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- W2981484227 abstract "Identified as a molecular chaperone constitutively being synthesized due to enhanced elevated temperature change, this heat shock protein HSP70 has shown to be intimately involved in many protein biogenesis, facilitating the synthesis and folding of proteins and trafficking of nascent peptides during cell growth. HSP70 also plays a vital role in protein assembly, regulation and interaction with a wide variety of proteins. Stress-induced cell death is under the control of the Bcl-2 family of apoptotic regulators and display either pro-apoptotic or anti-apoptotic activities. Subjected to stress conditions such as heat shock, cells have been reported to express elevated expressions of HSP70. Moreover, this molecular chaperon has shown to act at multiple levels to suppress stressed-induced apoptotic signals of some Bcl-2 members by repairing, re-synthesizing damaged proteins, and stabilizing unfolded proteins. Therefore, HSP70 synthesis can act as an essential recovery mode for cellular survival and adaptation during lethal conditions." @default.
- W2981484227 created "2019-11-01" @default.
- W2981484227 creator A5002855381 @default.
- W2981484227 creator A5087326372 @default.
- W2981484227 date "2019-06-20" @default.
- W2981484227 modified "2023-09-30" @default.
- W2981484227 title "Molecular Chaperone HSP70 and Key Regulators of Apoptosis - A Review" @default.
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- W2981484227 doi "https://doi.org/10.2174/1566524019666190326114720" @default.
- W2981484227 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30914024" @default.
- W2981484227 hasPublicationYear "2019" @default.
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