Pharmacological targeting of endoplasmic reticulum stress in disease
The accumulation of misfolded proteins in the endoplasmic reticulum (ER) leads to ER
stress, resulting in activation of the unfolded protein response (UPR) that aims to restore …
stress, resulting in activation of the unfolded protein response (UPR) that aims to restore …
Structure and molecular mechanism of ER stress signaling by the unfolded protein response signal activator IRE1
CJ Adams, MC Kopp, N Larburu, PR Nowak… - Frontiers in molecular …, 2019 - frontiersin.org
The endoplasmic reticulum (ER) is an important site for protein folding and maturation in
eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its …
eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its …
Activation of the integrated stress response by inhibitors of its kinases
M Szaruga, DA Janssen, C de Miguel… - Nature …, 2023 - nature.com
Phosphorylation of the translation initiation factor eIF2α to initiate the integrated stress
response (ISR) is a vital signalling event. Protein kinases activating the ISR, including PERK …
response (ISR) is a vital signalling event. Protein kinases activating the ISR, including PERK …
The role of endoplasmic reticulum stress in human pathology
SA Oakes, FR Papa - Annual Review of Pathology: Mechanisms …, 2015 - annualreviews.org
Numerous genetic and environmental insults impede the ability of cells to properly fold and
posttranslationally modify secretory and transmembrane proteins in the endoplasmic …
posttranslationally modify secretory and transmembrane proteins in the endoplasmic …
Endoplasmic reticulum stress sensing in the unfolded protein response
BM Gardner, D Pincus, K Gotthardt… - Cold Spring …, 2013 - cshperspectives.cshlp.org
Secretory and transmembrane proteins enter the endoplasmic reticulum (ER) as unfolded
proteins and exit as either folded proteins in transit to their target organelles or as misfolded …
proteins and exit as either folded proteins in transit to their target organelles or as misfolded …
[HTML][HTML] IRE1α induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress
AG Lerner, JP Upton, PVK Praveen, R Ghosh… - Cell metabolism, 2012 - cell.com
When unfolded proteins accumulate to irremediably high levels within the endoplasmic
reticulum (ER), intracellular signaling pathways called the unfolded protein response (UPR) …
reticulum (ER), intracellular signaling pathways called the unfolded protein response (UPR) …
IRE1α cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2
The endoplasmic reticulum (ER) is the primary organelle for folding and maturation of
secretory and transmembrane proteins. Inability to meet protein-folding demand leads to …
secretory and transmembrane proteins. Inability to meet protein-folding demand leads to …
Signal integration in the endoplasmic reticulum unfolded protein response
The endoplasmic reticulum (ER) responds to the accumulation of unfolded proteins in its
lumen (ER stress) by activating intracellular signal transduction pathways—cumulatively …
lumen (ER stress) by activating intracellular signal transduction pathways—cumulatively …
[HTML][HTML] The role of MAPK signalling pathways in the response to endoplasmic reticulum stress
NJ Darling, SJ Cook - Biochimica et Biophysica Acta (BBA)-Molecular Cell …, 2014 - Elsevier
Perturbations in endoplasmic reticulum (ER) homeostasis, including depletion of Ca 2+ or
altered redox status, induce ER stress due to protein accumulation, misfolding and …
altered redox status, induce ER stress due to protein accumulation, misfolding and …
Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
Maintenance of endoplasmic reticulum (ER) function is achieved in part through Ire1
(inositol-requiring enzyme 1), a transmembrane protein activated by protein misfolding in the …
(inositol-requiring enzyme 1), a transmembrane protein activated by protein misfolding in the …