IRE1 signaling affects cell fate during the unfolded protein response - Wikidata - wikimedia - TriplyDB

IRE1 signaling affects cell fate during the unfolded protein response

IRE1 signaling affects cell fate during the unfolded protein response

http://www.wikidata.org/entity/Q29615502

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HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease A crucial role for RACK1 in the regulation of glucose-stimulated IRE1alpha activation in pancreatic beta cells A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation Bifunctional apoptosis regulator (BAR), an endoplasmic reticulum (ER)-associated E3 ubiquitin ligase, modulates BI-1 protein stability and function in ER Stress BAX inhibitor-1 is a negative regulator of the ER stress sensor IRE1alpha A dual role for EDEM1 in the processing of rod opsin X-linked cone dystrophy caused by mutation of the red and green cone opsins CNOT2 depletion disrupts and inhibits the CCR4-NOT deadenylase complex and induces apoptotic cell death The role of the CNOT1 subunit of the CCR4-NOT complex in mRNA deadenylation and cell viability Divergent allosteric control of the IRE1α endoribonuclease using kinase inhibitors Identification of Toyocamycin, an agent cytotoxic for multiple myeloma cells, as a potent inhibitor of ER stress-induced XBP1 mRNA splicing A CHOP-regulated microRNA controls rhodopsin expression Endoplasmic reticulum stress and the inflammatory basis of metabolic disease One step at a time: endoplasmic reticulum-associated degradation Apoptosis, autophagy and unfolded protein response pathways in Arbovirus replication and pathogenesis Endoplasmic Reticulum Stress in the Diabetic Kidney, the Good, the Bad and the Ugly Protein Folding and Mechanisms of Proteostasis Neuronal endoplasmic reticulum stress in axon injury and neurodegeneration Emerging functions of the unfolded protein response in immunity Xenobiotic perturbation of ER stress and the unfolded protein response The unfolded protein response and diabetic retinopathy The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology The regulation of the autophagic network and its implications for human disease Pathological impact of hepatitis B virus surface proteins on the liver is associated with the host genetic background Autophagy attenuates diabetic glomerular damage through protection of hyperglycemia-induced podocyte injury XBP1 mitigates aminoglycoside-induced endoplasmic reticulum stress and neuronal cell death.Inactivation of VCP/ter94 suppresses retinal pathology caused by misfolded rhodopsin in Drosophila Divergent effects of PERK and IRE1 signaling on cell viability Coronavirus Infection Modulates the Unfolded Protein Response and Mediates Sustained Translational Repression Structure and mechanism of action of the hydroxy–aryl–aldehyde class of IRE1 endoribonuclease inhibitors The unfolded protein response signals through high-order assembly of Ire1 Crystal Structure of P58(IPK) TPR Fragment Reveals the Mechanism for its Molecular Chaperone Activity in UPR ER stress and apoptosis: a new mechanism for retinal cell death.Axon injury induced endoplasmic reticulum stress and neurodegeneration Cold-inducible proteins CIRP and RBM3, a unique couple with activities far beyond the cold Oxidative stress, unfolded protein response, and apoptosis in developmental toxicity Hepatoprotective role of Sestrin2 against chronic ER stress The cytosolic chaperone Hsc70 promotes traffic to the cell surface of intracellular retained melanocortin-4 receptor mutants

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IRE1 signaling affects cell fate during the unfolded protein response

http://www.wikidata.org/entity/Q29615502

description

2007 nî lūn-bûn

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2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

IRE1 signaling affects cell fate during the unfolded protein response

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IRE1 signaling affects cell fate during the unfolded protein response

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type

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IRE1 signaling affects cell fate during the unfolded protein response

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IRE1 signaling affects cell fate during the unfolded protein response

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IRE1 signaling affects cell fate during the unfolded protein response

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IRE1 signaling affects cell fate during the unfolded protein response

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IRE1 signaling affects cell fate during the unfolded protein response

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Cohen HR

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

Lavail MM

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

Li H

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Lin JH

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

Panning B

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

Shokat KM

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Walter P

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Yasumura D

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Zhang C

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

P2860

Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy

Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress

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

ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs

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

Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain

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

Signal integration in the endoplasmic reticulum unfolded protein response

IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

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318

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