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- W1984185436 abstract "mRNA translation plays an important role in tumor development and represents a valid target of pharmaceutical intervention in cancer. A key step in mRNA translation involves the regulation of initiation by the eukaryotic initiation factor eIF2. Eukaryotic cells respond to various forms of stress by inducing the phosphorylation of the α-subunit of eIF2 at S51, a modification that leads to protein synthesis inhibition. Phosphorylated eIF2α can act either as a promoter of cell survival or an inducer of cell death in response to distinct stimuli. Increased eIF2α phosphorylation has a cytoprotective function in response to genetic or pharmacological inhibition of the PI3K–Akt pathway but also exhibits a proapoptotic function downstream of the PTEN tumor suppressor, independent of PI3K–Akt signaling inhibition. The functional interplay between the PI3K–Akt and eIF2α phosphorylation pathways may have important implications in the design of anti-tumor therapies that depend on the cell fate decisions of phosphorylated eIF2α." @default.
- W1984185436 created "2016-06-24" @default.
- W1984185436 creator A5002284937 @default.
- W1984185436 creator A5029803492 @default.
- W1984185436 date "2013-07-01" @default.
- W1984185436 modified "2023-09-27" @default.
- W1984185436 title "Control of oncogenesis by eIF2α phosphorylation: implications in PTEN and PI3K–Akt signaling and tumor treatment" @default.
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- W1984185436 doi "https://doi.org/10.2217/fon.13.49" @default.
- W1984185436 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23837763" @default.
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