ArticleScience (New York, N.Y.)2024
A neutralizing antibody prevents postfusion transition of measles virus fusion protein.
Article in Science (New York, N.Y.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
22 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Insights into the multifunctionality of viral glycoproteins F and HN in the lifecycle and pathogenesis of Newcastle disease virus: a systematic review.Veterinary research · 2025Pooled it
- Antiviral GHP-88310 blocks contact-mediated and airborne transmission in a ferret model of measles-like disease.Nature microbiology · 2026Article
- Identification and structure-activity relationship analysis of minimal fusion inhibitors targeting measles virus F protein.RSC medicinal chemistry · 2026Article
- Comprehensive mapping of human CD4Cell reports. Medicine · 2026Article
- Identification of cannabichromevarin as a potent stabilizer of the measles virus prefusion F protein: structural insights from long-timescale molecular dynamics.Scientific reports · 2026Article
- Human neutralizing antibodies targeting the measles virus hemagglutinin and fusion surface proteins.Cell host & microbe · 2026Article
- Highly potent C-type nanoantibodies neutralize Nipah and Hendra viruses by cavity filling on fusion glycoprotein.Nature communications · 2026Article
- Structural and mechanistic basis for antibody neutralization of the measles fusion protein.Nature communications · 2026Article
- From Population Averaging to Single Event Resolution: Evolution of Sensing Platforms for Membrane Fusion.Sensors (Basel, Switzerland) · 2026Review
- Functional and antigenic constraints on the Nipah virus fusion protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Functional and antigenic constraints on the Nipah virus fusion protein.bioRxiv : the preprint server for biology · 2026Article
- Monoclonal antibody against canine distemper virus H protein potently neutralizes the giant panda-derived strain.AMB Express · 2025Article
- Stabilized Full-Length Measles Fusion Protein Elicits Potent Immunity and Protection In Vivo.bioRxiv : the preprint server for biology · 2025Article
- Article
- Structural and Mechanistic Basis for Antibody Neutralization of the Measles Fusion Protein.bioRxiv : the preprint server for biology · 2025Article
- A Short Peptide Inhibitor of Measles Virus Fusion Protein that Exhibits Passive Membrane Permeability.ChemMedChem · 2025Article
- Remdesivir postexposure prophylaxis limits measles-induced "immune amnesia" and measles antibody responses in macaques.JCI insight · 2025Article
- Systematic Comparison of Commercial Uranyl-Alternative Stains for Negative- and Positive-Staining Transmission Electron Microscopy of Organic Specimens.Advanced healthcare materials · 2025Article
- Measles Virus-Based Genetic Modifications: Progress in Hematological Malignancy Treatment.OncoTargets and therapy · 2025Review
- The role of ADAR1 in human pathophysiology.Frontiers in cell and developmental biology · 2025Review
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Authors and funding
22 authors.
Funding
Abstract
Measles virus (MeV) presents a public health threat that is escalating as vaccine coverage in the general population declines and as populations of immunocompromised individuals, who cannot be vaccinated, increase. There are no approved therapeutics for MeV. Neutralizing antibodies targeting viral fusion are one potential therapeutic approach but have not yet been structurally characterized or advanced to clinical use. We present cryo-electron microscopy (cryo-EM) structures of prefusion F alone [2.1-angstrom (Å) resolution], F complexed with a fusion-inhibitory peptide (2.3-Å resolution), F complexed with the neutralizing and protective monoclonal antibody (mAb) 77 (2.6-Å resolution), and an additional structure of postfusion F (2.7-Å resolution). In vitro assays and examination of additional EM classes show that mAb 77 binds prefusion F, arrests F in an intermediate state, and prevents transition to the postfusion conformation. These structures shed light on antibody-mediated neutralization that involves arrest of fusion proteins in an intermediate state.
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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.