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Targeting the Unfolded Protein Response with Natural Products: Therapeutic Potential in ER Stress-Related Diseases. [PDF]
Int J Mol SciMartinotti S, Ranzato E.
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Current Molecular Medicine, 2015
Eukaryotic cells respond to various types of stresses caused by changes in the extracellular environment. Intracellular factors, such as the accumulation of misfolded proteins in the endoplasmic reticulum (ER), also cause stress and activate the unfolded protein response (UPR), which induces the expression of chaperones and proteins involved in the ...
W-S, Lee, W-H, Yoo, H-J, Chae
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Eukaryotic cells respond to various types of stresses caused by changes in the extracellular environment. Intracellular factors, such as the accumulation of misfolded proteins in the endoplasmic reticulum (ER), also cause stress and activate the unfolded protein response (UPR), which induces the expression of chaperones and proteins involved in the ...
W-S, Lee, W-H, Yoo, H-J, Chae
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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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Science, 2011
Direct binding of unfolded proteins to a sensor in the endoplasmic reticulum triggers sensor oligomerization and a cellular stress response.
Shinichi Kawaguchi, Davis T. W. Ng
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Direct binding of unfolded proteins to a sensor in the endoplasmic reticulum triggers sensor oligomerization and a cellular stress response.
Shinichi Kawaguchi, Davis T. W. Ng
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Science's STKE, 2004
Cells monitor how well synthesis of new proteins in the endoplasmic reticulum (ER) is going, and when stressful conditions cause accumulation of unfolded proteins, the unfolded protein response (UPR) is initiated, which signals for appropriate changes in cellular systems. Ito et al .
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Cells monitor how well synthesis of new proteins in the endoplasmic reticulum (ER) is going, and when stressful conditions cause accumulation of unfolded proteins, the unfolded protein response (UPR) is initiated, which signals for appropriate changes in cellular systems. Ito et al .
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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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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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Science Signaling, 2010
Inositol trisphosphate receptors (IP 3 Rs) are central to the neuronal response to endoplasmic reticulum stress.
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Inositol trisphosphate receptors (IP 3 Rs) are central to the neuronal response to endoplasmic reticulum stress.
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Hepatitis C virus, ER stress, and oxidative stress
Trends in Microbiology, 2005Hepatitis C virus (HCV) replication is associated with the endoplasmic reticulum (ER), where the virus causes stress. Cells cope with ER stress by activating an adaptive program called the unfolded protein response (UPR), which alleviates this stress by stimulating protein folding and degradation in the ER and down-regulating overall protein synthesis.
Keith D, Tardif +2 more
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Inactivating PTP1B upon ER stress
Nature Reviews Molecular Cell Biology, 2012The gaseous signalling molecule hydrogen sulphide (H2S) regulates a range of cellular processes by causing the sulphydration of Cys residues (that is, the formation of Cys–SSH groups) in target proteins. Protein Tyr phosphatases (PTPs) use an essential Cys (Cys215) in their catalytic site to dephosphorylat e Tyr residues in target proteins. Krishnan et
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