ReviewBiological chemistry2014
The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor.
Review in Biological chemistry, 2014. 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.
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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
22 citing papers in PubMed, 26 citations in OpenAlex.
- Understanding protein ISGylation, a multifaceted posttranslational modification.Cell chemical biology · 2026Review
- Identification of a novel equine rhinitis B virus detected in horse from Japan.The Journal of veterinary medical science · 2026Article
- Use of virus-like particles and nanoparticle-based vaccines for combating picornavirus infections.Veterinary research · 2024Review
- Enzymatic characterization and dominant sites of foot-and-mouth disease virus 2C protein.Heliyon · 2024Article
- The antiviral response triggered by the cGAS/STING pathway is subverted by the foot-and-mouth disease virus proteases.Cellular and molecular life sciences : CMLS · 2024Article
- The Foot-and-Mouth Disease Virus Lb Protease Cleaves Intracellular Transcription Factors STAT1 and STAT2 to Antagonize IFN-β-Induced Signaling.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Foot-and-Mouth Disease Virus: Molecular Interplays with IFN Response and the Importance of the Model.Viruses · 2022Review
- Proteolytic Processing of Plant Proteins by Potyvirus NIa Proteases.Journal of virology · 2022Article
- Mutation of FMDV LFrontiers in veterinary science · 2022Article
- Inhibition of Antiviral Innate Immunity by Foot-and-Mouth Disease Virus LJournal of virology · 2021Article
- Virus-Host Interactions in Foot-and-Mouth Disease Virus Infection.Frontiers in immunology · 2021Review
- MDA5 cleavage by the Leader protease of foot-and-mouth disease virus reveals its pleiotropic effect against the host antiviral response.Cell death & disease · 2020Article
- Dissecting distinct proteolytic activities of FMDV Lpro implicates cleavage and degradation of RLR signaling proteins, not its deISGylase/DUB activity, in type I interferon suppression.PLoS pathogens · 2020Article
- Impairment of the DeISGylation Activity of Foot-and-Mouth Disease Virus Lpro Causes AttenuationJournal of virology · 2020Article
- Innate immune sensor LGP2 is cleaved by the Leader protease of foot-and-mouth disease virus.PLoS pathogens · 2018Article
- Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Different Tactics of Foot-and-Mouth Disease Virus to Evade Innate Immunity.Frontiers in microbiology · 2018Review
- Foot-and-mouth disease virus induces lysosomal degradation of host protein kinase PKR by 3C proteinase to facilitate virus replication.Virology · 2017Article
- A Naturally Occurring Recombinant Enterovirus Expresses a Torovirus Deubiquitinase.Journal of virology · 2017Article
- NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII.Protein science : a publication of the Protein Society · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The leader proteinase (Lpro) of the foot-and-mouth disease virus inhibits the host innate immune response by at least three different mechanisms. The most well-characterised of these is the prevention of the synthesis of cytokines such as interferons immediately after infection, brought about by specific proteolytic cleavage of the eukaryotic initiation factor 4G. This prevents the recruitment of capped cellular mRNA; however, the viral RNA can be translated under these conditions. The two other mechanisms are the induction of NF-κB cleavage and the deubiquitination of immune signalling molecules. This review focuses on the structure-function relationships in Lpro responsible for these widely divergent activities.
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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.