Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.27.5 (RNase)
 17,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Addition of the human placental RNase inhibitor at 10 mu/ml to a mixture of wheat germ extract and translation components, prior to the addition of mRNA from dog pancreas or influenza virus-infected cells, resulted in a significant increase in the yield of proteins synthesized. Analysis of the translation products by sodium dodecyl sulfate/polyacrylamide gel electrophoresis indicated that the inhibitor preferentially increased the yield of the larger proteins. In the presence of the inhibitor, yields of the preprocarboxypeptidases were increased 4.5-fold and yields of preamylase were increased 15-fold. Incubation of the wheat germ extract or individual translation components with dog pancreas mRNA, with or without the placental inhibitor, indicated significant RNase contamination among the fractions. Two other in vitro protein synthesis systems-the reticulocyte lysate system and the Krebs ascites system-were found to contain latent RNase activity (RNase in complex with the inhibitor) and an excess of RNase inhibitor. The addition of placental RNase inhibitor did not increase the yield in these systems, except in those cases in which the RNase contamination approached the amount of endogenous inhibitor. When used during the isolation of rat liver cell fractions, the placental inhibitor increased the yield (as measured by A(260)) of rough microsomes and detached polysomes by 24% and 4.6-fold, respectively. Analysis of translation products indicated that detached polysomes isolated in the presence of the inhibitor were intact; those isolated in the absence of inhibitor were degraded.
 ...
PMID:Role of mammalian RNase inhibitor in cell-free protein synthesis. 29 94

A clone of recombinant virus obtained from the cross between WSN and Hong Kong strains of influenza virus gave rise to progeny containing predominantly von Magnus particles. In the electropherogram of virus RNA, the P3 gene was markedly diminished, and a new species of RNA (extra RNA) was present in addition to eight gene segments. The origin of the extra RNA was studied by two-dimensional gel electrophoresis of T1 RNase-generated oligonucleotides. Four out of five large oligonucleotide spots present in the extra RNA matched to those contained by the P3 gene. It was concluded that the extra RNA was derived from the P3 gene probably by deletion. The possible origin of the spot which was present in the extra RNA but not in eight gene segments including P3 was discussed.
 ...
PMID:Origin of small RNA in von Magnus particles of influenza virus. 44 97

In freeze-thaw lysates of MDCK cells infected with 32P-labeled influenza virus A/WSN in the presence of added RNase, acid-precipitable radioactivity diminished to about 50% of initial values within 90 min after a 1-h virus adsorption period. A similar preparation containing rimantadine at a concentration of 50 micrograms/ml exhibited only a 10% reduction in acid-precipitable radioactivity. These findings suggest that rimantadine interferes with uncoating of influenza virus in infected cells.
 ...
PMID:Inhibition of influenza virus uncoating by rimantadine hydrochloride. 50 98

Ribonucleoproteins (RNPs) isolated from infectious and defective interfering (DI) influenza virus (WSN) contained three major RNP peaks when analyzed in a glycerol gradient. Peak I RNP was predominant in infectious virus but was greatly reduced in DI virus preparations. Conversely, peak III RNP was elevated in DI virus, suggesting a large increase in DI RNA in this fraction. Labeled [(32)P]RNA was isolated from each RNP region and analyzed by electrophoresis on polyacrylamide gels. Peak I RNP contained primarily the polymerase and some HA genes, peak II contained some HA gene but mostly the NP and NA genes, and peak III contained the M and NS genes. In addition, peak III RNP from DI virus also contained the characteristic DI RNA segments. Interference activity of RNP fractions isolated from infectious and DI virus was tested using infectious center reduction assay. RNP peaks (I, II, and III) from infectious virus did not show any interference activity, whereas the peak III DI RNP caused a reduction in the number of infectious centers as compared to controls. Similar interference was not demonstrable with peak I RNP of DI virus nor with any RNP fractions from infectious virus alone. The interference activity of RNP fractions was RNase sensitive, suggesting that the DI RNA contained in DI RNPs was the interfering agent, and dilution experiments supported the conclusion that a single DI RNP could cause interference. The interfering RNPs were heterogeneous, and the majority migrated slower than viral RNPs containing M and NS genes. These results suggest that DI RNP (or DI RNA) is also responsible for interference in segmented, negative-stranded viruses.
 ...
PMID:Defective influenza viral ribonucleoproteins cause interference. 50 5

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.
 ...
PMID:[Intranuclear centers of influenza virus reproduction during the early stage of infection]. 56 91

Two procedures for characterising the genomes of recombinant influenza viruses are described. The first of these involves ribonuclease T4 oligonucleotide fingerpart analysis of separated viral RNAs labelled either in vivo or in vitro and the second utilises polyacrylamide gel electrophoresis to identify the double-stranded molecules formed by hybridisation between the complementary and virion RNAs of two viruses. Although the latter method is more suitable for routine screening purposes, both procedures are suitable for distinguishing between equivalent RNA components of closely related viruses.
 ...
PMID:Procedures for characterisation of the genetic material of candidate vaccine strains. 60 97

Guanylyl- and methyltransferases, isolated from purified vaccinia virus, were used to specifically label the 5' ends of the genome RNAs of influenza A and B viruses. All eight segments were labeled with [alpha-(32)P]guanosine 5'-triphosphate or S-adenosyl[methyl-(3)H]methionine to form "cap" structures of the type m(7)G(5')pppN(m)-, of which unmethylated (p)ppN- represents the original 5' end. Further analyses indicated that m(7)G(5')pppA(m), m(7)G(5')pppA(m)pGp, and m(7)G(5')pppA(m)pGpUp were released from total and individual labeled RNA segments by digestion with nuclease P1, RNase T1, and RNase A, respectively. Consequently, the 5'-terminal sequences of most or all individual genome RNAs of influenza A and B viruses were deduced to be (p)ppApGpUp. The presence of identical sequences at the ends of RNA segments of both types of influenza viruses indicates that they have been specifically conserved during evolution.
 ...
PMID:Common sequence at the 5' ends of the segmented RNA genomes of influenza A and B viruses. 62 78

Influenza A viruses induce the accumulation of electron-dense inclusions in the cytoplasm of infected cells during the latter stages of the replication cycle. Cell fractionation studies showed that these inclusions could be recovered in subcellular fractions containing ribosomes and polysomes. Isolation of these inclusions was accomplished by procedures involving RNase treatment of these fractions followed by repurification, or by fluorocarbon extraction and gradient centrifugation. Electron microscopy indicated that the isolated inclusions exhibited a major periodicity of approximately 8 nm with minor periodicities of approximately 4 nm. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the influenza virus coded nonstructural protein was the only protein component present in isolated inclusions.
 ...
PMID:Isolation and characterization of cytoplasmic inclusions from influenza A virus-infected cells. 62 86

Purified influenza virus contains ribonuclease activity. The enzyme does not hydrolyze viral RNA but both 28 S and 18 S host cell RNA are degraded forming large (about 16 S) and small (about 5 S) fragments with the release of the acid-soluble material. It has an optimum temperature of 37 degrees C, requires no divalent ions, and is inhibited by 0.1 M EDTA and 1% SDS. Treatment with 4 M urea increases enzymatic activity considerably (42%) but is not a prerequisite for eliciting ribonuclease activity suggesting that the enzyme is probably located near the surface of the virus particle. Results show that the observed enzyme activity is virus-associated as no host cell protein is detectable in the purified virus.
 ...
PMID:Association of a ribonuclease with the purified influenza virus. 81 84

The nucleoprotein of the WSN strain of influenza was found to be phosphorylated in vitro. The phosphate-protein bond was stable to hot trichloroacetic acid, RNase, DNase, succinic acid, and succinic acid-hydroxylamine, but sensitive to hydrolysis by bacterial alkaline phosphatase. This suggested that the nucleoprotein is in the form of a phosphomonoester. Acid hydrolysis of the isolated nucleoprotein followed by thin-layer electrophoresis identified the phosphorylated amino acid residue as phosphoserine.
 ...
PMID:Phosphorylated protein component present in influenza virions. 90 30


1 2 3 4 5 6 7 8 9 Next >>