(Q38245870)

English

Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 3. Orchestrating the unfolded protein response in oncogenesis: an update

scientific article published on 03 September 2014

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 3. Orchestrating the unfolded protein response in oncogenesis: an update (English)

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

endoplasmic reticulum

0 references

author name string

Serge N Manié

1

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

Justine Lebeau

2

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

Eric Chevet

3

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

publication date

3 September 2014

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

American Journal of Physiology - Cell Physiology

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

307

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

10

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

C901-7

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

Paneth cells as a site of origin for intestinal inflammation.

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Transformation-associated gene regulation by ATF6alpha during hepatocarcinogenesis

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Inositol-requiring enzyme 1alpha is a key regulator of angiogenesis and invasion in malignant glioma

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Adapting proteostasis for disease intervention

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

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XBP1 promotes triple-negative breast cancer by controlling the HIF1α pathway

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Circadian clock-coordinated 12 Hr period rhythmic activation of the IRE1alpha pathway controls lipid metabolism in mouse liver

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Autocrine control of glioma cells adhesion and migration through IRE1α-mediated cleavage of SPARC mRNA.

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Anti-oncogenic role of the endoplasmic reticulum differentially activated by mutations in the MAPK pathway.

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Hexosamine pathway metabolites enhance protein quality control and prolong life.

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IRE1 signaling is essential for ischemia-induced vascular endothelial growth factor-A expression and contributes to angiogenesis and tumor growth in vivo.

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Epithelial-to-mesenchymal transition activates PERK-eIF2α and sensitizes cells to endoplasmic reticulum stress

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Allosteric inhibition of the IRE1α RNase preserves cell viability and function during endoplasmic reticulum stress.

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Patterns of somatic mutation in human cancer genomes

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Integrated analysis of somatic mutations and focal copy-number changes identifies key genes and pathways in hepatocellular carcinoma

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Hallmarks of Cancer: The Next Generation

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

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ER stress-mediated autophagy promotes Myc-dependent transformation and tumor growth

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Targeting the unfolded protein response in disease.

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Endoplasmic reticulum stress-activated transcription factor ATF6α requires the disulfide isomerase PDIA5 to modulate chemoresistance

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p58(IPK)-mediated attenuation of the proapoptotic PERK-CHOP pathway allows malignant progression upon low glucose.

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Clock and ATF4 transcription system regulates drug resistance in human cancer cell lines

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Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1

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VEGF Signals through ATF6 and PERK to promote endothelial cell survival and angiogenesis in the absence of ER stress.

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Nck-1 antagonizes the endoplasmic reticulum stress-induced inhibition of translation

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The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins

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GRP78 induction in cancer: therapeutic and prognostic implications.

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FGF-2 prevents cancer cells from ER stress-mediated apoptosis via enhancing proteasome-mediated Nck degradation

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Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis

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The role of the unfolded protein response in tumour development: friend or foe?

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Getting RIDD of RNA: IRE1 in cell fate regulation

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Dppa5 improves hematopoietic stem cell activity by reducing endoplasmic reticulum stress

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Integrated endoplasmic reticulum stress responses in cancer

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ER stress cooperates with hypernutrition to trigger TNF-dependent spontaneous HCC development

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Nck-dependent activation of extracellular signal-regulated kinase-1 and regulation of cell survival during endoplasmic reticulum stress

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ER stress transcription factor Xbp1 suppresses intestinal tumorigenesis and directs intestinal stem cells

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Glucose starvation induces cell death in K-ras-transformed cells by interfering with the hexosamine biosynthesis pathway and activating the unfolded protein response

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Posttranscriptional regulation of PER1 underlies the oncogenic function of IREα.

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HIF-2α protects human hematopoietic stem/progenitors and acute myeloid leukemic cells from apoptosis induced by endoplasmic reticulum stress.

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Regulation of basal cellular physiology by the homeostatic unfolded protein response

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ATF6alpha-Rheb-mTOR signaling promotes survival of dormant tumor cells in vivo

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Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress

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The unfolded protein response governs integrity of the haematopoietic stem-cell pool during stress.

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Spliced X-box binding protein 1 couples the unfolded protein response to hexosamine biosynthetic pathway

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Toll-like receptor activation suppresses ER stress factor CHOP and translation inhibition through activation of eIF2B.

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Interaction of Nck1 and PERK phosphorylated at Y⁵⁶¹ negatively modulates PERK activity and PERK regulation of pancreatic β-cell proinsulin content

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Identifiers

10.1152/AJPCELL.00292.2014

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 August 2017

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