The ER stress factor XBP1s prevents amyloid-beta neurotoxicity - Test2 - elhamkhani - TriplyDB

The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

http://www.wikidata.org/entity/Q24598012

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Neuronal endoplasmic reticulum stress in axon injury and neurodegeneration Drosophila as a model for unfolded protein response research Integration of UPRER and oxidative stress signaling in the control of intestinal stem cell proliferation Modeling the complex pathology of Alzheimer's disease in Drosophila Neuronal processing of noxious thermal stimuli mediated by dendritic Ca(2+) influx in Drosophila somatosensory neurons.The amyotrophic lateral sclerosis 8 protein, VAP, is required for ER protein quality control Tat-haFGF14-154 Upregulates ADAM10 to Attenuate the Alzheimer Phenotype of APP/PS1 Mice through the PI3K-CREB-IRE1α/XBP1 Pathway.Activation of JNK signaling mediates amyloid-ß-dependent cell death.Using membrane-targeted green fluorescent protein to monitor neurotoxic protein-dependent degeneration of Drosophila eyes Compensatory Motor Neuron Response to Chromatolysis in the Murine hSOD1(G93A) Model of Amyotrophic Lateral Sclerosis Drosophila XBP1 expression reporter marks cells under endoplasmic reticulum stress and with high protein secretory load.Novel neuroprotective function of apical-basal polarity gene crumbs in amyloid beta 42 (aβ42) mediated neurodegeneration Homeotic Gene teashirt (tsh) has a neuroprotective function in amyloid-beta 42 mediated neurodegeneration.A dopamine receptor contributes to paraquat-induced neurotoxicity in Drosophila.Dissociation of mitochondrial from sarcoplasmic reticular stress in Drosophila cardiomyopathy induced by molecularly distinct mitochondrial fusion defects.Ire1 mediated mRNA splicing in a C-terminus deletion mutant of Drosophila Xbp1 Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation.Drosophila Eye Model to Study Neuroprotective Role of CREB Binding Protein (CBP) in Alzheimer's Disease.Drosophila models of proteinopathies: the little fly that could.Mitochondrial- and endoplasmic reticulum-associated oxidative stress in Alzheimer's disease: from pathogenesis to biomarkers.Differential activation of the ER stress factor XBP1 by oligomeric assemblies Serum Amyloid P Component Ameliorates Neurological Damage Caused by Expressing a Lysozyme Variant in the Central Nervous System of Drosophila melanogaster.Anti-Aβ single-chain variable fragment antibodies exert synergistic neuroprotective activities in Drosophila models of Alzheimer's disease Direct Keap1-Nrf2 disruption as a potential therapeutic target for Alzheimer's disease.XBP1 depletion precedes ubiquitin aggregation and Golgi fragmentation in TDP-43 transgenic rats.Expression of amyloid-β in mouse cochlear hair cells causes an early-onset auditory defect in high-frequency sound perception.Purification of transcripts and metabolites from Drosophila heads Uncoupling neuronal death and dysfunction in Drosophila models of neurodegenerative disease Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation Polar substitutions in helix 3 of the prion protein produce transmembrane isoforms that disturb vesicle trafficking.Holdase activity of secreted Hsp70 masks amyloid-β42 neurotoxicity in Drosophila Increased Glucose Transport into Neurons Rescues Aβ Toxicity in Drosophila.The Role of IRE-XBP1 Pathway in Regulation of Retinal Pigment Epithelium Tight Junctions.ER-stress in Alzheimer's disease: turning the scale?Reduction of endoplasmic reticulum stress attenuates the defects caused by Drosophila mitofusin depletion.Spliced X-box binding protein 1 couples the unfolded protein response to hexosamine biosynthetic pathway.Role of unfolded protein response dysregulation in oxidative injury of retinal pigment epithelial cells.Drosophila enhancer-Gal4 lines show ectopic expression during development.The unfolded protein response in Alzheimer's disease.Functional and morphological impact of ER stress on mitochondria.

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The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

http://www.wikidata.org/entity/Q24598012

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

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The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

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The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

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type

label

The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

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The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

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The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

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prefLabel

The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

@ast

The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

@en

The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

@nl

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Human Molecular Genetics

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The ER stress factor XBP1s prevents amyloid-beta neurotoxicity

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Diego E Rincon-Limas

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

Jonatan Sanchez-Garcia

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

Melisa Gomez-Velazquez

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

Pedro Fernandez-Funez

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Yan Zhang

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P2860

XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

Protective effect against Parkinson's disease-related insults through the activation of XBP1

XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy

Unfolded protein response in a Drosophila model for retinal degeneration

Signal integration in the endoplasmic reticulum unfolded protein response

Targeted gene expression as a means of altering cell fates and generating dominant phenotypes

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

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

Proteasome inhibitors disrupt the unfolded protein response in myeloma cells

APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy

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2144-2160

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scholarly article

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526528

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10.1093/HMG/DDR100

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11

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20

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Sergio Casas-Tintó

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2011-03-09T00:00:00Z

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50351136

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21389082

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3090193

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