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- W1874817816 endingPage "213" @default.
- W1874817816 startingPage "200" @default.
- W1874817816 abstract "Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as well as other lysosome-dependent systems, function in the degradation of dysfunctional proteins. In this review, we examine how these systems interact to maintain proteostasis. Both the direct cellular data on heat shock control over autophagy and the time course of exercise-associated changes in humans support the model that heat shock response and autophagy are tightly linked. Studying the links between exercise stress and molecular control of proteostasis provides evidence that the heat shock response and autophagy coordinate and undergo sequential activation and downregulation, and that this is essential for proper proteostasis in eukaryotic systems." @default.
- W1874817816 created "2016-06-24" @default.
- W1874817816 creator A5045457303 @default.
- W1874817816 creator A5046088659 @default.
- W1874817816 creator A5053705167 @default.
- W1874817816 date "2015-02-01" @default.
- W1874817816 modified "2023-10-14" @default.
- W1874817816 title "Heat shock response and autophagy—cooperation and control" @default.
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