ArticleJournal of virology2004
Classical swine fever virus glycoprotein E rns is an endoribonuclease with an unusual base specificity.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 44 citations in OpenAlex.
- A dual role for ER-Golgi cargo receptor LMAN1 in supporting CSFV replication and restraining RLR signaling.Journal of virology · 2026Article
- First Identification, Recombinant Production, and Structural Characterization of a Putative Structural Protein from the Haseki Tick Virus Polyprotein.Biomolecules · 2025Article
- Strategies of Classical Swine Fever Immune Evasion.International journal of molecular sciences · 2025Review
- A double deletion prevents replication of the pestivirus bovine viral diarrhea virus in the placenta of pregnant heifers.PLoS pathogens · 2021Article
- The EViruses · 2021Article
- Downstream Sequences Control the Processing of the Pestivirus EJournal of virology · 2020Article
- Article
- Autonomously Replicating RNAs of Bungowannah Pestivirus: EJournal of virology · 2020Article
- Classical swine fever virus NJournal of virology · 2020Article
- Homodimerisation-independent cleavage of dsRNA by a pestiviral nicking endoribonuclease.Scientific reports · 2018Article
- Immune Responses Against Classical Swine Fever Virus: Between Ignorance and Lunacy.Frontiers in veterinary science · 2015Review
- Prolonged activity of the pestiviral RNase Erns as an interferon antagonist after uptake by clathrin-mediated endocytosis.Journal of virology · 2014Article
- Efficient sensing of infected cells in absence of virus particles by plasmacytoid dendritic cells is blocked by the viral ribonuclease E(rns.).PLoS pathogens · 2013Article
- A new type of signal peptidase cleavage site identified in an RNA virus polyprotein.The Journal of biological chemistry · 2010Article
- Mutation of cysteine 171 of pestivirus E rns RNase prevents homodimer formation and leads to attenuation of classical swine fever virus.Journal of virology · 2009Article
- Bovine viral diarrhea virus: prevention of persistent fetal infection by a combination of two mutations affecting Erns RNase and Npro protease.Journal of virology · 2007Article
- RNA recognition and cleavage by the SARS coronavirus endoribonuclease.Journal of molecular biology · 2006Article
- The carboxy-terminal sequence of the pestivirus glycoprotein E(rns) represents an unusual type of membrane anchor.Journal of virology · 2005Article
- Antibody responses of pigs to defined Erns fragments after infection with classical swine fever virus.Clinical and diagnostic laboratory immunology · 2005Article
- Major genetic marker of nidoviruses encodes a replicative endoribonuclease.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycoprotein E(rns) of pestiviruses is a virion-associated and -secreted RNase that is involved in virulence. The requirements at the cleavage site in heteropolymeric RNA substrates were studied for E(rns). Limited digestion of heteropolymeric RNA substrates indicated a cleavage 5' of uridine residues irrespective of the preceding nucleotide (Np/U). To further study specificity radiolabeled RNA, molecules of 45 to 56 nucleotides in length were synthesized that contained no or a single Np/U cleavage site. Cleavage was only observed in substrates containing an ApU, CpU, GpU, or UpU dinucleotide and occurred in two steps, an initial NpU-specific and a consecutive unspecific degradation. The NpU-specific cleavage was resistant to 7 M urea while the second-order cleavage was sensitive to denaturation. Kinetic analyses revealed that E(rns) is a highly active endoribonuclease (k(cat)/K(m) = 2 x 10(6) to 10 x 10(6) M(-1) s(-1)) with a strong affinity to NpU containing single-stranded RNA substrates (K(m) = 85 to 260 nM).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.