Results 61 to 70 of about 28,738 (248)

Gcn4p and novel upstream activating sequences regulate targets of the unfolded protein response. [PDF]

open access: yes, 2004
Eukaryotic cells respond to accumulation of unfolded proteins in the endoplasmic reticulum (ER) by activating the unfolded protein response (UPR), a signal transduction pathway that communicates between the ER and the nucleus.
Li, Hao   +2 more
core   +4 more sources

The non-canonical mechanism of ER stress-mediated progression of prostate cancer

open access: yesJournal of Experimental & Clinical Cancer Research, 2021
Background The development of persistent endoplasmic reticulum (ER) stress is one of the cornerstones of prostate carcinogenesis; however, the mechanism is missing.
Artem N. Pachikov   +20 more
doaj   +1 more source

Activating transcription factor 6 polymorphisms and haplotypes are associated with impaired glucose homeostasis and type 2 diabetes in dutch Caucasians [PDF]

open access: yes, 2007
Context: Activating transcription factor 6 (ATF6) is critical for initiation and full activation of the unfolded protein response. An association between genetic variation in ATF6 and type 2 diabetes (DM2) was recently reported in Pima Indians ...
Ayoubi, Torik A.   +12 more
core   +2 more sources

A conformational RNA zipper promotes intron ejection during non-conventional XBP1 mRNA splicing. [PDF]

open access: yes, 2015
The kinase/endonuclease IRE1 is the most conserved signal transducer of the unfolded protein response (UPR), an intracellular signaling network that monitors and regulates the protein folding capacity of the endoplasmic reticulum (ER).
Acosta-Alvear, Diego   +3 more
core   +1 more source

ER Stress Activates the TOR Pathway through Atf6

open access: yesJournal of Molecular Signaling, 2018
Cellular signaling pathways are often interconnected. They accurately and efficiently regulate essential cell functions such as protein synthesis, cell growth, and survival. The target of rapamycin (TOR) signaling pathway and the endoplasmic reticulum (ER) stress response pathway regulate similar cellular processes.
Dylan Allen, Jin Seo
openaire   +4 more sources

Beneficial effects of neuronal ATF6 activation in permanent ischemic stroke

open access: yesFrontiers in Cellular Neuroscience, 2022
Objective: Brain ischemia leads to the accumulation of unfolded/misfolded proteins in the endoplasmic reticulum (ER) lumen and consequently, ER stress. To help cells restore ER function, a series of adaptive stress response pathways, collectively termed the unfolded protein response (UPR), are activated.
Xuan Li   +5 more
openaire   +3 more sources

Mitochondrial Calcium Uniporter Drives Chemoresistance in Pancreatic Cancer via Glutathione‐Mediated Stemness Maintenance

open access: yesAdvanced Science, EarlyView.
PDAC has a poor prognosis due to chemoresistance. We revealed that MCU upregulation is associated with chemoresistance and stemness in PDAC. MCU‐mediated Ca2+ influx induced ER stress, activating the PERK‐ATF4/NRF2 axis to enhance PSAT1/SLC711 expression and glutathione synthesis, reducing ROS and maintaining stemness.
Zekun Li   +17 more
wiley   +1 more source

Mechanisms of selenomethionine developmental toxicity and the impacts of combined hypersaline conditions on Japanese medaka (Oryzias latipes). [PDF]

open access: yes, 2014
Selenium (Se) is an essential micronutrient that can cause embryotoxicty at levels 7-30 times above essential concentrations. Exposure to hypersaline conditions and 50 μM selenomethionine (SeMet) decreased embryo hatch and depleted glutathione in ...
Kupsco, Allison, Schlenk, Daniel
core   +1 more source

The Luminal Domain of ATF6 Senses Endoplasmic Reticulum (ER) Stress and Causes Translocation of ATF6 from the ER to the Golgi [PDF]

open access: yesJournal of Biological Chemistry, 2002
ATF6 is an endoplasmic reticulum (ER) transmembrane transcription factor that is activated by the ER stress/unfolded protein response by cleavage of its N-terminal half from the membrane. We find that ER stress induces ATF6 to move from the ER to the Golgi, where it is cut in its luminal domain by site 1 protease.
Xi, Chen, Jingshi, Shen, Ron, Prywes
openaire   +2 more sources

Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation

open access: yeseLife, 2016
Imbalances in endoplasmic reticulum (ER) proteostasis are associated with etiologically-diverse degenerative diseases linked to excessive extracellular protein misfolding and aggregation.
Lars Plate   +17 more
doaj   +1 more source

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