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- W2565453971 endingPage "66" @default.
- W2565453971 startingPage "58" @default.
- W2565453971 abstract "Abrogation of endoplasmic reticulum (ER) protein folding triggered by exogenous or endogenous factors, stimulates a cellular stress response, termed ER stress. ER stress re-establishes ER homeostasis through integrated signaling termed the ER-unfolded protein response (UPRER). In the presence of severe toxic or prolonged ER stress, the pro-survival function of UPRER is transformed into a lethal signal transmitted to and executed through mitochondria. Mitochondria are key for both apoptotic and autophagic cell death. Thus ER is vital in sensing and coordinating stress pathways to maintain overall physiological homeostasis. However, this function is deregulated in cancer, resulting in resistance to apoptosis induction in response to various stressors including therapeutic agents. Here we review the connections between ER stress and mitochondrial apoptosis, describing potential cancer therapeutic targets." @default.
- W2565453971 created "2017-01-06" @default.
- W2565453971 creator A5012219857 @default.
- W2565453971 creator A5012502014 @default.
- W2565453971 creator A5033228095 @default.
- W2565453971 creator A5056436394 @default.
- W2565453971 creator A5062006629 @default.
- W2565453971 creator A5063116970 @default.
- W2565453971 creator A5070100515 @default.
- W2565453971 creator A5084318911 @default.
- W2565453971 date "2017-01-01" @default.
- W2565453971 modified "2023-09-28" @default.
- W2565453971 title "Endoplasmic reticulum-mediated unfolded protein response and mitochondrial apoptosis in cancer" @default.
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