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Ribonuclease L or RNase L (for latent), ... is the cell's last stand against a virus before it attempts apoptosis. ...
Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases , and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes.
By the use of L-ribose or rather L-ribonucleotides, L-RNA can be synthesized. L-RNA is much more stable against degradation by RNase. [18] Like other structured biopolymers such as proteins, one can define topology of a folded RNA molecule. This is often done based on arrangement of intra-chain contacts within a folded RNA, termed as circuit ...
Ribonuclease L normally binds to 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) and inhibits the interferon-regulated 2-5A/RNase L pathway, which is used by viruses. ABCE1 heterodimerize with ribonuclease L and prevents its interaction with 2-5A, antagonizing the anti-viral properties of ribonuclease L, [ 6 ] and allow the virus to ...
In biochemistry, a ribonucleotide is a nucleotide containing ribose as its pentose component. It is considered a molecular precursor of nucleic acids.Nucleotides are the basic building blocks of DNA and RNA.
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Eosinophil cationic protein (ECP) also known as ribonuclease 3 is a basic protein located in the eosinophil primary matrix. [4] In humans, the eosinophil cationic protein is encoded by the RNASE3 gene. [5] ECP is released during degranulation of eosinophils. This protein is related to inflammation and asthma because in these cases, there are ...