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Inhibition of the nuclear export of poly(A)-containing mRNAs caused by the influenza A virus NS1 protein requires its effector domain. Additionally we are shipping Cleavage and Polyadenylation Specific Factor 4, 30kDa Antibodies (67) and many more products for this protein.
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Residues F103 and M106 within the NS1 (show PTPN11 Proteins)-CPSF4 binding region are important for viral replication.
Cleavage and polyadenylation specific factor 4 targets NF-kappaB (show NFKB1 Proteins)/cyclooxygenase-2 (show PTGS2 Proteins) signaling to promote the growth and survival of non-small cell lung carcinoma cells.
These findings support a role for iron in some zinc-finger proteins. Using electrophoretic mobility shift assays and fluorescence anisotropy, we report that CPSF30 selectively recognizes the AU-rich hexamer (AAUAAA) sequence present in pre-mRNA, providing the first molecular-based evidence to our knowledge for CPSF30/RNA binding.
unexpectedly found that CPSF subunits CPSF30 and Wdr33 directly contact AAUAAA
CPSF4 upregulates human TERT (show TERT Proteins) promoter activity, human TERT (show TERT Proteins) expression and telomerase activity.
Data show that 4 drug-like compounds from traditional Chinese Medicine (TCM) database were selected as potential inhibitors for the cleavage and polyadenylation specific factor CPSF30-binding site of influenza A virus of non-structural protein 1 (NS1A).
CPSF4 plays a critical role in regulating lung cancer cell proliferation and survival and may be a potential prognostic biomarker and therapeutic target for lung adenocarcinoma.
Data show that the NS1A protein of the pathogenic H5N1 influenza A/Hong Kong/483/97 (HK97) virus isolated from humans has an intrinsic defect in CPSF30 binding.
Inhibition of the nuclear export of poly(A)-containing mRNAs caused by the influenza A virus NS1 protein requires its effector domain. The NS1 effector domain functionally interacts with the cellular 30 kDa subunit of cleavage and polyadenylation specific factor 4, an essential component of the 3' end processing machinery of cellular pre-mRNAs. In influenza virus-infected cells, the NS1 protein is physically associated with cleavage and polyadenylation specific factor 4, 30kD subunit. Binding of the NS1 protein to the 30 kDa protein in vitro prevents CPSF binding to the RNA substrate and inhibits 3' end cleavage and polyadenylation of host pre-mRNAs. Thus the NS1 protein selectively inhibits the nuclear export of cellular, and not viral, mRNAs. Multiple alternatively spliced transcript variants that encode different isoforms have been described for this gene.
, cleavage and polyadenylation specific factor 4
, cleavage and polyadenylation specificity factor subunit 4
, cleavage and polyadenylation specific factor 4, 30kDa
, CPSF 30 kDa subunit
, cleavage and polyadenylation specific factor 4, 30kD subunit
, cleavage and polyadenylation specificity factor 30 kDa subunit
, clipper homolog
, clipper/CPSF 30K
, musculus clipper/cleavage and polyadenylation specificity factor 30 kDa subunit
, NS1 effector domain-binding protein 1
, cleavage-polyadenylation specificity factor, 30kD
, no arches homolog
, no arches-like zinc finger protein
, cleavage-polyadenylation specificity factor, 30 kD