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- W2891824314 endingPage "110" @default.
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- W2891824314 abstract "The islet in type 2 diabetes is characterized by beta-cell dysfunction and deficit, increased beta-cell apoptosis and amyloid deposits that derived from islet amyloid polypeptide (IAPP). In species such as humans that are vulnerable to developing type 2 diabetes, IAPP has the propensity to form toxic oligomers that contribute to beta-cell dysfunction and apoptosis, defining type 2 diabetes as a protein misfolding disorder. In this report, we review mechanisms known to contribute to protein misfolding and formation of toxic oligomers, and the deleterious consequences of these oligomers on beta-cell function and survival. Finally, we will consider approaches to prevent protein misfolding and formation of toxic oligomers as potential novel therapeutic targets for type 2 diabetes and other protein misfolding diseases." @default.
- W2891824314 created "2018-09-27" @default.
- W2891824314 creator A5018084483 @default.
- W2891824314 date "2018-12-01" @default.
- W2891824314 modified "2023-10-18" @default.
- W2891824314 title "Targeting protein misfolding to protect pancreatic beta-cells in type 2 diabetes" @default.
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- W2891824314 doi "https://doi.org/10.1016/j.coph.2018.08.016" @default.
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