Results 31 to 40 of about 1,308,915 (353)

Endoplasmic Reticulum Stress and Reactive Oxygen Species in Plants

open access: yesAntioxidants, 2022
The endoplasmic reticulum (ER) is a key compartment responsible for protein processing and folding, and it also participates in many signal transduction and metabolic processes. Reactive oxygen species (ROS) are important signaling messengers involved in
Jiajian Cao   +4 more
doaj   +1 more source

IRE1β negatively regulates IRE1α signaling in response to endoplasmic reticulum stress [PDF]

open access: yes, 2020
IRE1β is an ER stress sensor uniquely expressed in epithelial cells lining mucosal surfaces. Here, we show that intestinal epithelial cells expressing IRE1β have an attenuated unfolded protein response to ER stress.
Acosta-Alvear   +54 more
core   +1 more source

MFN2 mediates ER-mitochondrial coupling during ER stress through specialized stable contact sites

open access: yesFrontiers in Cell and Developmental Biology, 2022
Endoplasmic reticulum (ER) functions critically depend on a suitable ATP supply to fuel ER chaperons and protein trafficking. A disruption of the ability of the ER to traffic and fold proteins leads to ER stress and the unfolded protein response (UPR ...
Benjamin Gottschalk   +6 more
doaj   +1 more source

Sirtuin1 protects endothelial Caveolin-1 expression and preserves endothelial function via suppressing miR-204 and endoplasmic reticulum stress. [PDF]

open access: yes, 2017
Sirtuin1 (Sirt1) is a class III histone deacetylase that regulates a variety of physiological processes, including endothelial function. Caveolin1 (Cav1) is also an important determinant of endothelial function. We asked if Sirt1 governs endothelial Cav1
Gabani, Mohanad   +10 more
core   +3 more sources

Brucella abortus Infection of Placental Trophoblasts Triggers Endoplasmic Reticulum Stress-Mediated Cell Death and Fetal Loss via Type IV Secretion System-Dependent Activation of CHOP. [PDF]

open access: yes, 2019
Subversion of endoplasmic reticulum (ER) function is a feature shared by multiple intracellular bacteria and viruses, and in many cases this disruption of cellular function activates pathways of the unfolded protein response (UPR).
Atluri, Vidya L   +14 more
core   +1 more source

Regulation of podocyte survival and endoplasmic reticulum stress by fatty acids and its modification by Stearoyl-CoA desaturases and cyclic AMP [PDF]

open access: yes, 2011
Podocyte apoptosis is a hallmark in the development and progression of diabetic nephropathy (DN). Several factors of the diabetic milieu are known to induce podocyte apoptosis. Currently, the role of free fatty acids (FFAs) for podocytopathy and podocyte
Sieber, Jonas
core   +1 more source

MicroRNA-494 Regulates Endoplasmic Reticulum Stress in Endothelial Cells

open access: yesFrontiers in Cell and Developmental Biology, 2021
Defects in stress responses are important contributors in many chronic conditions including cancer, cardiovascular disease, diabetes, and obesity-driven pathologies like non-alcoholic steatohepatitis (NASH).
Namita Chatterjee   +5 more
doaj   +1 more source

Obesity Induces Hypothalamic Endoplasmic Reticulum Stress and Impairs Proopiomelanocortin (POMC) Post-translational Processing [PDF]

open access: yes, 2013
It was shown previously that abnormal prohormone processing or inactive proconverting enzymes that are responsible for this processing cause profound obesity.
Cakir, Isin   +6 more
core   +1 more source

The genetic architecture of the genome-wide transcriptional response to ER stress in the mouse.

open access: yesPLoS Genetics, 2015
Endoplasmic reticulum (ER) stress occurs when misfolded proteins accumulate in the ER. The cellular response to ER stress involves complex transcriptional and translational changes, important to the survival of the cell.
Clement Y Chow   +4 more
doaj   +1 more source

Endoplasmic reticulum stress as target for treatment of hearing loss

open access: yesSTEMedicine, 2020
The endoplasmic reticulum (ER) plays pivotal roles in coordinating protein biosynthesis and processing. Under ER stress, when excessive misfolded or unfolded proteins are accumulated in the ER, the unfolded protein response (UPR) is activated.
Yanfei Wang, Zhigang Xu
doaj   +1 more source

Home - About - Disclaimer - Privacy