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Endoplasmic Reticulum (ER) Stress and Protein Misfolding
 | | | A highly oxidative environment of the endoplasmic reticulum (ER) lumen is vital for the formation of disulfide bonds and proper folding of a variety of proteins before they are secreted. In addition, it also contains several molecular chaperones that assist in folding and stabilizing folding intermediates. However, unfavorable redox conditions can contribute to the accumulation of unfolded proteins in the ER, which elicits the unfolded protein response (UPR). The UPR helps ER to adapt to changed environment and re-establish normal ER function. The adaptive mechanisms include transcription of genes that enhance protein-folding capacity of the ER, and promote ER-associated protein degradation to remove misfolded proteins. Any prolonged stress on ER leads to apoptotic cell death.
It is reported that some adaptive responses to misfolded proteins in the ER provide protection from cell death. Over-expression of Grp78 and protein-disulfide isomerase is shown to reduce apoptosis induced by oxidative stress, hypoxia, and extreme disturbances in Ca2+ levels. | | |  Selected ER Stress Related Research Tools | | | | Chemical chaperones |
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| Sodium 4-Phenylbutyrate |
567616 |
| Tauroursodeoxycholic Acid, Sodium Salt |
580549 |
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| | | | Cytokines |
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| TNF-a, Human, Recombinant, E. coli |
654205 |
| TNF-a, Mouse, Recombinant, E. coli |
654245 |
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| | | | Caspases |
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| Caspase-8, Human, Recombinant, E. coli |
218769 |
| Caspase-9, Human, Recombinant, E. coli |
218807 |
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| | | | ER Stress Inhibitor |
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| eIF-2a Inhibitor, Salubrinal |
324895 |
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| | | | IKK Inhibitors | |
| | | | JNK Inhibitors |
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| JNK Inhibitor I, (L)-Form, Cell-Permeable |
420116 |
| JNK Inhibitor V |
420129 |
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