Results 301 to 310 of about 1,308,915 (353)
Integrin-specific signaling drives ER stress-dependent atherogenic endothelial activation. [PDF]
Ben Dhaou C +13 more
europepmc +1 more source
<i>Toxoplasma gondii</i> effector GRA35 mediates neuronal damage <i>via</i> ER stress and mitochondria-associated apoptosis. [PDF]
Wang J +9 more
europepmc +1 more source
ER-transiting bacterial toxins amplify STING innate immune responses and elicit ER stress
Catherine Schlenker +4 more
openalex +1 more source
Loss of BAP31 Is Detrimentally Aging Photoreceptors Through ER Stress-Mediated Retinal Degeneration. [PDF]
Gao F +6 more
europepmc +1 more source
ER stress tolerance is regulated by copper-dependent PERK kinase activity. [PDF]
Bond Newton SE +9 more
europepmc +1 more source
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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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources

