Endoplasmic Reticulum To Nucleus Signaling 2 (ERN2) ELISA Kits

Mouse (Murine) Endoplasmic Reticulum To Nucleus Signaling 2 (ERN2) interaction partners

1. Data show that LPS induces endoplasmic reticulum (ER) stress and P300 activity via the XBP1/IRE1 pathway.

2. Regulated IRE1-dependent mRNA decay sets the threshold for dendritic cell survival.

3. Data show that EIF2AK3/PERK-mediated downregulation of miR-424(322)-503 cluster regulates optimal activation of IRE1 protein and activating transcription factor 6 (ATF6) during conditions of endoplasmic reticulum stress.

4. Our results reveal a role for IRE1 in preventing a cell death-initializing step that emanates from the ER and provide a potential target for treating diseases characterized by ER stress, including diabetes and Wolfram syndrome.

5. Our data indicate that removal of XBP-1 confers a kinetic delay in early stages of MCMV infection and suggest that the late targeting of IRE1 is aimed at inhibiting activities other than the splicing of XBP-1 mRNA

6. ER stress accentuated CVB3-induced myocardial inflammation through the IRE1-associated NF-kappaB pathway.

7. This study provides the first in vivo evidence that PP2Ce is an essential regulator of normal lactation, possibly involving IRE1 signaling and endoplasmic reticulum stress regulation in mammary epithelium.

8. suggest that activation of IRE1-JNK pathway is a key linker of impaired hepatic insulin signaling transduction induced by HFru feeding

9. Regulated IRE1-dependent decay participates in curtailing immunoglobulin secretion from plasma cells.

10. Regulated IRE1-dependent decay pathway is activated during Japanese encephalitis virus and benefits viral replication.

11. required for airway epithelial mucin production

12. findings suggest that in goblet cells, IRE1beta, but not IRE1alpha, promotes efficient protein folding and secretion in the ER by optimizing the level of mRNA encoding their major secretory product, MUC2

13. Ire1beta regulates intestinal lipid absorption and that increased intestinal lipoprotein production contributes to atherosclerosis.

14. Inhibition of IRE1 endonuclease activity does not sensitize cells to the consequences of acute endoplasmic reticulum stress, but rather interferes with the expansion of secretory capacity.

15. early DENV-2 infection triggers and then suppresses PERK-mediated eIF2alpha phosphorylation and that in mid and late DENV-2 infection, the IRE1-XBP1 and ATF6 pathways are activated, respectively

16. Transcriptional and posttranscriptional mechanisms involving NR2F1 and IRE1beta ensure low microsomal triglyceride transfer protein expression in undifferentiated intestinal cells and avoid apolipoprotein B lipoprotein biosynthesis.

17. Endoplasmic reticulum stress blunts cytokine-triggered activation of NF-kappaB, in part through PERK- and IRE1-mediated preferential induction of C/EBPbeta.

18. IRE1-mediated unconventional mRNA splicing is involved in regulating XBP1 in signaling the unfolded protein response.

19. IRE1alpha, an ER-resident protein kinase, has a crucial function in insulin biosynthesis. IRE1alpha phosphorylation is coupled to insulin biosynthesis in response to transient exposure to high glucose.

20. Mouse hepatitis virus infection activates the Ire1/XBP1 pathway of the unfolded protein response

Human Endoplasmic Reticulum To Nucleus Signaling 2 (ERN2) interaction partners

1. ER stress-regulated IRE1 dependent decay is involved in regulation of hepatic diseases. (review)

2. The luminal event mediated by IRE1beta involves direct interaction with unfolded proteins rather than association/dissociation with BiP.

3. Data show that IRE1beta represses translation on the ER membrane but not in the cytosol, and that this selective repression depends on the RNase activity of IRE1beta.

4. The structural, biochemical, and functional studies in vivo altogether demonstrate that IRE1 and PERK have conserved a common molecular interface necessary and sufficient for dimerization and unfolded protein response (UPR) signaling.

5. RNase domain of IRE1 determines the functional specificities of each of these isoforms.