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RNASEL encodes a component of the interferon-regulated 2-5A system that functions in the antiviral and antiproliferative roles of interferons. Additionally we are shipping RNASEL Antibodies (65) and RNASEL Kits (4) and many more products for this protein.
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Thus, activation of RNase L does not require mouse hepatitis virus virus-induced interferon (show IFNA Proteins) but rather correlates with adequate levels of basal Oas (show SMOC1 Proteins) gene expression, maintained by basal interferon (show IFNA Proteins) signaling.
Thus, RNA cleavage events catalyzed by RNase L are required for optimal inflammasome activation during viral infections.
cellular functions of RNase L through protein-protein interactions in the spleen for immune response in mammals
Data indicate that deficiency of 2-5A-dependent RNase L (RNase L) in resulted in a significant delay of diabetes onset.
RNase L contributes to innate immunity through regulating macrophage functions.
By targeting the effector enzyme of this antiviral pathway, L* potently inhibits RNase L, underscoring the importance of this enzyme in innate immunity against Theiler's virus.
RNase-L deficiency exacerbates experimental colitis and colitis-associated cancer.
These studies highlight novel roles of RNase L in cigarette smoke plus virus induced inflammation, tissue remodeling, apoptosis, and cytokine elaboration
RNase L activation during mouse hepatitis virus infection is cell type specific and correlates with relatively high levels of expression of oligoadenylate synthetase genes, which are necessary for an effective RNase L antiviral response.
The results suggest that RNase L is not an evolutionarily-conserved host defense mechanism to counteract retroviruses in vivo.
This review outlines the role of RNase-L in antimicrobial immunity and the cytoskeleton-associated innate response. [review]
Data show that RNA decay by ribonuclease L (RNase L) has an important role in homeostasis and serves as a suppressor of cell adhesion.
Single Nucleotide Polymorphisms in RNASEL involved in the immune response are generally not associated with intraprostatic inflammation in men without a Prostate cancer diagnosis.
OAS3 displayed a higher affinity for dsRNA in intact cells than either OAS1 (show OAS1 Proteins) or OAS2 (show OAS2 Proteins), consistent with its dominant role in RNase L activation.
Tanslation of vaccinia virus A27L and B5R (show CYB5R3 Proteins) genes is independent of PKR (show PKLR Proteins) activation, but their expression is dependent on the RNase L activity.
Our results demonstrate a novel role of RNase L generated small RNAs in cross-talk between autophagy and apoptosis that impacts the fate of cells during viral infections and cancer.
Among 794 RNASEL Ssingle nucleotide polymorphism (SNPs) entries 124 SNPs were found nonsynonymous (ns) from which SIFT predicted 13 nsSNPs as nontolerable whereas PolyPhen-2 predicted 28.
Virus infection and RNase L activation disrupt its association with Filamin A (show FLNA Proteins) and release RNase L to mediate its canonical nuclease (show DCLRE1C Proteins)-dependent antiviral activities.
These data show that RNase L targets specific sites in both host and viral RNAs to restrict influenza virus replication when NS1 protein is disabled.
The IFNs inhibit viral infections in part through the 2',5'-oligoadenylate (2-5A) synthetase (OAS (show SMOC1 Proteins))/RNase L pathway.
A 2.5 A and 3.25 A X-ray crystal and small-angle X-ray scattering structure of RNase L bound to a natural 2-5A activator with and without ADP or the nonhydrolysable ATP mimetic AMP (show TMPRSS5 Proteins)-PNP (show NP Proteins) is functionally characterized.
This gene encodes a component of the interferon-regulated 2-5A system that functions in the antiviral and antiproliferative roles of interferons. Mutations in this gene have been associated with predisposition to prostate cancer and this gene is a candidate for the hereditary prostate cancer 1 (HPC1) allele.
, 2-5A-dependent RNase
, 2-5A-dependent ribonuclease
, RNase L
, ribonuclease 4
, 2',5'-oligoisoadenylate synthetase-dependent
, interferon-induced 2-5A-dependent RNase