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol","volume":"298","author":"Ma","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.molmed.2015.04.005_bib1235","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/S0896-6273(03)00606-8","article-title":"The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg","volume":"40","author":"Ciechanover","year":"2003","journal-title":"Neuron"},{"key":"10.1016\/j.molmed.2015.04.005_bib1240","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1056\/NEJMra1205406","article-title":"Autophagy in human health and disease","volume":"368","author":"Choi","year":"2013","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.molmed.2015.04.005_bib1245","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1152\/physrev.00030.2009","article-title":"Regulation of mammalian autophagy in physiology and pathophysiology","volume":"90","author":"Ravikumar","year":"2010","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.molmed.2015.04.005_bib1250","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1093\/hmg\/ddi458","article-title":"Rapamycin alleviates toxicity of different aggregate-prone proteins","volume":"15","author":"Berger","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.molmed.2015.04.005_bib1255","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1007\/s00125-009-1347-2","article-title":"Autophagy in human type 2 diabetes pancreatic beta cells","volume":"52","author":"Masini","year":"2009","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib1260","doi-asserted-by":"crossref","first-page":"3489","DOI":"10.1172\/JCI71981","article-title":"Autophagy defends pancreatic beta cells from human islet amyloid polypeptide-induced toxicity","volume":"124","author":"Rivera","year":"2014","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.molmed.2015.04.005_bib1265","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1111\/j.2040-1124.2010.00065.x","article-title":"Autophagy protects against human islet amyloid polypeptide-associated apoptosis","volume":"2","author":"Morita","year":"2011","journal-title":"J. Diabetes Investig."},{"key":"10.1016\/j.molmed.2015.04.005_bib1270","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.1172\/JCI69625","article-title":"Amyloidogenic peptide oligomer accumulation in autophagy-deficient beta cells induces diabetes","volume":"124","author":"Kim","year":"2014","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.molmed.2015.04.005_bib1275","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.cmet.2008.08.013","article-title":"Loss of autophagy diminishes pancreatic beta cell mass and function with resultant hyperglycemia","volume":"8","author":"Jung","year":"2008","journal-title":"Cell Metab."},{"key":"10.1016\/j.molmed.2015.04.005_bib1280","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/S0962-8924(00)01852-3","article-title":"Aggresomes, inclusion bodies and protein aggregation","volume":"10","author":"Kopito","year":"2000","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1285","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.molcel.2009.04.026","article-title":"A role for ubiquitin in selective autophagy","volume":"34","author":"Kirkin","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molmed.2015.04.005_bib1290","doi-asserted-by":"crossref","first-page":"2570","DOI":"10.1093\/hmg\/ddn157","article-title":"Autophagy-mediated clearance of aggresomes is not a universal phenomenon","volume":"17","author":"Wong","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.molmed.2015.04.005_bib1295","doi-asserted-by":"crossref","first-page":"e48243","DOI":"10.1371\/journal.pone.0048243","article-title":"An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregation","volume":"7","author":"Kirilyuk","year":"2012","journal-title":"PLoS ONE"},{"key":"10.1016\/j.molmed.2015.04.005_bib1300","doi-asserted-by":"crossref","first-page":"1883","DOI":"10.1083\/jcb.143.7.1883","article-title":"Aggresomes: a cellular response to misfolded proteins","volume":"143","author":"Johnston","year":"1998","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1305","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/cdd.2010.111","article-title":"Human-IAPP disrupts the autophagy\/lysosomal pathway in pancreatic beta-cells: protective role of p62-positive cytoplasmic inclusions","volume":"18","author":"Rivera","year":"2010","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.molmed.2015.04.005_bib1310","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1083\/jcb.200507002","article-title":"p62\/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death","volume":"171","author":"Bjorkoy","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1315","doi-asserted-by":"crossref","first-page":"e52868","DOI":"10.1371\/journal.pone.0052868","article-title":"p62\/SQSTM1-dependent autophagy of Lewy body-like alpha-synuclein inclusions","volume":"7","author":"Watanabe","year":"2012","journal-title":"PLoS ONE"},{"key":"10.1016\/j.molmed.2015.04.005_bib1320","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1074\/jbc.M109.024190","article-title":"Calcium-activated calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes","volume":"285","author":"Huang","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1325","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.molmed.2015.04.005_bib1330","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.molmed.2015.04.005_bib1335","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3109\/13506120009146834","article-title":"Amyloid peptide channels: blockade by zinc and inhibition by Congo red (amyloid channel block)","volume":"7","author":"Hirakura","year":"2000","journal-title":"Amyloid"},{"key":"10.1016\/j.molmed.2015.04.005_bib1340","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. U.S.A."},{"key":"10.1016\/j.molmed.2015.04.005_bib1345","doi-asserted-by":"crossref","first-page":"6033","DOI":"10.1073\/pnas.0708354105","article-title":"Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane","volume":"105","author":"Engel","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.molmed.2015.04.005_bib1350","doi-asserted-by":"crossref","first-page":"9228","DOI":"10.1021\/bi0510936","article-title":"Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation","volume":"45","author":"Abedini","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.molmed.2015.04.005_bib1355","doi-asserted-by":"crossref","first-page":"22894","DOI":"10.1074\/jbc.M110.215814","article-title":"Mechanism of amylin fibrillization enhancement by heparin","volume":"286","author":"Jha","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1360","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.molmed.2015.04.005_bib1365","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.mce.2008.05.015","article-title":"Mitochondrial dysfunction in pancreatic beta-cells in type 2 diabetes","volume":"297","author":"Mulder","year":"2009","journal-title":"Mol. Cell. Endocrinol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1370","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/nature05292","article-title":"Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases","volume":"443","author":"Lin","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.molmed.2015.04.005_bib1375","doi-asserted-by":"crossref","first-page":"2532","DOI":"10.1016\/j.bbamem.2013.06.026","article-title":"Mitochondrial membrane permeabilisation by amyloid aggregates and protection by polyphenols","volume":"1828","author":"Camilleri","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.molmed.2015.04.005_bib1380","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.biocel.2010.12.008","article-title":"Involvement of mitochondrial dysfunction in human islet amyloid polypeptide-induced apoptosis in INS-1E pancreatic beta cells: an effect attenuated by phycocyanin","volume":"43","author":"Li","year":"2011","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1385","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1016\/j.biocel.2009.01.002","article-title":"Phycocyanin protects INS-1E pancreatic beta cells against human islet amyloid polypeptide-induced apoptosis through attenuating oxidative stress and modulating JNK and p38 mitogen-activated protein kinase pathways","volume":"41","author":"Li","year":"2009","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1390","doi-asserted-by":"crossref","first-page":"4949","DOI":"10.1111\/j.1742-4658.2005.04903.x","article-title":"Thiol reducing compounds prevent human amylin-evoked cytotoxicity","volume":"272","author":"Konarkowska","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.molmed.2015.04.005_bib1395","doi-asserted-by":"crossref","first-page":"327","DOI":"10.2337\/db12-1326","article-title":"\u03b2-Cell failure in type 2 diabetes: a case of asking too much of too few?","volume":"62","author":"Costes","year":"2013","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1400","doi-asserted-by":"crossref","first-page":"2486","DOI":"10.1007\/s00125-007-0816-8","article-title":"The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients","volume":"50","author":"Marchetti","year":"2007","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib1405","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":"10.1016\/j.molmed.2015.04.005_bib1410","first-page":"1402","article-title":"[Tabes or diabetic neuropathy]","volume":"120","author":"Geissl","year":"1978","journal-title":"MMW Munch. Med. Wochenschr."},{"key":"10.1016\/j.molmed.2015.04.005_bib1415","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1038\/nrn3689","article-title":"Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases","volume":"15","author":"Hetz","year":"2014","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.molmed.2015.04.005_bib1420","first-page":"2438","article-title":"Common variants in PERK, JNK, BIP and XBP1 genes are associated with the risk of prediabetes or diabetes-related phenotypes in a Chinese population","volume":"127","author":"Feng","year":"2014","journal-title":"Chin. Med. J. (Engl.)"},{"key":"10.1016\/j.molmed.2015.04.005_bib1425","doi-asserted-by":"crossref","first-page":"8885","DOI":"10.1073\/pnas.1105564108","article-title":"Dual and opposing roles of the unfolded protein response regulated by IRE1\u03b1 and XBP1 in proinsulin processing and insulin secretion","volume":"108","author":"Lee","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.molmed.2015.04.005_bib1430","doi-asserted-by":"crossref","first-page":"247","DOI":"10.3109\/13506129809007297","article-title":"Macrophages and pancreatic islet amyloidosis","volume":"5","author":"de Koning","year":"1998","journal-title":"Amyloid"},{"key":"10.1016\/j.molmed.2015.04.005_bib1435","doi-asserted-by":"crossref","first-page":"2755","DOI":"10.4049\/jimmunol.1002854","article-title":"IL-1 blockade attenuates islet amyloid polypeptide-induced proinflammatory cytokine release and pancreatic islet graft dysfunction","volume":"187","author":"Westwell-Roper","year":"2011","journal-title":"J. Immunol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1440","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1159\/000026432","article-title":"Human amylin stimulates inflammatory cytokine secretion from human glioma cells","volume":"7","author":"Gitter","year":"2000","journal-title":"Neuroimmunomodulation"},{"key":"10.1016\/j.molmed.2015.04.005_bib1445","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1046\/j.1471-4159.2000.0741017.x","article-title":"Amyloid beta and amylin fibrils induce increases in proinflammatory cytokine and chemokine production by THP-1 cells and murine microglia","volume":"74","author":"Yates","year":"2000","journal-title":"J. Neurochem."},{"key":"10.1016\/j.molmed.2015.04.005_bib1450","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.2337\/db13-0863","article-title":"Resident macrophages mediate islet amyloid polypeptide-induced islet IL-1\u03b2 production and \u03b2-cell dysfunction","volume":"63","author":"Westwell-Roper","year":"2014","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1455","doi-asserted-by":"crossref","first-page":"812","DOI":"10.2337\/diabetes.52.3.812","article-title":"Inflammatory cytokines and the risk to develop type 2 diabetes: results of the prospective population-based European Prospective Investigation into Cancer and Nutrition (EPIC)-Potsdam Study","volume":"52","author":"Spranger","year":"2003","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1460","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1038\/ni.1935","article-title":"Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1\u03b2 in type 2 diabetes","volume":"11","author":"Masters","year":"2010","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1465","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1007\/s00125-014-3447-x","article-title":"IL-1 mediates amyloid-associated islet dysfunction and inflammation in human islet amyloid polypeptide transgenic mice","volume":"58","author":"Westwell-Roper","year":"2015","journal-title":"Diabetologia"},{"key":"10.1016\/j.molmed.2015.04.005_bib1470","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.molmed.2011.01.005","article-title":"Disease-associated amyloid and misfolded protein aggregates activate the inflammasome","volume":"17","author":"Masters","year":"2011","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.molmed.2015.04.005_bib1475","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1038\/sj.ki.5002305","article-title":"Amylin deposition in the kidney of patients with diabetic nephropathy","volume":"72","author":"Gong","year":"2007","journal-title":"Kidney Int."},{"key":"10.1016\/j.molmed.2015.04.005_bib1480","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1002\/ana.23956","article-title":"Amylin deposition in the brain: a second amyloid in Alzheimer disease?","volume":"74","author":"Jackson","year":"2013","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1485","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1161\/CIRCRESAHA.111.258285","article-title":"Hyperamylinemia contributes to cardiac dysfunction in obesity and diabetes: a study in humans and rats","volume":"110","author":"Despa","year":"2012","journal-title":"Circ. Res."},{"key":"10.1016\/j.molmed.2015.04.005_bib1490","doi-asserted-by":"crossref","first-page":"638083","DOI":"10.1155\/2013\/638083","article-title":"Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging","volume":"2013","author":"Cuanalo-Contreras","year":"2013","journal-title":"Int. J. Cell Biol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1495","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"Prusiner","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.molmed.2015.04.005_bib1500","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1016\/j.cell.2012.05.007","article-title":"Transmissible proteins: expanding the prion heresy","volume":"149","author":"Soto","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.molmed.2015.04.005_bib1505","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/nature12481","article-title":"Self-propagation of pathogenic protein aggregates in neurodegenerative diseases","volume":"501","author":"Jucker","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.molmed.2015.04.005_bib1510","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1126\/science.1222951","article-title":"Cell biology. A unifying role for prions in neurodegenerative diseases","volume":"336","author":"Prusiner","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.molmed.2015.04.005_bib1515","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.semcdb.2011.04.002","article-title":"Misfolded protein aggregates: mechanisms, structures and potential for disease transmission","volume":"22","author":"Moreno-Gonzalez","year":"2011","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1520","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.molmed.2015.04.005_bib1525","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1016\/S0896-6273(03)00787-6","article-title":"Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death","volume":"40","author":"Leissring","year":"2003","journal-title":"Neuron"},{"key":"10.1016\/j.molmed.2015.04.005_bib1530","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1126\/science.290.5500.2302","article-title":"Evidence for genetic linkage of Alzheimer's disease to chromosome 10q","volume":"290","author":"Bertram","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.molmed.2015.04.005_bib1535","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/j.nbd.2006.08.003","article-title":"Neuronal neprilysin overexpression is associated with attenuation of Abeta-related spatial memory deficit","volume":"24","author":"Poirier","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.molmed.2015.04.005_bib1540","doi-asserted-by":"crossref","first-page":"933","DOI":"10.3233\/JAD-2010-101197","article-title":"Neprilysin activity in cerebrospinal fluid is associated with dementia and amyloid-\u03b242 levels in Lewy body disease","volume":"22","author":"Maetzler","year":"2010","journal-title":"J. Alzheimers. Dis."},{"key":"10.1016\/j.molmed.2015.04.005_bib1595","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1038\/nature04723","article-title":"Loss of autophagy in the central nervous system causes neurodegeneration in mice","volume":"441","author":"Komatsu","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.molmed.2015.04.005_bib1545","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1038\/nature11729","article-title":"NLRP3 is activated in Alzheimer's disease and contributes to pathology in APP\/PS1 mice","volume":"493","author":"Heneka","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.molmed.2015.04.005_bib1550","doi-asserted-by":"crossref","first-page":"13046","DOI":"10.1073\/pnas.1002396107","article-title":"Mutant superoxide dismutase 1-induced IL-1\u03b2 accelerates ALS pathogenesis","volume":"107","author":"Meissner","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.molmed.2015.04.005_bib1600","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1126\/science.288.5464.335","article-title":"Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model","volume":"288","author":"Li","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.molmed.2015.04.005_bib1605","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1097\/MED.0b013e32833bf6dc","article-title":"Role of IL-1beta in type 2 diabetes","volume":"17","author":"Dinarello","year":"2010","journal-title":"Curr. Opin. Endocrinol. Diabetes Obes."},{"key":"10.1016\/j.molmed.2015.04.005_bib1555","doi-asserted-by":"crossref","first-page":"e1003537","DOI":"10.1371\/journal.ppat.1003537","article-title":"Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases","volume":"9","author":"Morales","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.molmed.2015.04.005_bib1560","doi-asserted-by":"crossref","first-page":"474","DOI":"10.2337\/diabetes.53.2.474","article-title":"Increased risk of type 2 diabetes in Alzheimer disease","volume":"53","author":"Janson","year":"2004","journal-title":"Diabetes"},{"key":"10.1016\/j.molmed.2015.04.005_bib1565","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/S1474-4422(05)70284-2","article-title":"Risk of dementia in diabetes mellitus: a systematic review","volume":"5","author":"Biessels","year":"2006","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1570","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/j.bbadis.2014.01.002","article-title":"Exogenous amyloidogenic proteins function as seeds in amyloid beta-protein aggregation","volume":"1842","author":"Ono","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.molmed.2015.04.005_bib1575","doi-asserted-by":"crossref","first-page":"928","DOI":"10.2174\/1567205011666141107124538","article-title":"Islet amyloid polypeptide (IAPP): a second amyloid in Alzheimer's disease","volume":"11","author":"Fawver","year":"2014","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.molmed.2015.04.005_bib1580","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1016\/j.neurobiolaging.2008.08.019","article-title":"Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes","volume":"31","author":"Miklossy","year":"2010","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.molmed.2015.04.005_bib1585","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1016\/j.ajpath.2014.11.016","article-title":"In vivo seeding and cross-seeding of localized amyloidosis: a molecular link between type 2 diabetes and Alzheimer disease","volume":"185","author":"Oskarsson","year":"2015","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.molmed.2015.04.005_bib1590","doi-asserted-by":"crossref","first-page":"2004","DOI":"10.2337\/db12-1045","article-title":"The type 2 diabetes-associated gene ide is required for insulin secretion and suppression of alpha-synuclein levels in beta-cells","volume":"62","author":"Steneberg","year":"2013","journal-title":"Diabetes"}],"container-title":["Trends in Molecular Medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1471491415000878?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1471491415000878?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,5,8]],"date-time":"2022-05-08T07:15:44Z","timestamp":1651994144000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1471491415000878"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,7]]},"references-count":162,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2015,7]]}},"alternative-id":["S1471491415000878"],"URL":"https:\/\/doi.org\/10.1016\/j.molmed.2015.04.005","relation":{},"ISSN":["1471-4914"],"issn-type":[{"value":"1471-4914","type":"print"}],"subject":[],"published":{"date-parts":[[2015,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Type 2 diabetes as a protein misfolding disease","name":"articletitle","label":"Article Title"},{"value":"Trends in Molecular Medicine","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.molmed.2015.04.005","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}