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- W4200565811 endingPage "109113" @default.
- W4200565811 startingPage "109113" @default.
- W4200565811 abstract "All proteins have the inherent ability to undergo transformation from their native structure to a β sheet rich fibrillar structure, called amyloid when subjected to specific conditions. Proteins with a high propensity to form amyloid fibrils have been implicated in a variety of disorders like Alzheimer's disease, Parkinson's disease, Type II diabetes, Amyotrophic Lateral Sclerosis (ALS) and prion diseases. Among the various critical factors that modulate the process of amyloid formation, disulfide bonds have been identified as one of the key determinants of amyloid propensity in proteins. Studies have shown that intra-molecular disulfide bonds impart stability to the native structure of a protein and decrease the tendency for amyloid aggregation, whereas intermolecular disulfide bonds aid in the process of aggregation. In this review, we will analyze the varying effects of both intra as well as inter-molecular disulfide bonds on the amyloid aggregation propensities of a few proteins associated with amyloid disorders." @default.
- W4200565811 created "2021-12-31" @default.
- W4200565811 creator A5026831865 @default.
- W4200565811 creator A5090298866 @default.
- W4200565811 date "2022-02-01" @default.
- W4200565811 modified "2023-10-05" @default.
- W4200565811 title "The role of intra and inter-molecular disulfide bonds in modulating amyloidogenesis: A review" @default.
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