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- W1567631042 abstract "Thermotolerance, the acquired resistance of cells to stress, is a well-established phenomenon. Studies of the key mediators of this response, the heat shock proteins (HSPs), have led to the discovery of the important roles played by these proteins in the regulation of apoptotic cell death. Apoptosis is critical for normal tissue homeostasis and is involved in diverse processes including development and immune clearance. Apoptosis is tightly regulated by both proapoptotic and antiapoptotic factors, and dysregulation of apoptosis plays a significant role in the pathophysiology of many diseases. In the recent years, HSPs have been identified as key determinants of cell survival, which can modulate apoptosis by directly interacting with components of the apoptotic machinery. Therefore, manipulation of the HSPs could represent a viable strategy for the treatment of diseases. Here, we review the current knowledge with regard to the mechanisms of HSP-mediated regulation of apoptosis." @default.
- W1567631042 created "2016-06-24" @default.
- W1567631042 creator A5020342144 @default.
- W1567631042 creator A5024400628 @default.
- W1567631042 creator A5059936154 @default.
- W1567631042 creator A5075855591 @default.
- W1567631042 date "2014-05-01" @default.
- W1567631042 modified "2023-10-12" @default.
- W1567631042 title "Regulation of apoptosis by heat shock proteins" @default.
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- W1567631042 doi "https://doi.org/10.1002/iub.1274" @default.
- W1567631042 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24861574" @default.
- W1567631042 hasPublicationYear "2014" @default.
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