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Protein aggregation and ER stress
Brain Research, 2016Protein aggregation is a common feature of the protein misfolding or conformational diseases, among them most of the neurodegenerative diseases. These disorders are a major scourge, with scarce if any effective therapies at present. Recent research has identified ER stress as a major mechanism implicated in cytotoxicity in these diseases.
Navit, Ogen-Shtern +2 more
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The FEBS Journal, 2007
Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the assistance of ER chaperones. Malfolded proteins are disposed of by ER‐associated protein degradation (ERAD). When the amount of unfolded protein exceeds the folding capacity of the ER, human cells activate a defense mechanism called the ER stress response, which induces
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Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the assistance of ER chaperones. Malfolded proteins are disposed of by ER‐associated protein degradation (ERAD). When the amount of unfolded protein exceeds the folding capacity of the ER, human cells activate a defense mechanism called the ER stress response, which induces
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A trip to the ER: coping with stress
Trends in Cell Biology, 2004The accumulation of unfolded proteins in the lumen of the endoplasmic reticulum (ER) induces a coordinated adaptive program called the unfolded protein response (UPR). The UPR alleviates stress by upregulating protein folding and degradation pathways in the ER and inhibiting protein synthesis.
D Thomas, Rutkowski, Randal J, Kaufman
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ER stress in cardiovascular disease
Journal of Molecular and Cellular Cardiology, 2010The endoplasmic reticulum (ER) is an organelle involved in protein folding, calcium homeostasis, and lipid biosynthesis. Various factors that interfere with ER function lead to accumulation of unfolded proteins, including oxidative stress, ischemia, disturbance of calcium homeostasis, and overexpression of normal and/or incorrectly folded proteins. The
Tetsuo, Minamino, Masafumi, Kitakaze
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Biologie aujourd'hui, 2021
Non-alcoholic fatty liver disease (NAFLD) is a highly prevalent pathology associated with obesity. It encompasses a spectrum of hepatic disorders ranging from steatosis to non-alcoholic steatohepatitis (NASH), which may lead to cirrhosis and hepatocellular carcinoma (HCC).
Floriane, Lachkar +3 more
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Non-alcoholic fatty liver disease (NAFLD) is a highly prevalent pathology associated with obesity. It encompasses a spectrum of hepatic disorders ranging from steatosis to non-alcoholic steatohepatitis (NASH), which may lead to cirrhosis and hepatocellular carcinoma (HCC).
Floriane, Lachkar +3 more
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Science Signaling, 2000
The presence of misfolded proteins in the endoplasmic reticulum (ER) is sensed by cells and initiates a stress response. In yeast, the transmembrane protein IRE1p senses misfolded proteins and produces signals that lead to appropriate changes in gene expression.
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The presence of misfolded proteins in the endoplasmic reticulum (ER) is sensed by cells and initiates a stress response. In yeast, the transmembrane protein IRE1p senses misfolded proteins and produces signals that lead to appropriate changes in gene expression.
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Science Translational Medicine, 2017
A new type of biological clock regulates the unfolded protein response.
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A new type of biological clock regulates the unfolded protein response.
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Science Signaling, 2001
PERK (protein kinase R-like kinase) is a transmembrane protein located in the endoplasmic reticulum (ER) that phosphorylates the eukaryotic translation initiation factor 2α (eIF2α). Phosphorylation eIF2α by PERK contributes to translational repression in response to ER stress.
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PERK (protein kinase R-like kinase) is a transmembrane protein located in the endoplasmic reticulum (ER) that phosphorylates the eukaryotic translation initiation factor 2α (eIF2α). Phosphorylation eIF2α by PERK contributes to translational repression in response to ER stress.
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ER and aging—Protein folding and the ER stress response
Ageing Research Reviews, 2009The endoplasmic reticulum (ER) is a multifunctional organelle which co-ordinates protein folding, lipid biosynthesis, calcium storage and release. Perturbations that disrupt ER homeostasis lead to the misfolding of proteins, ER stress and up-regulation of a signaling pathway called the ER stress response or the unfolded protein response (UPR).
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Science, 2004
STKE Cells monitor how well the synthesis of proteins in the endoplasmic reticulum (ER) is going, and when stressful conditions cause the accumulation of unfolded proteins, the unfolded protein response (UPR) is initiated. Ito et al. used a microarray screen to detect genes whose products were expressed specifically in response to an agent causing ER ...
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STKE Cells monitor how well the synthesis of proteins in the endoplasmic reticulum (ER) is going, and when stressful conditions cause the accumulation of unfolded proteins, the unfolded protein response (UPR) is initiated. Ito et al. used a microarray screen to detect genes whose products were expressed specifically in response to an agent causing ER ...
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