ArticleNature communications2018
Structures of Coxsackievirus A10 unveil the molecular mechanisms of receptor binding and viral uncoating.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 39 citations in OpenAlex.
- Open questions in enterovirus uncoating.Journal of virology · 2026Review
- Benchmarking deep learning methods for Cα atom prediction in cryo-EM density maps.Bioinformatics (Oxford, England) · 2026Article
- VP1-141 is a determinant of a Vero cell-adapted Coxsackievirus A10 for vaccine development.PLoS neglected tropical diseases · 2026Article
- Identification of key amino acids defining conformational neutralizing epitopes of coxsackievirus A5 using monoclonal antibody escape mutants.Frontiers in immunology · 2026Article
- Unveiling the enterovirus diversity in Barcelona, Spain (2020-2024) through wastewater and clinical surveillance.Emerging microbes & infections · 2025Article
- Cryo-EM structure of the Seneca Valley virus A-particle and related structural states.Journal of virology · 2025Article
- A single amino acid mutation in VP1 of coxsackievirus A6 determining efficiency of VP0 cleavage and proliferation.Journal of virology · 2025Article
- Article
- Virus-Receptor Interactions and Receptor-Mediated Virus Entry into Host Cells.Sub-cellular biochemistry · 2024Review
- Article
- VP2 residue N142 of coxsackievirus A10 is critical for the interaction with KREMEN1 receptor and neutralizing antibodies and the pathogenicity in mice.PLoS pathogens · 2023Article
- Pathogenesis of enterovirus infection in central nervous system.Biosafety and health · 2023Review
- Identification of a Conserved, Linear Epitope on VP3 ofViruses · 2023Article
- Human SCARB2 Acts as a Cellular Associator for Helping Coxsackieviruses A10 Infection.Viruses · 2023Article
- Article
- Identification of a neutralizing linear epitope within the VP1 protein of coxsackievirus A10.Virology journal · 2022Article
- Structural Insights into Common and Host-Specific Receptor-Binding Mechanisms in Algal Picorna-like Viruses.Viruses · 2022Article
- Molecular characteristics of a coxsackievirus A12 strain in Zhejiang of China, 2019.Virology journal · 2022Article
- Membrane-assisted assembly and selective secretory autophagy of enteroviruses.Nature communications · 2022Article
- Reverse-Phase Ultra-Performance Chromatography Method for Oncolytic Coxsackievirus Viral Protein Separation and Empty to Full Capsid Quantification.Human gene therapy · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coxsackievirus A10 (CVA10), a human type-A Enterovirus (HEV-A), can cause diseases ranging from hand-foot-and-mouth disease to polio-myelitis-like disease. CVA10, together with some other HEV-As, utilizing the molecule KREMEN1 as an entry receptor, constitutes a KREMEN1-dependent subgroup within HEV-As. Currently, there is no vaccine or antiviral therapy available for treating diseases caused by CVA10. The atomic-resolution structure of the CVA10 virion, which is within the KREMEN1-dependent subgroup, shows significant conformational differences in the putative receptor binding sites and serotype-specific epitopes, when compared to the SCARB2-dependent subgroup of HEV-A, such as EV71, highlighting specific differences between the sub-groups. We also report two expanded structures of CVA10, an empty particle and uncoating intermediate at atomic resolution, as well as a medium-resolution genome structure reconstructed using a symmetry-mismatch method. Structural comparisons coupled with previous results, reveal an ordered signal transmission process for enterovirus uncoating, converting exo-genetic receptor-attachment inputs into a generic RNA release mechanism.
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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.