Results 1 to 10 of about 23,988 (146)

Roles of eIF2α kinases in the pathogenesis of Alzheimer’s disease [PDF]

open access: yesFrontiers in Molecular Neuroscience, 2014
Cell signaling in response to an array of diverse stress stimuli converges on the phosphorylation of eukaryotic initiation factor-2α (eIF2α). Evidence is accumulating that persistent eIF2α phosphorylation at Ser51 through prolonged overactivation of ...
Masuo eOhno, Masuo eOhno
doaj   +3 more sources

Endoplasmic Reticulum Stress Mediated MDRV p10.8 Protein-Induced Cell Cycle Arrest and Apoptosis Through the PERK/eIF2α Pathway [PDF]

open access: goldFrontiers in Microbiology, 2018
In this study, the mechanism of Muscovy duck reovirus (MDRV) p10.8 protein-induced pathogenesis was investigated, with a focus on endoplasmic reticulum (ER) stress.
Quanxi Wang   +9 more
doaj   +2 more sources

Hypothalamic eIF2α Signaling Regulates Food Intake [PDF]

open access: goldCell Reports, 2014
The reversible phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF2α) is a highly conserved signal implicated in the cellular adaptation to numerous stresses such as the one caused by amino acid limitation.
Anne-Catherine Maurin   +15 more
doaj   +2 more sources

PKR and GCN2 stress kinases promote an ER stress-independent eIF2α phosphorylation responsible for calreticulin exposure in melanoma cells [PDF]

open access: goldOncoImmunology, 2018
The immunogenic cell death (ICD) process represents a novel therapeutic approach to treat tumours, in which cytotoxic compounds promote both cancer cell death and the emission of damage-associated molecular patterns (DAMPs) from dying cells, to activate ...
Paola Giglio   +10 more
doaj   +2 more sources

Regulation of G1 Arrest and Apoptosis in Hypoxia by PERK and GCN2-Mediated eIF2α Phosphorylation

open access: goldNeoplasia: An International Journal for Oncology Research, 2010
Hypoxia is a common microenvironment in solid tumors and is correlated with tumor progression by regulating cancer cell survival. Recent studies suggest that activation of double-stranded RNA-dependent protein kinase-like endoplasmic reticulum-related ...
Yan Liu   +6 more
doaj   +2 more sources

Genetic inhibition of phosphorylation of the translation initiation factor eIF2α does not block Aβ-dependent elevation of BACE1 and APP levels or reduce amyloid pathology in a mouse model of Alzheimer's disease. [PDF]

open access: goldPLoS ONE, 2014
β-site amyloid precursor protein (APP) cleaving enzyme 1 (BACE1) initiates the production of β-amyloid (Aβ), the major constituent of amyloid plaques in Alzheimer's disease (AD).
Katherine R Sadleir   +4 more
doaj   +3 more sources

تأثیر شش هفته تمرین هوازی بر بیان ژن‌های استرس اکسیداتیو شبکه آندوپلاسمی (X-box Binding Protein-1 و Eukaryotic Initiation Factor-2α) در بافت قلب موش‌های صحرایی نر دیابتی شده با استرپتوزوتوسین [PDF]

open access: yesمجله دانشکده پزشکی اصفهان, 2022
مقدمه: هدف از انجام پژوهش حاضر، بررسی تأثیر شش هفته تمرین هوازی بر بیان ژن‌های استرس اکسیداتیو شبکه‌ی آندوپلاسمی (Endoplasmic reticulum یا ER) شامل عامل شروع‌کننده‌ی ترجمه‌ی یوکاریوتی 2 (Eukaryotic Initiation Factor-2α یا eIF2α) و پروتئین ...
معصومه حسین‌زاده   +1 more
doaj   +1 more source

Modulation of GCN2 activity under excess light stress by osmoprotectants and amino acids

open access: yesPlant Signaling & Behavior, 2022
The protein kinase GCN2 (General Control Nonderepressible2) and its phosphorylation target, the eukaryotic translation initiation factor (eIF)2α represent the core module of the plant’s integrated stress response, a signaling pathway widely conserved in ...
Ansul Lokdarshi   +2 more
doaj   +1 more source

GCN2 upregulates autophagy in response to short-term deprivation of a single essential amino acid

open access: yesAutophagy Reports, 2022
The ability to adapt the proteolysis rates based on fluctuations in essential amino acid (EAA) availability is essential for life. The GCN2-eIF2α-ATF4 signaling pathway is involved in the adaptive response to EAA deprivations.
Anne-Catherine Maurin   +14 more
doaj   +1 more source

Glucose-stimulated Protein Synthesis in Pancreatic β-Cells Parallels an Increase in the Availability of the Translational Ternary Complex (eIF2-GTP·Met-tRNAi) and the Dephosphorylation of eIF2α [PDF]

open access: yesJournal of Biological Chemistry, 2004
In pancreatic beta-cells, glucose causes a rapid increase in the rate of protein synthesis. However, the mechanism by which this occurs is poorly understood. In this report, we demonstrate, in the pancreatic beta-cell line MIN6, that glucose stimulates the recruitment of ribosomes onto the mRNA, indicative of an increase in the rate of the initiation ...
E. Gomez   +3 more
openaire   +3 more sources

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