Divergent effects of PERK and IRE1 signaling on cell viability - Wikidata - thesis-toulmin - TriplyDB

Divergent effects of PERK and IRE1 signaling on cell viability

Divergent effects of PERK and IRE1 signaling on cell viability

http://www.wikidata.org/entity/Q27438124

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HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction Differential regulation of endoplasmic reticulum stress by protein tyrosine phosphatase 1B and T cell protein tyrosine phosphatase Xenobiotic perturbation of ER stress and the unfolded protein response Neurodegeneration and unfolded-protein response in mice expressing a membrane-tethered flexible tail of PrP Crystal Structure of P58(IPK) TPR Fragment Reveals the Mechanism for its Molecular Chaperone Activity in UPR Inflammation and cellular stress: a mechanistic link between immune-mediated and metabolically driven pathologies Inhibition of Eukaryotic Initiation Factor 2 Alpha Phosphatase Reduces Tissue Damage and Improves Learning and Memory after Experimental Traumatic Brain Injury Endoplasmic reticulum stress stimulates p53 expression through NF-κB activation Combined Gene Expression and RNAi Screening to Identify Alkylation Damage Survival Pathways from Fly to Human Age-enhanced endoplasmic reticulum stress contributes to increased Atg9A inhibition of STING-mediated IFN-β production during Streptococcus pneumoniae infection Pharmacological modulation of the retinal unfolded protein response in Bardet-Biedl syndrome reduces apoptosis and preserves light detection ability The effects of IRE1, ATF6, and PERK signaling on adRP-linked rhodopsins Low intensity focused ultrasound (LOFU) modulates unfolded protein response and sensitizes prostate cancer to 17AAG.Persistent ER stress induces the spliced leader RNA silencing pathway (SLS), leading to programmed cell death in Trypanosoma brucei.Activation of the unfolded protein response contributes toward the antitumor activity of vorinostat.Linking ER Stress to Autophagy: Potential Implications for Cancer Therapy.Inhibition of stearoyl-CoA desaturase 1 expression induces CHOP-dependent cell death in human cancer cells.Effect of exercise intensity on unfolded protein response in skeletal muscle of rat.A mouse model for inherited renal fibrosis associated with endoplasmic reticulum stress.Acetaminophen and NAPQI are toxic to auditory cells via oxidative and endoplasmic reticulum stress-dependent pathways.Transcriptional profiling of chondrodysplasia growth plate cartilage reveals adaptive ER-stress networks that allow survival but disrupt hypertrophy Impaired tissue growth is mediated by checkpoint kinase 1 (CHK1) in the integrated stress response.Role of CAAT/enhancer binding protein homologous protein in panobinostat-mediated potentiation of bortezomib-induced lethal endoplasmic reticulum stress in mantle cell lymphoma cells.Trans-splicing in trypanosomes: machinery and its impact on the parasite transcriptome.Fucoidan induces cancer cell apoptosis by modulating the endoplasmic reticulum stress cascades.A BAX/BAK and cyclophilin D-independent intrinsic apoptosis pathway C/EBP homologous protein (CHOP) deficiency aggravates hippocampal cell apoptosis and impairs memory performance Activation of the cellular unfolded protein response by recombinant adeno-associated virus vectors.Allosteric inhibition of the IRE1α RNase preserves cell viability and function during endoplasmic reticulum stress.Endoplasmic reticulum stress signaling is involved in mitomycin C (MMC)-induced apoptosis in human fibroblasts via PERK pathway.Remodeling the proteostasis network to rescue glucocerebrosidase variants by inhibiting ER-associated degradation and enhancing ER folding.Loss of subcellular lipid transport due to ARV1 deficiency disrupts organelle homeostasis and activates the unfolded protein response Using temporal genetic switches to synchronize the unfolded protein response in cell populations in vivo.C-C chemokine receptor 2 inhibitor ameliorates hepatic steatosis by improving ER stress and inflammation in a type 2 diabetic mouse model.The unfolded protein response is a major mechanism by which LRP1 regulates Schwann cell survival after injury.The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress.Pancreatic endoplasmic reticulum kinase activation promotes medulloblastoma cell migration and invasion through induction of vascular endothelial growth factor A Unfolding the unfolded protein response: unique insights into brain ischemia.Activation of the unfolded protein response pathway causes ceramide accumulation in yeast and INS-1E insulinoma cells.The unpredictability of prolonged activation of stress response pathways.

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Divergent effects of PERK and IRE1 signaling on cell viability

http://www.wikidata.org/entity/Q27438124

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2009 nî lūn-bûn

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Divergent effects of PERK and IRE1 signaling on cell viability

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Divergent effects of PERK and IRE1 signaling on cell viability

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Divergent effects of PERK and IRE1 signaling on cell viability

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type

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Divergent effects of PERK and IRE1 signaling on cell viability

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Divergent effects of PERK and IRE1 signaling on cell viability

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Divergent effects of PERK and IRE1 signaling on cell viability

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Divergent effects of PERK and IRE1 signaling on cell viability

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Divergent effects of PERK and IRE1 signaling on cell viability

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Divergent effects of PERK and IRE1 signaling on cell viability

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Divergent effects of PERK and IRE1 signaling on cell viability

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Han Li

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

Jonathan H Lin

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Peter Walter

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Yuhong Zhang

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P2860

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

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

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

Signal integration in the endoplasmic reticulum unfolded protein response

Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.

Perk is essential for translational regulation and cell survival during the unfolded protein response

Proteasome inhibitors disrupt the unfolded protein response in myeloma cells

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

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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