Results 71 to 80 of about 52,959 (267)

The endoplasmic reticulum in plant immunity and cell death [PDF]

open access: yes, 2012
The endoplasmic reticulum (ER) is a highly dynamic organelle in eukaryotic cells and a major production site of proteins destined for vacuoles, the plasma membrane, or apoplast in plants.
Eichmann, Ruth, Schäfer, P. (Patrick)
core   +2 more sources

Lifespan Extension Conferred by Endoplasmic Reticulum Secretory Pathway Deficiency Requires Induction of the Unfolded Protein Response [PDF]

open access: yes, 2014
Cells respond to accumulation of misfolded proteins in the endoplasmic reticulum (ER) by activating the unfolded protein response (UPR) signaling pathway.
Delaney, Joe R.   +6 more
core   +3 more sources

Endoplasmic Reticulum Stress and Lipid Metabolism: Mechanisms and Therapeutic Potential

open access: yesBiochemistry Research International, 2012
The endoplasmic reticulum (ER) plays a crucial role in protein folding, assembly, and secretion. Disruption of ER homeostasis may lead to accumulation of misfolded or unfolded proteins in the ER lumen, a condition referred to as ER stress. In response to
Sana Basseri, Richard C. Austin
doaj   +1 more source

The Endoplasmic Reticulum Unfolded Protein Response in Neurodegenerative Disorders and Its Potential Therapeutic Significance

open access: yesFrontiers in Molecular Neuroscience, 2017
In eukaryotic cells, the endoplasmic reticulum (ER) is the cell compartment involved in secretory protein translocation and quality control of secretory protein folding.
Paolo Remondelli, Maurizio Renna
doaj   +1 more source

Mifepristone increases mRNA translation rate, triggers the unfolded protein response, increases autophagic flux, and kills ovarian cancer cells in combination with proteasome or lysosome inhibitors [PDF]

open access: yes, 2016
The synthetic steroid mifepristone blocks the growth of ovarian cancer cells, yet the mechanism driving such effect is not entirely understood. Unbiased genomic and proteomic screenings using ovarian cancer cell lines of different genetic backgrounds and
Callegari, Eduardo A.   +13 more
core   +1 more source

Unfolded protein response in cancer: the Physician's perspective

open access: yesJournal of Hematology & Oncology, 2011
The unfolded protein response (UPR) is a cascade of intracellular stress signaling events in response to an accumulation of unfolded or misfolded proteins in the lumen of the endoplasmic reticulum (ER). Cancer cells are often exposed to hypoxia, nutrient
Li Zihai, Zhang Kezhong, Li Xuemei
doaj   +1 more source

Dihydroorotate dehydrogenase (DHODH) regulates trophoblast syncytialization through organelle stress–induced cellular senescence

open access: yesFEBS Open Bio, EarlyView.
The inhibition of mitochondrial dihydroorotate dehydrogenase (DHODH) impairs syncytialization and induces cellular senescence via mitochondrial and endoplasmic reticulum stress in human trophoblast stem cells, elevating sFlt1/PlGF levels, a hallmark of placental dysfunction in hypertensive disorders of pregnancy.
Kanoko Yoshida   +6 more
wiley   +1 more source

ZIKV infection activates the IRE1-XBP1 and ATF6 pathways of unfolded protein response in neural cells. [PDF]

open access: yes, 2018
BACKGROUND: Many viruses depend on the extensive membranous network of the endoplasmic reticulum (ER) for their translation, replication, and packaging. Certain membrane modifications of the ER can be a trigger for ER stress, as well as the accumulation ...
Fu, Z   +11 more
core   +1 more source

The physiological role of the unfolded protein response in the nervous system

open access: yesNeural Regeneration Research
The unfolded protein response (UPR) is a cellular stress response pathway activated when the endoplasmic reticulum, a crucial organelle for protein folding and modification, encounters an accumulation of unfolded or misfolded proteins.
Shuangchan Wu, Wensheng Lin
doaj   +1 more source

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

Home - About - Disclaimer - Privacy