| Source: HalifaxProj(induce) |
| Type: |
| Endoplasmic reticulum (ER) stress is a condition that arises when the ER, a cellular organelle responsible for protein folding, lipid synthesis, and calcium storage, becomes overwhelmed by misfolded or unfolded proteins. This stress can trigger a cellular response known as the unfolded protein response (UPR), which aims to restore normal function by enhancing the protein-folding capacity of the ER, degrading misfolded proteins, and, if necessary, initiating apoptosis (programmed cell death). Cancer cells often experience high levels of ER stress due to rapid proliferation, hypoxia, and nutrient deprivation. |
| 2720- | BetA, | Betulinic acid induces apoptosis of HeLa cells via ROS-dependent ER stress and autophagy in vitro and in vivo |
| - | in-vitro, | Cerv, | HeLa |
| 4776- | CoQ10, | Antitumor properties of Coenzyme Q0 against human ovarian carcinoma cells via induction of ROS-mediated apoptosis and cytoprotective autophagy |
| - | vitro+vivo, | Ovarian, | SKOV3 |
| 4996- | Sal, | The Molecular Basis for Inhibition of Stemlike Cancer Cells by Salinomycin |
Query results interpretion may depend on "conditions" listed in the research papers. Such Conditions may include : -low or high Dose -format for product, such as nano of lipid formations -different cell line effects -synergies with other products -if effect was for normal or cancerous cells
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