PMID: 18086388, 15546383, 10526569 Binding of type I IFNs to their receptor (composed of the IFNAR1 and IFNAR2 subunits) activates the receptor-associated tyrosine kinases Jak1 and Tyk2 causing phosphorylation of the receptor and, subsequently, recruitment and phosphorylation of the Stat transcription factors

PMID: 18086388 The receptor-associated Jak1 and Jak2 tyrosine kinases are activated and phosphorylate the receptor, thereby generating a docking site for the SH2 domain of Stat1.

PMID: 18086388 The receptor-associated Jak1 and Jak2 tyrosine kinases are activated and phosphorylate the receptor, thereby generating a docking site for the SH2 domain of Stat1.

PMID: 18086388 After phosphorylation by Jaks Stat1:Stat1 dimers translocate to the nucleus and activate transcription by binding to the GAS elements of IFN-¦Ã responsive genes.

PMID: 18086388 After phosphorylation by Jaks Stat1:Stat1 dimers translocate to the nucleus and activate transcription by binding to the GAS elements of IFN-¦Ã responsive genes.

PMID: 18086388 After phosphorylation by Jaks Stat1:Stat1 dimers translocate to the nucleus and activate transcription by binding to the GAS elements of IFN-¦Ã responsive genes.

PMID: 18086388 After phosphorylation by Jaks Stat1:Stat1 dimers translocate to the nucleus and activate transcription by binding to the GAS elements of IFN-¦Ã responsive genes.

PMID: 18086388 After phosphorylation by Jaks Stat1:Stat1 dimers translocate to the nucleus and activate transcription by binding to the GAS elements of IFN-¦Ã responsive genes.

PMID: 18086388, 15972639 The work by Hu and colleagues shows that IFN-¦Ã suppresses the expression of the IL-1 receptor in macrophages making the cells refractory to IL-1

PMID: 18086388, 12553906 Twist proteins are transcriptional repressors that bind to the E-boxes in gene promoters, such as the TNF-¦Á promoter, and inhibit transcription

PMID: 18086388, 11067899 Both IFN-¦Á and IFN-¦Ã were found to decrease the IL-4 receptor gene expression

PMID: 18086388, 15546383, 10526569 Binding of type I IFNs to their receptor (composed of the IFNAR1 and IFNAR2 subunits) activates the receptor-associated tyrosine kinases Jak1 and Tyk2 causing phosphorylation of the receptor and, subsequently, recruitment and phosphorylation of the Stat transcription factors

PMID: 18086388 type I IFNs increase the amount of Twist proteins in cells and, consequently, the pre-treatment of macrophages with type I IFNs reduces the capability of immunoglobulin complexes or LPS to stimulate the NF-¦ÊB-mediated expression of TNF-¦Á.

PMID: 18086388 type I IFNs increase the amount of Twist proteins in cells and, consequently, the pre-treatment of macrophages with type I IFNs reduces the capability of immunoglobulin complexes or LPS to stimulate the NF-¦ÊB-mediated expression of TNF-¦Á.

PMID: 18086388 The up-regulation of Twist by IFNs was indirect and required the IFN-induced expression of the receptor tyrosine kinase Axl.

PMID: 18086388 type I IFNs increase the amount of Twist proteins in cells and, consequently, the pre-treatment of macrophages with type I IFNs reduces the capability of immunoglobulin complexes or LPS to stimulate the NF-¦ÊB-mediated expression of TNF-¦Á.

PMID: 18086388 type I IFNs increase the amount of Twist proteins in cells and, consequently, the pre-treatment of macrophages with type I IFNs reduces the capability of immunoglobulin complexes or LPS to stimulate the NF-¦ÊB-mediated expression of TNF-¦Á.

PMID: 18086388 type I IFNs increase the amount of Twist proteins in cells and, consequently, the pre-treatment of macrophages with type I IFNs reduces the capability of immunoglobulin complexes or LPS to stimulate the NF-¦ÊB-mediated expression of TNF-¦Á. PMID: 18086388 TTP limits the production of TNF-¦Á under these conditions

PMID: 18086388, 16571725 In their paper, Ho and Ivashkiv show that IFN-¦Á-activated Stat3 inhibited, in a dose-dependent manner, the transcription of genes that are regulated by Stat1:Stat1 homodimers while the transcription of the ISGF3 (Stat1:Stat2:IRF9) target genes remained unaffected.

PMID: 18086388 The up-regulation of Twist by IFNs was indirect and required the IFN-induced expression of the receptor tyrosine kinase Axl.

PMID: 18086388, 16571725 In their paper, Ho and Ivashkiv show that IFN-¦Á-activated Stat3 inhibited, in a dose-dependent manner, the transcription of genes that are regulated by Stat1:Stat1 homodimers while the transcription of the ISGF3 (Stat1:Stat2:IRF9) target genes remained unaffected.

PMID: 18086388 Stat1 is recruited to the TTP promoter regardless of p38 MAPK activation, but it requires p38 MAPK to become transcriptionally active.

PMID: 18086388, 11226159, 12671680, 14670297, 7543024 For full responses to both type I and type II IFNs the transactivation domain of Stat1 needs to be phosphorylated on serine 727

PMID: 18086388 Stat1 is recruited to the TTP promoter regardless of p38 MAPK activation, but it requires p38 MAPK to become transcriptionally active.

PMID: 18086388 We have demonstrated that both types of IFNs can, in a Stat1-dependent way, induce TTP provided the stress-regulated p38 MAPK is activated simultaneously.

PMID: 18086388 We have demonstrated that both types of IFNs can, in a Stat1-dependent way, induce TTP provided the stress-regulated p38 MAPK is activated simultaneously.

PMID: 18086388 TTP limits the production of TNF-¦Á under these conditions

PMID: 18086388 The cytoprotection was caused by the IFN-¦Ã-mediated induction of ER stress via activation of the pancreatic ER kinase (PERK).

PMID: 18086388 in human endothelial cells IFN-¦Á can stimulate TTP transcription even without simultaneous p38 MAPK activation, suggesting that in these cells type I IFNs may directly elicit the TTP-dependent anti-inflammatory responses

PMID: 18086388 ER stress and PERK activation result in phosphorylation of the ¦Á subunit of the eukaryotic translation initiation factor 2 (eIF2¦Á).

PMID: 18086388 eIF2a phosphorylation imposes a strong reduction in translation that was previously associated with increased resistance to stress

PMID: 18086388, 8608598, 16571725, 8608597 Stat1 and Stat2 are essential for type I IFN responses whereas the still largely elusive role of Stat3 phosphorylation has only recently begun to emerge

PMID: 18086388 After translocation to the nucleus Stat complexes bind to distinct enhancer elements and activate transcription of the type I IFN-responsive genes.

PMID: 18086388 Herein, the ISGF3 complex consisting of a Stat1:Stat2 heterodimer and the DNA-binding subunit IRF9, which binds to ISRE elements, plays a more important role than the Stat1:Stat1 homodimer that binds to GAS elements.

PMID: 18086388 Herein, the ISGF3 complex consisting of a Stat1:Stat2 heterodimer and the DNA-binding subunit IRF9, which binds to ISRE elements, plays a more important role than the Stat1:Stat1 homodimer that binds to GAS elements.

PMID: 18086388 Type II IFN signalling is initiated by binding of IFN-¦Ã to its receptor consisting of the IFNGR1 and IFNGR2 subunits.

PMID: 18086388 The receptor-associated Jak1 and Jak2 tyrosine kinases are activated and phosphorylate the receptor, thereby generating a docking site for the SH2 domain of Stat1.