Titlebook: Endoplasmic Reticulum Stress in Health and Disease; Patrizia Agostinis,Samali Afshin Book 2012 Springer Science+Business Media Dordrecht 2

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ER Stress and Inflammationrocesses, such as the acute-phase response (APR) and those instigated by transcriptional factors like NF-κB and AP-1. ER stress-mediated inflammation has been found to be associated with several diseases, such as obesity, type 2 diabetes, intestinal bowel disease and cancer. The role of ER stress-me

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ER Stress in Intestinal Inflammatory Diseaseus attention on intestinal epithelial cells (IEC) which are unique as they are highly secretory cells that are exposed to a great number of ER stress inducers such as bacteria, xenobiotics, toxins, and hypoxia amongst many other factors (Kaser and Blumberg, Mucosal Immunol 3:11–16, 2010). At the sam

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Endoplasmic Reticulum (ER) Stress in Amyotrophic Lateral Sclerosis (ALS)with the identification of mutations in 4 key genes, TARDBP, FUS, VCP and VAPB that cause familial ALS. The strong association of TDP-43 with ubiquitinated protein aggregates in motor neurons, a hallmark of ALS in sporadic cases of ALS, clearly demonstrates the importance of these findings for under

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Signaling the Unfolded Protein Response in cancernmental challenges such as hypoxia, nutrient deprivation, remodeling of the environmental space or presence of chemotherapeutic agents. Moreover cancer cells also have to cope with elevated oxidative stress, high DNA replication and protein synthesis rates. As a consequence cancer cells must show hi

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Rheinisch-Westf?lischen Kohlen-Syndikatrly studies focused on the structure, which was then followed by biochemical and functional studies associated with calcium storage and release from the ER, protein folding and secretion, ER associated degradation (ERAD) and ER stress responses. Currently there is a significant interest in the role

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Immersive Ruin: Chernobyl and Virtual Decayd degradation of terminally misfolded proteins. Different physiological as well as pathological stress conditions however, can lead to an imbalance between the ER protein folding capacity and protein load, giving rise to an accumulation of misfolded proteins in the ER lumen, a condition dubbed as ‘E