Results 21 to 30 of about 33,130 (117)

Targeting the IRE1α/XBP1s pathway suppresses CARM1-expressing ovarian cancer

open access: yesNature Communications, 2021
The unfolded protein response (UPR) promotes cell survival in cancers with hyperactive ER stress response. Here the authors show that CARM1, an arginine methyltransferase, controls the IRE1α/XBP1 pathway of the UPR and the inhibition of this pathway can ...
Jianhuang Lin   +13 more
doaj   +1 more source

Deciphering ER stress-unfolded protein response relationship by visualizing unfolded proteins in the ER

open access: yesCell Reports
Summary: Despite the consensus that accumulation of unfolded proteins in the endoplasmic reticulum (ER) lumen, i.e. ER stress, activates the unfolded protein response (UPR), studies under physiological and pathophysiological conditions suggest that ER ...
Fenfen Xu, Likun Wang
doaj   +1 more source

A mechanism of ineffective erythropoiesis in β-thalassemia/Hb E disease

open access: yesHaematologica, 2010
Background Cells respond to stress stimuli through a number of response pathways, of which one of the most important and well characterized is the unfolded protein response.
Pathrapol Lithanatudom   +5 more
doaj   +1 more source

The Impact of Endoplasmic Reticulum-Associated Protein Modifications, Folding and Degradation on Lung Structure and Function

open access: yesFrontiers in Physiology, 2021
The accumulation of unfolded/misfolded proteins in the endoplasmic reticulum (ER) causes ER stress and induces the unfolded protein response (UPR) and other mechanisms to restore ER homeostasis, including translational shutdown, increased targeting of ...
Emily M. Nakada   +7 more
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

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

Cellular stress signaling and the unfolded protein response in retinal degeneration: mechanisms and therapeutic implications

open access: yesMolecular Neurodegeneration, 2022
Background The retina, as part of the central nervous system (CNS) with limited capacity for self-reparation and regeneration in mammals, is under cumulative environmental stress due to high-energy demands and rapid protein turnover.
Todd McLaughlin   +5 more
doaj   +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

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

The unfolded protein response in multiple sclerosis

open access: yesFrontiers in Neuroscience, 2015
The unfolded protein response (UPR) occurs in response to endoplasmic reticulum (ER) stress caused by the accumulation of unfolded or misfolded proteins in the ER.
Wensheng eLin, Sarrabeth eStone
doaj   +1 more source

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