Journal
NATURE REVIEWS DRUG DISCOVERY
Volume 12, Issue 9, Pages 703-719Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nrd3976
Keywords
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Funding
- FONDECYT [1100176]
- Millennium Institute [P09-015-F]
- Ring Initiative [ACT 1109]
- FONDEF [D11I1007]
- ALS Therapy Alliance
- Muscular Dystrophy Association
- Michael J. Fox Foundation
- Alzheimer's Disease Association
- Institut National de la Sante et la Recherche Medicale (INSERM)
- Institut National du Cancer, France
- Ligue contre le cancer, France
- Wellcome Trust [084812/Z/08/Z]
- Wellcome Trust [084812/Z/08/Z] Funding Source: Wellcome Trust
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Stress induced by the accumulation of unfolded proteins in the endoplasmic reticulum (ER) is a feature of specialized secretory cells and is also observed in many diseases, including cancer, diabetes, autoimmune conditions, liver disorders, obesity and neurodegenerative disorders. Cellular adaptation to ER stress is achieved by the activation of the unfolded protein response, which is an integrated signal transduction pathway that modulates many aspects of ER physiology. When these mechanisms of adaptation are insufficient to handle the unfolded protein load, cells undergo apoptosis. Here, we discuss recent advances in the design of novel compounds and therapeutic strategies to manipulate levels of ER stress in disease.
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