Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. - Test2 - elhamkhani - TriplyDB

Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis.

Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis.

http://www.wikidata.org/entity/Q36393034

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XBP1 mRNA splicing triggers an autophagic response in endothelial cells through BECLIN-1 transcriptional activation The ER stress factor XBP1s prevents amyloid-beta neurotoxicity XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy XBP-1 regulates signal transduction, transcription factors and bone marrow colonization in B cells Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases Protein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applications Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction Control of dopaminergic neuron survival by the unfolded protein response transcription factor XBP1 The bHLH transcription factor CHF1/Hey2 regulates susceptibility to apoptosis and heart failure after pressure overload.The Role of Unfolded Protein Response and Mitogen-Activated Protein Kinase Signaling in Neurodegenerative Diseases with Special Focus on Prion Diseases Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease.The PERK arm of the unfolded protein response regulates satellite cell-mediated skeletal muscle regeneration Altered Ca2+ homeostasis induces Calpain-Cathepsin axis activation in sporadic Creutzfeldt-Jakob disease XBP-1-deficient plasmablasts show normal protein folding but altered glycosylation and lipid synthesis.Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress.Cellular Stress in the Context of an Inflammatory Environment Supports TGF-β-Independent T Helper-17 Differentiation.Activation of pro-survival CaMK4β/CREB and pro-death MST1 signaling at early and late times during a mouse model of prion disease.Protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity.RTCB-1 mediates neuroprotection via XBP-1 mRNA splicing in the unfolded protein response pathway.Dual and opposing roles of the unfolded protein response regulated by IRE1alpha and XBP1 in proinsulin processing and insulin secretion.Getting the better of ER stress.Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy.Transcription factor CHF1/Hey2 regulates EC coupling and heart failure in mice through regulation of FKBP12.6.Differential activation of the ER stress factor XBP1 by oligomeric assemblies Familial prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP.Activation of the unfolded protein response promotes axonal regeneration after peripheral nerve injury Bortezomib alleviates drug-induced liver injury by regulating CYP2E1 gene transcription.Autoantibody-boosted T-cell reactivation in the target organ triggers manifestation of autoimmune CNS disease.Interplay of endoplasmic reticulum stress and autophagy in neurodegenerative disorders.From endoplasmic-reticulum stress to the inflammatory response.XBP1 governs late events in plasma cell differentiation and is not required for antigen-specific memory B cell development Molecular pathology of human prion diseases.De novo prion aggregates trigger autophagy in skeletal muscle.Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome.The Endoplasmic Reticulum Chaperone GRP78/BiP Modulates Prion Propagation in vitro and in vivo.Emerging roles for XBP1, a sUPeR transcription factor.Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration The role of the unfolded protein response in diabetes mellitus.Targeting the unfolded protein response in disease.

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P2860

Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis.

http://www.wikidata.org/entity/Q36393034

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2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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Unfolded protein response tran ...... n replication or pathogenesis.

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Unfolded protein response tran ...... n replication or pathogenesis.

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Unfolded protein response tran ...... n replication or pathogenesis.

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Unfolded protein response tran ...... n replication or pathogenesis.

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Unfolded protein response tran ...... n replication or pathogenesis.

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Proceedings of the National Academy of Sciences of the United States of America

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Unfolded protein response tran ...... on replication or pathogenesis

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Ann-Hwee Lee

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Claudio Hetz

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Claudio Soto

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Dennisse Gonzalez-Romero

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Laurie H Glimcher

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Peter Thielen

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P2860

Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta

Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1

Plasma cell differentiation requires the transcription factor XBP-1

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

ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats

Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53

Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

Unfolded protein response in a Drosophila model for retinal degeneration

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Prion protein family

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