Matches in SemOpenAlex for { <https://semopenalex.org/work/W2024079970> ?p ?o ?g. }
- W2024079970 endingPage "451" @default.
- W2024079970 startingPage "429" @default.
- W2024079970 abstract "Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of post-translational modifications in sHsp chaperone function, particularly in the context of disease." @default.
- W2024079970 created "2016-06-24" @default.
- W2024079970 creator A5026525980 @default.
- W2024079970 creator A5046433490 @default.
- W2024079970 creator A5058121216 @default.
- W2024079970 creator A5083304343 @default.
- W2024079970 date "2014-10-29" @default.
- W2024079970 modified "2023-10-10" @default.
- W2024079970 title "Small heat-shock proteins: important players in regulating cellular proteostasis" @default.
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