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- W1977353914 endingPage "127" @default.
- W1977353914 startingPage "116" @default.
- W1977353914 abstract "Amyloid fibrils arise from the aggregation of misfolded proteins into highly-ordered structures. The accumulation of these fibrils along with some non-fibrillar constituents within amyloid plaques is associated with the pathogenesis of several human degenerative diseases. A number of plasma apolipoproteins, including apolipoprotein (apo) A-I, apoA-II, apoC-II and apoE are implicated in amyloid formation or influence amyloid formation by other proteins. We review present knowledge of amyloid formation by apolipoproteins in disease, with particular focus on atherosclerosis. Further insights into the molecular mechanisms underlying their amyloidogenic propensity are obtained from in vitro studies which describe factors affecting apolipoprotein amyloid fibril formation and interactions. Additionally, we outline the evidence that amyloid fibril formation by apolipoproteins might play a role in the development and progression of atherosclerosis, and highlight possible molecular mechanisms that could contribute to the pathogenesis of this disease." @default.
- W1977353914 created "2016-06-24" @default.
- W1977353914 creator A5022335510 @default.
- W1977353914 creator A5027963116 @default.
- W1977353914 creator A5085160372 @default.
- W1977353914 date "2011-02-01" @default.
- W1977353914 modified "2023-10-18" @default.
- W1977353914 title "Apolipoproteins and amyloid fibril formation in atherosclerosis" @default.
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