ArticleJournal of virology2012
Formation of higher-order foot-and-mouth disease virus 3D(pol) complexes is dependent on elongation activity.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
The trial behind it
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
22 citing papers in PubMed, 32 citations in OpenAlex.
- Interactions between the 2C protein of foot-and-mouth disease virus and components of the viral replication machinery are mediated by endoplasmic reticulum-derived membranes.The Journal of general virology · 2026Article
- Aptamer-Based Detection of Foot-and-Mouth Disease Virus Using Single-Stranded DNA Probe.Applied biochemistry and biotechnology · 2025Article
- Nucleic Acid Aptamers for Human Norovirus GII.4 and GII.17 Virus-Like Particles (VLPs) Exhibit Specific Binding and Inhibit VLPs from Entering Cells.International journal of nanomedicine · 2025Article
- RNA-dependent RNA polymerase of predominant human norovirus forms liquid-liquid phase condensates as viral replication factories.Science advances · 2024Article
- RNA-dependent RNA polymerase of predominant human norovirus forms liquid-liquid phase condensates as viral replication factories.bioRxiv : the preprint server for biology · 2024Article
- Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers.Nature communications · 2024Article
- Dual role of the foot-and-mouth disease virus 3B1 protein in the replication complex: As protein primer and as an essential component to recruit 3Dpol to membranes.PLoS pathogens · 2023Article
- Higher-order structures of the foot-and-mouth disease virus RNA-dependent RNA polymerase required for genome replication.Communications biology · 2022Article
- Insight Into the Interaction Between RNA Polymerase and VPg for Murine Norovirus Replication.Frontiers in microbiology · 2018Article
- Structure and Function of Caliciviral RNA Polymerases.Viruses · 2017Review
- Foot-and-mouth disease virus genome replication is unaffected by inhibition of type III phosphatidylinositol-4-kinases.The Journal of general virology · 2016Article
- Both cis and trans Activities of Foot-and-Mouth Disease Virus 3D Polymerase Are Essential for Viral RNA Replication.Journal of virology · 2016Article
- Gene overlapping and size constraints in the viral world.Biology direct · 2016Article
- The Structure of the RNA-Dependent RNA Polymerase of a Permutotetravirus Suggests a Link between Primer-Dependent and Primer-Independent Polymerases.PLoS pathogens · 2015Article
- Picornavirus RNA polyadenylation by 3D(pol), the viral RNA-dependent RNA polymerase.Virus research · 2015Review
- Inhibition of the foot-and-mouth disease virus subgenomic replicon by RNA aptamers.The Journal of general virology · 2014Article
- Common and unique features of viral RNA-dependent polymerases.Cellular and molecular life sciences : CMLS · 2014Review
- Inhibition of hepatitis C virus production by aptamers against the core protein.Journal of virology · 2014Article
- Article
- Inhibition of hepatitis C virus infection by DNA aptamer against envelope protein.Antimicrobial agents and chemotherapy · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The replication of many viruses involves the formation of higher-order structures or replication "factories." We show that the key replication enzyme of foot-and-mouth disease virus (FMDV), the RNA-dependent RNA polymerase, forms fibrils in vitro. Although there are similarities with previously characterized poliovirus polymerase fibrils, FMDV fibrils are narrower, are composed of both protein and RNA, and, importantly, are seen only when all components of an elongation assay are present. Furthermore, an inhibitory RNA aptamer prevents fibril formation.
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What OpenQuestion holds
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.