ArticleScience (New York, N.Y.)2013
Preferential recognition of avian-like receptors in human influenza A H7N9 viruses.
Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
94 citing papers in PubMed, 152 citations in OpenAlex.
- D347G in PA is critical for the pathogenicity of H9N2 avian influenza A virus in mice.Virulence · 2026Article
- The receptor landscape of influenza A viruses.Journal of virology · 2026Review
- Single-component self-assembling protein nanoparticles displaying stabilized prefusion-closed hemagglutinin trimers for influenza vaccine development.Nature communications · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Divergent Avian Influenza H10 Viruses from Sympatric Waterbird Species in Italy: Zoonotic Potential Assessment by Molecular Markers.Microorganisms · 2025Article
- A broadly neutralizing antibody recognizes a unique epitope with a signature motif common across coronaviruses.Nature communications · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis of different neutralization capabilities of monoclonal antibodies against H7N9 virus.Journal of virology · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.bioRxiv : the preprint server for biology · 2025Article
- Molecular Markers and Mechanisms of Influenza A Virus Cross-Species Transmission and New Host Adaptation.Viruses · 2024Review
- Human neutralizing antibodies target a conserved lateral patch on H7N9 hemagglutinin head.Nature communications · 2024Article
- Pathogenicity and virulence of influenza.Virulence · 2023Review
- Allosteric Neutralization by Human H7N9 Antibodies.Research square · 2023Article
- Article
- Influence of Host Sialic Acid Receptors Structure on the Host Specificity of Influenza Viruses.Viruses · 2022Review
- Epidemiologic, Clinical, and Genetic Characteristics of Human Infections with Influenza A(H5N6) Viruses, China.Emerging infectious diseases · 2022Article
- Bioengineered pseudovirus nanoparticles displaying the HA1 antigens of influenza viruses for enhanced immunogenicity.Nano research · 2022Article
- Spatio-temporal spread and evolution of influenza A (H7N9) viruses.Frontiers in microbiology · 2022Article
- Article
- Article
34 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The 2013 outbreak of avian-origin H7N9 influenza in eastern China has raised concerns about its ability to transmit in the human population. The hemagglutinin glycoprotein of most human H7N9 viruses carries Leu(226), a residue linked to adaptation of H2N2 and H3N2 pandemic viruses to human receptors. However, glycan array analysis of the H7 hemagglutinin reveals negligible binding to humanlike α2-6-linked receptors and strong preference for a subset of avian-like α2-3-linked glycans recognized by all avian H7 viruses. Crystal structures of H7N9 hemagglutinin and six hemagglutinin-glycan complexes have elucidated the structural basis for preferential recognition of avian-like receptors. These findings suggest that the current human H7N9 viruses are poorly adapted for efficient human-to-human transmission.
Indexed as
Identifiers
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.