Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress. - Wikidata - wikimedia - TriplyDB

Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress.

Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress.

http://www.wikidata.org/entity/Q35221396

about

The unfolded protein response induces the angiogenic switch in human tumor cells through the PERK/ATF4 pathway Cellular interplay between neurons and glia: toward a comprehensive mechanism for excitotoxic neuronal loss in neurodegeneration Melanoma and the Unfolded Protein Response Cancer Microenvironment and Endoplasmic Reticulum Stress Response Protein Folding and Mechanisms of Proteostasis The unfolded protein response in retinal vascular diseases: implications and therapeutic potential beyond protein folding The stress-regulated transcription factor CHOP promotes hepatic inflammatory gene expression, fibrosis, and oncogenesis Cellular stress response and innate immune signaling: integrating pathways in host defense and inflammation.PERK Integrates Oncogenic Signaling and Cell Survival During Cancer Development IRES-mediated translation of utrophin A is enhanced by glucocorticoid treatment in skeletal muscle cells Regulation of PERK signaling and leukemic cell survival by a novel cytosolic isoform of the UPR regulator GRP78/BiP De-differentiation confers multidrug resistance via noncanonical PERK-Nrf2 signaling Elaborate uORF/IRES features control expression and localization of human glycyl-tRNA synthetase Tumorigenic and Immunosuppressive Effects of Endoplasmic Reticulum Stress in Cancer The unfolded protein response in immunity and inflammation Endoplasmic Reticulum Stress, Unfolded Protein Response, and Cancer Cell Fate PERK regulates the proliferation and development of insulin-secreting beta-cell tumors in the endocrine pancreas of mice RNAi screen of endoplasmic reticulum-associated host factors reveals a role for IRE1alpha in supporting Brucella replication.Transcriptional regulation of VEGF-A by the unfolded protein response pathway.Regulation of G(1) arrest and apoptosis in hypoxia by PERK and GCN2-mediated eIF2alpha phosphorylation.New Insights into the Pathogenesis of Alcohol-Induced ER Stress and Liver Diseases Nonsense-mediated RNA decay regulation by cellular stress: implications for tumorigenesis.Structural determinants of PERK inhibitor potency and selectivity Integrated transcriptomic response to cardiac chronic hypoxia: translation regulators and response to stress in cell survival.Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease.Stressed to death: targeting endoplasmic reticulum stress response induced apoptosis in gliomas.Stress signaling and the shaping of the mammary tissue in development and cancer.PERK promotes cancer cell proliferation and tumor growth by limiting oxidative DNA damage Generation and characterization of an analog-sensitive PERK allele.C/EBP homologous protein (CHOP) deficiency aggravates hippocampal cell apoptosis and impairs memory performance Cell-extrinsic effects of tumor ER stress imprint myeloid dendritic cells and impair CD8⁺ T cell priming.The Unfolded Protein Response, Degradation from Endoplasmic Reticulum and Cancer Dual activators of protein kinase R (PKR) and protein kinase R-like kinase PERK identify common and divergent catalytic targets.Intersection of the unfolded protein response and hepatic lipid metabolism Lipid phosphate phosphatase-3 regulates tumor growth via β-catenin and CYCLIN-D1 signaling.PERK integrates autophagy and oxidative stress responses to promote survival during extracellular matrix detachment.Translational regulation in nutrigenomics.PERK-mediated Autophagy in Osteosarcoma Cells Resists ER Stress-induced Cell Apoptosis Signaling through alternative Integrated Stress Response pathways compensates for GCN2 loss in a mouse model of soft tissue sarcoma Identification of mRNAs that continue to associate with polysomes during hypoxia.

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P2860

Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress.

http://www.wikidata.org/entity/Q35221396

description

2006 nî lūn-bûn

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2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Perk-dependent translational r ...... in response to hypoxic stress.

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Perk-dependent translational r ...... in response to hypoxic stress.

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type

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Perk-dependent translational r ...... in response to hypoxic stress.

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Perk-dependent translational r ...... in response to hypoxic stress.

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Perk-dependent translational r ...... in response to hypoxic stress.

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Perk-dependent translational r ...... in response to hypoxic stress.

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Molecular and Cellular Biology

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Perk-dependent translational r ...... in response to hypoxic stress.

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P2093

Christina L Addison

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Huijun Zhao

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Jaime D Blais

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Kishore Wary

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Robert Edge

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P2860

Superinduction of metallothionein I by inhibition of protein synthesis: role of a labile repressor in MTF-1 mediated gene transcription

Gene expression during acute and prolonged hypoxia is regulated by distinct mechanisms of translational control.

Murine lipid phosphate phosphohydrolase-3 acts as a cell-associated integrin ligand

Grb10 prevents Nedd4-mediated vascular endothelial growth factor receptor-2 degradation

Hypoxia-inducible factor-1alpha mRNA contains an internal ribosome entry site that allows efficient translation during normoxia and hypoxia

Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha.

Hypoxia inhibits protein synthesis through a 4E-BP1 and elongation factor 2 kinase pathway controlled by mTOR and uncoupled in breast cancer cells

Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene

Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival

Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP

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9517-9532

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scholarly article

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10.1128/MCB.01145-06

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24

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26

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Heather P Harding

Costas Koumenis

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2006-10-09T00:00:00Z

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6763829

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17030613

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1698539

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