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Pref-1 (show DLK1 Proteins) mRNA is a novel substrate of RNase-L.
RNAse L stimulates fibroblast migration.
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
By sequencing abundant RNA fragments generated by RNase L in cell lines, we identify site-specific cleavage of two groups of noncoding RNAs: Y-RNAs, whose function is poorly understood, and cytosolic tRNAs, which are essential for translation.
RNASEL rs3738579 genotype was significantly related to severe necroinflammatory activity (NIA) grade of chronic hepatitis C patients.
Serum RNase-L levels were inversely associated with metabolic syndrome and age.
We show that mutations in RNase L found in HPC patients may promote prostate cancer by increasing expression of AR-responsive genes and cell motility and identify novel roles of RNase L as a prostate cancer susceptibility gene.
Suggest that naturally occurring mutations in the RNase L gene might promote enhanced prostate cancer cell migration and metastasis.
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.
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