Results 71 to 80 of about 8,105,112 (196)

Cytomegalovirus downregulates IRE1 to repress the unfolded protein response. [PDF]

open access: yesPLoS Pathogens, 2013
During viral infection, a massive demand for viral glycoproteins can overwhelm the capacity of the protein folding and quality control machinery, leading to an accumulation of unfolded proteins in the endoplasmic reticulum (ER). To restore ER homeostasis,
Sebastian Stahl   +9 more
doaj   +1 more source

Secretopathies emerge as a new class of neurocristopathies

open access: yesDevelopmental Dynamics, EarlyView.
Abstract Neural crest cells are a transient embryonic population of cells that give rise to a wide range of structures, including craniofacial cartilage and bone, peripheral neurons and glia, as well as components of the cardiac outflow tract, among others.
Amanda Teixeira   +3 more
wiley   +1 more source

The Unfolded Protein Response Pathway in the Yeast Kluyveromyces lactis. A Comparative View among Yeast Species

open access: yesCells, 2018
Eukaryotic cells have evolved signalling pathways that allow adaptation to harmful conditions that disrupt endoplasmic reticulum (ER) homeostasis.
Mariana Hernández-Elvira   +7 more
doaj   +1 more source

Methods for Monitoring Endoplasmic Reticulum Stress and the Unfolded Protein Response

open access: yesInternational Journal of Cell Biology, 2010
The endoplasmic reticulum (ER) is the site of folding of membrane and secreted proteins in the cell. Physiological or pathological processes that disturb protein folding in the endoplasmic reticulum cause ER stress and activate a set of signaling ...
Afshin Samali   +3 more
doaj   +1 more source

Metrnl: A Novel Therapeutic Target in Atherosclerosis

open access: yesiNew Medicine, EarlyView.
ABSTRACT Atherosclerosis is a chronic inflammatory vascular disease and the main pathological basis of cardiovascular and cerebrovascular events. Exploration of endogenous protective factors in the disease is beneficial for the establishment of new therapeutic strategies.
Pin Wang, Dao‐Xin Wang, Chao‐Yu Miao
wiley   +1 more source

Structural dynamics of IRE1 and its interaction with unfolded peptides

open access: yeseLife
The unfolded protein response (UPR) is a crucial signaling network that preserves endoplasmic reticulum (ER) homeostasis, impacting both health and disease. When ER stress occurs, often due to an accumulation of unfolded proteins in the ER lumen, the UPR
Elena Spinetti   +3 more
doaj   +1 more source

A New Role for Estrogen Receptor α in Cell Proliferation and Cancer: Activating the Anticipatory Unfolded Protein Response

open access: yesFrontiers in Endocrinology, 2018
Cells react to a variety of stresses, including accumulation of unfolded or misfolded protein, by activating the endoplasmic reticulum (EnR) stress sensor, the unfolded protein response (UPR).
Mara Livezey   +3 more
doaj   +1 more source

The Effects of Angiotensin Receptor Neprilysin Inhibitor on Endoplasmic Reticulum Stress in Doxorubicin‐Mediated Cardiomyopathy‐Associated Heart Failure Model in Rats

open access: yesJournal of Applied Toxicology, EarlyView.
ABSTRACT One of the most serious complications associated with the use of the chemotherapeutic agent doxorubicin (DOX) is cardiomyopathy. Although cardioprotective drugs such as angiotensin receptor‐neprilysin inhibitors (ARNI) are used to prevent cardiomyopathy in DOX patients, no studies have reported the relationship between ARNI and endoplasmic ...
Mert Unvan   +3 more
wiley   +1 more source

Translation attenuation mechanism in unfolded protein response

open access: yes, 2008
Endoplasmic Reticulum is a cellular organelle where membrane and extracellular proteins are folded with the help of chaperons. Insulin is one example of such extracellular proteins. Unfolded Protein Response (UPR) is a cell response to an increased level
Trusina, Ala, Papa, Feroz, Tang, Chao
core   +1 more source

Bisphenol Analog‐Induced Cytotoxicity: Unraveling Endoplasmic Reticulum (ER) Stress and Apoptotic Pathways

open access: yesJournal of Applied Toxicology, EarlyView.
ABSTRACT Bisphenol A (BPA) is increasingly replaced by structural analogs, yet their safety remains insufficiently characterized. This study investigated whether BPA and selected analogs, bisphenol AF (BPAF), bisphenol AP (BPAP), bisphenol P (BPP), and bisphenol E (BPE), induce cytotoxicity through activation of endoplasmic reticulum (ER) stress and ...
Rafia Afroze Rifa, Ramon Lavado
wiley   +1 more source

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