ArticleFrontiers in immunology2017
Isolation of Single-Domain Antibody Fragments That Preferentially Detect Intact (146S) Particles of Foot-and-Mouth Disease Virus for Use in Vaccine Quality Control.
Article in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- Article
- Single-Domain Antibodies That Specifically Recognize Intact Capsids of Multiple Foot-and-Mouth Disease Serotype O Strains.Vaccines · 2025Article
- Foot-and-mouth disease virus antigenic landscape and reduced immunogenicity elucidated in atomic detail.Nature communications · 2024Article
- A broadly reactive ultralong bovine antibody that can determine the integrity of foot-and-mouth disease virus capsids.The Journal of general virology · 2024Article
- Effect of different inactivants and preservatives on the stability of 146S fraction of foot-and-mouth diseases virus.Veterinary research forum : an international quarterly journal · 2024Article
- Characterization of Foot-and-Mouth Disease Virus Serotype O-Specific Single Domain Antibody Expressed in the pET Expression System.Indian journal of microbiology · 2023Article
- Antibody Phage Display Technology for Sensor-Based Virus Detection: Current Status and Future Prospects.Biosensors · 2023Review
- Article
- Review
- Structural and molecular basis for foot-and-mouth disease virus neutralization by two potent protective antibodies.Protein & cell · 2022Article
- Article
- Generation of a High-Affinity Nanobody Against CD147 for Tumor Targeting and Therapeutic Efficacy Through Conjugating Doxorubicin.Frontiers in immunology · 2022Article
- Mapping of foot-and-mouth disease virus antigenic sites recognized by single-domain antibodies reveals different 146S particle specific sites and particle flexibility.Frontiers in veterinary science · 2022Article
- A novel single-domain antibody multimer that potently neutralizes tetanus neurotoxin.Vaccine: X · 2021Article
- A Heat-Induced Mutation on VP1 of Foot-and-Mouth Disease Virus Serotype O Enhanced Capsid Stability and Immunogenicity.Journal of virology · 2021Article
- Camelid Single-Domain Antibodies for the Development of Potent Diagnosis Platforms.Molecular diagnosis & therapy · 2021Review
- Article
- Development of a Potent Stabilizer for Long-Term Storage of Foot-and-Mouth Disease Vaccine Antigens.Vaccines · 2021Article
- Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.Frontiers in cellular and infection microbiology · 2021Review
- Towards improvements in foot-and-mouth disease vaccine performance.Acta veterinaria Scandinavica · 2020Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Intact (146S) foot-and-mouth disease virus (FMDVs) can dissociate into specific (12S) viral capsid degradation products. FMD vaccines normally consist of inactivated virions. Vaccine quality is dependent on 146S virus particles rather than 12S particles. We earlier isolated two llama single-domain antibody fragments (VHHs) that specifically recognize 146S particles of FMDV strain O
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Registered trials
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