Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.9 (ribonuclease)
 6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

At 1--3 hours after infection of chick fibroblasts and a continuous dog kidney cell line MDCK with WSN and FPV viruses large virus specific structures were found containing parent nucleocapsids, newly synthesized virus-specific RNA and newly synthesized protein. The buoyant density of these structures in cesium chloride was 1.30--1.32 g/ml. The amount of newly synthesized RNA and protein in these structures increased linearly for 3 hours of infection. The parent and newly synthesized RNA in the structures were resistant to ribonuclease. When protein synthesis was inhibited by cycloheximide, parent nucleocapsids were also found in the large structures, and primary transcription of the viral genome occurred there as well. Some structures were destroyed upon sonication of the nuclei. It is suggested that in the observed structure the parent nucleocapsids are associated with cell components (possibly, nuclear chromatin), and centers of influenza virus reproduction arise in the sites of association.
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PMID:[Intranuclear centers of influenza virus reproduction during the early stage of infection]. 56 91

The properties of the ribonucleic acid (RNA) synthesized by the influenza (WSN) virion polymerase have been investigated. Most of the product RNA is synthesized in association with virion RNA species from which it can be released by heat treatment as single-stranded, ribonuclease-sensitive polynucleotides (average molecular weight, 2-hr sample, about 10(5) daltons). At least 95% of the product is complementary to the viral RNA species. On the basis of the molar ratio of the RNA species isolated from a (3)H-uridine-labeled virus preparation, it was calculated that the WSN genome consists of seven pieces of RNA with a sum molecular weight of about 5 x 10(6) daltons.
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PMID:Transcription of the influenza ribonucleic acid genome by a virion polymerase. II. Nature of the in vitro polymerase product. 510 47

By serial subculture of MDCK cells which survived high multiplicity infections with AWBY-140, a weakly cytolytic mutant of influenza virus A/WSN (H1N1), we established a variant cell line (MDCK-L cells) that was uniquely resistant to infection with influenza A and B viruses, yielding 3 to 4 orders lower amount of progeny virus compared with MDCK cells. Competitive polymerase chain reaction revealed that the amount of primary transcript produced in MDCK-L cells infected with 10 PFU/cell of influenza virus A/Aichi was suppressed to 1/100 of that in MDCK cells similarly infected, although the amount of virus adsorbed to MDCK-L cells was 1/4 of MDCK cells. Even when MDCLK-L cells were infected with 40 PFU/cell of Aichi to overcome the lower amount of internalized virus in those cells, the results were the same. The synthesis of v-, c- and mRNAs, as well as proteins of infected A/Aichi was below detectable level in MDCK-L cells, in contrast with MDCK cells, where they were clearly demonstrable by ribonuclease protection assay or polyacrylamide gel electrophoresis.
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PMID:A variant of MDCK cell line which restricted growth of influenza viruses mainly through suppression of viral primary transcription. 867 37

A novel series of metal-free artificial ribonucleases (aRNases) was designed, synthesized and assessed in terms of ribonuclease activity and ability to inactivate influenza virus WSN/A33/H1N1 in vitro. The compounds were built of two short peptide fragments, which include Lys, Ser, Arg, Glu and imidazole residues in various combinations, connected by linkers of different hydrophobicity (1,12-diaminododecane or 4,9-dioxa-1,12-diaminododecane). These compounds efficiently cleaved different RNA substrates under physiological conditions at rates three to five times higher than that of artificial ribonucleases described earlier and displayed RNase A-like cleavage specificity. aRNases with the hydrophobic 1,12-diaminododecane linker displayed ribonuclease activity 3-40 times higher than aRNases with the 4,9-dioxa-1,12-diaminododecane linker. The assumed mechanism of RNA cleavage was typical for natural ribonucleases, that is, general acid-base catalysis via the formation of acid/base pairs by functional groups of amino acids present in the aRNases; the pH profile of cleavage confirmed this mechanism. The most active aRNases under study exhibited high antiviral activity and entirely inactivated influenza virus A/WSN/33/(H1N1) after a short incubation period of viral suspension under physiological conditions.
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PMID:Design, RNA cleavage and antiviral activity of new artificial ribonucleases derived from mono-, di- and tripeptides connected by linkers of different hydrophobicity. 2689 94