ArticleJournal of virology2000
Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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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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Who cites it
50 citing papers in PubMed, 84 citations in OpenAlex.
- Single amino acid substitution in RdRp reduces viral recombination frequency of NADC30-like porcine reproductive and respiratory syndrome virus type 2.PLoS pathogens · 2026Article
- Mechanistic insights into bismuth(iii) inhibition of SARS-CoV-2 helicase.Chemical science · 2024Article
- Classification, replication, and transcription ofFrontiers in microbiology · 2023Review
- Ensemble cryo-EM reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex.Nature structural & molecular biology · 2022Article
- Identification of an Intramolecular Switch That Controls the Interaction of Helicase nsp10 with Membrane-Associated nsp12 of Porcine Reproductive and Respiratory Syndrome Virus.Journal of virology · 2021Article
- Structural basis for backtracking by the SARS-CoV-2 replication-transcription complex.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for backtracking by the SARS-CoV-2 replication-transcription complex.bioRxiv : the preprint server for biology · 2021Article
- Coronavirus replication-transcription complex: Vital and selective NMPylation of a conserved site in nsp9 by the NiRAN-RdRp subunit.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Native Mass Spectrometry-Based Screening for Optimal Sample Preparation in Single-Particle Cryo-EM.Structure (London, England : 1993) · 2021Article
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- Review
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- Structural Characterization of the Helicase nsp10 Encoded by Porcine Reproductive and Respiratory Syndrome Virus.Journal of virology · 2020Article
- Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex.bioRxiv : the preprint server for biology · 2020Article
- Helicase of Type 2 Porcine Reproductive and Respiratory Syndrome Virus Strain HV Reveals a Unique Structure.Viruses · 2020Article
- Phytochemicals from Selective Plants Have Promising Potential against SARS-CoV-2: Investigation and Corroboration through Molecular Docking, MD Simulations, and Quantum Computations.BioMed research international · 2020Article
- Mapping the Nonstructural Protein Interaction Network of Porcine Reproductive and Respiratory Syndrome Virus.Journal of virology · 2018Article
- Identification of the strain-specifically truncated nonstructural protein 10 of porcine reproductive and respiratory syndrome virus in infected cells.Journal of integrative agriculture : JIA · 2018Article
- Antiviral activity of K22 against members of the order Nidovirales.Virus research · 2018Article
- Induction of Apoptosis by the Nonstructural Protein 4 and 10 of Porcine Reproductive and Respiratory Syndrome Virus.PloS one · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The arterivirus equine arteritis virus nonstructural protein 10 (nsp10) has previously been predicted to contain a Zn finger structure linked to a superfamily 1 (SF1) helicase domain. A recombinant form of nsp10, MBP-nsp10, was produced in Escherichia coli as a fusion protein with the maltose-binding protein. The protein was partially purified by affinity chromatography and shown to have ATPase activity that was strongly stimulated by poly(dT), poly(U), and poly(dA) but not by poly(G). The protein also had both RNA and DNA duplex-unwinding activities that required the presence of 5' single-stranded regions on the partial-duplex substrates, indicating a 5'-to-3' polarity in the unwinding reaction. Results of this study suggest a close functional relationship between the arterivirus nsp10 and the coronavirus helicase, for which NTPase and duplex-unwinding activities were recently demonstrated. In a number of biochemical properties, both arterivirus and coronavirus SF1 helicases differ significantly from the previously characterized RNA virus SF1 and SF2 enzymes. Thus, the combined data strongly support the idea that nidovirus helicases may represent a separate group of RNA virus-encoded helicases with distinct properties.
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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.