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- W4387007347 abstract "The protein αB-crystallin represents the archetypical small heat-shock protein (sHSP), and together with αA-crystallin makes up the primary chaperone system in the eye lens, where they play a critical role in maintaining proteostasis. To achieve transparency, the lens undergoes a loss of organelles and both protein turnover halts, requiring that proteins remain functional for long periods of time as they accumulate chemical damage. The α-crystallins are highly abundant in the lens to stabilize proteostasis for multiple decades. Over time though, the small heat-shock proteins become overwhelmed by a high burden of destabilized clients and their own accumulated chemical damage. Mechanistic insights into the function and failure of the α-crystallins remain poorly understood though, largely driven by the high degree of polydispersity exhibited by this family of proteins." @default.
- W4387007347 created "2023-09-26" @default.
- W4387007347 creator A5064779947 @default.
- W4387007347 date "2023-09-25" @default.
- W4387007347 modified "2023-09-27" @default.
- W4387007347 title "Mechanisms of Fibrillar Aggregation of the Lens Small Heat Shock Proteins" @default.
- W4387007347 doi "https://doi.org/10.15760/etd.3650" @default.
- W4387007347 hasPublicationYear "2023" @default.
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