Abstract
Tumor cells undergo higher rate of protein synthesis, which leads to accumulation of unfolded/misfolded proteins in the lumen of the endoplasmic reticulum (ER). To restore normal function, ER induces a stress response, known as the unfolded protein response (UPR) and induces the expression of molecular chaperones, such as Hsps that try to correct protein misfolding. If the correction machinery fails to control erroneous protein burden, UPR aims to initiate programmed cell death (apoptosis). We propose to exploit UPR-targeted apoptosis for cancer therapy.
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