Publication for STAT1 and STAT2

Species Symbol Function* Entrez Gene ID* Other ID Gene
coexpression		 CoexViewer
hsa STAT1 signal transducer and activator of transcription 1 6772 [link]
hsa STAT2 signal transducer and activator of transcription 2 6773

Pubmed ID Priority Text
27780205 0.98 STAT1 in cells that expressed STAT2 compared to cells that lacked it (Fig 1A).
0.98 STAT1, namely replacement with alanine of phenylalanine 77 in the N domain, affected its colocalization with STAT2.
0.98 STAT1 failed to colocalize with STAT2 (Fig 1B, panels 9 and 10).
0.98 STAT1 and mutant STAT2 that harbored alanine in the STAT1 F77 homologous position leucine 82 (Fig 1B, panels 11 and 12) or the functionally equivalent double mutation LL81,82AA (S3 Fig).
0.98 STAT2 retained cytoplasmic accumulation, but STAT1 failed to redistribute.
0.98 STAT1 homodimers and its heterodimers with STAT2 assembled via identical N domain-mediated interactions.
0.98 STAT1-CFP and STAT2-YFP variants were singly or coexpressed in HeLa cells and their localization was determined by deconvolution fluorescence microscopy.
0.98 STAT1 in the presence of the indicated STAT2 variants.
0.98 STAT2 nuclear import inhibition was specific for STAT1 but not linked to a specific cytokine stimulus.
0.98 STAT1 (anti-phospho-Y701 STAT1 antibody) and STAT3 (anti-phospho-Y705 STAT3 antibody) in STAT2-YFP-reconstituted U6A cells left untreated (top) or cotreated with IL-6/soluble IL-6 receptor (middle) or with IL-27 (bottom).
0.98 STAT2 as a crucial component of a filtering mechanism for IL-27 and other cytokines whose biological outcomes critically depend upon balancing the transcriptional potency of STAT1 and competing STAT proteins.
0.98 STAT1 and STAT2 are well known to bind the transcription factor IRF9.
0.98 STAT2 does not target the activation of STAT1, but the subsequent step, its nuclear import.
0.97 STAT2 attenuated crucial immunomodulatory and antimicrobial effector functions of IFN-gamma; and in IL-27-mediated transcription, STAT2 shifted the balance away from STAT1 to STAT3.
0.97 STAT2 Binds to STAT1 through Exceptionally Strong N Domain Interactions
0.97 STAT1 and STAT2 tagged with cyan fluorescent protein (CFP) and yellow fluorescent protein (YFP), respectively.
0.97 STAT2 overexpression was not observed with the two STAT proteins most closely related to STAT1, STAT3 and STAT4 (S1 Fig).
0.97 STAT2 mutants phenocopied STAT1-F77A.
0.97 STAT2 binds STAT1 via high affinity N Domain interactions.
0.97 STAT1 (black bars) and STAT2 (white bar) acquired as described in (A).
0.97 STAT1 and STAT2 and determined dissociation constants for homo- and heterodimers using analytical ultracentrifugation (Fig 1C).
0.97 STAT1 nuclear import in response to type 1 IFN, in contrast, was unaffected by disrupted STAT1:STAT2 heterodimerization (S4A Fig).
0.97 STAT2 interferes with STAT1 DNA binding, we used electrophoretic mobility shift assays (EMSAs) with extracts from STAT2-deficient human U6A fibrosarcoma cells and stable derivatives expressing WT STAT2 or mutant STAT2-L82A (Fig 2D, S5 Fig).
0.97 STAT1, in contrast, entered the nucleus in the presence of mutated STAT2 (panels 12, 20), but not WT STAT2 (panels 10, 18), similar to the results with IFN-gamma (Fig 2B).
0.97 STAT1, STAT2, and hybrid STAT2 structure accompanying widefield microscopy detecting the endogenous STAT1 (anti-STAT1 C terminus antibody decorated with Cy3) in cells expressing YFP-tagged hybrid STAT2.
0.97 STAT2 abrogated its inhibition of STAT1 nuclear import.
0.97 STAT2-mediated reduction in nuclear STAT1 translates directly in diminished transcription, similar to the effects on IFN-gamma.
0.97 STAT1 is present in excess over STAT2, and that the STAT1:STAT2 ratio of these IFN-stimulated genes was increased further by treatment with IFNs.
0.96 STAT1 inhibition and generate a novel biological tool with which we can dissociate STAT2's activating and inhibitory effects on STAT1.
0.96 STAT2 exclusively forms heterodimers with concurrently activated STAT1, which associate with another DNA-binding protein, IRF9, and form the transcription factor interferon-stimulated gene factor 3 (ISGF3).
0.96 STAT1 and STAT2 recombinant N domains.
0.96 STAT1 splice variants (alphaS1alpha/beta) and STAT2 (alphaS2).
0.96 STAT2 as a pervasive cytokine regulator due to its inhibition of STAT1 in multiple signaling pathways.
0.96 STAT1:STAT2 protein ratio as a key determinant for the functioning of STAT1 moreover invalidates the assumption that STAT1 tyrosine phosphorylation can be equated with its biological activity.
0.95 STAT1 and STAT2 demonstrated the cytoplasmic redistribution of STAT1 (Fig 1B, panels 7 and 8).
0.95 STAT1 and STAT2.
0.95 STAT1 and STAT3, but only STAT1 nuclear translocation was inhibited by STAT2 (Fig 3B).
0.95 STAT2 can be described as a gain-of-function phenotype for STAT1, of which unrestrained IFN-gamma activity is an important consequence, as shown here.
0.94 STAT1 and STAT2 are essential for the classic host immune defense system against viral infections known as the type 1 interferon response.
0.94 STAT1 distributed throughout the cell (Fig 1B, panels 1-4), while separately expressed STAT2 accumulated in the cytoplasm (Fig 1B, panels 5 and 6).
0.94 STAT2 (aa 1-702) lacking NES activity, demonstrating that cytoplasmic retention of activated STAT1 is independent of STAT2 nuclear export (Fig 2C, panels 5 and 6).
0.94 STAT1 were used to account for the nuclear import inhibition caused by STAT2.
0.93 STAT2 coprecipitated with tyrosine-phosphorylated WT STAT1 (lane 12).
0.93 STAT2 that functions as a STAT1 inhibitor.
0.93 STAT1, which not only is unaffected by STAT2 but moreover an insufficient measure for the biological activity of STAT1 and IFN-gamma, as we have discussed above.
0.93 STAT2-dependent IFN-SS feedback loop, may abolish the STAT1 gain-of-function phenotype associated with STAT2 deficiency.
0.93 STAT1-binding mutant described in this work, as it allows the dissociation of STAT2's effects on type 1 and type 2 IFN.
0.93 STAT2 quencher-through its N domain-and hence rather as a promoter of cytokines that signal via STAT1.
0.92 STAT1 and unphosphorylated STAT2, whereby the semiphosphorylated dimers adopted a conformation incapable of importin-alpha binding.
0.92 STAT2 NES, either by genetic removal of the NES-containing C terminal transactivation domain or by chemical inhibition of the NES receptor protein CRM1, resulted in similar pancellular distribution of both STAT2 and STAT1 (S2 Fig).
0.92 STAT1 (S1) and STAT2 (S2) are indicated.
0.92 STAT2 inhibits specifically STAT1 in response to both IL-27 and IL-6.
0.92 STAT1:STAT2 Heterodimers Adopt Antiparallel Conformation Incompatible with Importin-alpha5 Binding
0.91 STAT2 coprecipitated with WT STAT1 and STAT1-Y701F (lanes 2, 4), but not STAT1-F77A and the STAT1-F77A, Y701F double mutant (lanes 3, 5).
0.90 STAT2-deficient human U6A cells (S2-/-) and parental 2fTGH cells (WT) were treated for 1 h with 1 U/ml IFN-gamma, fixed and processed for immunostaining using anti-phospho-Y701 STAT1 antibody, nuclear counterstaining was with DAPI.
0.90 STAT1 activation is its ability to bind specific DNA sequences with high affinity, namely to the interferon-stimulated response element (ISRE) as part of ISGF3, and to the gamma interferon-activated site (GAS) as a homodimer (gamma interferon-activated factor; GAF).
0.89 STAT2-deficient macrophages contained reduced STAT1 protein, which could be normalized to WT levels by IFN-gamma priming (S7B Fig), which further accentuated the enhanced IFN-gamma-inducible gene expression of the STAT2-deficient cells (Fig 5B).
0.89 STAT2-mediated inhibition of STAT1 is expected to shift promoter occupancy away from STAT1 to STAT3 and possibly other STATs with difficult-to-predict consequences for the IL-27 transcriptome.
0.88 STAT1:STAT2-P) and their natural IFN-gamma-induced counterparts (P-STAT1:STAT2-U) are not identical, they are both defective in carrier-mediated nuclear import, which suggests that they can be used interchangeably to study importin binding.
0.87 STAT2 and STAT1 are exceedingly tight, yet highly vulnerable to mutation of either STAT1 (F77A) or STAT2 (L82A), suggesting strong evolutionary pressure in favor of heterodimerization.
0.86 STAT2 functioning as an import inhibitor of activated STAT1, we performed STAT2 coimmunoprecipitation assays with FLAG-tagged WT STAT1 and three STAT1 mutants deficient either in tyrosine phosphorylation (Y701F), or specifically antiparallel dimerization (F77A), or both (F77A, Y701F), to infer the conformation of unphosphorylated, semiphosphorylated, and fully phosphorylated STAT1:STAT2 heterodimers in vivo (Fig 4A).
0.86 STAT1 into STAT2, which led to the IFN-gamma-inducible tyrosine phosphorylation of the hybrid STAT2 reported by Darnell's group.
0.85 STAT2 binding to STAT1 enhanced gene expression in response to IFN-gamma, but was without overt consequences for type 1 IFN signaling.
0.83 STAT1 and STAT3, which take part in multiple signaling pathways, STAT2 is considered to be involved in only a single intracellular pathway, which emanates from the receptors of type 1 and type 3 IFNs.
0.81 STAT2, like the endogenous STAT2, inhibited STAT1 nuclear accumulation (Fig 2C, panels 1 and 2), in agreement with a previous observation by Julkunen and colleagues.
0.79 STAT2 overexpression in HeLa cells resulted in significantly reduced STAT1 reporter gene activity (Fig 5A).
0.79 STAT2, namely differences in STAT1 tyrosine and serine phosphorylation, but found comparable phosphorylation levels in both cell types using western blotting (Fig 3A, S7E Fig).
0.74 STAT2 has pervasive activation-independent activities as a STAT1 negative regulator in multiple signaling pathways.
0.73 STAT1 or STAT3, respectively, and compared their induction using IL-27 in STAT2-deficient U6A cells and U6A cells reconstituted with WT STAT2 or the L82A mutant.
0.71 STAT2, like WT, accumulated in the cytoplasm together with STAT1 (Fig 4C, panels 1 and 2).
0.67 STAT1 protein concentrations are reduced by 50%-80% in STAT2-deficient cells from both patients and mice compared to WT.
0.64 STAT2 and STAT1 was exceptional, namely at least 1,000 times stronger than STAT1 homodimers.
0.64 STAT2, as expected, but no difference was seen between cells expressing WT and mutant STAT2, in line with undisturbed type 1 IFN-induced activation and nuclear import of STAT1 and STAT2 (Fig 2A; S4B Fig).
0.63 STAT1-Y701F coprecipitation with importin-alpha5 (lane 4), despite abundant phosphorylated STAT2 in the extract (lane 22).
0.58 STAT2 shifts the transcriptional output of IL-27 from STAT1 to STAT3.
0.56 Stat2-deficient human U6A cells (S2-/-) and parental 2fTGH cells (WT) were fixed and processed for immunostaining using STAT1 antibody, nuclear counterstaining was with DAPI.
0.54 STAT2 coprecipitated similarly well with the activated STAT1-F77A dimerization mutant (lane 13), presumably through mutual src kinase homology 2 (SH2):phosphotyrosine interactions.
0.53 STAT2 constitutively bound to STAT1, but not STAT3, via a conserved interface.
0.53 STAT2, but as predicted, hybrid STAT2 did not inhibit the nuclear import of activated STAT1, which accumulated strongly in the nucleus upon IFN-gamma treatment (Fig 4C, panels 3 and 4).
0.52 STAT1 and STAT2, but only in extracts from IFN-SS-treated cells (lanes 1 and 2 for STAT1; and 7 and 8 for STAT2), which agrees with the requirement of STAT activation for importin-alpha5 binding.
24065129 0.98 STAT1, STAT2, and IRF9 mediate resistance to viruses and DNA damage
0.98 STAT1, STAT2, and IRF9 mediate resistance to viruses and DNA damage
0.98 STAT1 and STAT2 (lanes 2, 3, and 6) and between STAT2 and IRF9 (lanes 6 and 7) were clearly observed in the nuclear fractions.
0.98 STAT1, U-STAT2, or IRF9 and cell survival (Figure 6B).
0.98 STAT1, and STAT2, or tyrosine-phosphorylated STATs (PY-701-STAT1 or PY-690-STAT2) were analysed by the western method.
0.98 STAT1, U-STAT2, and IRF9 form U-ISGF3, which binds to ISREs on the target gene promoters.
0.98 PY-701-STAT1 or PY-690-STAT2) were examined by the western method.
0.97 -STAT1, U-STAT2, and IRF9 together in hTERT-HME1 cells significantly increased the expression of the target genes, IFI27, OAS1, OAS2, MX1, IFIT1, and IFIT3 (Figure 2C), indicating that STAT1 tyrosine phosphorylation was not involved.
0.97 STAT1, STAT2, and IRF9 proteins varies widely in different cell types, as shown here by comparing normal human mammary epithelial cells to normal human fibroblasts.
0.97 STAT1, the high expression of STAT1, STAT2, and IRF9 might be due to the constitutive production of low levels of IFN.
0.96 STAT2 and IRF9, we stably increased the expression of STAT2 and IRF9, together with STAT1, in hTERT-HME1 cells.
0.96 STAT1, STAT2, or IRF9, or comparable amounts of normal rabbit IgG, were used for immunoprecipitations.
0.95 STAT2 and IRF9 together with Y701F-STAT1 readily increased those three ISGs (Figure 2E), but not the transiently induced ISGs MYD88, IFI16, and IRF1 (Figure 2F).
0.94 STAT1 led to increased expression of 30 genes without IFN stimulation in BJ cells, which already express substantial amounts of STAT2 and IRF9, but not in hTERT-HME1 cells, which express little STAT2 and IRF9, indicating that U-STAT1 may not induce gene expression without a sufficient amount of STAT2 and IRF9.
0.94 STAT1, U-STAT2, or IRF9 were increased one at a time without treatment with IFNbeta (Figure 2B, columns 2-4).
0.94 STAT1/STAT2/IRF9 (WT), virus replication was inhibited more efficiently in the presence of IFNbeta (Supplementary Figure S3B), because increased levels of ISGF3 formed by wild-type STAT1/STAT2/IRF9 sensitize cells to IFNs.
0.94 -STAT1, and we assumed that these are induced by U-ISGF3. reported that IFNgamma induces the expression of anti-viral genes through another form of ISGF3, consisting of PY-STAT1, U-STAT2, and IRF9.
0.94 STAT1-null fibroblasts were stably transfected with empty pLV vector (Vec), or pLV-Y701F-STAT1, pLV-STAT2, and pLV-IRF9 together (YF-S1S2I9).
0.93 STAT1-induced gene expression, finding that IFNbeta also induces the expression of un-phosphorylated STAT2 (U-STAT2) and IRF9, which combine with U-STAT1 to form un-phosphorylated ISGF3 (U-ISGF3), a novel transcription factor in which these proteins form a ternary complex without tyrosine phosphorylation.
0.93 STAT1, U-STAT2, and IRF9 are necessary and sufficient for the induction of some anti-viral genes
0.93 STAT1, STAT2, and IRF9 proteins.
0.93 ISGF3 (PY-701-STAT1, PY-690-STAT2, and IRF9), which binds to standard ISREs in ISG promoters.
0.92 STAT1, STAT2, and IRF9 proteins are necessary and sufficient for the induction of some anti-viral genes without IFN-induced phosphorylation.
0.91 STAT1 plus U-STAT2 or U-STAT1 plus IRF9 still did not increase the expression of these genes in hTERT-HME1 cells (Figure 2B, columns 5 and 6).
0.91 ISGF3 but not sustained at late times after IFN treatment, was not increased by higher levels of Y701F-STAT1, U-STAT2, and IRF9 (Figure 2D).
0.91 STAT1, STAT2, or IRF9, and the DNAs were amplified by real-time PCR, using primers spanning the most highly conserved IFN stimulated response elements (ISREs) (striped triangles in Supplementary Figure S4A) in each promoter, identified by using the transcription factor search program TFSEARCH (http://www.cbrc.jp/research/db/TFSEARCH.html).
0.91 STAT1/STAT2/IRF9 (WT) or Y701F-STAT1/STAT2/IRF9 (YF) were used.
0.90 STAT1, STAT2, IRF9, and several U-STAT1-induced genes (IFI27, OAS2, and MX1) lasted for at least 12 days after a single treatment with IFNbeta (50 IU/ml), while the expression of ISGs (MYD88, IRF1, and IFI16) that are not induced by U-STAT1 returned to basal levels after 3 days or sooner (Supplementary Figure S1).
0.90 STAT1, U-STAT2, and IRF9 in the absence of IFN treatment.
0.89 STAT1 or phosphorylated STAT2 after 48 h (Figure 1B).
0.89 STAT1 and DNA damage resistance in SCLC cell lines (Figure 6A), suggesting that DNA damage-resistant cancer cells produce IFNs in sufficient quantity to induce higher levels of STAT1, STAT2, and IRF9 proteins but not enough to induce cytotoxic genes, compared to sensitive cancer cell lines or normal cells.
0.87 STAT2 and IRF9 were increased together (column 7) and increased even more when U-STAT1 expression, already significant, was increased further (column 8).
0.87 STAT1, STAT2, and IRF9 proteins protect cells from various RNA viruses in an IFN-independent manner.
0.86 -STAT1/STAT2/IRF9-transfected cells showed similar levels of resistance, confirming that the anti-viral effects were induced by high levels of U-STAT1, U-STAT2, and IRF9 proteins independently of virally induced IFN stimulation.
0.86 -STAT1/STAT2/IRF9 reduced VSV replication after 8 h (Figure 3C, P<0.01).
0.86 STAT1, STAT2, and IRF9 (H196 and H2195) are much more resistant to DNA damage.
0.84 STAT1/U-STAT2/IRF9, by >10-fold 48 h after infection (P<0.01).
0.83 STAT1, STAT2, or IRF9.
0.82 STAT1, STAT2, and IRF9 are likely to be important for the prolonged expression of anti-viral genes, while tyrosine phosphorylation of STATs 1 and 2 is important for initial gene expression.
0.81 STAT1, STAT2, and IRF9 in the lentiviral vector pLV.
0.80 ISGF3 complex is increased in response to high levels of U-STAT1, U-STAT2, and IRF9 without IFN-induced phosphorylation and is present on ISREs in the promoters of U-ISGF3 target genes.
0.79 STAT1, U-STAT2, and IRF9 form U-ISGF3, which binds to IFN stimulated response elements in target gene promoters
0.75 STAT1/U-STAT2/IRF9 also inhibited significantly the replication of YFV (a positive ssRNA virus), by 30% 48 h after infection with 100 MOI of virus (P<0.01).
0.74 STAT1, U-STAT2, and IRF9 protect cells from virus infection
0.70 STAT1, PY-690- or total STAT2, and total IRF9 was examined by the western method in six different small cell lung carcinoma cell lines.
0.65 -STAT1, pLV-STAT2, and pLV-IRF9 together (YF-S1S2I9).
0.57 STAT1, and U-STAT2 were increased and in which the tyrosine phosphorylation of STATs 1 and 2 had been downregulated by negative regulators, leading to sustained U-ISGF3-induced gene expression.
0.56 -STAT1/STAT2/IRF9 (YF) were not influenced by IFNbeta in the media (Supplementary Figure S3B), showing that the Y701F-STAT1/STAT2/IRF9-induced anti-viral effects resulted solely from the high levels of U-STAT1, U-STAT2, and IRF9 proteins rather than the IFN-induced phosphorylation of STATs 1 and 2.
30455980 0.98 STAT1 and STAT2 protein levels, but not JAK1, are involved in the activities of ISREs in senescent cells.
0.98 STAT1, STAT2, and IRF9 localized to the nucleus of NHDFs at passage 23 (p23).
0.98 STAT1 and STAT2 protein levels were significantly increased in senescent cells (Fig. 3c), whereas, despite the marked increases in their levels in Huh7 cells after IFN treatment, the phosphorylated forms of STAT1 and STAT2 were not detected (Fig. 3c).
0.98 STAT1 and STAT2 levels are increased in fibroblasts from a patient with Werner syndrome.
0.98 STAT1 and STAT2 are crucial for induction of ISG expression in senescent cells.
0.98 STAT1 and STAT2 phosphorylation, whereas the classical JAK-STAT paradigm involves a strict correlation between STAT activity and STAT tyrosine phosphorylation.
0.97 ISGF3, which is composed of IRF9 and the phosphorylated forms of STAT1 and STAT2, in the presence of IFNs.
0.97 STAT1 and STAT2 mRNA levels (GEO accession #GSE107483 and Supplementary Table 1), the protein levels of STAT1 and STAT2 were higher in senescent cells (Fig. 3a).
0.97 STAT1 and Tyr 690 in STAT2).
0.97 STAT1 and Tyr 690 in STAT2 and assessed the levels of the phosphorylated forms of STAT1 and STAT2 in senescent cells by phos-tag assay.
0.97 STAT1 and STAT2 levels were higher in fibroblasts from a patient with Werner syndrome at passage 10 (W) than in NHDFs at passage 13 (N).
0.97 STAT1, STAT2, and IRF9 localized to the nucleus of fibroblasts from a patient with Werner syndrome.
0.97 STAT1 and STAT2 were not detected, whereas the level of unphosphorylated ISGF3 (comprising STAT1, STAT2, and IRF9) was increased (Fig. 4d).
0.97 STAT1 or STAT2 knockdown but not by JAK1 knockdown in NHDFs at passage 24.
0.97 STAT1 and STAT2 phosphorylation, we next examined the involvement of JAK1, a key upstream kinase of the STAT1 and STAT2 signaling pathway.
0.97 STAT1 and STAT2 phosphorylation status was unchanged, it is possible that modifications of STAT1 and STAT2 other than phosphorylation are involved in the high expression levels of ISGs under physiological conditions in the absence of IFN production in senescent cells.
0.96 STAT1, STAT2, and IRF9 protein levels were increased and their nuclear localization was enhanced in NHDFs at passage 23 (p23) compared with passage 5 (p5).
0.96 STAT1 and STAT2 in Huh7 cells (Fig. 3d), these forms were increased in senescent cells, although some phosphorylated forms of STAT1 and STAT2 were also detected in both early passage and senescent cells (Fig. 3d).
0.96 STAT1, STAT2, and IRF9 into the nucleus in fibroblasts from a patient with Werner syndrome at passage 8 compared with NHDFs at passage 13 (Fig. 4e).
0.96 STAT1 and STAT2 proteins.
0.95 STAT1, STAT2, and IRF9 were localized to both the cytoplasm and the nucleus in early passage cells but exclusively to the nucleus in senescent cells (Fig. 2c).
0.95 STAT1 and STAT2 proteins were increased in NHDFs at passage 23 (p23) compared with passage 5 (p5).
0.95 STAT1 and STAT2 translocate into the nucleus independently of IFN production under physiological conditions in senescent cells.
0.95 STAT1 and STAT2, similar to the case in senescent NHDFs.
0.94 STAT1, STAT2, and IRF9 were localized to the nucleus of aged cells.
0.93 ISGF3, which is composed of IRF9 and the phosphorylated forms of STAT1 and STAT2.
0.93 STAT1, STAT2, IRF9, and Mx1 protein levels were increased; the STAT3 protein level was unchanged; and the SIRT1 protein level was decreased in the nucleus of NHDFs.
0.91 STAT1, STAT2, and IRF9 protein levels were increased and their nuclear localizations were enhanced in fibroblasts from a patient with Werner syndrome at passage 8 (p8) compared with those in NHDFs at passage 13 (p13).
0.87 ISGF3, together with STAT1 and STAT2, translocates into the nucleus, which leads to significant, and IFN-independent, upregulation of ISG expression in senescent cells.
0.86 STAT1 and STAT2 levels were not increased in NHDFs at passage 23 (p23).
0.82 STAT1 and STAT2 protein levels were increased in the nucleus of NHDFs at passage 23 (p23) compared with passage 5 (p5).
0.71 signal transducer and activator of transcription 1 (STAT1) and STAT2 are phosphorylated, promoting the formation of Stat1-Stat2 heterodimers, which associate with IFN regulatory factor 9 (IRF9) to form interferon (IFN)-stimulated gene factor 3 (ISGF3).
0.57 STAT1 and STAT2.
0.50 ISGF3, which translocates into the nucleus after its formation via complexation of IRF9, phosphorylated STAT1, and phosphorylated STAT2.
31374104 0.98 STAT1 or STAT2 and polyubiquitin specific antibodies (FK2).
0.98 STAT1 or STAT2 and FLAG specific antibodies (yellow).
0.98 STAT2 and PDLIM2 increased greater than 2 fold upon interferon treatment in the presence of MG132 whereas the interactions between STAT1 and PDLIM2, while significant, were much lower.
0.98 STAT1, STAT2, and NF-kappaB. We found that all 3 were lower in HCV infected hepatocytes compared with surrounding bystander cells, both in vivo in chimeric mouse livers and in Huh7.5 cells, indicating that the interferon response seen during HCV infection is due to uninfected or newly infected hepatocytes.
0.98 STAT1 is not degraded and is retained in the nucleus when STAT2 degradation is inhibited by MG132.
0.98 STAT1 and selective depletion of STAT2 by PDLIM2 during IFNalpha administration is also consistent with the shift in expression from uniquely IFN-alpha/beta induced proteins at early times after IFN-alpha treatment, to proteins that are also induced by IFN-gamma at later time points.
0.97 STAT2 but not STAT1 and the proteasome-dependent degradation of STAT2, predominantly within the nucleus.
0.97 STAT2 but not STAT1 is degraded predominantly in the nucleus following interferon treatment.
0.97 STAT2 and also between PDLIM2 and STAT2; however, it does not change STAT1 interactions to the same extent.
0.97 STAT1, STAT2, and NF-kappaB in HCV infected cells were due to degradation.
0.97 STAT1 and STAT2 down-regulation in HCV infected cells in the context of interferon treatment.
0.96 STAT1 and STAT2 during HCV infection in order to investigate the paradoxical induction of an innate immune response by HCV despite a multitude of mechanisms combating the host response.
0.96 STAT2 can homodimerize and stimulate ISG expression independently, and while STAT1 is essential for IFN-gamma and IFN-lambda signaling, STAT2 is essential for both IFN-lambda and IFN-alpha signaling in Huh7.5 cells.
0.96 STAT1, inclusion of MG132 during IFNalpha treatment resulted in significantly increased levels of STAT2 in infected cells indicating that STAT2 is degraded following IFNalpha treatment.
0.96 STAT1, STAT2 or actin as a loading control.
0.96 STAT1 or STAT2 interacted with PDLIM2 after IFNalpha treatment.
0.96 STAT1 or STAT2 with the tagged PDLIM2 by PLA (Fig 4B).
0.95 STAT1/STAT2/IRF9 (ISGF3) and the transcription of numerous IFN stimulated genes (ISGs) which in turn inhibit viral replication.
0.94 STAT1 and STAT2 protein levels in uninfected livers and infected livers using confocal microscopy revealed that STAT1 levels increased 1.7+-1.3 fold in infected livers while STAT2 increased 1.5+-0.45 fold in infected livers.
0.94 STAT1 or C) STAT2 (green).
0.94 STAT1 and STAT2 levels and location (Fig 2A and 2B).
0.94 STAT2 degradation by MG132 also results in nuclear retention of STAT1, its partner in ISGF3.
0.90 STAT1 or STAT2 were associated with ubiquitin using PLA (Fig 4A).
0.89 STAT1 and STAT2).
0.85 STAT1 and STAT2 levels were measured by western blot analysis.
0.82 STAT2 but not STAT1 with ubiquitin and PDLIM2 after IFNalpha treatment.
0.81 STAT1, STAT2, or NF-kappaB. Since PDLIM2 was shown to act in the nucleus following NF-kappaB activation, we investigated the effects of viral infection on PDLIM2 expression in the human hepatocyte cell line Huh7.5.
0.75 STAT1 or STAT2 was quantified in at least 594 of each of either uninfected or HCV infected cells.
0.74 STAT1, STAT2, and NF-kappaB during an ongoing interferon response
0.74 STAT1, STAT2 and likely PDLIM2 protein levels vary among cell types and during infection, we cannot rule out that PDLIM2 does not direct interferon independent degradation of STAT1 in other situations.
0.68 STAT1 or STAT2 (green).
0.67 STAT2 by PDLIM2, followed by ubiquitination, and degradation in a nuclear proteasome, while STAT1 is preserved.
0.65 STAT1 and STAT2 bind IRF9 to form the transcription factor ISGF3, which migrates to the nucleus to induce ISG transcription.
20937132 0.98 ISGF3), STAT1 and STAT2 proteins were experimentally tested in cervical carcinoma cell lines.
0.98 STAT1-STAT2 complex occurs through the V protein Trp-motif (W174, W178, W189) and Glu95 residue close to the Arg409 and Lys415 of the nuclear localization signal (NLS) of STAT2, leaving exposed STAT1 Lys residues (K85, K87, K296, K413, K525, K679, K685), which are susceptible to proteasome degradation.
0.98 STAT1-STAT2 heterodimer with IRF9 constitutes the IFN-stimulated gene factor 3 (ISGF3) transcription factor, which binds to IFN-stimulated response elements (ISRE) at IFN-stimulated genes (ISG).
0.98 STAT1-STAT2 heterodimer.
0.98 STAT1: Lys410 and Lys413, in STAT2 Arg409 and Lys415 (pink), potential ubiquitylation sites in STAT1 (K85, K87, K296, K413, K525, K679, K685) and STAT2 (K178, K182, K543, K681) (blue).
0.97 STAT1 phosphorylation, whereas VGly had no inhibitory effect on either STAT1 or STAT2 phosphorylation.
0.97 STAT1-STAT2 heterodimer.
0.97 STAT1 and STAT2 form a heterodimer that creates a nuclear localization signal (NLS).
0.97 STAT1 and STAT2 in vitro.
0.97 STAT1 and Y690-STAT2 phosphorylated proteins.
0.97 STAT1 proteins, pTyr690-STAT2 and IRF9 (ISGF-gamma3).
0.97 STAT1 and STAT2 phosphorylated proteins by Western blot in human cervical carcinoma cell line.
0.97 STAT1, pTyr690-STAT2 and beta-actin.
0.97 STAT1-STAT2 (purple), Cys-rich motif C4HC3 (residues in pink).
0.97 STAT1-STAT2 heterodimer activated by IFN, the 3D structure of STAT1 was obtained from PDB: 1YVL (structure of unphosphorylated STAT1) and the 3D theoretical model of STAT2 by homology from templates PDB: 1BF5 (tyrosine phosphorylated STAT-1/DNA complex) and PDB: 1YVL with the purpose of obtaining the 3D model that includes Tyr690 required for interaction with STAT1 (identity was 46% with STAT1).
0.97 STAT2) was set in positions 690 and 698 and the ligand binding site (STAT1) was set in positions 701 and 708, which included the amino acids Tyr690 and Tyr701 of STAT2 and STAT1, respectively, to achieve formation of the dimer by interaction of their SH2-domains (573- 670 in STAT1 and 572-667 in STAT2).
0.97 STAT1-STAT2 dimer corresponded to the solution of lowest overall energy (-43.71) with attractive and repulsive van der Waals energy of -29.86 and 14.05, respectively; an atomic contact energy of -5.27 and an energy of -3.35 derived from formation of hydrogen bonds.
0.97 STAT2 to promote the degradation of STAT1 through the proteasome.
0.97 STAT2 would leave STAT1 susceptible to ubiquitination.
0.97 STAT2 could maintain the heterodimer in the cytoplasm where the ubiquitin/proteasome labels the lysine-susceptible residues exposed in STAT1.
0.96 STAT2 but far from the NLS of STAT1 and STAT2 (Figure 3C, box).
0.96 STAT1-STAT2. (A) Heterodimer model of STAT1-STAT2 by the SH2-domain (STAT1 PDB: 1YVL and 3D model of STAT2 from 1YVL and 1BF5).
0.95 STAT1-STAT2 heterodimer occurs in a region far from the NLS of STAT2 without blocking of Lys residues in both STAT1 and STAT2.
0.95 STAT1-STAT2 heterodimers result from intermolecular interactions between Src homology 2 (SH2) domains and phosphorylated Tyr residues at each protein.
0.95 STAT2 near Arg409 and Lys415 of NLS without interference from amino acids Lys410 and Lys413 in NLS of STAT1 (Figure 3B, checkbox).
0.92 STAT1-STAT2 heterodimer: experimental and theoretical studies
0.90 STAT1 protein was always determined in the heterodimer with STAT2 phosphorylated protein with the subsequent blockade of the IFN system.
0.86 ISGF3 complex formation in response to IFN-alpha2b by detecting STAT1, STAT2 and IRF9 proteins in cells stimulated with IFN and the proteasome inhibitor MG132.
0.86 STAT1-STAT2 showed that the contact occurs through STAT2 as in VWT but in a region far from residues of the NLS on STAT1/STAT2.
0.64 STAT1-STAT2 proteins.
0.56 STAT1-STAT2 (both phosphorylated), DDB1, Cullin 4A and Roc1.
25364701 0.98 STAT1 or STAT2 play in maintaining the survival of STAT3-dependent cells.
0.98 STAT1 or STAT2 expression.
0.98 STAT1 or STAT2 expression in STAT3-dependent cancer cell lines did not affect viability
0.98 STAT1 nor STAT2 synergized with STAT3 (thereby contributing to apoptosis), pairs of pooled siRNAs at 250 nM each (i.e., STAT1 plus STAT3 or STAT2 plus STAT3) were transfected into DU-145 and PANC-1 cells.
0.98 STAT1 or STAT2 had no effect on the survival of DU-145 prostate cancer or PANC-1 pancreatic cells (Figure 3 and Table 1), yet transfection of STAT3 siRNA induced significant apoptosis in these cells lines (Tables 1 and 2).
0.98 STAT1-null U3A, and STAT2-null U6A cells were fixed, permeabilized, blocked appropriately and then incubated with PE-anti-phospho-STAT3 (Y-705) Ab.
0.98 STAT1- and STAT2-null cells.
0.97 STAT1 and STAT2; however the contributions of STAT3:STAT1 and STAT3:STAT2 heterodimers to the survival of malignant cells have not been investigated in detail.
0.97 STAT1-null and STAT2-null fibrosarcoma cell lines U3A and U6A, as well as in the parental fibrosarcoma cell line 2fTGH.
0.97 STAT1 and STAT2 regulate cytokine-stimulated growth; however STAT1 may be a tumor suppressor in some cells.
0.97 STAT1 nor STAT2 activity contribute to STAT3-mediated survival of transformed cells.
0.97 STAT1 or STAT2, oligonucleotide inhibitors of STAT3 activity were transfected into 2fTGH, U3A, and U6A cells.
0.97 STAT1 or STAT2 expression or activity.
0.97 STAT1 nor STAT2 contribute to the survival of malignant cells, siRNA was used to silence their expression in DU-145 and PANC-1 cells.
0.97 STAT1 or STAT2 siRNA, no significant apoptosis was observed in DU-145 or PANC-1 cells.
0.97 STAT1 or STAT2, in DU-145 and PANC-1 cells.
0.96 STAT1, and to a lesser extent, STAT2 are implicated in tumorigenesis, however, STAT1 activity appears to have both pro- and anti-tumorigenic effects.
0.96 STAT1-null and STAT2-null fibrosarcoma cell lines and transfecting them with STAT3-inhibiting oligonucleotides, we observed the induction of apoptosis by STAT3 inhibitors in the absence of STAT1 or STAT2 signaling.
0.96 STAT1 or STAT2 activation.
0.96 STAT1 nor STAT2 contributed to the survival of STAT3-addicted tumor cells.
0.96 STAT1 or STAT2 to promote tumor cell survival.
0.96 STAT1 or STAT2 may regulate tumor cell response to interferons.
0.95 STAT1 or STAT2 in promoting the survival of cancer cells and that our novel STAT3 inhibitors 13410 and 13410 are selective STAT3 inhibitors.
0.95 STAT1 and STAT2 can regulate cytokine-stimulated growth, even in opposition to STAT3 effects.
0.94 STAT1, STAT2, or control siRNA (P value was 0.99 for DU-145 cells and 0.43 for PANC-1 cells; Table 2).
0.90 STAT1 nor STAT2 play significant roles in the maintenance of these cells, and by extension that STAT3:STAT1 and STAT3:STAT2 heterodimers regulate a different set of genes from STAT3:STAT3 homodimers.
0.90 STAT1 nor STAT2 siRNA synergized with STAT3 siRNA to induce apoptosis; the amount of apoptosis seen with 250 nM STAT3 siRNA was nearly the same in the presence or absence of either STAT1 or STAT2 siRNA (Table 2).
0.90 STAT1 or STAT2 in melanoma cell lines did not correlate with interferon-alpha as adjuvant therapy.
0.89 STAT1, and to a lesser extent, STAT2, are implicated in tumorigenesis; however STAT1 activity appears to have both pro- and anti-tumorigenic effects depending upon STAT1 activation (transient or constitutive).
0.88 STAT1 and STAT2 (in common with STAT3) recruit p300/CBP in the course of trans-activation, albeit to different extents.
0.69 STAT1 and STAT2 can regulate cytokine-stimulated growth, even in opposition to STAT3 effects.
26335850 0.98 STAT1 and STAT2 factors in the induction of p150 ADAR1 by IFN in human cells.
0.98 STAT1 or STAT2 was observed to the PA promoter region with untreated MEFs above the control level without specific antibody seen for untreated wild-type or Stat1(Delta221-365)-/- MEFs (Fig. 5A, 5B).
0.98 STAT1 and STAT2 are phosphorylated and form heterodimers that associate with IRF9 to form ISGF3 that translocates to the nucleus and binds the ISRE element to drive transcription.
0.98 Stat1(Delta1-124)-/- and Stat2-/- MEFs, that IFNalpha induction of p150 is STAT1- independent and STAT2-dependent.
0.98 STAT2 binds to the ISRE-containing IFN-inducible Adar1 promoter region even in the absence of STAT1 in Stat1(Delta221-365)-/- MEFs whereas both STAT1 and STAT2 bind in wild-type MEFs
0.98 STAT1 and STAT2 bind to the ISRE-containing IFN-inducible Adar1 PA promoter region in parental 2fTGH but not mutant U3A cells
0.97 STAT2 at the PA promoter in IFN-treated Stat1-/- cells, whereas IFN-treated wild-type cells showed both STAT1 and STAT2 bound at PA.
0.97 STAT2 to the Adar1 PA promoter region was IFN-dependent and observed only in the parental 2fTGH cells and not in U3A mutant cells (Fig. 6), consistent with the results showing STAT1 and STAT2 dependence for induction of the exon 1A RNA and p150 protein analyses (Fig.1).
0.97 STAT1 (U3A) mutant cells, using either no antibody (-) or with antibody (+) against STAT1 or STAT2 as indicated.
0.96 STAT2, both in Stat1-/- MEFs and human U3C (STAT1 mutant) cells, was recently described to produce a STAT1-independent IFNalpha inducible expression of Oas2 and Ifit1.
0.95 STAT1 and STAT2 (Fig. 1), unlike the p150 induction observed in mouse MEF cells that was STAT1 independent.
0.95 STAT2 also bound at the Adar1 inducible promoter in Stat1(Delta221-365)-/- mutant MEFs in an IFN-dependent manner, although the IFN-induced STAT2 binding in the mutant MEFs lacking STAT1 was less than that observed in wild-type MEFs possessing STAT1 (Fig. 5B).
0.95 STAT1 is required in addition to STAT2 to activate Adar1 inducible transcription, whereas in mouse cells STAT2 is able to function in the absence of STAT1.
0.94 Stat1(Delta1-124)-/- MEFs as well as in Stat1(Delta221-365)-/- MEFs by IFNalpha, the IFN-induced expression of Adar1 exon 1A RNA and p150 protein were not observed in mutant human cells lacking either STAT1 (U3A) or STAT2 (U6A).
0.94 Stat1(Delta1-124)-/- MEFs is STAT1-independent but STAT2-dependent, and induction of IRF7 following lymphocytic choriomeningitis virus (LCMV) infection or IFNalpha treatment is STAT2- and IRF9-dependent but independent of STAT1 based on Stat1(Delta1-124)-/- knockout.
0.93 STAT2 (Fig. 3) and IRF9 (Fig. 4) are required for induction of ADAR1, but that in Stat1(Delta221-365)-/- MEFs (Fig. 3) like in Stat1(Delta1-124)-/- MEFs (Fig. 2) the induction of ADAR1 is not dependent in an obligatory manner on STAT1.
0.92 Stat1-/-, Stat2-/- and IRF9-/- MEFs that induction of ADAR1 p150 occurs by STAT2- and IRF9-dependent signaling that is enhanced by, but not obligatorily dependent upon, STAT1.
0.92 STAT1 and STAT2 in human 2fTGH cells
0.92 Stat1(Delta221-365)-/- mutant MEFs but not detectably by treatment of Stat2-/- MEFs as revealed by quantitation of western immunoblots (Fig. 3C).
0.92 STAT1 and STAT2.
0.92 STAT2 binding to PA; the binding of STAT2 was observed in Stat1-/- MEFs following IFNalpha treatment (Fig. 5).
0.92 Stat1(Delta221-365)-/- and Stat2-/- mutant MEFs, either untreated or IFN-treated, as indicated under Materials and Methods.
0.92 Stat1(Delta221-365)-/- MEFs, using either no antibody (-) or with antibody (+) against STAT1 (A) or STAT2 (B).
0.89 STAT1 and STAT2 transcription factors leads to their dimerization and association with transcription factor IRF9 to form the heterotrimeric ISGF3 complex.
0.89 STAT2 also bound the promoter region of Oas1b in Stat1-/- MEFs.
0.88 STAT1 and STAT2.
0.88 Stat1(Delta221-365)-/- MEFs but not in Stat2-/- or IRF9-/- MEFs
0.87 STAT1 (U3A) and STAT2 (U6A) mutant lines, and U3A mutant cells reconstituted for STAT1 expression (U3A-RH) were left untreated or treated with IFN-alphaA/D for 24h.
0.82 STAT2 functions with IRF9 as a STAT2 homodimer in type I IFN-treated Stat1-/- MEFs to activate transcription.
0.71 STAT1 protein and mutant U6A cells lacking STAT2 protein (Fig. 1B), exon 1A RNA levels were low and comparable to that of untreated cells (Fig. 1A).
30682178 0.98 STAT1/STAT2 and IFN regulatory factor 9 (IRF9).
0.98 STAT1/STAT2 phosphorylation.
0.98 STAT1/STAT2/IRF9 DNA-binding in promoters of IFIT1 and IFIT2 in HeLa WT and HeLa Bclaf1-KO cells simulated with PBS or human IFNalpha (500U/mL) for 1h.
0.98 STAT1, STAT2 and IRF9.
0.98 STAT1/STAT2 phosphorylation is catalyzed by JAK1 and TYK2 activated by IFN-induced receptor dimerization, which occurs rapidly in the membrane.
0.98 STAT1/STAT2/IRF9 entered the nucleus following the IFNalpha treatment, more STAT1/STAT2/IRF9 was found to bind to Bclaf1 and the promoter of the ISGs as well.
0.97 STAT1/STAT2/IRF9 to the promoters of ISGs was also greatly decreased in Bclaf1-KO HeLa cells (Fig 5A) and Bclaf1-silenced HEp-2 cells (S5 Fig) compared with that in relative control cells.
0.97 STAT1/STAT2/IRF9 as well as increased concentrations of purified Bclaf1 followed by a streptavidin-bead pull-down.
0.97 STAT1/STAT2/IRF9 is required for its ability to enhance IFNalpha transcription, we overexpressed Bclaf1 full-length and the indicated fragments in HEp-2 followed by IFNalpha treatment.
0.97 STAT1/STAT2 phosphorylation is unknown.
0.96 STAT1/STAT2/IRF9 antibodies respectively.
0.96 STAT1, STAT2, IRF9 and Bclaf1.
0.96 STAT1/STAT2 phosphorylation without affecting the expression of upstream components suggests that Bclaf1 may be involved in pre-existing modifications of STAT1/STAT2 by regulating relevant enzymes.
0.95 STAT1 and STAT2 induced by IFNalpha; 3) Bclaf1 binds with ISRE and facilitates the binding of ISGF3 complex to promoters of the ISGs; 4) Bclaf1 interacts with ISGF3 through STAT2; 5) Bclaf1 is degraded by US3 during PRV and HSV-1 infection; and 6) In the absence of US3, PRV and HSV-1 become more sensitive to IFNalpha treatment, which is partly due to the unreduced level of Bclaf1 in the cells.
0.95 STAT1/STAT2/IRF9-mediated transcription of ISGs in the nucleus is not fully understood.
0.94 STAT1, STAT2, IRF9 and Flag-Bclaf1 in nuclear immunoprecipitates of a HEp-2-Flag-Bclaf1 cell line transfected with si-control or si-STAT2 followed by PBS or human IFNalpha (500U/mL) treatment for 3h. (E) IB analysis of Bio-ISRE pull-down STAT1, STAT2, IRF9 and Bclaf1.
0.93 STAT1/STAT2/IRF9 (Fig 6D).
0.93 STAT1/STAT2/IRF9.
0.92 STAT1, P-STAT2, STAT1, STAT2 and Bclaf1 in HeLa WT and HeLa Bclaf1-KO cells treated with human IFNalpha (500U/mL) for the indicated time.
0.92 STAT1/STAT2/IRF9 to Bio-ISRE in a dose-dependent manner, and Bclaf1 was present in the Bio-ISRE pull-down complex (Fig 5B).
0.92 STAT1, STAT2 or IRF9 by co-expressing various Flag tagged Bclaf1 fragments with Ha tagged STAT1, STAT2 or IRF9 in HEK293T cells and performing co-IPs, and identified the region 236-620 responsible for binding to these proteins (Fig 6C).
0.91 STAT1/STAT2 to be efficiently phosphorylated in response to IFN; on the other hand, it interacts with ISGF3 complex in the nucleus mainly through STAT2 and facilitates their interactions with the promoters of ISGs.
0.90 STAT1/STAT2/IRF9 occurred in the absence of IFNalpha treatment and was increased after IFNalpha treatment, correlating with more STAT1/STAT2/IRF9 being translocated into the nucleus (Fig 6A and 6B and S6 Fig).
0.89 STAT1/STAT2 phosphorylation.
0.85 STAT1/STAT2/IRF9 and GST-Bclaf1 F2. (B) IB analysis of immunoprecipitates of HEK293T cells co-transfected with Flag-tagged Bclaf1, Ha-tagged STAT1 or STAT2/IRF9 expression plasmids.
0.82 STAT1 and STAT2, between the Bclaf1 knockdown or knockout cells and the WT controls was observed (S4C and S4D Fig).
0.76 STAT1/STAT2 (S4A and S4B Fig).
0.72 STAT1, -STAT2 or -IRF9 with GST-Bclaf1 F2 followed by GST pull-down assays.
0.65 STAT1/STAT2 to the ISGs promoters in the Bclaf1-knockdown cells was due to the reduced nuclear STAT1/STAT2 in these cells, we performed a DNA pull-down assay to directly measure whether STAT1/STAT2/IRF9 binding to the promoters was enhanced by Bclaf1.
0.59 STAT1/STAT2 in the Bclaf1-knockdown cells was reduced accordingly (Fig 4C).
30940163 0.98 STAT1 phosphorylation by IFNa stimulation is independent from STAT2 (Fig. 3b), suggesting that receptor recruitment is different in JAK2V617F-positive cells.
0.98 STAT1/STAT2 signaling in the clonal cells themselves, cell-extrinsic effects such as IFNa-mediated activation of the immune system is certainly important.
0.97 STAT1 or STAT2, respectively, was performed in 32D-BCR-ABL and 32D-JAK2V617F cells to evaluate the role of these transcription factors for IFNa efficacy.
0.97 STAT1, STAT2, and STAT3 were analyzed to potentially explain the striking differences of STAT2(Y/F) reconstitution in BCR-ABL- and JAK2V617F-positive-S2ko cells.
0.97 STAT1 and STAT2.
0.97 STAT1 and STAT2 in BCR-ABL- and JAK2V617F-positive cells.
0.97 STAT2(Y/F) cells were sensitized to low doses of IFNa, presumably due to upregulation of STAT1 protein expression (Fig. 4a, b).
0.96 STAT1, STAT2, STAT1Y701F, or STAT2Y689F to analyze the importance of wild-type and phosphomutant STATs for the IFNa response.
0.96 STAT1 and IRF1: controls: n = 16, CML: n = 13, PV: n = 8; STAT2: controls: n = 5, CML: n = 8, PV: n = 6.
0.96 STAT1/STAT1 and STAT1/STAT3 dimers shifts in dependence of the amount of active STAT2.
0.94 STAT1 and STAT2 knockout cell lines, we were able to demonstrate that, in BCR-ABL-positive cells, STAT2 is essential for IFNa-induced STAT1 phosphorylation (Fig. 3a), supported by the observation that pY-STAT2 recruits STAT1 to the activated IFNa receptor.
0.94 STAT2 is partially phosphorylated leading to ISG repression and is not capable to induce STAT1 expression.
0.94 STAT2, although not phosphorylated in JAK2V617F-positive cells, can induce STAT1 expression in the presence of histone marks representing active promoters (i.e., H3K9ac and H3K27ac).
0.93 STAT1, STAT2, and STAT3 in their unphosphorylated and phosphorylated states could probably help to predict the response to IFNa.
0.92 STAT2 reconstitution (and to a lesser extent, STAT2Y/F) was able to rescue ISG transcription (Stat1 and Irf7, while Irf9 was not decreased in the absence of STAT2) in JAK2V617F- but not BCR-ABL-positive cells (Fig. 4d).
0.90 STAT1 and Y689 in STAT2) STAT1/2 in a BCR-ABL or JAK2V617F background, 32D-BCR-ABL- and 32D-JAK2V617F-S1ko or 32D-JAK2V617F-S2ko cells were reconstituted with wt-STAT1, wt-STAT2, the dominant negative form STAT1Y701F (STAT1Y/F), or the phospho-deficient STAT2Y689F (STAT2Y/F) mutant, respectively.
0.89 STAT2 disruption, IFNa-induced STAT1 phosphorylation was preserved in JAK2V617F cells, with the latter showing nearly complete loss of STAT1 protein (Fig. 3a, b).
0.89 STAT1 or STAT2 ko cells was abrogated but strongly induced in STAT1- (and to a lesser extent, STAT1Y/F)-reconstituted BCR-ABL- and JAK2V617F-positive cells (Additional file 8: Figure S9A, B).
0.89 Stat1, Stat2, Irf1, and Irf9 in 32D-BCR-ABL cells, but increased it in all four promoter regions in 32D-JAK2V617F cells (Fig. 5b).
0.88 STAT2ko is less effective in repression of ISG expression (Fig. 3f and Additional file 10: Figure S8A, B) in comparison to JAK2V617F-STAT1ko cells, presumably due to the retained pY-STAT1 after IFNa stimulation (Fig. 3b).
0.82 STAT2 is essential for STAT1 phosphorylation at its tyrosine residue Y701 in BCR-ABL-positive cells (indicated by red arrow).
0.81 STAT1 and STAT2 in the sensitivity of JAK2V617F- vs. BCR-ABL-positive cells to interferon alpha
0.80 STAT1 or STAT2 alters IFNa sensitivity of 32D-JAK2V617F cells
0.76 STAT2, in BCR-ABL-positive cells, led to a strong downregulation of STAT1 protein, including induction of pY-STAT1 by IFNa.
0.75 STAT1, STAT2, and STAT3 was analyzed.
0.64 Stat1, Stat2, Irf7, and Irf9 mRNA expression in the indicated cell lines.
0.64 STAT1 led to a decrease of STAT2 protein while preserving IFNa-induced STAT2 phosphorylation and to an abrogation of most IFNa-induced effects (ISG expression, reduced cell viability, and with a tendency for induction of apoptosis), suggesting that both the JAK2V617F-induced sensitization to IFNa as well as IFNa-induced effects are STAT1-mediated (Fig. 3b, d-f, and Additional file 8: Figure S9a, b).
0.62 STAT1ko and STAT2ko cells.
0.56 STAT1ko or STAT2ko cells reconstituted with wt-STAT1, wt-STAT2, STAT1Y701F (Y/F), or STAT2Y689F (Y/F) were applied in a MTT assay and treated with the indicated concentrations of IFNa (0-104 U/ml) for 72 h. MTT assays have been performed four times in independent experiments, and untreated controls were analyzed with one-way ANOVA and Dunn's multiple comparison test.
24069549 0.98 STAT1 and STAT2 in the interferon JAK-STAT pathway
0.98 STAT1 or STAT2 SH2 domains.
0.98 STAT1 and STAT2 occupancy is observed at an unannotated region of chromosome 2 at position 146,449,900-146,451,900, and appears to be dependent on IFN stimulation (Fig. 2C).
0.97 STAT1 and STAT2 proteins are key mediators of type I and type III interferon (IFN) signaling, and are essential components of the cellular antiviral response and adaptive immunity.
0.97 STAT1 and STAT2 in association with IFN regulatory factor 9 (IRF9).
0.97 ISGF3 complex is thought to occur by sequential phosphorylation of STAT1 and STAT2.
0.97 STAT1 and STAT2 targets
0.97 STAT1 or STAT2 (Fig. 2B).
0.96 STAT1 and STAT2 interacting with IRF9 to form an active transcription factor may not completely explain the range of transcriptional regulation phenomena associated with STAT-driven target genes in the IFN response and points toward the need for additional genome-scale studies of STAT protein occupancy.
0.96 STAT1- and STAT2-regulated transcription.
0.95 STAT2 recruitment following IFNalpha treatment, some genes were found to contain unphosphorylated STAT2, invoking the involvement of a transcription factor complex distinct from ISGF3.
0.93 STAT1 and STAT2 primarily associate to form ISGF3, but have also been reported to form other transcription factor complexes in response to IFN stimulation.
0.93 STAT1 and STAT2 at the unannotated locus.
0.92 STAT1 and STAT2 interact with IRF9 to form ISGF3.
0.91 STAT1 and STAT2 and association with IRF9 to form the active transcription factor complex ISGF3.
0.91 STAT1, a STAT2/IRF9 complex, and ISGF3II.
0.90 STAT2 may also associate with tyrosine-phosphorylated STAT1 and IRF9 to form ISGF3II and stimulate low levels of ISRE-containing gene expression in response to prolonged IFNgamma treatment (Fig. 1B).
0.89 STAT1 and STAT2 primarily drives dimerization and formation of the ISGF3 complex.
0.88 ISGF3-mediated gene regulation are thought to be common features applicable to several ISGs, there are also many reports of distinct cases of non-canonical STAT1 or STAT2 signaling events and distinct patterns of co-regulators that contribute to gene-specific transcription.
0.85 STAT1 and STAT2 signal at the ISG54 promoter reaffirms it as a direct target of ISGF3.
0.80 STAT1 and STAT2 occupancy
0.75 STAT1 and STAT2 at unannotated loci might reflect a role in regulating non-coding RNA genes or may represent experimental artifacts.
0.75 STAT1 and STAT2 are known to interact with transcriptional co-activation machinery, but STAT2 has a prominent transcriptional activation domain at its C-terminus that has been recognized as the predominant ISGF3 component responsible for recruiting co-regulators.
0.75 STAT1, and STAT2 were not sensitive to BRG1.
0.69 STAT1 and STAT2 at all target sites.
0.63 STAT1 or STAT2, IRF9 is thought to be transcriptionally inert.
0.59 STAT1 and STAT2 are key components of the transcription factor complex in the IFN signaling pathways.
0.58 STAT2 is capable of pre-associating with the IFNAR2 chain, where it can become phosphorylated first, providing a docking site for the STAT1 SH2 domain.
25588716 0.98 STAT1, STAT2, and IRF-7 in AI-resistant MCF-7:5C breast cancer cells and AI-sensitive MCF-7 and T47D cells.
0.98 STAT1 and STAT2 form homodimers or heterodimers, move to the nucleus and activate the transcription of interferon response genes.
0.98 STAT1 and p-STAT2 expression in the resistant cells, thus suggesting a critical role for the IFNalpha canonical signaling pathway in driving the constitutive expression of the ISGs in the resistant cells.
0.97 STAT1, STAT2, IRF-7, and IFNalpha expression.
0.97 STAT1/STAT2 completely suppressed IFITM1, PLSCR1, p-STAT1, and p-STAT2 expression in the resistant cells, thus confirming the involvement of the canonical IFNalpha signaling pathway in driving the overexpression of IFITM1 and other interferon-stimulated genes (ISGs) in the resistant cells.
0.97 STAT1 and STAT2 revealed complete suppression of IFITM1, PLSCR1, p-STAT1 and p-STAT2 in the resistant cells, thus confirming a critical role for canonical IFNalpha signaling in the regulation of IFITM1 and other ISGs in the resistant cells.
0.97 STAT1 and p-STAT2 protein expression in the resistant cells (Figure 3F).
0.97 STAT1, anti-phospho-STAT1 (Y701), anti-IFNAR1, anti-STAT2, anti-phospho-STAT2 (Tyr690) and anti-beta-actin.
0.97 STAT1 and STAT2 regulate IFITM1 and PLSCR1 expression in resistant MCF-7:5C cells
0.97 STAT1/STAT2 knockdown reduces IFITM1 and PLSCR1 expression.
0.97 STAT1 siRNA (siSTAT1) or STAT2 siRNA (siSTAT2) and STAT1, STAT2, IFITM1 and PLSCR1 protein levels were assessed at 24 and 48 hours by Western blot analysis (left panels).
0.97 STAT1 and STAT2 are members of the signal transducers and activators of transcription family of transcription factors that play a pivotal role in regulating type I (alpha/beta) and type II (gamma) interferon signaling.
0.97 STAT1 and STAT2 completely suppressed IFITM1 and PLSCR1 expression in resistant MCF-7:5C cells (Additional file 6: Figure S6), thereby confirming a critical role for STAT1 and STAT2 in the regulation of IFITM1 and PLSCR1 expression.
0.97 STAT1/STAT2 signaling pathway and that knockdown of STAT1 and STAT2 and blockade of IFNalpha function dramatically suppressed IFITM1 and PLSCR1 expression in the resistant cells.
0.97 STAT1, STAT2, MX1 and OAS1 were overexpressed approximately 10- to 300-fold in AI-resistant MCF-7:5C cells compared to AI-sensitive parental MCF-7 cells (Additional file 1: Figure S1).
0.97 STAT1 and STAT2 play a critical role.
0.96 STAT1 siRNA (siSTAT1) or STAT2 siRNA (siSTAT2) and the effect of knockdown on IFITM1 and PLSCR1 expression was assessed at 24 and 48 hours using Western blot analysis.
0.95 STAT1 and STAT2, resulting in the formation of STAT1-STAT1 homodimers and STAT1-STAT2 heterodimers.
0.95 STAT1 or STAT2 is capable of altering their expression in MCF-7:5C cells.
0.95 STAT1, STAT2, IRF-7, IRF-9, IFIT1, OAS1 and MX1 are constitutively overexpressed in AI-resistant breast cancer cells.
0.92 STAT1 and STAT2 dramatically reduced IFITM1 expression in the resistant cells.
0.88 STAT1 and STAT2 were constitutively overexpressed in AI-resistant MCF-7:5C cells compared with MCF-7 cells (Additional file 1: Figure S1).
0.87 STAT1, p-STAT1 (Y701), STAT2, p-STAT2 (Tyr690) and IFNAR1 were determined by Western blot analysis.
0.84 STAT1, p-STAT1, STAT2, p-STAT2 and IFNAR1 protein expression in a time-dependent manner with maximum induction of PLSCR1, IFITM1, STAT1, STAT2 and IFNAR1 observed at 24 hours and for p-STAT1 and p-STAT2 at 30 minutes (Figure 4A, left panel).
0.82 STAT2, STAT2, p-STAT1, STAT1, and IRF-7 protein expression in resistant MCF-7:5C cells.
0.78 STAT2 protein; however, it did not further increase the level of IFITM1, PLSCR1 or STAT1 at any of the time points except at 24 hours where we detected a <2-fold increase in PLSCR1 and IFITM1 (Figure 4A, right panel; Additional file 2: Figure S2).
0.78 STAT1 and Y690 for STAT2) which drives the expression of ISGs.
0.64 STAT1, and p-STAT2 expression in the resistant cells.
25812002 0.98 STAT1, STAT2, and HDAC1 on ISG54 and CXCL10 promoters after UV-HCMV infection.
0.98 STAT1, STAT2, HDAC1, HDAC2, and PML (Fig. 6A), whereas immunoprecipitation with control IgG did not coprecipitate any of these proteins in the control (Fig. 6A).
0.98 STAT1, STAT2, HDAC1, HDAC2, and PML during infection.
0.98 STAT1 or STAT2 levels.
0.98 STAT1, STAT2, HDAC1, and HDAC2, and with ISG promoters, which concurs with previous findings regarding the direct interactions between PML and HDAC1 and HDAC2 and the association between PML and STAT1 in IFNgamma-treated cells.
0.97 STAT1, STAT2, and their phosphorylated forms.
0.97 STAT1, STAT2, and their activated forms.
0.97 STAT1 in PML-knockdown HF was decreased to 60% of control cells, while STAT2 transcription was unaffected (Fig. 2F).
0.97 STAT1, STAT2, HDAC1, and HDAC2 in UV-HCMV-infected cells but not in uninfected cells (Fig. 3A).
0.97 STAT1 and STAT2, but also affects ISG expression by directly associating with ISGF3 and HDACs.
0.97 STAT1, STAT2, HDAC1, HDAC2, and PML (PG-M3).
0.97 STAT1, STAT2, HDAC1, HDAC2, and PML during infection and the binding of IE1(Delta290-320) with STAT2 and HDACs.
0.97 STAT1 and STAT2 and of their activated forms were comparable in cells infected with wild-type or mutant viruses (Fig. 7A).
0.95 STAT1, STAT2, and HDACs in virus-infected cells.
0.95 STAT1 and STAT2.
0.95 STAT1, STAT2, HDAC1, and HDAC2, but not with IRF9 and ribonucleotide reductase R1 (as negative controls), were also observed in cells treated with IFNbeta (S3A Fig).
0.95 STAT1 and STAT2 and directly acting on ISG promoter to regulate ISGF3.
0.94 STAT1 and resulted in higher levels of the activated forms of STAT1 and STAT2 than in control cells (Fig. 2D).
0.94 STAT1 and STAT2 mRNA levels in shC and shPML HF cells were measured by qRT-PCR.
0.94 STAT1 and STAT2 components of ISGF3.
0.92 STAT1 and STAT2.
0.91 STAT1 and STAT2) via Janus kinase 1 (Jak1).
0.89 STAT1, STAT2, HDAC1, HDAC2, and PML during infection
0.87 STAT1, STAT2, HDAC1, and HDAC2, we investigated whether IE1 simultaneously interacts with PML, STAT1, STAT2, and HDACs during infection.
0.84 STAT1, STAT2, HDAC1, and HDAC2 and with ISG promoters
0.84 STAT1, STAT2, HDAC1, and HDAC2 and with ISG promoters are induced after UV-HCMV infection.
0.73 STAT1, STAT2, and their activated forms was observed in 293 cells treated with IFNbeta (Fig. 2C).
0.70 STAT1 and STAT2 expression, although it can partly affect the activation of STAT proteins via an autoregulatory loop (Fig. 2E).
27907166 0.98 STAT1 and STAT2.
0.98 signal transducer and activator of transcription 1 (STAT1) and STAT2.
0.98 STAT1 and STAT2, an immunoprecipitation of STAT1 from IFNalpha-stimulated cells was performed in cells transiently transfected with C6 or N1, a VACV Bcl-2-like protein that does not inhibit IFNalpha signalling.
0.98 STAT2 bound to STAT1 either before or after stimulation (Fig 3).
0.98 STAT1 and STAT2.
0.98 STAT1 (Fig 4A) or STAT2 (Fig 5A).
0.98 STAT1 and STAT2 increased to approximately 50% (Fig 4B) and 70% (Fig 5B), respectively.
0.98 STAT1 could not be assessed in PiV5-V expressing cells due to its degradation by this viral protein, however, PiV5-V expression inhibited the translocation of STAT2 completely (Fig 5A).
0.98 STAT2 and a constitutively active ISGF3 mimic, IRF-9-S2C, were still able to bind to the ISRE in the presence of C6 (Fig 7), indicating C6 exerts its inhibitory effect after ISGF3 binding to the ISRE.
0.97 STAT1 and STAT2 phosphorylation, nuclear translocation and binding of the interferon stimulated gene factor 3 (ISGF3) complex to the interferon stimulated response element (ISRE).
0.97 STAT1 or STAT2, whereas PiV5-V protein inhibited the phosphorylation of both proteins as expected (Fig 2).
0.97 STAT2 was found associated with STAT1.
0.97 STAT1 and STAT2 before and after IFNalpha stimulation was assessed by confocal microscopy.
0.97 ISGF3 complex formation, a plasmid encoding IRF-9 fused to the C-terminal region (amino acids 747-851) of the transcriptional activation domain of STAT2 (referred to as IRF9-S2C) was utilised.
0.97 ISGF3 complex, an immunoprecipitation assay using FLAG-tagged STAT1, STAT2 and IRF-9 was performed.
0.97 STAT2 but not with STAT1 or IRF-9 (Fig 8A).
0.97 STAT1, STAT2 or IRF-9 expressing plasmids for 16 h (A), or co-transfected with TAP-tagged C6 or N1 and HA-STAT2 (B) or infected with the viruses shown for 16 h at 2 PFU/cell (C) or co-transfected with TAP-tagged C6 or N1 and IRF9-S2C or HA-IRF9 expressing plasmids for 16 h (D).
0.97 STAT2 and not STAT1, whilst N1 did not associate with either protein (Fig 8C), confirming the specific interaction between STAT2 and C6 at endogenous protein levels during viral infection.
0.97 STAT2 (Fig 8A-8C) and the transactivation domain (aa 747-851) of STAT2 fused to IRF-9 (Fig 8D) but not with STAT1 or IRF-9 (Fig 8A).
0.97 STAT1 or STAT2 as with PiV5 and PiV2 V proteins, respiratory syncytial virus NS1 and NS2 proteins and dengue NS5 protein, by inhibition of STAT phosphorylation as with Sendai virus C protein, or by cytoplasmic sequestration of the ISGF3 complex as with NiV and Hendra virus V proteins.
0.96 STAT2 bound to STAT1 in each condition.
0.92 STAT1 and STAT2 were examined and C6 was found to have no effect on these early events of this signalling pathway (Figs 2, 4 and 5).
0.90 STAT1 and STAT2 in cells expressing C6 following IFNalpha treatment was examined.
0.75 ISGF3- promoter binding but does so through interacting with and preventing the functioning of HATs and histone ubiquitylating complexes required for full ISG transcriptional activation and not through a direct interaction with STAT2.
0.72 ISGF3, likely through this C-terminal domain of STAT2, signals to and promotes transcription of ISGs by RNA polymerase II remains unclear.
0.62 STAT1 and STAT2 (VH1).
0.53 STAT1 and STAT2 and is delivered into cells by the invading virion immediately after infection.
28680969 0.98 STAT2 and impaired IFN-beta-induced phosphorylation but did not affect STAT1 or its translocation to the nucleus.
0.98 STAT2, STAT2 phosphorylated at Tyr690, STAT1, STAT1 phosphorylated at Ser727 or Tyr701, actin, and V5 with the appropriate antibodies.
0.98 STAT1 or STAT2 was observed.
0.98 STAT1 in immunoprecipitated samples, suggesting that the interaction of HRTV NSs or SFTSV NSs with STAT2 is stronger than that with STAT1.
0.98 STAT2 (but not STAT1) phosphorylation is inhibited by SFTSV NSs, another study has shown that the phosphorylation of STAT2 as well as of STAT1 at position Ser727 is blocked by SFTSV NSs.
0.98 STAT1 and STAT2 to the nucleus upon IFN stimulation to that of SFTSV NSs.
0.98 STAT1, no nuclear translocation of STAT2 was detected in cells transiently expressing V5-tagged HRTV or SFTSV NSs upon IFN treatment (Fig. 6G).
0.98 STAT1-STAT2 heterodimers.
0.98 STAT1 and STAT2, respectively.
0.97 ISGF3, composed of STAT1, STAT2, and IRF-9, which binds to the interferon-stimulated response element (ISRE) and enhances transcription of numerous antiviral interferon-stimulated genes (ISGs).
0.97 STAT1 and STAT2 in NSs-containing, round, cytoplasmic inclusion bodies (IB) or viroplasms.
0.97 STAT1 (F) and STAT2 (G) antibodies to visualize the subcellular localization of endogenous STATs (red), V5-tagged NSs (green), and DAPI-stained nuclei (blue) by confocal microscopy.
0.97 STAT1 and STAT2 were coimmunoprecipitated with HRTV NSs, suggesting that the IFN signaling interacting partners of these two proteins are conserved (Fig. 6C).
0.97 STAT2 levels in IP eluates were higher than those of STAT1 (relative to the respective total expression levels in the whole-cell lysate).
0.97 STAT1 and STAT2 proteins to the nucleus to activate the promoter of ISGs occurs via their phosphorylation and dimerization.
0.97 STAT1 or STAT2 phosphorylation using UUKV NSs as a negative control, as UUKV NSs did not block type I IFN signaling (Fig. 6A).
0.97 STAT2 (but not STAT1) results in the efficient inhibition of IFN-beta-induced STAT2 nuclear translocation.
0.97 STAT2, SFTSV NSs can also indirectly sequester IKKepsilon, IRF-3, and STAT1 into the inclusion bodies.
0.97 STAT1 and STAT2 translocation to the nucleus operates through their spatial isolation in inclusion bodies.
0.97 STAT1-STAT2 heterodimers, in association with IRF-9, translocate to the nucleus and bind to ISREs.
0.95 STAT1 and STAT2 (Fig. 6C).
0.95 STAT1 or STAT2 was observed in the presence of HRTV NSs, suggesting simply that an interaction between HRTV NSs and STAT2 may block phosphorylation of STAT2 and its heterodimerization with STAT1, consequently inhibiting the translocation of STAT1-2 heterodimers to the nucleus and thus inhibiting type I and type III IFN signaling.
0.94 STAT1 and STAT2 antibodies (C) or with a STAT3 antibody (D).
0.94 STAT1 and STAT2 in HEK293T cells upon treatment with recombinant IFN-beta.
0.90 STAT2 than with STAT1.
0.75 STAT2, but not STAT1, were efficiently inhibited in the presence of HRTV or SFTSV NSs proteins (Fig. 6E to G).
0.61 STAT1 and STAT2 into SFTSV NSs-formed inclusion bodies.
25564224 0.98 STAT1 KO cells overexpressing STAT2 recapitulate IFNalpha response
0.98 STAT1 KO cells is recapitulated by increasing STAT2 levels
0.98 STAT1-independent IFNalpha signalling pathway, where STAT2/IRF9 can substitute for the role of ISGF3.
0.97 STAT1 termed interferon-stimulated gene factor 3 (ISGF3) that binds to the interferon-stimulated response element (ISRE) in ISG promoters.
0.97 STAT2 and IRF9 in the residual IFNalpha-induced gene expression in the STAT1 KO cells, we next generated human and mouse STAT1 KO cells overexpressing STAT2 (hST2-U3C and mST2-MS1KO, respectively) or empty vector (Migr1-U3C and Migr1-MS1KO, respectively).
0.96 STAT1 and STAT2, members of the signal transducer and activator of transcription (STAT) family, mediated by Janus kinases (JAKs).
0.96 STAT1 KO cells correlates with diminished STAT2 phosphorylation
0.96 STAT2/IRF9 complex in the prolonged IFNalpha response in the absence of STAT1 and suggest an ISGF3-like function.
0.95 ISGF3, it is clear that STAT2 plays an essential role in the transcriptional responses to IFN with a strong dependence on STAT1.
0.95 STAT2/IRF9-containing complex is responsible for the IFNalpha response in the STAT1 KO cells overexpressing STAT2, we performed additional experiments.
0.95 STAT1 KO cells overexpressing STAT2 as opposed to WT cells.
0.95 STAT1 to impair the formation of ISGF3.
0.94 STAT1 expression in MEF WT (data not shown), suggesting that activation of STAT2/IRF9-dependent transcription depends on the level of STAT1 in WT cells.
0.93 STAT2 in STAT1 KO the IFNalpha response can be restored.
0.92 STAT2/IRF9 complex effectively drives transcription of the RIG-G (IFIT-3) gene in NB4 cells upon signalling cross-talk between retinoic acid and IFNalpha, in a STAT1-independent manner.
0.91 STAT1-independent IFNalpha signalling pathway in human liver cells that depended on STAT2 and IRF9.
0.89 STAT1 acetylation does not affect STAT2, it could be that under certain conditions STAT2/IRF9 may allow continuation of the IFNalpha response and prolonged transcription.
0.86 STAT2 to the ISRE in an IFNalpha-dependent manner in the absence of STAT1.
0.84 signal transducer and activator of transcription 2 (STAT2)/interferon regulatory factor 9 (IRF9)-dependent, STAT1-independent interferon alpha (IFNalpha) signalling pathway.
0.80 STAT1-defeicient U3C cells stably overexpressing human STAT2 (hST2-U3C) and STAT1-deficient murine embryonic fibroblast cells stably overexpressing mouse STAT2 (mST2-MS1KO) we observed that the IFNalpha-induced expression of 2'-5'-oligoadenylate synthase 2 (OAS2) and interferon-induced protein with tetratricopeptide repeats 1 (Ifit1) correlated with the kinetics of STAT2 phosphorylation, and the presence of a STAT2/IRF9 complex requiring STAT2 phosphorylation and the STAT2 transactivation domain.
0.80 STAT1 KO cells this ISGF3-dependent IFNalpha-response was severely abrogated, highlighting the importance of STAT1.
0.79 STAT1 in the ISGF3 complex (which can be achieved by HDACi or IFN pre-stimulation) seems incompatible with prolonged IFNalpha-dependent transcription.
0.72 STAT2/IRF9 dependent signaling pathway can induce a prolonged ISGF3-like transcriptome and generate an antiviral response analogous to ISGF3, independent of STAT1.
0.71 STAT2/IRF9 induces a prolonged ISGF3-like transcriptome and generates an antiviral response in the absence of STAT1.
0.56 STAT2 recapitulates interferon-stimulated gene expression in the absence of STAT1.
22634037 0.98 STAT1, or STAT2 levels, suggesting that an alternative mechanism must account for HSV-mediated inhibition of type-I interferon signaling pathways in these cell-lines.
0.98 STAT1 or STAT2 by phosphorylation.
0.98 STAT1 or STAT2 3'UTR.
0.98 STAT1, STAT2, IRF9, HSV gB and actin expression at 0, 4, 8, and 16 hpi.
0.97 ISGF3 consists of three subunits: signal transducers and activators of transcription 1 (STAT1); STAT2; and interferon regulatory factor 9 (IRF9).
0.97 STAT1 and STAT2; however, only STAT1 was phosphorylated in IFNbeta treated HSV-2 infected cells (Fig 7A and B: IFNbeta), indicating that HSV-2 specifically inhibited the phosphorylation of STAT2 but not STAT1.
0.97 STAT1, but not STAT2, irrespective of HSV-2 infection (Fig. 7B:IFNgamma), indicating that HSV-2 would not subvert type-II interferon responses through inhibition of STAT1 phosphorylation.
0.97 STAT2- or ISGF3-associated.
0.97 ISGF3 complex (STAT2, STAT1 and IRF9) in mock- or HSV-2-infected early phase-inhibited (A) and late phase-inhibited (B) cells at 0, 4, 8, and 16 hpi.
0.97 STAT1 or STAT2 cloned downstream of a luciferase reporter open reading frame.
0.97 STAT1 3'UTR or STAT2 3'UTR in early phase-inhibited 293A or late phase-inhibited C33A cells.
0.97 STAT1 and STAT2.
0.97 STAT1 or STAT2 phosphorylation in mock infected or in the context of an HSV-1 or HSV-2 infection was determined by western blot analysis.
0.96 STAT2, STAT1, IRF9, HSV1/2 gB, or actin.
0.95 STAT1 and STAT2.
0.95 STAT2 protein loss resulted from a complexly orchestrated series of events: 1) HSV-2 infection initiated the degradation of STAT2 transcripts, but did not affect either STAT1 or IRF9 mRNAs; 2) In cells that exhibited early replicative phase inhibition of IFN signaling, HSV-2 infection altered either translation or mRNA stability of transcripts that specified the 3'UTR of STAT2 more so than it affected transcripts with no 3'UTR or the 3'UTR of STAT1; 3) Nascent STAT2 proteins were targeted for cellular proteosomal degradation.
0.94 STAT2 protein was markedly reduced 8 hpi and completely absent by 16 hpi in HSV-2 infected early phase-inhibited cells; whereas neither STAT1 nor IRF9 protein levels were affected (Fig. 5A).
0.94 STAT2 translocates from the cytoplasm to the nucleus where it functions as a tripartite complex with STAT1 and IRF9 to initiate transactivation of ISGs.
0.93 STAT1 and STAT2; whereas, type-II IFN (IFNgamma) stimulates phosphorylation of only STAT1.
0.87 STAT1 or STAT2 expression levels in late phase-inhibited C33A (Fig. 7A: alphaSTAT1; alphaSTAT2) or 293alpha/beta (Fig. 7B) cells.
0.86 STAT2 3'UTR in a manner nearly analogous to what was seen for transcripts with the STAT1 3'UTR (Fig. 4E).
0.82 STAT2 is unique and critical to the type-I IFN signaling pathways; whereas, STAT1 functions both in type I and type II IFN signaling.
0.63 STAT1, or STAT2 transcript levels (Fig. 3B).
23431397 0.98 STAT1 or STAT2.
0.97 STAT2 phosphorylation, but show varied abilities to block IFNalpha and INF-gamma induced STAT1 phosphorylation.
0.97 STAT1 and STAT2.
0.97 STAT1/STAT2 and possibly other proteins as shown by Yokota et al., 2003 and hence, when the V protein is pulled down, Jak1 or Tyk2 is also being co-precipitated in the complex.
0.97 STAT1 and STAT2.
0.97 STAT1 and/or STAT2 with the paramyxovirus V proteins has been taken by a number of groups as a measure of direct binding of STATs to the V proteins, since STAT1 and STAT2 can only form heterodimers after phosphorylation; however, it has to be born in mind that we could still be looking at the precipitation of another, as yet uncharacterised, complex of V with other host cell proteins, although the variation in the ratio of STAT1 to STAT2 in the V-precipitated complexes argues against this.
0.97 STAT1 and STAT2.
0.95 STAT1/STAT2 phosphorylation in infected cells with any virus except RPV-Sa.
0.95 STAT1 or nuclear STAT2 (note that we were unable to get satisfactory results with antibody to phosphorylated STAT2, so took STAT2 accumulation in the nucleus as a measure of the phosphorylation of this protein, and prevention of STAT2 accumulation as an indication of a block of STAT2 phosphorylation, although it remains possible that STAT2 could be being phosphorylated in some of our studies but being prevented from entering the nucleus).
0.95 STAT2 plus goat anti-PPRV or (b, c) mouse anti-phospho-STAT1 (STAT1P) plus rabbit anti-RPV.
0.94 STAT1/STAT2 phosphorylation, we found that all the morbillivirus V proteins studied, except the V proteins from MeV-Edm and CDV-Ond, were efficient blockers of type I IFN induced STAT1/STAT2 phosphorylation.
0.93 STAT1 and STAT2 activation in cells infected with wild-type strains of the four morbilliviruses.
0.91 STAT1 (STAT1P) or (b) anti-STAT2 as in "Material and methods".. Representative confocal images from three independent experiments are shown.
0.89 STAT1 and STAT2.
0.89 STAT1 and STAT2 with different efficiencies, suggesting that they may have different affinities for the host cell proteins (Fig. 5).
0.89 STAT1 and STAT2 co-precipitated with the different V proteins.
0.86 STAT1 and STAT2, and in some cases no apparent binding, despite good expression of all the relevant V proteins.
0.75 STAT2 (Fig. 1a); however, they showed varying abilities to block IFNalpha or IFNgamma induced STAT1 phosphorylation (Fig. 1b, 1c).
0.72 STAT1 and STAT2 respectively (essentially the same as RPV-Sa V, as shown in Fig. 2a, 2c).
0.67 STAT2 (with RPV and PPRV V proteins being 2-3-fold more effective), there is a much bigger difference in the apparent ability to bind STAT1, with RPV and PPRV V proteins co-precipitating many times more STAT1 than CDV-5804p V, which in turn brought down more than MeV-Dub V.
0.64 STAT1 and STAT2 were detected with different antibodies, and therefore we cannot determine the actual ratio of STAT1 to STAT2 in any co-precipitate, we could use the light signal emitted from the Western blots to compare the ratio between V proteins; we found signal ratios (STAT1:STAT2) from STAT1 and STAT2 associated with the different V proteins varying from 7.8 (RPV RBOK) to 0.3 (MeV Dub).
0.60 STAT1 or STAT2 using rabbit anti-STAT1 and rabbit anti-STAT2 antibodies respectively.
0.56 STAT1 and STAT2 by the different V proteins using co-immunoprecipitation.
24416652 0.98 STAT2 and STAT1 activation.
0.98 STAT2-deficient cells other than U6A, STAT1 tyrosine phosphorylation is unaffected.
0.98 STAT2 and STAT1 exist as dimers in resting cells, this suggested that a pre-initiation complex of IFNAR2:STAT2:STAT1 was critical for proper type I IFN signaling.
0.98 STAT1 in STAT2.
0.97 STAT2 was suggested to be important for proper formation of the active STAT2:STAT1 dimer.
0.97 STAT2 and T288A-STAT1 suggest that phosphorylation of S287 accelerates dephosphorylation of STAT2 thus contributing to termination of JAK-STAT signaling.
0.97 STAT2:STAT1 and STAT2 homodimers could bind a version of gamma-activated sequence, the consensus sequence that several STAT-dimers bind to including STAT1, in gel-shift assays, but with much lower affinity than STAT1 homodimers.
0.97 STAT2:STAT1 complex, not containing IRF9 and relying on both STAT2 and STAT1 for DNA-binding, was suggested to be the complex affected by the DNA-binding deficient STAT2 mutant, but no direct evidence for this was found.
0.97 STAT2, pY701-STAT1, and IRF9 assembled after 24 h of IFN-gamma treatment, and induced a subset of ISGs.
0.95 STAT1 and STAT2, triggering their dimerization and association with the DNA-binding Interferon regulatory factor 9 (IRF9) resulting in the formation of the IFN stimulated gene factor 3 (ISGF3) complex.
0.95 STAT2, as well as both forms of STAT1, were phosphorylated at tyrosine (Y)-690 (STAT2) and Y701 (STAT1) in response to IFN-alpha.
0.95 STAT1-activation was dependent on STAT2 in type I IFN signaling, but not in response to type II IFN (IFN-gamma).
0.95 STAT2 complexes have been identified in vitro, including STAT2:STAT1 heterodimers without IRF9, STAT2 homodimers and STAT2:STAT3 heterodimers.
0.93 STAT2, STAT1, and IRF9 form the ISGF3 complex, which translocates to the nucleus by binding to importin-alpha5.
0.92 STAT2 and STAT1.
0.92 STAT2 was critical for STAT1-activation most likely due to the pre-association of IFNAR2 with STAT2 in untreated cells.
0.92 STAT2 and STAT1 activation.
0.88 STAT2:STAT1 heterodimer was not affected leading to increased ISGF3 assembly in the presence of active IKKepsilon and higher expression of ISGs with low-affinity ISREs.
0.80 STAT1 and IRF9, whereas STAT2 is responsible for recruiting transcriptional co-activators through its TAD.
0.76 STAT1, phosphorylation (or any other PTM) could potentially direct the formation or stability of a specific STAT2-complex.
0.73 STAT2 to phenylalanine, which is also close to the SH2-pY interface based on the crystal structure of STAT1, prolonged STAT1-activation and ISGF3-signaling due to a decrease in STAT1 dephosphorylation.
0.72 STAT2 and IRF9, in the absence of STAT1.
0.68 STAT2 in STAT1 is T288.
29581268 0.98 STAT1 or U-STAT2.
0.98 STAT1 may assist by inducing the expression of U-STAT2 and IRF9 as target genes of phosphorylated ISGF3.
0.98 STAT1-NF-kappaB and STAT3-NF-kappaB complexes are likely to form in the cytosol, and we know that U-STAT2 is required for the translocation of p65 into the nucleus in bone marrow-derived macrophages.
0.98 STAT2-IRF9 and U-ISGF3 might be the principal mediators of collaboration with activators of NF-kappaB in cancer cells, and we did observe that high levels of U-STAT2 and IRF9 correlate with poor prognoses in lung adenocarcinoma.
0.97 STAT2 and IRF9 that help to drive IL6 expression are achieved late in response to type I IFNs, since the STAT1, STAT2, and IRF9 genes are all ISGs that are activated strongly by tyrosine-phosphorylated ISGF3 during the initial response to these IFNs.
0.96 STAT2 contributes its strong transactivation domain to ISGF3, IRF9 contributes the principal DNA binding domain, and STAT1 stabilizes the complex and also provides additional DNA contacts.
0.96 STAT2 and IRF9 were increased in BJ human foreskin fibroblasts and STAT1-null fibroblasts, respectively, followed by q-PCR analysis of IL6 mRNA expression.
0.96 STAT1, STAT2, and IRF9 were used for immunoprecipitation of Flag-tagged proteins.
0.95 STAT2 plus IRF9 increased IL6 expression by about 2-fold in STAT1-null fibroblasts and by about 3-fold in wild-type fibroblasts (Fig. 1J), similarly to the effects on DDX58 expression (SI Appendix, Fig. S3B).
0.95 STAT1, U-STAT2, and p65 in HME cells following stimulation with IFNbeta (Fig. 3D).
0.95 STAT2, IRF9, and IL6 correlated with poor overall survival in lung adenocarcinoma patients, and STAT1 and IFNB expression did not (SI Appendix, Fig. S8).
0.94 ISGF3 target gene, was also decreased after 48 h compared with 24 h of IFNbeta treatment in BJ cells (SI Appendix, Fig. S1F), but the induction of STAT1, IRF9, and STAT2 were not decreased at 48 h (Fig. 1E), similarly to the induction of IL6.
0.92 STAT2, STAT1, and IRF9 are shown.
0.91 STAT1, STAT2, and IRF9 genes are all ISGs that are strongly induced by type I IFNs.
0.88 STAT2- and IRF9-dependent, but STAT1-independent manner.
0.86 ISGF3, STAT1 can participate in ISRE-dependent activation of IL6 expression, but it is not required since the U-STAT2-IRF9 complex functions well even without STAT1.
0.85 STAT1, U-STAT2, or IRF9 showed that p65 binds strongly to U-STAT1 and U-STAT2, but not to IRF9 (Fig. 3C).
0.84 STAT1 is not related to IL6 secretion or to the level of tyrosine- phosphorylated STAT3 in these cells, confirming that STAT2 and IRF9 but not STAT1 are principally required for the production of autocrine IL6.
0.83 ISGF3, STAT2 and IRF9 interact with components of other signaling pathways to stimulate transcription.
0.80 STAT2-IRF9 complex, U-ISGF3, or both, may also interact with transcription factors other than NF-kappaB to induce the expression of genes that facilitate the growth of cancer cells.
0.73 STAT2 and DDX58, was less in IFNbeta-treated STAT1-null cells than in wild-type cells (Fig. 1E and SI Appendix, Fig. S1F).
0.65 STAT2 and IRF9 is similar to the induction of a subset of IFN-induced genes in response to U-ISGF3, but quite different from the induction of classical ISGs in response to phosphorylated ISGF3 (SI Appendix, Fig. S1E); therefore, the IL6 gene is not a classical ISG.
0.64 STAT2, STAT1, and p-STAT3 levels by the Western method.
21178011 0.98 STAT1 and IRF9 were upregulated with each treatment, but STAT2 was not.
0.98 STAT1, STAT2, and IRF9 proteins in the cytoplasm.
0.98 STAT1 allows these accumulated proteins to favorably interact to form ISGF3II even though STAT2 is not phosphorylated.
0.98 STAT1 and STAT2, resulting in formation of the classical ISGF3 complex that has high affinity for ISRE sequences.
0.98 STAT1 (via phosphorylation at Y701) and STAT2 (via phosphorylation at Y689) activation as well as total STAT1, STAT2, and IRF9 expression.
0.98 ISGF3 components (STAT1, STAT2, and IRF9) was performed on the immunoprecipitated samples.
0.98 STAT2 and STAT1 on immunoprecipitated samples, as described in A.
0.98 STAT2, and incubated with 10 IU/ml IFN-alpha or IFN-gamma for 24 h. Cell lysates containing equivalent amounts of protein were added to each well and subjected to SDS-PAGE, after which Western blots were performed with STAT1, STAT2, or IRF9 Abs.
0.97 STAT1 and IRF9 that precipitated with STAT2 at 24 h decreased when an Ab that neutralized IFN-gamma signaling was added to the media after 15 h of IFN-gamma treatment (Fig. 4A, lane 10).
0.97 STAT1 activation in IFN-gamma-treated cells and accumulation of ISGF3 lacking STAT2 phosphorylation.
0.97 STAT1, (B) STAT2, and (C) IRF9 after IFN-gamma and IFN-alpha2a treatment.
0.96 ISGF3 containing unphosphorylated STAT2 (ISGF3II) complex in human A549 cells after treatment with IFN-gamma.
0.96 ISGF3/ISGF3II formation to the total amount of STAT1, STAT2, and IRF9 in each treatment group (Fig. 4A, lanes 1-5).
0.96 STAT1 and STAT2, also play a role in IFN signaling.
0.95 STAT1 and STAT2 were phosphorylated after IFN-alpha and IFN-gamma treatment.
0.93 ISGF3 complex, the complex containing unphosphorylated STAT2 will be referred to as ISGF3II.
0.91 ISGF3/ISGF3II formation after IFN treatment, we used siRNA to knock down STAT2 and IRF9.
0.91 STAT1 and IRF9, or 2 microg Ab against STAT2.
0.87 STAT1, STAT2, and IRF9 physically bind to the promoters of the ISRE-containing genes following IFN-gamma treatment.
0.83 STAT1-, STAT2-, and IRF9-containing transcription factor complexes are also recruited to the PKR promoter after treatment with IFN-gamma (Fig. 7).
0.69 STAT1 and IRF9 can lead to transient ISRE activation by homodimers of STAT1 or STAT2 complexed with IRF9, and STAT2 and IRF9 can associate with each other prior to IFN treatment.
21255624 0.98 STAT1 and STAT2 in response to IFN-beta is blocked in RSV-infected BMDCs
0.98 STAT1 and STAT2 in response to IFN-beta are blocked in RSV-infected BMDCs.
0.97 STAT1 and STAT2 phosphorylation and translocation were abolished by UV inactivation.
0.97 STAT2 facilitates the IFN-beta-stimulated phosphorylation of STAT1 by serving as a docking site for STAT1; STAT2 must be phosphorylated in response to IFN-beta prior to recruitment and subsequent phosphorylation of STAT1.
0.97 STAT1, RSV infection significantly inhibited IFN-beta-mediated phosphorylation of STAT2 in BMDCs (Fig. 3A).
0.97 STAT1 and STAT2 are key cellular events in mediating IFN-beta-transduced signaling.
0.97 STAT1 and STAT2 to translocate to the nucleus in response to IFN-beta treatment were unaltered (Fig. 5).
0.97 STAT1 (5A) and STAT2 (5B) were detected with a rabbit anti-STAT1 and anti-STAT2 antibody followed by incubation with a goat anti-rabbit-conjugated Cy3 antibody (green), while RSV (red) infection was detected using a mouse anti-RSV-F protein antibody and a goat anti-mouse Cy5 antibody.
0.95 STAT1 and STAT2 in BMDCs, but impaired the IFN beta-dependent phosphorylation and nuclear localization of STAT1 and STAT2.
0.95 STAT1 and STAT2 in the mouse BMDCs and, therefore, do not suggest that degradation of STAT2 serves as the inhibitory mechanism in BMDCs.
0.94 STAT2 (p-STAT2) and STAT1 (p-STAT1), leading to STAT2-STAT1 heterotrimerization with interferon regulatory factor (IRF) 9 and nuclear localization.
0.92 STAT1 phosphorylation in lung epithelial cells by targeting STAT2 for proteasomal degradation.
0.91 STAT1 in response to IFN-beta, we investigated whether RSV also impairs IFN-beta-mediated STAT2 phosphorylation and transcriptional activation in BMDCs.
0.91 STAT1 and STAT2 during RSV infection and in response to IFN-beta signaling.
0.90 STAT1 and STAT2 for proteasome degradation by polyubiquitination.
0.89 STAT1 and STAT2 phosphorylation and translocation.
0.85 STAT1 and STAT2 (Fig. 5A and B).
0.70 STAT1 and STAT2 to be redistributed to cytoplasmic aggregates and can inhibit both IFN-alpha and IFN-gamma-dependent STAT1 and STAT2 nuclear localization.
0.65 STAT1 and STAT2 phosphorylation and nuclear translocation.
0.60 STAT1 and STAT2 into the nucleus as was seen in the mock-infected and IFN-beta-treated cells (Fig. 5A and B).
0.55 STAT1 and STAT2, but impaired the IFN-alpha-and IFN-beta-dependent phosphorylation of STAT1 and STAT2.
26897526 0.98 STAT1 and STAT2 proteins were also reduced following IFNalpha and IRF7 knockdown (Fig. 4c).
0.98 STAT1, STAT2, and IFITM1 after STAT1 and STAT2 genes were knocked down in SUM149 cells using siSTAT1 and siSTAT2.
0.98 STAT2 knockdown cells in SUM149 as compared with STAT1 (Fig. 7c), suggesting that STAT2 played a critical role in IFITM1 induction in these cells.
0.98 STAT1 and STAT2 protein expression in both cell lines, but the induction of STAT1 and STAT2 by exogenous IFNalpha was less robust than that of IFITM1.
0.98 STAT2 can homodimerize upon phosphorylation, and bind interferon regulatory factor 9 (IRF9) to form a non-ISGF3 complex that is capable of binding the GAS or ISRE/IRF sequences at the promoter region of a subset of ISGs and induce their transcription without the participation of STAT1 in a noncanonical interferon signaling pathway.
0.98 STAT2 complexes, without STAT1, are capable of inducing a subset of ISGs without the formation of ISGF3.
0.97 STAT1, and STAT2 after interferon receptor (IFNR)-alpha/beta was neutralized using mouse anti-human IFNR-alpha/beta chain 2 monoclonal antibody (Ab) in SUM149 cells.
0.97 STAT1 and STAT2 protein levels in these cells.
0.97 STAT1 and STAT2 knockdown on 2-D colony formation in SUM149 cells.
0.97 STAT1 and STAT2 knockdowns on the ability of SUM149 cells to migrate.
0.97 STAT1 and STAT2 in the regulation of IFITM1 in SUM149 cells, siRNAs were used to knock down their expression.
0.97 STAT1, STAT2, and IRF9.
0.96 STAT1 and STAT2 are transcription factors that play a critical role in regulating type I IFNalpha/beta signaling.
0.96 STAT1 and STAT2 on promoter activity, we knocked down STAT1 and STAT2 in the cells that were transfected with the -750/-1 construct and measured the luciferase activity in the cells.
0.96 STAT1, and STAT2 in these cells; however, the further induction of these ISGs in SUM149 cells did not alter the growth or aggressive phenotype of these cells.
0.95 STAT1, STAT2, and the formation of the complex interferon-stimulated gene factor 3 (ISGF3), ultimately inducing many ISGs, including IFITM1.
0.91 STAT2, not STAT1, plays a dominant role in regulating IFITM1 transcriptional activation in SUM149 cells through binding to multiple consensus sequences such as ISRE/IRF and GAS.
0.87 STAT2 completely suppressed IFITM1 expression in SUM149 cells, whereas knockdown of STAT1 did not significantly reduce IFITM1 protein expression in these cells.
0.87 STAT2 was reported to mediate STAT1-independent protection against dengue virus infection in mice that were deficient in STAT1 through the formation of non-ISGF3 complexes that involved STAT2 homodimers, and did not require STAT1.
0.84 signal transducer and activator of transcription 1 (STAT1), and STAT2 protein expression following the suppression of IRF7 and IFNalpha in SUM149 cells.
0.73 STAT1, p-STAT1, STAT2, and p-STAT2) in the SUM149 and SUM190 cells.
30283459 0.98 STAT2-SH2 domain, on the other hand, remained in a similar position as in STAT1 and STAT3-SH2 domains.
0.98 STAT1, STAT2, and STAT3 (A).
0.98 STAT1, STAT2 and STAT3 (B).
0.98 STAT1, STAT2 and STAT3 and binding to target gene promoters and their expression
0.97 STAT1, STAT2, and STAT3 activity and pro-inflammatory target gene expression may be a promising strategy to treat CVDs.
0.97 STAT1, STAT2 and STAT3 (B).
0.94 STAT1, STAT2 and STAT3 in a concentration dependent manner (STATTIC: between 10 and 2.5 muM for 8 h; STX-0119: between 25 and 6.25 muM for 24 h).
0.92 STAT1-BS (9.84), as well as STAT1-CBAV (3.6 for STAT2 and 4.14 for STAT3).
0.92 STAT1, R601 in STAT2 and R609 in STAT3, which were experimentally proven to be crucial for STAT phosphorylation and reciprocal binding of the pTyr-linker to the STAT-SH2 domain [STAT1-R602; STAT2-R601; STAT3-R609 ].
0.92 STAT1, STAT2, and STAT3 have been recognized as prominent modulators of inflammation, especially in immune and vascular cells during atherosclerosis.
0.88 STAT1, STAT2, and STAT3, NF-kappaB and different IRFs coordinates robust expression of multiple chemokines, adhesion molecules, antiviral and antimicrobial proteins.
0.85 STAT1 targets; IFIT1, IFIT2, IFIT3, OAS1, OAS2, MX1, MX2, ISG15 as STAT1-STAT2 targets; SOCS3, CCND1, MMP3, FAS PIM1, VEGF, S1PR1 as STAT3 targets) could be recognized.
0.84 STAT1, STAT2, and STAT3 was followed.
0.84 hSTAT1, hSTAT2, and hSTAT3 (Figure 6).
0.78 STAT1, STAT2, and STAT3 with similar affinity.
0.70 STAT1-CBAV for STAT2 and STAT3, 1.74 and 2.08 respectively, whereas the STAT1-BS was lower by 1.5 than for C01L_F03 (Table 3).
0.70 STAT1, STAT2, and STAT3 activity.
0.62 STAT1 and STAT2 (Table 4) similar to STAT3.
0.60 STAT1, STAT2, and STAT3 with the same affinity and simultaneously blocks their activity and expression of multiple STAT-target genes in HMECs in response to IFNalpha.
0.60 STAT1, R601 in STAT2 and R609 in STAT3, resulted in a significant decrease in binding stability (DeltaG0) between the SH2 domains of STAT1, STAT2 and STAT3 and all three inhibitors.
0.52 STAT1/STAT2)-target genes, CXCL10, IFIT2 and OAS2, as well as the STAT1 target gene, IRF1 and the STAT3 target gene, SOCS3.
31426476 0.98 STAT2 and IRF9 depends to a large extent on the STAT1-dependent canonical pathway, but that a significant response occurs in the absence of STAT1.
0.98 STAT1-independent, but STAT2- and IRF9-dependent, gene expression in response to IFNbeta + TNF.
0.98 STAT2/IRF9 complex is also supported by our recent observation of a high affinity of IRF9 for STAT2 with an equilibrium dissociation constant (Kd) of 10 nM. A recent report of experiments, performed in murine bone marrow-derived macrophages proposes a model in which murine STAT2/IRF9 complex drives basal expression of ISGs, while IFNbeta-inducible expression of ISGs depends on a switch to the ISGF3 complex.
0.97 STAT1-independent, but STAT2/IRF9-dependent, pathway mediates gene expression through a restricted ISRE site usage compared to the ISGF3-dependent regulation.
0.97 STAT1 and to document the role of STAT2 and IRF9 in this response.
0.97 STAT1-independent genes positively regulated by STAT2 and IRF9 (Category A).
0.97 STAT1-independent differentially expressed genes (DEGs) and their regulation by STAT2 and IRF9.
0.96 STAT1 and STAT2, and to a lesser extent other STAT members in a cell-specific manner.
0.96 STAT1, we next sought to gain insight into the role of STAT2 and IRF9.
0.96 STAT2 and IRF9 in the absence of STAT1 in response to IFNbeta and TNF (Supplemental Table S1 and Figure 5C), but is also inducible by IFNbeta alone in the presence of STAT1 (Figure 1 and Figure 2A).
0.96 STAT2/IRF9 pathway compared to the ISGF3 pathway.
0.96 STAT2 and IRF9 actions most likely result from the formation of specific complexes that coexist with ISGF3 upon IFNbeta and TNF stimulation.
0.91 STAT2 and IRF9 are involved in the regulation of a subset of the genes induced in response to the co-stimulation by IFNbeta and TNF in the absence of STAT1.
0.91 STAT2- or STAT1-dependent.
0.90 STAT1-independent, but STAT2 and IRF9-dependent, manner raised the question of the ISRE site usage compared to the ISGF3 pathway.
0.89 STAT2/IRF9-containing complex mediating gene expression in the absence of STAT1 has been reported, but with limited DNA-binding affinity for the typical ISRE sequence.
0.85 STAT1 and define the role of STAT2 and IRF9, the U3A cells were transfected with Control (Ctrl)-, STAT2- or IRF9-RNAi and further left untreated or stimulated with IFNbeta (1000 U/mL) + TNF (10 ng/mL) for 24 h (Figure 2C).
0.83 STAT2 and IRF9 activation, i.e., STAT2 Tyr690 phosphorylation and induction of IRF9, were observed in the U3A cells following stimulation with IFNbeta + TNF, although to reduced levels compared to the parental 2ftGH cells expressing endogenous STAT1 (Figure 2B).
0.83 STAT1-P-Tyr701, total STAT1, STAT2-P-Tyr690, total STAT2, IRF9, or actin antibodies.
0.67 ISGF3, but not STAT2/IRF9, to specific ISRE sequences upon IFNbeta + TNF.
0.65 STAT1-Independent IFNbeta + TNF Induced DEGs According to their Regulation by STAT2 and IRF9
17325370 0.98 STAT1 itself does not interact directly with PIV5/V, but as STAT1 and STAT2 form transient heterodimers even under non-induced conditions, it is recruited into the complex via its association with STAT2.
0.98 STAT1 and STAT2 phosphorylation.
0.97 STAT1 and STAT2 were stabilized in MPRV-infected cells, as they were still detectable after 24 h infection.
0.97 STAT1 or Tyr689-phosphorylated STAT2.
0.97 STAT1, STAT2 and against the P proteins of the different viruses.
0.96 STAT1 or STAT2 for proteasomal degradation.
0.96 STAT1, STAT2, STAT3 and cellular actin, as well as with an antiserum raised against the P and V proteins of MPRV.
0.95 STAT1 and STAT2 that were induced by MPRV infection could still be detected more than 24 h p.i., which would seem to suggest that these forms are stabilized in MPRV-infected cells.
0.94 STAT1 is necessary to recruit STAT2 into the complex.
0.92 STAT2 degradation, but induced degradation of STAT1 rather than STAT2 in the bat cells.
0.92 STAT1 (green), or against (b) the V protein of MPRV (red) and STAT2 (green).
0.88 STAT1 or STAT2 depending on the species of origin.
0.87 STAT2, PIV5 does not induce degradation of STAT1 in murine cells, but is able to use exogenously supplied human STAT2 to form a functional complex that induces the degradation of endogenous murine STAT1.
0.86 STAT1 and STAT2 only became detectable in infected cells after IFN treatment (Fig. 3b, bottom panels).
0.71 STAT1 or STAT2 by MPRV in a wide variety of cells, it seems likely that MPRV/V also blocks IFN signalling in cells of its natural host via sequestration of STAT1 and STAT2 in an inactive form in the cytoplasm, rather than targeting them for degradation.
0.68 STAT1 and STAT2 in the cytoplasm and prevents their import into the nucleus.
0.67 STAT1 and STAT2 (signal transducers and activators of transcription) are activated by phosphorylation and form heterodimers that associate with a third factor, p48 [also called IFN regulatory factor 9 (IRF-9) or ISGF3gamma].
0.62 STAT1 and STAT2 in cytoplasmic or nuclear complexes that affect their localization and, in the case of Nipah virus (NiV), also their activation by Tyr-phosphorylation.
0.51 STAT1 and STAT2, but not DDB1.
22355301 0.98 Stat1 or Stat2 accumulation in cells infected with WT or F170S HPIV1, in contrast to what is seen with Rubulavirus infection (also see Figure 2).
0.97 Stat1 (Figure 8 and Videos S9, S10, S11, S12), but not Stat2 (Figure 9 and Videos S13, S14, S15, S16).
0.96 Stat1 and Stat2.
0.96 Stat1/2 degradation and that phosphorylation of Stat1 and Stat2 was reduced in WT HPIV1- and F170S HPIV1-infected cells following stimulation with IFN-alpha and IFN-beta.
0.96 Stat2 appeared to be diffusely distributed in the cytoplasm of cells infected with either WT or F170S HPIV1, in contrast to the aggregated state of Stat1.
0.95 Stat1 and Stat2 were retained in the cytoplasm during infection with WT HPIV1 but not F170S HPIV1, we investigated whether retention might be due to physical interaction with the C proteins, as has been reported for SeV C proteins, and whether the C proteins interacted with both phosphorylated and unphosphorylated Stat proteins.
0.93 Stat1, an effect that involved the two longer C proteins, C' and C, but not the shorter Y1 and Y2 forms, and which could be mimicked by the first 23 amino acids of C. Another line of experiments indicated that neither Stat1 nor Stat2 is degraded, and that the C proteins inhibit signaling from the IFN receptor by blocking phosphorylation of both Stat1 and Stat2, with the impaired phosphorylation of Stat2 being the more important effect.
0.92 Stat1 and Stat2.
0.89 Stat1 and Stat2 phosphorylation
0.88 Stat1 or Stat2 was not observed.
0.87 Stat1-containing granules do not appear to contain Stat2 suggests that the C proteins bind predominantly to monomeric Stat1 rather than to the ISGF3 complex (Stat1:Stat2:IRF9).
0.81 Stat1 and Stat2 in WT or F170S HPIV1-infected Vero cells following treatment with IFN-alpha, -beta, or -gamma.
0.81 Stat1 and Stat2, as well as for the HPIV1 C protein and HPIV2 P protein.
0.81 Stat1, but not Stat2, with M6PR
0.70 Stat2, nor a functional IFN receptor, nor Jak1 were required for the SeV-mediated increase in pY701-Stat1 accumulation, supporting the idea that the increase in pStat1 resulted from virus-mediated inhibition of dephosphorylation, with the phosphorylation signal probably stemming from a background level of IFN-independent phosphorylation.
0.68 Stat1 and Stat2 to the nucleus
0.67 Stat1 or Stat2 phosphorylation or stability between WT and F170S HPIV1-infected cells, we next examined translocation of Stat1 and Stat2 to the nucleus by confocal microscopy.
0.56 Stat2-containing aggregates were not as well defined and not as dense as Stat1 aggregates.
0.52 Stat1 (Figure 3) or Stat2 (Figure 4).
27929099 0.98 STAT2 can also homodimerize and associate with IRF9 to form an ISGF3-like complex.
0.98 STAT1 or STAT2 abolishes the inhibition of HCV replication by IFN-lambda.
0.97 STAT2 was discovered as a component of ISGF3 (ref.).
0.97 ISGF3, STAT2 can homodimerize and associate with IRF9 to form an ISGF3-like complex.
0.97 STAT1 and STAT2 and increase expression of similar sets of ISGs in hepatocytes, but with distinct kinetics.
0.97 ISGF3, a transcription factor complex composed of STAT1, STAT2, and IRF9 (ref.).
0.97 STAT1, and STAT2 in control cells (Fig. 5A and B).
0.97 STAT1 and STAT2 in control Huh-7.5 cells (Fig. 7A and B).
0.97 STAT1 knockout (KO) cells (clones #1 and #2), and STAT2 KO cells (clone #1) were treated with IFN-alpha (1,000 U/ml) (A) or IFN-lambda (1,000 U/ml) (B) for the indicated times.
0.96 STAT1 and STAT2 is required for ISGF3 formation.
0.94 STAT1, and STAT2 similarly to treatment with IFN-alpha in HCVcc-infected control cells (Fig. 6A).
0.93 STAT1 and STAT2 are essential for the inhibition of HCV replication by IFN-lambda
0.93 STAT1 and STAT2.
0.92 STAT2 in STAT1 knockout cells.
0.91 STAT2 complex lacking STAT1 can substitute for ISGF3 in IFN-alpha signaling.
0.84 STAT1 KO cells (clones #1 and #2), and STAT2 KO cells (clone #1) were treated with IFN-alpha (1,000 U/ml) or IFN-lambda (1,000 U/ml) for the indicated times.
0.79 STAT1 but are abolished by knockout of STAT2.
0.78 STAT1 and STAT2 are involved in the early induction of ISGs in response to IFN-alpha, most likely through the formation of ISGF3, but that when IFN-alpha stimulation is prolonged, ISGs can be induced by a STAT2-dependent, STAT1-independent pathway (Fig. 8).
0.77 STAT1 and STAT2 are required for the inhibition of HCV replication by IFN-lambda, control Huh-7.5 cells, STAT1 knockout cells, and STAT2 knockout cells were infected with HCVcc and treated with IFN-lambda.
20159032 0.98 STAT1 without directly interacting with it, as in the ISGF-3 complex in which CBP/p300 interacts with STAT2, but not STAT1.
0.98 STAT1 and STAT2 by trapping them into cytoplasmic high molecular weight complexes.
0.98 STAT1, its V protein interacts with STAT1, STAT2, STAT3 and IRF9, forming high molecular weight complexes that are packaged to cytoplasmic bodies containing an assembly of viral proteins and nucleic acid material of viral origin.
0.97 STAT1 belongs to the STAT family of transcription factors, which comprises seven factors: STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6.
0.97 STAT2 to which STAT1 binds through its SH2 domain, and STAT1 on tyrosine 701.
0.97 STAT1 and STAT2, thereby inhibiting the JAK-STAT IFN signaling pathway; however, the mechanisms involved for each V protein are different.
0.97 STAT1 and STAT2, preventing phosphorylation by JAK1.
0.96 STAT1 for proteasome-mediated degradation, some proteins target STAT1 only, others target both STAT1 and STAT2, some target only STAT2 and some target STAT3 for degradation.
0.95 STAT1/STAT2 dimer is then released from the IFNAR2 chain (Fig. 2B).
0.95 STAT1 and STAT2 resulting in their degradation by the proteasome, an action that is inhibited by proteasome inhibitors such as lactacystine or MG132.
0.95 STAT1, STAT2 and STAT3 and also specific degradation of STAT2 -an action that is prevented by proteasome inhibitors.
0.95 STAT1 by forming a complex with STAT2, and its expression into cells results in STAT1 being relocalised to the cytoplasm.
0.93 STAT1 belongs to a family of transcription factors comprising STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6.
0.92 ISGF-3 complex comprising STAT1, IRF9 and STAT2 which binds the ISRE DNA motif, and the GAF complex comprising a STAT1 homodimer which binds the GAS DNA motif.
0.91 ISGF-3 components STAT1, STAT2 and IRF9.
0.90 STAT2 by the viral 72 kDa protein IE1 which forms physical complexes with STAT1 and STAT2, thereby preventing correct nuclear localisation and association with the promoters of IFN-responsive genes.
0.87 STAT1, or heterodimerisation with STAT2, although it interacts much more strongly with phosphorylated STAT1 than with non-phosphorylated STAT1.
0.51 STAT1/STAT2 dimers, resulting in the polyubiquitylation of either STAT1 or STAT2.
23342031 0.98 STAT1 and some very limited binding to STAT2 as reported above, whereas no interaction was detected with the GST protein alone or a control protein corresponding to nsP4 from chikungunya virus (CHIKV) (Figure 7C).
0.98 STAT2 co-expression (compare cell lysates in Figure 7B and 7C), thus corroborating reports showing that STAT1 degradation by MuV-V is dependent on STAT2 binding.
0.98 STAT1 and STAT2 (150 ng/well of each vector).
0.98 STAT2, a model where both STAT2 binding and induction of STAT1 degradation by the V protein of PIV5 is restored.
0.98 STAT2, does not induce STAT1 degradation and is unable to block signal transduction downstream of IFN-alpha/beta and IFN-lambda receptors.
0.97 STAT2, does not degrade STAT1, and cannot block IFN-alpha/beta signaling in human cells.
0.97 STAT2 and DDB1 to recruit and degrade STAT1.
0.97 STAT2 or STAT1.
0.97 STAT1 or STAT2 expression levels (Figure 7C).
0.96 STAT2 binding and STAT1 targeting for proteasomal degradation.
0.96 STAT1 rather than STAT2 alike the V protein of hPIV2.
0.96 STAT1/STAT2 dimers that co-purified with MuV-V.
0.95 STAT1 as an adaptor to target STAT2 for degradation (although in some cases it can directly target STAT1 for degradation).
0.94 STAT2 (A) or STAT1 (B).
0.94 STAT1 degradation and the binding of TioV-V or MuV-V to endogenous STAT2.
0.86 STAT2 when STAT1 and STAT2 were co-expressed.
0.86 STAT2 and does not induce STAT1 degradation.
20939906 0.98 Stat1 and Stat2 fused with GFP either at the N-terminal or C-terminal ends.
0.97 Stat1 and Stat2 proteins were impaired in the R15-3 cells.
0.97 Stat1 or Stat2 protein could induce IFN promoter activation.
0.96 Stat1 and Stat2 proteins.
0.96 Stat1-GFP and Stat2-GFP fusion protein translocated to the nucleus of S9-13 cells 30 minutes after IFN-alpha treatment and returned to the cytoplasm by 24 hours (Fig. 2).
0.96 Stat1 and Stat2 phosphorylation and the subsequent impairment of nuclear translocation of ISGF3.
0.94 Stat1 or Stat2 was previously engineered.
0.94 Stat1-GFP and Stat2-GFP proteins were phosphorylated in the S9-13 cells but not in the R15-3 cells (Fig. 3).
0.94 Stat1-GFP or Stat2-GFP.
0.92 Stat1 and Stat2 proteins was prevented due to the lack of phosphorylation; whereas the nuclear translocation of IRF9 protein was not affected.
0.92 Stat1, Stat2 and IRF9 plasmid clones illustrated in Fig. 1A were used to establish the dynamics of nuclear translocation in the S9-13 and R15-3 cells in the presence and absence of IFN-alpha.
0.90 Stat1 and Stat2 then disassociate from the receptor and form the hetero-trimeric IFN-stimulated gene factor 3 (ISGF3) complex which then translocates into the nucleus and induces antiviral gene transcription.
0.82 Stat1 and Stat2 fusion proteins in the R15-3 cell line activated the ISRE-luciferase promoter in a concentration dependent manner.
0.75 Stat1-GFP and Stat2-GFP chimera proteins was efficient in the S9-13 cell line; however the nuclear localization of Stat1-GFP and Stat2-GFP did not occur in the R15-3 cells that possess defective Jak-Stat signaling.
0.72 Stat1 or Stat2 molecule of the Jak-Stat signaling pathway was examined.
0.66 Stat1 (IRF9-S1C) or Stat2 (IRF9-S2C) protein.
30355451 0.98 STAT2 were reduced while the STAT1 protein level did not change (Figure 5D).
0.98 ISGF3 subunits STAT2 than the normal or cancerous human kidney cells.
0.98 ISGF3 subunits STAT2 and IRF9 than that in kidney cancer cells, and this could disrupt the detection of ISGF3 mRNA expression in the cancer cells.
0.98 ISGF3 is traditionally activated by interferon stimulation through phosphorylation of STAT1 and STAT2.
0.98 STAT2 and IRF9, thus it might activate U-ISGF3 (Figure 5:figure supplement 1).
0.97 STAT2 +IRF9 or all three factors strongly induced ISGF3 targets PLSCR1 and MX1 (Figure 8A) and we chose the cells expressing STAT2 +IRF9 for further analysis.
0.97 STAT1 or STAT2 with immune and tumor cell markers within the TCGA dataset.
0.95 STAT1 or STAT2-suppressed cells were subjected to xenograft analysis.
0.95 STAT1, STAT2 or IRF9.
0.95 STAT2 staining was not associated with worse patient survival (Figure 9D), suggesting that other ISGF3 components are the more dominant players in the human ccRCC.
0.85 ISGF3 can be activated by either interferon-induced phosphorylation on STAT1 and STAT2 or increased unphosphorylated protein levels.
0.82 ISGF3 is a heterotrimeric transcription factor composed of STAT1, STAT2, and IRF9, and it can be activated either by interferon-induced posttranslational modifications or increased protein levels.
0.78 STAT2 +IRF9 did not change cell growth in culture (Figure 8B), however, overexpression of these ISGF3 components strongly suppressed tumor growth by PBRM1-deficient 786-O cells in a xenograft model (Figure 8C and D).Thus depletion of ISGF3 greatly enhanced tumor growth while its activation very potently blocked it, suggesting that ISGF3 is a central player in ccRCC tumor growth that is targeted by most of the cancer genes.
0.75 STAT2, IRF9 and PLSCR1, suggesting that BAP1's impact on ISGF3 is specific.
0.62 STAT1 or STAT2 with indicated genes within the TCGA dataset.
0.57 STAT1 or STAT2 in 786-O cells then performed xenograft analysis.
24058798 0.98 STAT1:STAT2 heterodimers can translocate to the nucleus and bind atypical gamma activated sequence (GAS)-like elements, the canonical interferon-stimulated gene factor-3 (ISGF3) complex of STAT2:STAT1:IRF-9 regulates a large fraction of the interferon pathway genes.
0.98 STAT1:STAT2 complexes by Nipah V protein is sufficient to prevent IFN-alpha/beta signaling even in the absence of the NES.
0.98 STAT1 degradation in a STAT2-dependent manner in human.
0.98 STAT1 via STAT2, mouse STAT2 does not interact with the PIV5 V protein.
0.98 STAT2 restores the ability of PIV5 V protein to mediated degradation of STAT1.
0.97 STAT2 recruitment and activation by both receptors involves tyrosine phosphorylation of STAT2 by JAK kinases and subsequent oligomerization with STAT1 and IRF-9.
0.97 STAT2 to the IFN-gammaR, IFN-gamma signaling can drive the formation of an ISGF3-like complex containing STAT2, inhibit viral replication and induce expression of IFN-alpha/beta target genes, perhaps through the pairing of phosphorylated STAT1 with latent STAT2.
0.97 STAT2 in a STAT1 dependent manner through distinct regions of the V protein mapping outside the boundary of the CTD.
0.97 STAT1 and blocking activation of STAT2.
0.97 STAT2 but not STAT1.
0.97 STAT2's dimerization partner STAT1 displays roughly 5-fold greater sequence similarity than STAT2 within primates (based on sequence identity within the phylogenetic analysis in Fig. 2), making STAT2 the most divergent member of the STAT family.
0.97 STAT1 and STAT2 among select mammals and non-human primates.
0.97 STAT1 and STAT2 for each species shown were aligned with the Clustal algorithm within MacVector.
0.92 STAT2 in STAT1-deficient fibroblast can limit DENV replication without any significant ISG expression.
27367734 0.98 STAT1 or STAT2 or both either directly or indirectly as described above by interaction with JAKs or altering the levels of JAKs.
0.97 STAT1 and STAT2.
0.97 STAT1 and STAT2 to prevent phosphorylation by way of their N-terminal and C-terminal regions.
0.97 STAT2, thereby inhibiting the transcriptional activation of the STAT2-containing ISGF3 complex.
0.97 STAT1 and STAT2 in response to IFN-gamma and IFN-alpha/beta.
0.96 STAT1 phosphorylation prevents either homodimerisation in the case of IFN-gamma induced signalling to form GAF, or the formation of a trimeric complex of ISGF3 with STAT2 and IRF9 in IFN-alpha/beta induced signalling.
0.93 STAT1 or STAT2 for degradation using their accessory V protein encoded by the P gene.
0.92 STAT1 and STAT2 are targets for the majority of viruses that manipulate the JAK/STAT pathway and the mechanisms involve ubiquitination and degradation and dephosphorylation.
0.91 STAT1 and STAT2 to prevent nuclear accumulation and the mumps virus NP protein co-localises with STAT2 in punctate aggregates in the cytoplasm.
0.89 STAT1, a role of STAT2 in IFN-gamma signalling has been reported by a number of investigators.
0.88 STAT1 (Tyr701) and STAT2 (Tyr690) form a heterodimer that binds IFN regulatory factor IRF9 (also known as p48 or ISGF3 gamma) in the cytoplasm forming the heterotrimeric transcriptional factor complex IFN-stimulated gene factor 3 (ISGF3).
0.86 STAT1 and STAT2.
0.56 STAT1 and STAT2 phosphorylation by interaction of its V protein (N-terminal domain) with JAK1.
0.56 STAT1 and STAT2 phosphorylation and nuclear translocation.
15883169 0.98 STAT2, which allows for the recruitment of STAT1.
0.98 STAT2, p-Tyr701 STAT1, STAT1, and beta-actin.
0.97 STAT1 but requires STAT2 for the inhibition of IFN-gamma responses.
0.96 STAT1 was not found in the pM27-STAT2 complex (unpublished data).
0.96 STAT1, but not STAT2, is required for IFNGR signaling, although the levels of STAT1 expression are decreased in STAT2-deficient fibroblasts.
0.96 STAT2, ruling out the possibility that STAT2 effected STAT1 function (Fig. 4 A).
0.95 STAT2 as well as STAT1 are indeed physically associated with IFNAR1 and IFNGR2 after IFN-gamma treatment, providing a possible pM27 checkpoint to interfere with.
0.94 STAT2, p-Tyr701 STAT1, and beta-actin.
0.93 STAT2 exclusively, whereas STAT1-dependent functions remained unaffected.
0.93 STAT2, STAT1, pM27, and beta-actin.
0.88 STAT1, but not STAT2, has a central role in both IFNAR and IFNGR signaling.
0.80 STAT1 dimers, but also STAT2 phosphorylation and thus ISGF3 autonomously, is of great biological advantage.
0.56 STAT2 occurred also in STAT1-/- fibroblasts (reference; unpublished data) and thus affects STAT2 monomers, indicating that the molecular mechanism used by pM27 is thoroughly different from the parainfluenza virus V protein that recognizes only STAT1/STAT2 heterodimers.
21994561 0.98 STAT1 and STAT2.
0.98 STAT1 degradation in murine cell culture, however, expression of human STAT2 in mouse fibroblasts enabled PIV5 to effectively disrupt murine IFN signaling and to support specific degradation of the endogenous murine STAT1.
0.97 STAT1, and prevents activation of both STAT1 and STAT2.
0.96 STAT2 targeting by hPIV2, however, is more promiscuous compared to STAT1 degradation by PIV5.
0.96 STAT1, Jak1, and STAT2) allow MeV V to form a multiprotein complex with IFN-alpha/beta signaling components and block signaling downstream of the IFN-alpha/beta receptor.
0.95 STAT1 and STAT2 tyrosine phosphorylation, and others showed that the C proteins cause prolonged tyrosine phosphorylation of STAT1, and impaired STAT1 serine phosphorylation.
0.95 STAT2 as a species-specific host range determinant and corroborated its importance as a cofactor for STAT1 targeting by PIV5.
0.92 STAT2 and is weakly associated with STAT1.
0.92 STAT1, STAT2, DDB1, and Cul4A.
0.87 STAT1/STAT2 heterodimers, which can ubiquitinate STAT1 in the presence of additional cellular proteins.
0.82 STAT1 for polyubiquitylation and proteasomal degradation, MuV V protein eliminates both STAT1 and STAT3, leaving STAT2 intact, and hPIV2 V protein targets STAT2.
0.81 STAT1 and not STAT2.
0.74 STAT2, with phosphorylation of STAT1 performed by Jak1 on tyrosine 701.
25973608 0.98 STAT2, whereas STAT1 levels were not affected.
0.97 STAT1 and STAT2.
0.97 STAT1 and STAT2 were unchanged (Fig 5A, upper panel).
0.97 STAT1 and GAPDH expression were also affected in these samples, but when we normalized STAT1 and STAT2 expression to GAPDH expression the reduction in STAT1 or STAT2 levels was not significant when ORF63 was expressed (Fig 5E).
0.96 STAT1 and STAT2 expression relative to GAPDH expression in the same samples.
0.96 STAT1 and STAT2 dimerize, which results in the loss of the NES of STAT2.
0.93 STAT1, STAT2 and IFN regulatory factor 9 (IRF9) complex termed ISGF3.
0.91 STAT2 nuclear translocation correlated with a SVV-mediated reduction in steady state levels of ISGF3 members or impaired STAT1/STAT2 phosphorylation.
0.91 STAT1, STAT2 and IRF9 in SVV-infected cells compared to unstimulated mock-infected cells (set at 100%).
0.91 STAT1, phosphorylated STAT1, STAT2, phosphorylated STAT2 (pSTAT2) and IRF9 using SDS-PAGE and western blot with specific antibodies.
0.86 STAT2, but downregulation of STAT1 was inconsistent between the experiments and inhibition of STAT1 phosphorylation was not observed.
0.85 STAT1, STAT2, ORF63 and GAPDH.
0.56 STAT1 phosphorylation was not reduced in SVV-infected TRFs it is unlikely that SVV interferes upstream of STAT1/STAT2 since the binding of IFN to its receptor triggers the activation of the tyrosine kinases JAK1 and TYK2 which in turn phosphorylate STAT1 and STAT2 resulting in the formation of the ISGF3 complex.
18494930 0.98 STAT2 binds to IFNAR2 and recruited STAT1 or STAT6 to the receptor.
0.97 STAT1, STAT2 and STAT6 (Fig. 3C-E).
0.96 STAT2 by RNAi reduced the phosphorylation of STAT1 (data not shown).
0.96 STAT2 seems to provide a docking site for STAT1 and STAT6, where they are subsequently activated following phosohprylation at Tyr 701 and 641, respectively.
0.95 STAT1: STAT2 het-erodimer will associate with IFN regulatory factor 9 (IRF9, p48) to form a STAT1: STAT2: IRF9 trimer, also known as ISGF3-(interferon-stimulated gene factor 3);this trimer then binds to cis-acting IFN-stimulated response elements (ISREs) to induce transcription of many IFN-stimulated genes (ISGs).
0.95 STAT1 and STAT2.
0.93 STAT1, STAT2, STAT3, STAT5 and STAT6 in HuH7 (A) and Hep3B (B) cells.
0.92 STAT2, the phosphorylation of STAT1 is weak.
0.90 STAT1, p-STAT2, p-STAT3, p-STAT5, p-STAT6).
0.90 STAT1, STAT2, and STAT3 by IFN-alpha and beta in human hepatocytes contributed in part to the effectiveness of IFN-alpha and beta anti-viral therapy hepatitis C patients.
0.89 STAT1, STAT2, STAT3, STAT5, STAT6 and betaactin antibodies to ensure equal loading of the cell extracts.
0.80 STAT2 at Tyr 690 is required for efficient activation of STAT1.
20084112 0.98 STAT2 and STAT1, which in turn heterodimerize and associate with interferon regulatory factor 9 (IRF9) to form a complex that is translocated into the nucleus to activate genes involved in antiviral response (reviewed in).
0.98 STAT1, MARV infection resulted in an inhibition of both STAT1 and STAT2 tyrosine phosphorylation.
0.98 STAT1 (A and B) or STAT2 (A).
0.98 STAT1-GFP or STAT2-GFP were co-transfected into Huh-7 cells with empty vector or with plasmids expressing ZEBOV VP40, ZEBOV VP24, MARV VP40 or MARV VP24.
0.97 STAT1 or STAT2 tyrosine phosphorylation and Tyk2 tyrosine phosphorylation is greatly reduced or eliminated.
0.97 STAT1 and STAT2 phosphorylation and on IFNgamma-induced STAT1 phosphorylation was compared.
0.97 STAT1 and STAT2 induced by IFNalpha (Fig. 1A).
0.96 STAT1-GFP (Fig. 4A, left panel) or STAT2-GFP (Fig. 4A, right panel).
0.93 STAT1 or STAT2 tyrosine phosphorylation (Fig. 4A).
0.88 STAT1 and STAT2 is strongly reduced in MARV- but not in ZEBOV-infected Huh-7 cells treated with IFNalpha.
0.82 STAT1 and STAT2.
0.64 STAT1 and STAT2 but also of the upstream kinases Jak1 and Tyk2.
20956346 0.98 STAT1 levels are similarly expressed in primary human leukocytes and STAT2 is activated normally in B cells
0.98 STAT1, STAT2 and STAT3.
0.98 STAT2 preceded the activation of STAT1 in fibrosarcoma cells and that STAT2-null cells are severely hampered in their capacity to activate STAT1.
0.98 STAT1 in primary human B cells at every IFN-beta concentration and in CD4+ T cells at lower IFN-beta concentrations, despite normal activation of STAT2.
0.98 STAT1, could be explained by the binding of either STAT2dimer/IRF9 or STAT2/STAT6/IRF9 to the ISRE, because primary human B cells can activate both STAT2 and STAT6 (Fig. 8B, and preliminary results).
0.97 ISGF3 (STAT1/STAT2/IRF9), which induces the expression of many genes.
0.97 ISGF3, a complex of phosphorylated STAT1, STAT2 and unphosphorylated IRF-9, binds to ISREs present in the promoters of many ISGs.
0.97 STAT2 in response to IFN-beta (Fig. 8B), and therefore failure to activate STAT2 is not the cause of low STAT1 activation in B cells.
0.97 STAT1 could be decreased activation of STAT2, because activation of STAT1 depends on the activation of STAT2 in fibrosarcoma cells and primary fibroblasts.
0.97 STAT2-deficient peritoneal macrophages retained the ability to activate STAT1, highlighting intriguing differences in the ability of the IFNAR to activate STAT1 in fibroblasts and monocytic cells.
0.97 STAT1 activation cannot be explained by differences in IFNAR2 expression levels, STAT2 activation or STAT1 levels
0.80 STAT2 (B), or intra-cellular STAT1 (C).
21075352 0.98 hISGF3-FLAG (hSTAT2-FLAG, STAT1-FLAG and IRF9-FLAG) or mISGF3-FLAG (mSTAT2-FLAG, STAT1-FLAG and IRF9-FLAG) plus ISRE-CAT-GFP, pCAGGS-Firefly luciferase and either E-Ub-NS5-HA 278-900, E-Ub-NS5-HA 10-900 or E-Ub-NS5-HA 1-900.
0.97 hSTAT2 expression during DENV infection does not require IRF9 or STAT1.
0.97 hSTAT2 (1-124, 1-239 and 1-316) in place of the STAT1 homologous region with the remainder of the downstream sequence derived from STAT1.
0.97 STAT2, STAT1-GFP and HA-tagged constructs.
0.97 hSTAT2 (1-124, 1-239 and 1-316) in place of the STAT1 homologous region with the remainder of the downstream sequence derived from STAT1.
0.97 hSTAT2-FLAG and lower arrows indicates expected mobility STAT1-FLAG and chimeras.
0.96 STAT1-GFP, and either hSTAT2-FLAG or mSTAT-FLAG.
0.94 STAT1, STAT2 and IRF9 proteins.
0.93 STAT1 deficient) to determine whether additional factors of the ISGF3 complex were required for DENV mediated hSTAT2 degradation, as is the case with some paramyxoviruses that degrade STAT proteins.
0.79 hSTAT2-FLAG and STAT1-GFP resulted in significant decreases in hSTAT2-FLAG protein level, as compared to the negative control lane where no E-NS5-HA was included (Fig. 7E lane 2 versus lane 1).
0.60 hSTAT2-FLAG as a similar decrease was not observed in the STAT1-GFP protein which serves as an internal negative control.
0.55 STAT1 and STAT2 form a heterodimer and when subsequently bound to Interferon Regulatory Factor 9 (IRF9) form the transcription factor complex Interferon Stimulated Gene Factor 3 (ISGF3).
29857509 0.98 STAT1 and STAT2) and two ubiquitination-related enzymes (UBA7 and UBE2L6).
0.96 STAT1 and STAT2 are transcription factors belonging to the STAT protein family.
0.95 STAT1 (signal transducer and activator of transcription 1), STAT2 (signal transducer and activator of transcription 2), UBA7 (ubiquitin-like modifier activating enzyme 7), and UBE2L6 (ubiquitin-conjugating enzyme E2L6), which significantly affected downstream apoptosis factors Caspase-3 (cysteinyl aspartate specific proteinase-3), Bcl-2 (B-cell lymphoma gene-2), Bax (BCL2-Associated gene X), and Caspase-9 (cysteinyl aspartate specific proteinase-9).
0.95 STAT1 and STAT2) and two ubiquitination-related enzymes (UBA7 and UBE2L6).
0.95 STAT1 and STAT2 in the cell nucleus increased, the fluorescence signal of UBA7 in the cell nucleus weakened, and the one of UBE2L6 seemed to exhibit no obvious change, when comparing them with the control.
0.95 STAT1 and STAT2 entered into the cell nucleus with the aim of regulating the expression of several apoptotic proteins after the stimulation of furosine; UBA7 usually locates in the whole cell, and it tended to translocate into cell cytosol and degradate proteins in apoptosis course in the furosine treatment group; UBE2L6 always locates in cell cytosol and still participates in protein degradation in cytosol, so its location seemed to display no change with the treatment of furosine.
0.95 STAT1 in cell; (B) STAT2 in cell; (C) UBA7 in cell; (D) UBE2L6 in cell.
0.91 STAT1, STAT2, P-STAT1, P-STAT2, UBA7, and UBE2L6 in the whole cells increased significantly (p < 0.05) with the treatment of furosine, in a dose-dependent manner, when compared with the control (Figure 3A,B).
0.90 STAT1, STAT2, UBA7, and UBE2L6, which might play a key role in participating cell apoptosis induced by furosine.
0.87 STAT1/STAT2/UBA7/UBE2L6 + furosine (100 mg/L), there seemed to be no obvioius up-regulation of apoptosis rates compared with the STAT1/STAT2/UBA7/UBE2L6 SiRNAs groups.
0.69 STAT1, STAT2, UBA7, and UBE2L6, etc.
0.52 STAT1, STAT2, UBA7, and UBE2L6
30558110 0.98 STAT2 (discussed below), which is required for the formation of transcription complexes involved in type I and III IFN signaling, the intracellular balance of STAT-containing complexes shifts to STAT1-STAT1 dimers, resulting in increased IFN-gamma-induced gene expression.
0.97 STAT1, STAT2, and IRF9, are sustained for several days, resulting in increased levels of the unphosphorylated forms of these proteins.
0.97 STAT1 and induce the degradation of STAT2.
0.97 STAT2 frees up STAT1 proteins to homodimerize and translocate to the nucleus to selectively activate ISGs controlled by gamma activated sites (GAS).
0.97 ISGF3 binding to ISRE promoter elements in the nucleus, or by preventing IRF9 association with STAT1/2 heterodimers in the cytoplasm.
0.95 STAT1 and STAT2 dimerize and then associate with a third protein, interferon regulatory factor 9 (IRF9).
0.95 STAT1 and STAT2 phosphorylation, but further investigation is required for this conclusion.
0.94 STAT2 contributes a potent transactivation domain, and STAT1 stabilizes the complex through additional DNA interactions.
0.93 STAT1 and STAT2).
0.87 STAT1 and STAT2 induces a conformational change within STAT2 that allows for NS5 binding.
0.84 ISGF3-like transcriptome in the absence of STAT1.
0.69 STAT1, STAT2, Tyk2, and JAK1.
28165510 0.98 STAT2 and STAT1, which results in formation of the DNA binding STAT1/STAT2/IRF9 ternary complex IFN-stimulated gene factor 3 (ISGF3).
0.98 STAT2 CC/DB counteracted the negative effect of USP18, resulting in increased STAT1 phosphorylation.
0.98 STAT2 is well known as an unique effector of type I and type III IFN signaling not only by being an integral component of the ISGF3 complex responsible for the induction of ISGs, , but also by positively regulating STAT1 phosphorylation .
0.98 STAT2 CC/DB has an inhibitory effect on the function of USP18 and thus increases STAT1 phosphorylation.
0.97 STAT2 mutant Y690F in U6A cells did not enhance IFNalpha-induced STAT1 phosphorylation (Fig. 6d).
0.97 STAT1, USP18, and the STAT2 CC/DB fragment were co-expressed in HEK 293T cells (Fig. 7a).
0.97 STAT2 CC/DB 3A retained its ability to disrupt the USP18 inhibitory effect on STAT1 phosphorylation (Fig. 7a, right lane).
0.96 STAT2 is responsible for recruitment of USP18 to IFNAR2 and is critical for the negative effect of USP18 on type I IFN-induced JAK1 phosphorylation (Fig. 2i-k), which is upstream of type I IFN-induced STAT1 activation.
0.95 STAT2 is not only critical for ISGF3 formation and ISG regulation, but also for STAT2-mediated STAT1 phosphorylation .
0.92 STAT1 phosphorylation in STAT2 deficient U6A cells (Fig. 2f), suggesting that STAT2 is required for USP18-mediated inhibition.
0.65 STAT2-USP18 interaction is not affected by this mutation (Supplementary Fig. 6d), USP18 expression still reduced phosphorylation of STAT1 in STAT2 Y690F-expressing U6A cells stimulated with IFNalpha (Fig. 6d).
29137231 0.98 STAT1, STAT2, and IRF9 mRNA expression levels in NOKs (1,5,9), NOKs+HPV16 (2,6,10), NOKs+HPV16 B (3,7,11) and HTK+HPV16 using GAPDH as an endogenous control gene.
0.98 STAT1 expression, an already identified HR-HPV target, the down regulation of IRF9 demonstrates that HPV16 directly targets the ISGF3 complex for down regulation in oral keratinocytes.
0.97 ISGF3 (STAT1-STAT2-IRF9), U-ISGF3, is downregulated by HPV16 in this oral keratinocyte model.
0.97 STAT1 and STAT2 in the cytoplasm promoting their dimerization and complexing with IRF9 resulting in an ISGF3 complex that translocates to the nucleus.
0.95 STAT1 and IRF9 and the increased expression of these factors extends several days following interferon treatment resulting in an un-phosphorylated (U)-ISGF3 complex that elevates expression of a 29 gene signature set.
0.95 STAT1 and STAT2; and E7 complexes with cytosolic IRF9 preventing translocation to the nucleus therefore hindering ISGF3 function.
0.92 STAT1 and IRF9 gene expression, it seems likely that the reduction in expression of IFNkappa contributes somewhat to the reduced expression of STAT1 and IRF9 and the consequent repression of the U-ISGF3 gene set by HPV16.
0.89 ISGF3 components STAT1 and IRF9 in NOKs+HPV16
0.83 ISGF3 is a transcription factor complex comprised of STAT1, IRF9 and STAT2.
0.83 ISGF3 include STAT1 and IRF9, which themselves are regulated by a positive feedback loop.
0.75 STAT1 and STAT2 which form a ternary complex with IRF9 resulting in the transcriptional activator ISGF3 that locates to the nucleus and activates transcription of interferon stimulated genes (ISGs).
29580840 0.98 STAT1 and STAT2 degradation; while Mumps protein V promotes degradation of STAT1, STAT2 and STAT3 via formation of a Cul4A-DDB1-dependent E3 complex.
0.98 STAT1, (B) STAT2, (C) STAT3 and (D) p65 antibodies (kDa ladder weights included on right of blots).
0.98 STAT1, (B) STAT2 and (C) STAT3 antibodies (kDa ladder weights included on right of blots).
0.98 STAT1, STAT2 and STAT3 protein expression was examined using immunoblotting.
0.98 STAT1 and STAT3 protein levels, while STAT2 expression was not significantly affected (Fig. 2A-C).
0.98 STAT1 and STAT3, but not STAT2.
0.97 STAT1, STAT2 and IFN Regulatory Factor (IRF)9, called the IFN-Stimulated Gene Factor (ISGF)3.
0.97 STAT1, STAT2 and STAT3 proteins were measured by Western blotting and quantified by densitometric analysis.
0.97 STAT1 and STAT3 protein levels were significantly reduced, while STAT2 expression was unaffected (Fig. 1A-C).
0.97 STAT1, STAT2 or STAT3 interacted with Vif.
0.81 STAT1 and STAT3, (but not STAT2), and its expression promotes ubiquitination and MG132-sensitive, proteosomal degradation of both proteins.
30240626 0.98 STAT2 and IRF9 mapped to TSS loci compared with STAT1 and may reflect the unique and obligatory association of STAT2 and IRF9 in gene regulation.
0.97 STAT1 peaks (top), 3,209 STAT2 peaks (middle), and 2,129 IRF9 peaks (bottom).
0.96 STAT1, STAT2, IRF9, and cofactors GCN5 and BRD2
0.94 ISGF3 occupancy and chromatin dynamics, ChIP time course assays were performed to examine the kinetics of promoter binding by ISGF3 components STAT1, STAT2, and IRF9, as well as Pol II (Figure 1A).
0.94 STAT1, STAT2, and IRF9 occupancy after mock or 2-hr IFNalpha treatment in HeLa cells.
0.93 STAT1 (top), STAT2 (middle), and IRF9 (bottom) binding at 2,531, 3,209 and 2,129 genomic loci representing sites with a >= 2-fold increase in occupancy after IFNalpha treatment.
0.93 STAT1, phosphotyrosine 701 STAT1, STAT2, phosphotyrosine 690 STAT2, and GAPDH protein expression in control or H2A.Z knockdown HeLa cells with or without 1-hr IFNalpha treatment.
0.92 STAT1 peaks (top), 3,209 STAT2 peaks (middle), and 2,129 IRF9 peaks (bottom) as described in Table S1.
0.90 ISGF3 occupancy was examined by ChIP-seq at steady state and after 2-hr IFN stimulation using STAT1, STAT2, and IRF9 antisera.
0.65 ISGF3 activity, H2A.Z loss was examined in a series of cell lines with single gene defects in ISGF3 components STAT1, STAT2, or IRF9.
0.54 ISGF3 was observed throughout the genome following IFN stimulation, with STAT1, STAT2, and IRF9 recruitment to 2,531, 3,209 and 2,129 target loci, respectively (Figure 1C and Table S1).
30944204 0.98 STAT1 and STAT2 were associated with unfavorable prognosis in moderately differentiated type GC, but with favorable prognosis in poorly differentiated type GC (Figure 4A-D).
0.98 STAT1, high STAT2 mRNA expression was associated with better OS in poorly differentiated and stage III GC patients.
0.97 STAT1 (Affymetrix ID: 200887_s_at), (C) STAT2 (Affymetrix ID: 225636 _at), (D) STAT4 (Affymetrix ID: 206118 _at), (E) STAT5a (Affymetrix ID: 203010 _at), and (F) STAT5b (Affymetrix ID: 212549 _at) are plotted for all GC patients.
0.97 STAT1, STAT3, and STAT6 mRNA expression in intestinal type GC patients were significantly associated with unfavorable OS, while STAT2 was modestly associated with unfavorable OS (Figure 3E-H).
0.97 STAT1 and (B) STAT2 are plotted for moderately differentiated type GC patients.
0.97 STAT1, (D) STAT2, and (E) STAT6 are plotted for poorly differentiated type GC patients.
0.97 STAT1, STAT2, and STAT4 were associated with favorable OS, while STAT5b was associated with poor OS (Table 1).
0.96 STAT1 (HR: 0.71; 95% CI: 0.57-0.89; P=0.0025), STAT2 (HR: 0.75; 95% CI: 0.57-1; P=0.05), STAT4 (HR: 0.76; 95% CI: 0.61-0.94; P=0.013), STAT5a (HR: 0.81; 95% CI: 0.66-1; P=0.05), and STAT5b (HR: 0.81; 95% CI: 0.67-0.98; P=0.029) were associated with better OS (Figure 1B-F).
0.96 STAT1, STAT2, STAT4, STAT5a, and STAT5b were significantly correlated to a favorable OS in GC patients.
0.88 STAT1, (F) STAT2, (G) STAT3 (Affymetrix ID: 225289 _at), and (H) STAT6 are plotted for intestinal type GC patients.
0.59 STAT1 and STAT2 between the moderately and poorly differentiated subtypes.
31485610 0.98 STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6.
0.98 STAT1, STAT2, STAT4, and STAT6, have more restricted functions.
0.98 STAT1 and STAT2 were demonstrated to decrease the growth capacity of HepG2 cells via increased expression stimulated by phosphatidyl-ethanolamine.
0.98 STAT1, (F) STAT2, (G) STAT3, (H) STAT4, (I) STAT5A, (J) STAT5B and (K) STAT6.
0.97 STAT1, STAT2, STAT3, STAT4, STAT5B and STAT6 genes had diagnostic significance for HCC in the GSE14520 cohort.
0.97 STAT1, (F) STAT2, (G) STAT3, (H) STAT4, (I) STAT5A, (J) STAT5B and (K) STAT6.
0.97 STAT1, (F) STAT2, (G) STAT3, (H) STAT4, (I) STAT5A, (J) STAT5B and (K) STAT6.
0.97 STAT1, (F) STAT2, (G) STAT3, (H) STAT4, (I) STAT5A, (J) STAT5B and (K) STAT6.
0.94 STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6 genes exhibited differentially expressed levels in the GSE14520 cohort (all P<=0.05; Fig. 1A), and JAK1, JAK2, TYK2, STAT3, STAT4 and STAT5B demonstrated differentially expressed levels in the TCGA cohort (all P<=0.05; Fig. 1B).
0.92 STAT1, STAT2, STAT3, STAT4, STAT5B and STAT6 genes all indicated diagnostic significance for HCC [Fig. 2B-H, J-K; P<=0.05; area under curve (AUC) >0.5].
0.92 STAT1 mutations are susceptible to mycobacterial and virus infections, STAT2 mutations predispose patients to virus infection, and individuals with STAT3 mutations are susceptible to fungal infection.
31992798 0.98 STAT1 mediated signaling pathway resulting in the induction of STAT1 regulated genes was confirmed by real time (q)PCR of STAT1, STAT2 and of the most strongly induced STAT1 regulated gene we had identified downstream in this pathway, PLSCR1 (Fig. 1D-F).
0.98 STAT1 phosphorylation, STAT1 and STAT2 upregulation, and the expression of the main STAT1 targets at the protein level (Fig. 2A,B and Fig. S3A, left and center panel) and mRNA level (arrows in Fig. 2C,D).
0.97 STAT1 and STAT2 are key regulators of the IFN-I pathway.
0.97 STAT1 that drives cancer stemness is dependent on STAT2, but is inhibited by STAT3.
0.96 STAT1, STAT2 and of the three STAT1 targets (Fig. 6E), which was further induced by the addition of IFNbeta (note: the fold change was lower in STAT3 k.o.
0.96 STAT2 is part of a preactivation complex with IRF9 cooperating with NF-kappaB and unphosphorylated ISGF3 in general is believed to prime cells for a rapid response to microbial infections.
0.95 STAT1 or STAT2 (Fig. 6C).
0.94 STAT1 and STAT2 resulting in upregulation of the double stranded (ds)RNA sensor proteins RIG-I and MDA5, and a release of a subset of endogenous retroviruses.
0.94 STAT1 and STAT2 both mediate the innate immune response seen in CD95 stimulated cells, a process that is antagonized by STAT3.
0.78 STAT1 to be essential for IFN-I mediated pro-tumorigenic activities of CD95 and now demonstrate that STAT2 but not STAT3 is also essential for the activation the IFN-I pathway downstream of CD95.
0.69 STAT1 knock-out did not completely block induction of RIG-I, MDA5, TLR3, or IRF7 when stimulated with either CD95L and/or IFNbeta (Fig. 6B) or of ERVs (Fig. 5B), we tested the contribution of STAT2 and STAT3 to the CD95 induced gene induction.
20068068 0.98 STAT1 and STAT2 are recruited to the IFN-alpha/beta receptor and become tyrosine phosphorylated by JAKs.
0.98 STAT2 deficient H123 cells resulted in similar levels of tyrosine phosphorylated STAT1 (Fig. 3A).
0.97 STAT1 homodimers or STAT1/STAT2 heterodimers that when bound to IRF9 form the IFN-stimulated gene factor-3 (ISGF3) complex.
0.95 STAT1 and STAT2 expression are infrequent in melanoma cell lines and tumor samples and this did not correlate with IFN resistance.
0.81 STAT2 is not always required for STAT1 activation.
0.80 STAT2 results in impaired activation of the mitochondrial death dependent pathway but not that of STAT1 mediated responses triggered by type I IFNs.
0.73 STAT1 and STAT2 in their tumors, which correlated with stable disease or objective response.
0.70 STAT2, STAT1 antibodies to verify for equal protein loading.
29662014 0.98 ISGF3 (U-ISGF3) harbors serine monophosphorylated STAT1 or completely unphosphorylated STAT1 (lacking both tyrosine and serine phosphorylation), since previous reports of U-ISGF3 only focused on tyrosine phosphorylation without examining serine phosphorylation.
0.97 STAT1 and STAT3, as well as serine phosphorylation of STAT-2, STAT-5, or STAT-6, were not observed.
0.97 STAT2, STAT5, and STAT6 was observed in HBMECs exposed to HIV-1 virion.. Therefore, it is also notable that available data implies a correlation between viral-induced serine monophosphorylation of STATs (STAT1 and STAT3) and pro-inflammatory responses caused by virus infection.
0.96 STAT2 can form alternative complexes with IRF9 without STAT1, which is different from the canonical IFN-alpha signaling.
0.96 STAT1, STAT2, STAT3, STAT5b, and STAT6, and is reviewed elsewhere.
0.94 STAT1 to STAT6, and heterodimers, including STAT1-STAT3, STAT1-STAT4, STAT1-STAT5, STAT2-STAT3, and STAT5-STAT6.
0.84 Stat1-/- cells demonstrated the occurrence of STAT1-independent, STAT2-dependent gene expression is a delayed event during the transcriptional response to type I IFNs.
0.59 STAT1 and U-STAT2, along with IRF9, can support the formation of unphosphorylated ISGF3 (U-ISGF3).
31288481 0.98 STAT1, anti-p-STAT2, anti-STAT1, anti-STAT2, and anti-beta-Actin antibodies, respectively.
0.97 STAT1, STAT2, and IRF9 expressing plasmids.
0.92 STAT1, anti-p-STAT2, anti-STAT1, anti-STAT2, and anti-beta-Actin antibodies, respectively.
0.84 STAT1 phosphorylation triggered by IFN-beta or IFN-gamma normally leads to STATs dimerization, an essential step for STAT1 nuclear transport, we investigated whether N protein affected the phosphorylation STAT1 and STAT2 or STATs dimerization induced by IFN-beta or IFN-gamma.
0.75 STAT1) and STAT2 resulting in the impairment of host IFN responses.
0.73 STAT1, STAT2, or IRF9.
0.61 STAT1, STAT2, and IRF9 expressing plasmids.
0.60 STAT1 or STAT2 stimulated by IFN-beta was not affected by expression of N protein.
25710482 0.98 STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6.
0.98 STAT1, STAT2, STAT3 and STAT4, while a smaller group only by STAT5A, STAT5B and STAT6.
0.98 hSTAT1, hSTAT2, hSTAT5B and hSTAT6 (Table 2) similar to hSTAT3.
0.97 hSTAT1, hSTAT2, hSTAT3, hSTAT4, hSTAT5A, hSTAT5B and hSTAT6 SH2 domain and pTyr-linker interaction site was determined, with respect to their complete protein structure.
0.77 STAT1 phosporylation and, to a lesser extent, of STAT2 phosphorylation.
0.62 STAT1, STAT2, STAT3 and STAT4, and the other of STAT5A, STAT5B and STAT6.
0.56 hSTAT1 and hSTAT2.
31843895 0.98 STAT1, STAT2, and STAT3 are more stable.
0.94 STAT2 is an essential component of the IFN-alpha/beta signaling pathway, and IFN-alpha binding to IFNalphaR1-IFNalphaR2 leads to formation of the ternary IFN-stimulated gene factor 3 (ISGF3) complex that is composed of STAT1, STAT2, and IFN regulatory factor 9 (IEF9).
0.93 STAT2 induces the expression of antiviral genes by enhancing the interaction between STAT1 and STAT2, and mutations of STAT2 S287 increase ISGF3's DNA-binding ability.
0.92 STAT1; red, STAT2; blue, STAT3.
0.88 STAT2 and c-Myc protein levels than FBXW7 WT HCT116 cells (HCT116FBXW7+/+); however, STAT1 and STAT3 protein levels did not show a similar relationship (Fig. 2E).
0.82 STAT1, STAT2, and STAT3.
0.70 STAT2 structure showed overall similar structure with STAT1 and STAT3 (Fig. 5D).
16934001 0.98 STAT1 may not be recruited at all to IFNAR-bound phospho-STAT2.
0.97 STAT1 molecules and nonphosphorylated STAT2 were observed in resting cells.
0.93 STAT1 mutant proteins being no better recruited than WT STAT1 proteins to phospho-STAT2 and the IFNAR.
0.75 STAT2-mediated recruitment of STAT1, which is then phosphorylated at Tyr-701.
0.65 STAT1 molecules are not associated with phosphorylated STAT2 upon IFNA stimulation, revealing a second impact of L706S, in addition to the loss of Y701 phosphorylation, accounting in part for the recessive nature of this mutation for ISGF3 activation; and (2) the E320Q and Q463H STAT1 mutants are normally recruited by phosphorylated STAT2, with which they form phosphorylated heterodimers.
28273453 0.98 STAT1 is phosphorylated by Janus-activated kinases (JAK) 1, JAK2 and TYK2 resulting in its tyrosine phosphorylation, dimerization and translocation to the nucleus either as a homodimer or heterodimer with STAT2 or STAT3 where it activates a large number of IFN regulated genes.
0.98 STAT1/STAT2 heterodimers together with IFN-regulatory factor (IRF) 9.
0.98 STAT1, STAT2 and STAT3.
0.97 STAT1 not only blunted the ability of CD95L or type I IFN to mediate cancer stemness, but also completely blocked the phosphorylation of STAT2 and STAT3.
0.96 STAT2 and STAT3 were also tyrosine phosphorylated, and STAT2 (just like STAT1) showed higher expression after 4 days of CD95 stimulation (Figure 1J).
27434509 0.98 STAT2 ubiquitination in IFNs signaling, given that IFNs signaling activates STAT2 (pY690-STAT2), which then forms a heterodimer with STAT1.
0.62 STAT1 rather than STAT2.
26546155 0.97 STAT1 and STAT2, but inhibits the type I IFN-induced phosphorylation and nuclear translocation of both STAT1 and STAT2.
0.97 STAT2 protein, though not with STAT1, and with the inhibition of STAT phosphorylation and subsequent nuclear translocation.
0.96 STAT1 or STAT2, it does prevent the IFN-induced phosphorylation and nuclear translocation of STAT1 and STAT2 thereby inhibiting cellular responses to IFN alpha/beta
0.96 STAT2 on tyrosine 690 and STAT1 49) on tyrosine 701.
0.95 STAT1 and STAT2 but instead inhibited the type I IFN-activated phosphorylation of STAT1 and STAT2.
0.95 STAT1 and STAT2 proteins for degradation.
0.95 STAT1, STAT2, HA and Actin.
0.94 STAT1 and STAT2, thus preventing formation of the ISGF3 complex and the subsequent binding at the ISRE of ISGs.
0.94 STAT2 and not STAT1 (Fig 5D).
0.92 STAT1 and anti-STAT2 antibodies.
0.90 STAT1 and STAT2 are the targets of several Paramyxovirus V proteins.
0.89 STAT1 and STAT2 nuclear import without degrading STATs and preventing STATs phosphorylation.
0.88 STAT1 and STAT2 thereby inhibiting cellular responses to IFN alpha/beta.
0.77 STAT1 and STAT2 translocate to the nucleus.
0.75 STAT1 and STAT2 and preventing STATs phosphorylation and translocation.
0.71 STAT1 and STAT2 or both, we examined whether LPMV-V protein has the ability to bind STAT1 and STAT2 using co-immunoprecipitation assays.
0.70 STAT1 and STAT2 heterodimerize and associate with interferon regulatory factor 9 (IRF9) to form IFN-stimulated gene factor 3 (ISGF3), which translocate to the nucleus and binds the IFN-stimulated response elements (ISREs) within interferon-stimulated gene (ISG) promoters thereby inducing the expression of more than 100 ISGs to establish an antiviral state that limits viral replication and dissemination.
0.68 STAT1 and STAT2 phosphorylation..
0.67 STAT1 and STAT2 and the type I and type II IFN-induced phosphorylation of STAT1 and STAT2.
0.65 STAT1 and STAT2 activity in cells that express LPMV-V, NipahV-V, and PIV5-V proteins.
0.63 STAT1 and STAT2 but reduced the type I IFN-induced phosphorylation of STAT1 and STAT2, we hypothesized that the STATs protein would be retained in the cytoplasm in the presence of LPMV-V protein.
0.57 STAT2 and preventing phosphorylation of STAT2 and STAT1.
21147189 0.97 STAT1 and STAT2 heterotrimerize with IRF9 to form the ISGF3 complex.
0.97 STAT1 (A), STAT2 (B) or IRF9 (C) for 3 days and incubated with 100 ng/ml IL28B or mock for 3 days.
0.96 STAT1 and STAT2.
0.96 STAT1, STAT2, or IRF9.
0.96 STAT1 and STAT2 phosphorylation and ISRE reporter activity
0.95 STAT1, STAT2 and IRF9 are required for the antiviral activity of IL28B.
0.95 STAT1, STAT2 or IRF9.
0.94 STAT1, STAT2 and IRF9 form the trimetric ISGF3 complex and subsequently undergo nuclear translocation.
0.94 STAT1, STAT2 and IRF9 are required for the antiviral effects of all three types of IFNlambda.
0.93 STAT1, STAT2, and IRF9 using chemical, antibody, or siRNA inhibition.
0.90 STAT1 and STAT2 was validated by Western blotting (Fig. 6A, B, D, and E).
0.88 STAT2 or IRF9, the induction of STAT1, MxA, and ISG15 by IL28B was reduced (Fig. 6B, C, E and F).
0.87 STAT1, STAT2 and IRF9.
0.86 STAT1, STAT2 and IRF9.
0.86 STAT1, STAT2 or IRF9 for 3 days and then treated with 100 ng/ml IL28A, IL28B, IL29 or mock treatment for 3 days.
0.76 STAT1/STAT2 and ISRE luciferase reporter activities and subsequently induced the expression of known ISGs.
0.74 STAT1, STAT2 and IRF9 are required for IL28B antiviral signaling.
0.65 STAT1 (D), STAT2 (E) or IRF9 (F) for 3 days and incubated with 100 ng/ml IL28B or mock for 3 days.
0.61 STAT1 and STAT2 induced by IL28B.
0.61 STAT1 and STAT2 phosphorylation was assessed.
25211074 0.97 STAT2 only in cells that have been stimulated with IFN-I. This NS5-STAT2 interaction requires IFN-I-induced tyrosine phosphorylation of STAT1 and the K63-linked polyubiquitination at a lysine in the N-terminal region of YFV NS5.
0.97 STAT1 with DENV-2 NS5/STAT2 complexes was also induced by IFN-I treatment.
0.97 STAT2 interaction by inducing STAT1 tyrosine phosphorylation.
0.97 STAT2 and preventing ISGF3 engagement with ISREs.
0.97 STAT1 is also required for NS5-STAT2 interaction, most likely by promoting conformational changes in STAT2 that trigger its association with ubiquitinated NS5.
0.95 STAT1 and STAT2 components, even though only one of the STAT proteins is targeted for degradation.
0.95 STAT2 in response to IFN-I treatment when cells were reconstituted with wild-type but not mutant (Y701F) STAT1.
0.95 STAT1 is necessary for IFN-I induced YFV NS5-STAT2 interaction
0.94 STAT2 both in the cytoplasm and nucleus only after IFN treatment, and appears to inactivate ISGF3 within the nucleus.
0.93 STAT1 and STAT2, resulting in the formation of IFN-stimulated gene factor 3 (ISGF3), a transcription factor complex comprised of IRF9 and phosphorylated STAT1 and STAT2.
0.93 STAT2 preventing its transcriptional activity by: 1) increasing K63-linked polyubiquitination at residue K6 of YFV NS5 thereby promoting the capacity of YFV NS5 to inhibit IFN-I signaling via STAT2 binding, and 2) promoting STAT1 tyrosine (Tyr) phosphorylation, which is required for NS5/STAT2 binding.
0.93 STAT2 and STAT1 (Figure 7A).
0.91 STAT1 tyrosine phosphorylation is required for YFV NS5/STAT2 association and inhibition of ISGF3 engagement with the ISRE.
0.89 STAT1 and STAT2 levels were not reduced by YFV infection.
0.89 STAT2 did, confirming the identity of the complex as ISGF3 (Figure 1G).
0.84 STAT2 in STAT1-deficient cells as previously described.
0.80 STAT1 is necessary for IFN-I-induced YFV NS5-STAT2 interaction
0.77 STAT2 is likely due to the fact that 1) the complexes are made in different lysates decreasing complex formation; 2) DENV NS5 may interact directly with STAT2 while YFV NS5 interaction may be indirect; 3) YFV NS5 may require both STAT1/2 to be complexed before its interaction with STAT2 whereas DENV NS5 does not.
0.75 STAT1 was not precipitated along with STAT2 after YFV NS5 immunoprecipitation (Figure 2D).
0.54 STAT1 for YFV NS5 to interact with STAT2 since it did not bind STAT2 in STAT1-deficient cells.
22305622 0.97 STAT2 or blocking STAT1 and STAT2 phosphorylation.
0.97 STAT1- and STAT2-dependent while that of Oas1b was STAT1-independent and STAT2-dependent indicating that these two duplicated genes are differentially regulated by IFN beta.
0.97 STAT1 and STAT2 are phosphorylated in WNV Eg101 infected cells, the present study showed that nuclear translocation of these TFs was blocked.
0.97 STAT1 and STAT2.
0.97 STAT1 and STAT2 with ISG promoters in WNV Eg101-infected MEFs
0.96 STAT1, STAT2 and IFN regulatory factor-9 (IRF-9) form a trimeric transcription factor complex referred to as IFN stimulated gene factor 3 (ISGF3) that translocates to the nucleus and binds to IFN-stimulated response elements (ISREs) in the promoters of IFN-stimulated genes (ISGs).
0.96 STAT1 or STAT2 to the Oas1a, Oas1b or Irf7 promoters or of STAT1 to the Irf1 promoter was observed.
0.96 STAT1 (Tyr 701) were detected at 2, 6 and 12 h after infection, while robust phosphorylation was seen at 24 and 48 h. Low levels of STAT2 phosphorylation (Tyr 690) were detected at 2 through 6 h and high levels were seen at 12 and 24 h after infection but not at 48 h. IRF-9 upregulation was detected as early as 6 h and was robust by 24 h after infection and also after a 3 h incubation with IFN beta.
0.96 STAT1 and STAT2 occupancy on the Oas1a, Oas1b and Irf7 promoters and STAT1 occupancy on the Irf1 promoter in vivo was analyzed with a chromatin immunoprecipitation (ChIP) assay done as described in Materials and Methods using tC3H/He MEFs that were mock-infected, infected with WNV Eg101 (MOI of 5) for 7, 16 or 24 h or treated with 1000 U/ml of murine IFN beta for 30 m. Briefly, in vivo crosslinked DNA-protein complexes were immunoprecipitated using anti-STAT1, anti-STAT2 or a nonspecific IgG antibody.
0.95 STAT1 and STAT2.
0.94 STAT1 and STAT2 were phosphorylated in WNV Eg101-infected MEFs suggested that upregulation of the Oas1a, Oas1b, Irf7 and Irf1 genes might be mediated by the canonical type I IFN pathway.
0.93 STAT1-/-, STAT2-/-, and IFN alpha/beta receptor -/- MEFs.
0.90 STAT1 and STAT2 proteins primarily reside in the cytoplasm and the formation and nuclear translocation of the ISGF3 complex depends on IFN-mediated phosphorylation of STAT1 on Tyr701 and STAT2 on Tyr690.
0.89 STAT1-/-, STAT2-/- and IFN alpha/beta R-/- MEFs indicating that these ISGs were not upregulated by the canonical type 1 IFN-mediated Jak-STAT pathway or by an alternative IFN alpha/beta R-mediated signaling pathway.
0.89 STAT1 and STAT2 nuclear translocation by blocking phosphorylation of these proteins in primate cells and the WNV NY99 NS5 protein was shown to mediate this suppression.
0.83 STAT1 and STAT2 was blocked in the WNV Eg101-infected cells.
0.74 STAT1- and STAT2-independent manner.
0.66 STAT1 and STAT2 levels was also observed from 12 h through 48 h after WNV Eg101 infection.
0.56 STAT1, STAT2 and IRF-9.
25704559 0.97 STAT2 for proteasomal degradation whereas PIV5 V does not directly affect STAT2 levels, but, as described above, simply requires STAT2 for VDC formation and degradation of STAT1.
0.97 STAT1 or STAT2, the V protein of MuV catalyzes proteasomal degradation of STAT1 and STAT3.
0.97 STAT1, as reported by Hong et al.. The IFN signaling is further diminished by downregulating phosphorylation of STAT1, STAT2, and TYK2 through direct interaction with TYK2.
0.94 STAT1 and STAT2 is inhibited, as well as serine phosphorylation of STAT1.
0.93 STAT1 and STAT2 in high molecular weight cytoplasmic complexes.
0.93 STAT1 and STAT2.
0.90 STAT1 weakens signaling by types I, II, and III IFNs, whereas the lack of STAT2 will abrogate non-canonical STAT1-independent signaling by type I and III IFN.
0.87 STAT1 and STAT2 are required for VDC formation, only one of the two STAT proteins is actually degraded, and this differs among viruses.
0.85 STAT1, STAT2, and JAK1, it has been found that MeV V also interacts with STAT3 and IRF9.
0.81 STAT1 and STAT2 is inhibited by the MeV V protein by a mechanism that involves its interaction with JAK1.
0.77 STAT1 and STAT2 independently through distinct N-terminal and C-terminal sites, respectively.
0.76 STAT1 and STAT2.
0.74 STAT1, and STAT2.
0.71 STAT1 is targeted for destruction in a process involving a VDC and requires STAT2, whereas STAT3 targeting is STAT2-independent.
0.70 STAT1, whereas a similar complex containing the human PIV2 (hPIV2) V protein primarily targets STAT2 for degradation.
0.62 STAT1 and STAT2 form a stable heterodimer, which binds to the DNA-binding subunit IFN regulatory factor (IRF) 9.
0.57 STAT1 and STAT2, followed by formation of a heterotrimeric complex with IFN-regulatory factor 9 (IRF9).
30158934 0.97 STAT1 and STAT2, STAT3 is a negative regulator of IFN-I response, as the absence of STAT3 enhances IFN-I-mediated reporter activity, ISG induction, and antiviral response.
0.96 STAT1 and STAT2, as the N-terminal domain (NTD) of STAT3 is sufficient to confer its effects.
0.95 STAT1 and STAT2 to form ISGF3, which translocates into the nucleus and initiates transcription of IFN-stimulated genes (ISGs).
0.95 STAT2 antibody was much abundant than that by the anti-STAT1 antibody (Figures S6C,D in Supplementary Material).
0.94 STAT1 and STAT2 was also comparable between WT and PLSCR2KO ML-1 cells (Figure 6B).
0.93 STAT1 and STAT2 by tyrosine phosphorylation.
0.93 STAT1, STAT2, or STAT3 (Figure S6A in Supplementary Material).
0.93 STAT2, and not with STAT1 or IRF9 (Figure 1D).
0.92 STAT1, STAT2, or IRF9, while it did slightly reduce the association of unphosphorylated STAT1 and STAT2 (Figure S6C in Supplementary Material).
0.87 STAT1, STAT2, or IRF9.
0.86 STAT1, STAT2, and STAT3.
0.75 STAT1, STAT2, and IRF9 for 48 h and then treated with or without IFN-alpha2 for 60 m. The nuclear lysates were added together in vitro as indicated before EMSA.
0.72 STAT1 and STAT2 form ISGF3 complex with IRF9, translocate into the nucleus, bind the promoters, and transactivate downstream IFN-stimulated genes (ISGs) resulting in an antiviral response.
0.69 ISGF3, which was supershifted by anti-STAT1 or anti-IRF9 antibody (Figure 6F).
0.69 STAT1, and STAT2.
28139375 0.97 STAT1 and STAT2) at specific tyrosine residues.
0.97 STAT1, STAT2 was found to interact with IRF9 to form an ISGF3-like complex to mediate specific ISG transcription.
0.96 STAT1 homodimers, whereas type I and III IFNs activate both STAT1 and STAT2 to form ISGF3 together with IRF9.
0.95 STAT1 and STAT2 are the most important STATs with respect to IFN signaling.
0.95 STAT1 and STAT2 bind to the ISRE region together with IRF9 to exert strong pro-transcriptional activity.
0.93 ISGF3 formed by IFN-induced IRF9 and unphosphorylated STAT1 and STAT2 can lead to increased expression of a subset of ISGs.
0.93 STAT1 and STAT2, STAT5 is also involved in type I IFN-induced ISG transcription.
0.92 STAT1 and STAT2.
0.89 ISGF3 complexes have been identified, including ISGF3II, the STAT2-IRF9 complex, and unphosphorylated ISGF3 (U-ISGF3).
0.88 STAT1 and STAT2 to avoid excessive and detrimental responses.
0.83 STAT1, STAT2, STAT3, STAT4, STAT5a, STAT5b, and STAT6.
0.73 STAT1 and STAT2.
0.66 ISGF3 complex (ISGF3II) containing phosphorylated STAT1, unphosphorylated STAT2, and IRF9.
22504331 0.97 STAT1 and STAT2 plays a key role not only in host defense against HCV infection but also in IFN-alpha treatment-induced HCV clearance.
0.96 STAT1 and STAT2 and the subsequent induction of a variety of anti-viral proteins that inhibit HCV replication (Fig. 1).
0.96 STAT1 and STAT2.
0.95 STAT1 and STAT2 activation by binding to a receptor complex comprised of the IL-10R2 and the unique IFN-lambdaR1 (also known as IL-28R) chain.
0.95 STAT1 and STAT2 activation.
0.94 STAT1 and STAT2 in viral hepatitis
0.93 STAT1 and STAT2 in viral hepatitis
0.93 STAT1 and STAT2 induce many anti-viral proteins (e.g., Mx1, OAS, IRF-7, etc.) that subsequently inhibit HCV replication.
0.90 STAT1 and STAT2 activation through several mechanisms.
0.66 STAT1 and STAT2, the functions of other STATs in viral infection remain largely unknown.
0.58 STAT1 and STAT2 activation, modulating IFN expression, and controlling immune cell activation.
31293595 0.97 STAT1, STAT2, and IRF9 form ISGF3 complex which transactivates downstream IFN-stimulated genes and mediates antiviral response.
0.97 STAT1 and STAT2, nuclear translocation of activated STATs, or assembly of ISGF3 complex.
0.97 STAT1, STAT2, IRF9, and several ISGs in a human glioma cell line.
0.97 STAT1 and STAT2 expression indirectly to antagonize IFN-I response (Figure 2A).
0.95 STAT1 and STAT2, the actual functions and biological significance of STAT3 in IFN-I response are less appreciated, probably due to relatively transient activation compared to STAT1, impaired IFN-I-mediated, STAT3-dependent transcriptional activity or a dispensable role in some IFN-I-mediated activities.
0.92 STAT2 has also been reported to negatively regulate IFN-I response, either by constitutive phosphorylation at T387 to block ISGF3 formation and its DNA binding or by IFN-I-induced phosphorylation at S287 or S734 with mechanisms yet to be defined.
0.88 STAT1, STAT2, and STAT3 are activated in response to IFN-I stimulation.
0.86 STAT1, STAT2, and STAT3 by tyrosine phosphorylation.
0.85 ISGF3 components, including STAT1, STAT2, and IRF9 to reduce their de novo protein synthesis.
0.84 STAT1, STAT2, and STAT3 and the formation of ISGF3 heterotrimer, consisting of STAT1, STAT2, and IRF9, and homodimers of STAT1:STAT1 or STAT3:STAT3 and heterodimer of STAT1:STAT3.
0.84 ISGF3 components, including STAT1, STAT2, and IRF9 and suppress their expression.
30671058 0.97 STAT1, STAT2, IRF9 themselves, several other ISGs are also implicated in the regulation of JAK-STAT signaling.
0.96 STAT1, STAT2, and IRF9 belong to another subset of ISGs that amplify JAK-STAT signaling to reinforce IFN responses.
0.96 STAT1, and STAT2 are highly critical for their downstream transcriptional activation, and therefore these phosphorylation events are commonly targeted by viruses.
0.95 STAT1 and STAT2 in a proteasome-dependent manner.
0.94 STAT1/STAT2 heterodimer and STAT1/STAT1 homodimer, type I IFNs can also activate STAT3/STAT3, STAT4/STAT4, STAT5/STAT5, and STAT6/STAT6 homodimers as well as STAT1/STAT3, STAT1/STAT4, STAT1/STAT5, STAT2/STAT3, and STAT5/STAT6 heterodimers.
0.94 STAT1 and STAT2 but retain these transcription factors in the cytoplasm.
0.80 STAT1 and STAT2 in the cytoplasm, and the N protein of Nipah virus restricts the complex formation of STAT1/STAT2, which along with the CRM1-dependent nuclear export of STAT1 and STAT2 additively result in the accumulation of STAT1 and STAT2 in the cytoplasm.
0.65 STAT1, STAT2, and IRF9 cycle back to the cytoplasm in a CRM1-dependent nuclear export manner.
30483250 0.97 STAT2, but not STAT1.
0.96 STAT2 compared with that of STAT1.
0.95 STAT1-STAT2 dimer associates with interferon regulatory factor 9 (IRF9) to form a transcriptionally active IFN-stimulated gene factor 3 (ISGF3).
0.93 STAT1 and Y690 on STAT2).
0.90 STAT1 and STAT2, the resulting heterodimer forms an ISRE-dependent complex with IRF9 called ISGF3.
0.76 ISGF3, the STAT1/STAT2/IRF9 heterotrimer.
0.68 ISGF3 or other complexes containing either STAT1 or STAT2.
31142600 0.97 stat1 and stat2 genes are induced by viral infections in different fish species, suggesting that they are implicated in the antiviral response as their homologs in mammals.
0.97 stat1 copies for only a single stat2 copy.
0.97 stat1 and stat2 loci in salmonid fish. (A) Phylogenetic tree of Stat1 and Stat2 in rainbow trout and Chinook salmon.
0.97 stat1 and stat2 as measured by deep sequencing showed that only the stat1b1 paralogue and stat2 were found upregulated in EC, and neither in GS2, corresponding to the 6th and 37th genes in Fig. 4, respectively.
0.96 STAT1 and of STAT2 in IFN signaling is therefore still undefined.
0.92 STAT1 and Y690 for STAT2).
0.87 STAT1 and STAT2, which combine with IFN regulatory factor (IRF)-9 to form a heterotrimeric complex termed IFN stimulated gene (ISG) factor 3 (ISGF3) that translocates into the nucleus and activates IFN-stimulated response elements (ISRE) within the promoters of a set of ISGs.
24699362 0.97 Signal Transducer and Activator of Transcription 1 and 2 (STAT1 and STAT2) via Src Homology 2 (SH2) domains and tyrosine phosphorylation and heterodimerization of the STATs.
0.96 STAT1-STAT2 heterodimers forms complexes with interferon regulatory factor (IRF)9 that translocates to the nucleus and binds Interferon Stimulated Response Elements (ISRE) in the promoters of type I IFN induced genes.
0.95 STAT1, although these studies revealed that the C-terminal region of IE1 was required for interaction with STAT2.
0.95 STAT1 and STAT2.
0.95 STAT1, IE1 and STAT2 and the antibody reactive bands were visualized by chemiluminescence.
0.82 STAT2 colocalize in ND10 structures and metaphase chromosomes; (ii) in human fibroblasts, phophorylated STAT2 does not accumulate in the nucleus upon IFNgamma treatment ( and this report); (iii) there are conflicting reports of an interaction between IE1 of the Towne strain and STAT1 and we were unable to find compelling evidence for a specific interaction between IE1 of strain AD169 and STAT1; and (iv) nevertheless, IE1 expression interferes with binding of STAT1 molecules to GAS elements.
28536310 0.97 STAT1, STAT2, STAT3, STAT4, STAT5a, STAT5b, STAT6).
0.96 STAT1, STAT2, STAT3, STAT4, STAT5a, STAT5b, STAT6).
0.96 STAT2 and STAT3 are correlated to a better OS for all the ovarian cancer patients, especially the high level of STAT1 and STAT4 are significantly related to a favorable OS for serous ovarian cancer patients.
0.95 STAT2 and STAT3 showed no effect on the OS of ovarian cancers, i.e. high mRNA expression of STAT1, STAT4, STAT5a, STAT5b, and STAT6 was correlated to a better OS for ovarian cancer patients, especially the high level of STAT1 and STAT4 was significantly related to a favorable OS for serous ovarian cancer patients.
15504906 0.97 STAT1, STAT2, and STAT3.
0.78 STAT1/STAT2 heterodimers, however, singly tyrosine-phosphorylated dimers were detected in vitro, but whether or not these molecules participated in cytokine-induced nuclear import was not resolved.
0.63 STAT1 homodimer and the STAT1/STAT2 heterodimer.
19161415 0.97 STAT2 and likely STAT1.
0.92 STAT1 and STAT2 are activated at the IFN-alpha/betaR signaling complex by tyrosine phosphorylation, with subsequent formation of STAT1:STAT2 heterodimers and STAT1:STAT1 homodimers.
0.79 STAT1 relative to STAT2 and STAT3 activation results in enhanced expression of STAT1-dependent inflammatory genes such as the chemokines CXCL9 and CXCL10 and a shift to a more inflammatory phenotype.
22022391 0.96 STAT1 and STAT2 are induced and promote downstream ISGs expression that, in turn, inhibits HCV expression.
0.96 STAT1 and STAT2 mRNAs is increased as evidenced by elongation of mRNA half-life (Fig. 6B) and leads to the up-regulated protein level of the two signaling molecules (Fig. 4C).
0.95 STAT1 and STAT2 were inserted into a pGEM-3zf vector containing a T7 promoter.
0.95 STAT1 and STAT2 is specific.
0.95 STAT1 and STAT2, and it has been demonstrated that C-rich tracts in their 3'UTR are the binding sites of PCBP2.
0.95 STAT1 and STAT2, or suppress STAT1 phosphorylation, which may explain the extremely low expression levels of STAT1 and STAT2 in R1b cells (Fig. 2B).
0.93 STAT1 and STAT2 mRNA suggests that control over their mRNA levels might be mediated by an effect on mRNA stability.
0.90 STAT1 and STAT2 are PCBP2 binding sites
0.90 STAT1 and STAT2.
0.90 STAT1 and STAT2 mRNA levels by RPA analysis.
0.89 STAT1 and STAT2 mRNA and up-regulates the expression of the two signal molecules
0.85 STAT1 and STAT2 through binding the C-rich tracts in the 3'UTR of the two pivotal IFN-alpha signaling pathway molecule.
0.85 STAT1 and STAT2 mRNAs and up-regulates their protein levels.
0.84 STAT1 and STAT2 are PCBP2 binding sites.
0.84 STAT1 and STAT2 3'-UTR used in synthesis of sense RNA probe in vitro and sequences position in the 3'-UTR.
0.83 STAT1 and STAT2 mRNA serve as binding substrates of PCBP2 and are stabilized by PCBP2.
0.81 STAT1 and STAT2 mRNAs are a PCBP2 binding site (Fig. 5).
0.79 STAT1 and STAT2 mRNA decay course.
0.78 STAT1 and STAT2 mRNA and up-regulates the expression of the two signal molecules in IFN-alpha pathway.
0.78 STAT1 and STAT2.
0.75 STAT1 and STAT2, but exerted no influence on JAK1 and TYK2.
0.68 STAT1 and STAT2 mRNAs corresponded to that of alpha-globin.
0.67 STAT1 and STAT2 after the treatment of IFN-alpha while other factors remained intact.
0.56 STAT1 and STAT2 mRNA interacted with PCBP2, we decided to test which regions of STAT1 and STAT2 3'-UTR interacted with PCBP2 by RNA pull-down assay.
0.50 STAT1 and STAT2 through stabilizing their mRNA
23707527 0.96 STAT2:STAT1 interaction was mainly regulated by STAT2 acetylation on Lys390, which dissociates DBD of STAT2 from STAT1, a step required for the active ISGF3 complex formation.
0.94 STAT-1; the interleukin-6 (IL-6) family members including IL-6, leukemia inhibitory factor (LIF) primarily activate STAT-3; STAT2 is almost uniquely tyrosine phosphorylated and activated in the presence of IFNalpha/beta; STAT4 is predominantly activated in response to IL-12 and STAT6 is primarily activated by IL-4 and the highly related cytokine IL-13.
0.93 STAT1, STAT2, STAT3, STAT5b and STAT6 has been identified.
0.93 STAT1, STAT2, STAT3, STAT5b has been recently characterized (Table 1 and 2).
0.93 STAT1 and STAT2, the first members of STAT family.
0.88 STAT1 homodimers and STAT1/STAT2 heterodimers.
0.76 STAT1, STAT2, and IRF9 in IFN signaling enable acetylation as a positive regulator of STAT1 signaling (Figure 3).
0.72 STAT1, STAT2, STAT3, STAT4, STAT5a/b, and STAT6.
0.70 ISGF3 complex, which includes IRF9, STAT1 and STAT2.
0.51 STAT1, STAT2, STAT3, STAT5b and STAT6 has been identified.
23856440 0.96 STAT1 and STAT2.
0.96 STAT1/STAT2 complex, called interferon-stimulated gene factor 3, translocates into the nucleus and binds to the IFN-stimulated response element present in target promoters.
0.96 STAT2 (Fig. 1B, compare STAT1 and STAT2 sequences).
0.96 STAT1 phosphorylation, while V sequesters STAT1 and STAT2 in high molecular complexes.
0.81 STAT1, MV-V, which shares the amino-terminal half of P but has a different carboxyl-terminal domain, interacts with both STAT1 and STAT2.
0.79 STAT1/STAT2 heterodimer then interacts with the DNA-binding protein IRF-9.
0.59 STAT1 and STAT2 interact with each other through their Src-homology 2 (SH2) domains.
30567349 0.96 STAT1 phosphorylation more efficiently in response to IFN-beta than to IFN-gamma, thus suggesting that MetYPCP interfered more specifically with one or several components or regulators of the JAK/STAT pathway triggered by IFN-I. Activation of the JAK/STAT pathway by type II IFN involves a specific receptor (IFNGR) and the phosphorylation of JAK1, JAK2 and STAT1, but not TYK2 and STAT2, which are activated by IFN-I only.
0.95 STAT1/STAT2 heterodimers are released in the cytoplasm, where they interact with IFN response factor 9 (IRF9) to form IFN-stimulated gene (ISG) factor 3 (ISGF3).
0.95 STAT1 activation, as STAT2 phosphorylation was not affected by the expression of this ORF1 product.
0.92 STAT1 but Not STAT2 Phosphorylation after IFN-beta Treatment
0.90 STAT2, p-STAT2 and p-STAT1 by immunoblotting.
0.88 STAT1 and STAT2 are then recruited and phosphorylated by the JAK kinases on tyrosine 701 and tyrosine 690, respectively.
0.85 STAT2 and found that MetYPCP had no significant effect on the level of total and phosphorylated STAT2 (Figure 4a,c), suggesting that MetYPCP interfered with the activation of STAT1 but not STAT2 following IFN-I treatment.
19752753 0.96 Stat1 and Stat2 at tyrosine residues 701 and 690, respectively, followed by the release of tyrosine phosphorylated STATs from the receptors.
0.96 Stat1:Stat2 heterodimer assembles with the DNA binding protein IFN regulatory factor 9 (IRF9, also called ISGF3gamma or p48) to form a heterotrimeric complex called IFN-stimulated gene factor 3 (ISGF3).
0.93 Stat1:Stat1 homodimer or Stat1:Stat2 heterodimer.
20949125 0.96 STAT1 and STAT2 proteins led to their impaired nuclear translocation and IFN-alpha resistance (21-22).
30901970 0.95 ISGF3 complex (IRF9/p-STAT1/p-STAT2) which then acts as a transcription factor driving the expression of interferon stimulated genes.
0.94 STAT1 and p-STAT2 have returned to basal levels.
0.94 STAT1 and STAT2 are critical regulators of type III dependent ISG induction.
0.94 ISGF3 complex (IRF9/p-STAT1/p-STAT2).
0.93 STAT1 and STAT2 through their SH2 domain.
0.92 ISGF3 transcriptional complex made of STAT1:STAT2 heterodimer and of IRF9, almost all combination of STAT homo- and heterodimers can be found: STAT1:STAT1, STAT3:STAT3, STAT4:STAT4, STAT5:STAT5, STAT6:STAT6, STAT1:STAT2, STAT1:STAT3, STAT1:STAT4, STAT1:STAT5, STAT2:STAT3 STAT5:STAT6.
0.90 STAT1 and STAT2 recruitment, while the IFNAR1 tyrosine Y466 has been shown to be important for STAT2 activation.
0.83 STAT1, STAT2 and IRF9 are ISGs, they are produced in large amounts following stimulation by both type I and III IFNs.
0.77 STAT1, STAT2 and STAT3 are induced downstream type I IFNs in most all cell types, STAT4, STAT5 and STAT6 are induced in a cell type dependent manner and results in unique signaling complexes in these cell types (e.g., STAT5 activation along with the CrkL adapter lead to the induction of a specific subset of ISGs).
0.51 STAT1, STAT2 and IRF9.
29317535 0.95 STAT1:STAT2 heterodimer binds to the ISRE.
0.94 STAT1/STAT2 heterodimer that interacts with IRF9, a member of the IRF family of transcription factors.
0.92 STAT1 and IRF9 appear to interact functionally on certain promoters even in the absence of STAT2.
0.91 STAT1:STAT2 heterodimer and assayed its ability to bind to the ISRE DNA.
0.90 STAT1 and IRF dimers, we propose a composite model for ISGF3, containing a 1:1:1 complex of STAT1:STAT2 and IRF9 bound to the ISRE DNA element of the IFN-inducible adenosine deaminase ADAR1 gene (Fig. 4C).
0.75 STAT1, STAT2, and IRF9 and regulates expression of IFN-stimulated genes.
0.55 STAT2, F174, is conserved in STAT1 and STAT3.
27131212 0.95 STAT1, STAT2, and IRF9, culminating in the expression of anti-viral effector molecules.
0.93 STAT1 and STAT2 phosphorylation and thereby block the association and nuclear translocation of the ISGF3 transcription factor.
0.92 STAT1, which then heterodimerizes with STAT2 and traffics to the nucleus.
0.77 STAT1 (Tyr701) and STAT2 (Tyr689), which together with IRF9 form a transcription factor, interferon stimulated gene factor 3 (ISGF3) capable of binding to promoter elements for genes associated with the anti-viral response.
31354696 0.95 STAT2 level in GOF patients, but this is an important future research direction, especially given the difficulties with viral infections in STAT1 GOF disease.
0.91 STAT1 protein level 30 min after IFNalpha or IFNgamma stimulation and baseline STAT2 protein level, as measured by flow cytometry.
23555265 0.94 STAT1 (hSTAT1) cannot bind NS5, chimeric proteins that replace the first 301 amino acids of mSTAT2 (h/mSTAT2) or the first 316 amino acids of hSTAT1 (hSTAT2/1) with those of hSTAT2 can bind NS5.
0.69 hSTAT2 = human STAT2; mSTAT2 = mouse STAT2; hSTAT1 = human STAT1; h/mSTAT2 = a chimeric protein with the first 301 amino acids of mouse STAT2 replaced by the corresponding human STAT2 sequence; hSTAT2/1 = a chimeric protein with the first 316 of human STAT1 amino acids replaced by the corresponding human STAT2 sequence.
32123171 0.94 STAT1 or another STAT family member STAT2 (Supplementary Fig. 2a).
0.70 STAT1, and STAT2 in HEK293T cells cotransfected with Flag-LUBAC and HA-Ub-K0 (HA-K0, all lysines on Ub are mutated to arginine) using a HA antibody.
17032459 0.93 STAT1 functions as a component of the IFN stimulated gene factor 3 (ISGF3) transcription factor complex, which also includes STAT2 and interferon regulatory factor-9 (IRF9).
0.91 STAT1 binding, STAT2 binding, and differential expression, was also apparent for the responses of cells to IFN-alpha (Figure 1B,C).
0.90 STAT1 binding, STAT2 binding, and mRNA transcription in response to IFN-alpha.
0.89 STAT1 and STAT2 are predominantly quantitative rather than qualitative.
0.71 STAT1 binding in response to IFN-gamma, our analysis of Hartman et al.'s Chromosome 22 tiling array data for STAT binding and mRNA transcription in response to IFN revealed probe level correlations for various combinations of STAT1 binding, STAT2 binding, and mRNA transcription in response to treatment with either IFN-gamma or IFN-alpha.
24810717 0.90 STAT1, but not STAT2 and STAT3 during apoptosis.
0.89 STAT1, Actin (loading control), STAT2, STAT3, HSP90, p53 and BCL-XL were monitored by immunoblot.
0.88 STAT1, STAT2, caspase-3 full length, and Actin as loading control were determined by Western blot analyses E) Butyrate induces apoptosis time-dependently.
27387064 0.59 STAT1 and STAT2 usually act anti-viral due to their essential roles in IFN signaling.



The preparation time of this page was 0.1 [sec].