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The full length cDNA sequence of Atlantic salmon (Salmo salar) ssSTAT2 was determined and phylogenetic analysis of the amino acid sequence grouped this novel salmon gene to the STAT2 clade.
Surface features in the interacting domains of IRF9 and STAT2 have diverged to enable specific interaction between these family members and to enable the antiviral response.
Data show that RNF2 promotes STAT1/STAT2 disassociation from DNA.
this study shows that STAT2 plays a critical role in TLR-induced dendritic cell activation and cross-presentation, and
this study shows that STAT2 plays a critical role in TLR-induced dendritic cell activation and cross-presentation
these studies identify phosphorylation of S734-STAT2 as a new regulatory mechanism that negatively controls the type I IFN-antiviral response.
IFN-I can mediate ISG expression inmixed glial cell cultures (MGCs) via ISGF3-independent signaling pathways but with reduced efficiency, with delayed and prolonged kinetics, and is more dependent on STAT1 and STAT2 than IRF9; and 2) signaling pathways not involving STAT1, STAT2, or IRF9 play a minor role only in mediating IFN-alpha-stimulated genes expression in MGCs.
transcriptional activation of Adar1 by IFN occurs in the absence of STAT1 by a non-canonical STAT2-dependent pathway in mouse but not human cells.
IFN-alpha/beta is able to drive the formation of a Stat2 and IRF-9 complex that drives the expression of a subset of IFN-stimulated genes, but with substantially delayed kinetics.
Activation of STAT2/IRF9 induces a prolonged ISGF3-like transcriptome and generates an antiviral response.
In a mouse syngeneic tumor transplantation model STAT2 expression reduces tumor growth.
Data suggest a role for Vc in Nanog regulation networks and reveal a novel role for STAT2 in regulating Nanog expression.
Stat2 loss leads to reduced expression of NF-kappaB target genes by affecting nuclear translocation of NF-kappaB.
STAT1, not STAT2 or IRF9, prevent the emergence of a lethal antiviral CD4(+) T-cell response after lymphocytic choriomeningitis virus infection.
Activation of Oas1a gene expression by type I IFN requires both STAT1 and STAT2.
In a constructive process, pM27 recruits DDB1 to exploit ubiquitin ligase complexes catalyzing the obstruction of the STAT2-dependent antiviral state of cells to permit viral replication.
NS5 is able to bind and degrade human STAT2, but not mouse STAT2; demonstrate that mouse STAT2 restricts early dengue virus replication in vivo
Our findings identify STAT2 as a novel contributor to colorectal and skin carcinogenesis
In this study we have characterized the Stat2-IFNaR2 interaction and examined its role in IFNalpha signaling
viruses subvert the known antiviral effect of type I IFN through STAT2-specific signaling to benefit their survival
Stat2 arbitrates contradictory growth signals elicited by alpha/beta interferons in T-lymphocytes.
Signal transducer and activator of transcription 2 (STAT2) is relocated to nonstructural protein NSs-induced cytoplasmic inclusion bodies (IBs) during infection of severe fever with thrombocytopenia syndrome phlebovirus. Consequently, NSs inhibited IFN-alpha-stimulated tyrosine phosphorylation and nuclear translocation of STAT2.
Priming cells with IFNbeta synergistically enhances IL6 induction in response to treatments that activate NF-kappaB, in a process that depends upon the recruitment of STAT2, IRF9.
These findings suggest that IFN-a can inhibit HCV replication through a STAT2-dependent but STAT1-independent pathway, whereas IFN-g induces ISG expression and inhibits HCV replication exclusively through a STAT1- and STAT2-dependent pathway.
mRNA expression of survivin was positively correlated with STAT2 mRNA in psoriasis vulgaris lesion tissues
Based on the proposition that NS5 utilizes SIAH2-mediated proteasomal degradation of STAT2, an in-silico study was carried out to characterize the protein-protein interactions between NS5, SIAH2 and STAT2 proteins.
The pathways related to tumorigenicity and tumor progression, STAT2 and AdipoR1/AMPK/SIRT1 could be restrained by miR-3908. In conclusion, restoration of miR-3908 expression induced suppression of cancer progression and glioblastoma tumorigenicity.
propose that one molecule of C protein associates with the STAT1:STAT2 heterodimer, inducing a conformational change to an antiparallel form, which is easily dephosphorylated
highlight the existence of a STAT1-independent IFN-I signaling pathway, where STAT2/IRF9 can potentially substitute for the role of ISGF3 and offer a back-up response against viral infection.
Decreased phosphorylated STAT2 expression was accompanied by increased replication of hepatitis C virus and hepatitis E virus.
6-Hydroxy-3-O-methyl-kaempferol 6-O-glucopyranoside potentiated the inhibitory effect of IFN-alpha on hepatocellular carcinoma cell proliferation through activation of the JAK/STAT signaling pathway by inhibiting SOCS3 expression.
data suggest that STAT2 plays a role in the psoriasis pathogenesis by regulating the expression of CXCL11 and CCL5, and thereby attracting IFNgamma-producing immune cells to the skin
Interferon-alpha-enhanced IL-10 expression in human CD4 T cells is regulated by STAT3, STAT2, and BATF transcription factors.
the rate-limiting transition state for binding between the TAZ1 domain of CREB binding protein and the intrinsically disordered transactivation domain of STAT2 (TAD-STAT2) by site-directed mutagenesis and kinetic experiments (Phi-value analysis) and found that the native protein-protein binding interface is not formed at the transition state for binding.
Data show that moringin (GMG-ITC) had a limited inhibitory effect on IFNalpha-induced STAT1 and STAT2 activity, indicating differentially targeting JAK/STAT signaling pathways.
study demonstrates that overexpression of Porcine deltacoronavirus (PDCoV) nsp5 also antagonizes IFN signaling by cleaving STAT2, an essential component of transcription factor complex ISGF3, and that PDCoV infection reduces the levels of STAT2, which may affect the innate immune response
PKV VP3 associated with STAT2 and IRF9, and interfered with the formation of the STAT2-IRF9 and STAT2-STAT2 complex.
The authors have discovered a novel phosphorylation of STAT2 on T387 that negatively regulates signal from the type I interferon receptor to the genome by transcription factor ISGF3.
STAT2 recruits USP18 to the type I IFN receptor subunit IFNAR2 via its constitutive membrane-distal STAT2-binding site.
While La Piedad Michoacan Mexico Virus V protein does not affect the protein levels of STAT1 or STAT2, it does prevent the interferon-induced phosphorylation and nuclear translocation of STAT1 and STAT2 thereby inhibiting cellular responses to interferon alpha/beta.
Taken together, results of these experiments describe for the first time a novel mechanism by which foot-and-mouth disease virus evolves to inhibit IFN signaling via blocking STAT1/STAT2 nuclear translocation.
Nsp1beta inhibits interferon-activated STAT1/STAT2 signal transduction by inducing karyopherin-alpha1 degradation.
the majority of the STAT1/STAT2/IRF9 (IFN regulatory factor 9) heterotrimers remained in the cytoplasm of PRRSV-infected cells, which indicates that the nuclear translocation of the heterotrimers was blocked
Prolonged treatment with IFN-alpha (12-48 h) resulted in increased expression of STAT1 and, to a lesser extent, STAT2.
The protein encoded by this gene is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. In response to interferon (IFN), this protein forms a complex with STAT1 and IFN regulatory factor family protein p48 (ISGF3G), in which this protein acts as a transactivator, but lacks the ability to bind DNA directly. Transcription adaptor P300/CBP (EP300/CREBBP) has been shown to interact specifically with this protein, which is thought to be involved in the process of blocking IFN-alpha response by adenovirus. Multiple transcript variants encoding different isoforms have been found for this gene.
, signal transducer and activator of transcription 2
, signal transducer and activator of transcription (AGAP000099-PA)
, interferon alpha induced transcriptional activator