Activation of PERK signaling attenuates Abeta-mediated ER stress. - Wikidata - awgldk - TriplyDB

Activation of PERK signaling attenuates Abeta-mediated ER stress.

Activation of PERK signaling attenuates Abeta-mediated ER stress.

http://www.wikidata.org/entity/Q33576967

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The endoplasmic reticulum stress response in aging and age-related diseases Killing Me Softly: Connotations to Unfolded Protein Response and Oxidative Stress in Alzheimer's Disease The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in Neurodegeneration Experimental Evidence Shows Salubrinal, an eIF2α Dephosphorylation Inhibitor, Reduces Xenotoxicant-Induced Cellular Damage Mechanism-based screen for G1/S checkpoint activators identifies a selective activator of EIF2AK3/PERK signalling The small molecule '1-(4-biphenylylcarbonyl)-4-(5-bromo-2-methoxybenzyl) piperazine oxalate' and its derivatives regulate global protein synthesis by inactivating eukaryotic translation initiation factor 2-alpha Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease.Role of Endoplasmic Reticulum Stress in Learning and Memory Impairment and Alzheimer's Disease-Like Neuropathology in the PS19 and APPSwe Mouse Models of Tauopathy and Amyloidosis.Functional characterization of the ER stress induced X-box-binding protein-1 (Xbp-1) in the porcine system miRNAs at the interface of cellular stress and disease ER stress response plays an important role in aggregation of α-synuclein Deletion of the eIF2α Kinase GCN2 fails to rescue the memory decline associated with Alzheimer's disease.Rifampicin protects PC12 cells from rotenone-induced cytotoxicity by activating GRP78 via PERK-eIF2α-ATF4 pathway.Regulation of subtilase cytotoxin-induced cell death by an RNA-dependent protein kinase-like endoplasmic reticulum kinase-dependent proteasome pathway in HeLa cells Mitochondrial- and endoplasmic reticulum-associated oxidative stress in Alzheimer's disease: from pathogenesis to biomarkers.ABCA7 Deficiency Accelerates Amyloid-β Generation and Alzheimer's Neuronal Pathology.Modulation of 5-lipoxygenase in proteotoxicity and Alzheimer's disease.Roles of eIF2α kinases in the pathogenesis of Alzheimer's disease.Loss of endoplasmic reticulum Ca2+ homeostasis: contribution to neuronal cell death during cerebral ischemia.Signaling pathways involved in endoplasmic reticulum stress-induced neuronal apoptosis.The unfolded protein response in Alzheimer's disease.Functional and morphological impact of ER stress on mitochondria.Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging.Signaling pathways from the endoplasmic reticulum and their roles in disease Endoplasmic reticulum dysfunction in Alzheimer's disease.Endoplasmic reticulum stress as a novel neuronal mediator in Alzheimer's disease.ATF4 orchestrates a program of BH3-only protein expression in severe hypoxia.Brain metabolic stress and neuroinflammation at the basis of cognitive impairment in Alzheimer's disease miR-98-5p Acts as a Target for Alzheimer's Disease by Regulating Aβ Production Through Modulating SNX6 Expression.The entangled ER-mitochondrial axis as a potential therapeutic strategy in neurodegeneration: A tangled duo unchained.Avarol induces apoptosis in pancreatic ductal adenocarcinoma cells by activating PERK-eIF2α-CHOP signaling.The unfolded protein response in the therapeutic effect of hydroxy-DHA against Alzheimer's disease.The integrated stress response.The role of endoplasmic reticulum stress in neurodegenerative disease.Endoplasmic reticulum-mediated unfolded protein response and mitochondrial apoptosis in cancer.Hypoxia-triggered m-calpain activation evokes endoplasmic reticulum stress and neuropathogenesis in a transgenic mouse model of Alzheimer's disease.Modulation of AβPP and GSK3β by Endoplasmic Reticulum Stress and Involvement in Alzheimer's Disease.Sevoflurane-Induced Endoplasmic Reticulum Stress Contributes to Neuroapoptosis and BACE-1 Expression in the Developing Brain: The Role of eIF2α.HtrA2/Omi is involved in 6-OHDA-induced endoplasmic reticulum stress in SH-SY5Y cells.ER Stress and Neurodegenerative Disease: A Cause or Effect Relationship?

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Activation of PERK signaling attenuates Abeta-mediated ER stress.

http://www.wikidata.org/entity/Q33576967

description

2010 nî lūn-bûn

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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2010 թվականի մայիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@ast

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@en

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@nl

type

label

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@ast

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@en

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@nl

prefLabel

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@ast

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@en

Activation of PERK signaling attenuates Abeta-mediated ER stress.

@nl

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Activation of PERK signaling attenuates Abeta-mediated ER stress.

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Dae Kyong Kim

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Do Hee Kim

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Do Yeon Lee

http://www.w3.org/2001/XMLSchema#string

Hee-Yeon Jung

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Hyun Jung Lee

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Jun Young Lee

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Kyu-Sun Lee

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Sang Hyung Lee

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Sung Su Kim

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Won Bok Lee

http://www.w3.org/2001/XMLSchema#string

P2860

Roles of CHOP/GADD153 in endoplasmic reticulum stress

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The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response

Translational control is required for the unfolded protein response and in vivo glucose homeostasis

S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration

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A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress

Reduced eIF2alpha phosphorylation and increased proapoptotic proteins in aging

Endoplasmic reticulum stress inhibition protects against excitotoxic neuronal injury in the rat brain

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