Results 311 to 320 of about 1,308,915 (353)

Sensing ER Stress

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
openaire   +1 more source

Tolerating ER Stress

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 .
openaire   +2 more sources

Protein aggregation and ER stress

Brain Research, 2016
Protein 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, Tamuz, Ben David, Gerardo Z, Lederkremer   +2 more
openaire   +2 more sources

ER stress in cardiovascular disease

Journal of Molecular and Cellular Cardiology, 2010
The 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
openaire   +2 more sources

Neuronal ER Stress

Science Signaling, 2010
Inositol trisphosphate receptors (IP 3 Rs) are central to the neuronal response to endoplasmic reticulum stress.
openaire   +1 more source

Hepatitis C virus, ER stress, and oxidative stress

Trends in Microbiology, 2005
Hepatitis 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, Gulam, Waris, Aleem, Siddiqui   +2 more
openaire   +2 more sources

Inactivating PTP1B upon ER stress

Nature Reviews Molecular Cell Biology, 2012
The 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
openaire   +2 more sources

Surf’s up for ER stress

Science Translational Medicine, 2017
A new type of biological clock regulates the unfolded protein response.
openaire   +2 more sources

Responding to ER Stress

Science's STKE, 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.
openaire   +2 more sources

Plant hormone regulation of abiotic stress responses

Nature Reviews Molecular Cell Biology, 2022
Rainer Waadt, Charles A Seller, Po-Kai Hsu   +2 more
exaly