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- W4311611414 abstract "Molecular chaperones and their associated co-chaperones are essential in health and disease as they are key facilitators of protein-folding, quality control and function. In particular, the heat-shock protein (HSP) 70 and HSP90 molecular chaperone networks have been associated with neurodegenerative diseases caused by aberrant protein-folding. The pathogenesis of these disorders usually includes the formation of deposits of misfolded, aggregated protein. HSP70 and HSP90, plus their co-chaperones, have been recognised as potent modulators of misfolded protein toxicity, inclusion formation and cell survival in cellular and animal models of neurodegenerative disease. Moreover, these chaperone machines function not only in folding but also in proteasome-mediated degradation of neurodegenerative disease proteins. This chapter gives an overview of the HSP70 and HSP90 chaperones, and their respective regulatory co-chaperones, and explores how the HSP70 and HSP90 chaperone systems form a larger functional network and its relevance to counteracting neurodegenerative disease associated with misfolded proteins and disruption of proteostasis.KeywordsHSP70HSP90ChaperoneCo-chaperonesProtein degradationProtein quality controlNeurodegeneration" @default.
- W4311611414 created "2022-12-27" @default.
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- W4311611414 creator A5033165235 @default.
- W4311611414 creator A5065343122 @default.
- W4311611414 creator A5078167774 @default.
- W4311611414 date "2022-12-16" @default.
- W4311611414 modified "2023-10-13" @default.
- W4311611414 title "HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease" @default.
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