The impact of the unfolded protein response on human disease
By Shiyu Wang, R. Kaufman. Journal of Cell Biology, 2012
948 citations recorded by the source corpus.
A central function of the endoplasmic reticulum (ER) is to coordinate protein biosynthetic and secretory activities in the cell. Alterations in ER homeostasis cause accumulation of misfolded/unfolded proteins in the ER. To maintain ER homeostasis, eukaryotic cells have evolved the unfolded protein response (UPR), an essential adaptive intracellular signaling pathway that responds to metabolic, oxidative stress, and inflammatory response pathways. The UPR has been implicated in a variety of diseases including metabolic disease, neurodegenerative disease, inflammatory disease, and cancer. Signaling components of the UPR are emerging as potential targets for intervention and treatment of human disease.
Subfields: Cell Biology, Epidemiology, Surgery
View Paper: https://www.semanticscholar.org/paper/aae4687e9161517e0bd175a86fde68c568eed094
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Citations in the corpus
- Metabolic control of cell death (2014, neutral): “synthesis and activates several transcription factors (85).”
- Endoplasmic Reticulum Stress and Oxidative Stress in Cell Fate Decision and Human Disease (2014, background): “Both type 1 and type 2 diabetes involve cell dysfunction and/or apoptosis, which are associated with ER stress and oxidative stress (6,178).”
- NRF2, a Transcription Factor for Stress Response and Beyond (2020, background): “Aberrant aggregation of misfolded or denatured proteins has been observed in many diseases, such as cardiovascular disease, metabolic syndrome, cancer, and neurodegenerative disease [95].”