ReviewVirulence2023
Receptor Binding Properties of Neuraminidase for influenza A virus: An Overview of Recent Research Advances.
Review in Virulence, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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.
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
14 citing papers in PubMed, 22 citations in OpenAlex.
- Narrowed host ranges do not constrain future host range expansion in RNA phage Φ6.Journal of virology · 2026Article
- Research Progress on Avian Influenza Virus and Autophagy: A Review.Pathogens (Basel, Switzerland) · 2026Review
- Structural analysis of antigenic variation and adaptive evolution of the H5N1 neuraminidase gene.PLoS computational biology · 2026Article
- Discovery of Influenza Neuraminidase Inhibitors: Structure-Based Virtual Screening and Biological Evaluation of Novel Chemotypes.Molecules (Basel, Switzerland) · 2025Article
- Organoid Models to Study Human Infectious Diseases.Cell proliferation · 2025Review
- Heterogeneity across mammalian- and avian-origin A(H1N1) influenza viruses influences viral infectivity following incubation with host bacteria from the human respiratory tract.Microbiology spectrum · 2025Article
- Construction of a replication-defective recombinant virus and cell-based vaccine for H9N2 avian influenza virus.Veterinary research · 2025Article
- Research trends and hotspots on global influenza and inflammatory response based on bibliometrics.Virology journal · 2024Review
- Rifaximin ameliorates influenza A virus infection-induced lung barrier damage by regulating gut microbiota.Applied microbiology and biotechnology · 2024Article
- Review
- Exploring Potential Intermediates in the Cross-Species Transmission of Influenza A Virus to Humans.Viruses · 2024Review
- Dual Gene Detection of H5N1 Avian Influenza Virus Based on Dual RT-RPA.Molecules (Basel, Switzerland) · 2024Article
- Insight into Antiviral Activity of Ag/TiOInternational journal of nanomedicine · 2024Article
- Advances in protein subunit vaccines against H1N1/09 influenza.Frontiers in immunology · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A viruses (IAVs) pose a serious risk to both human and animal health. IAVs' receptor binding characteristics account for a major portion of their host range and tissue tropism. While the function of neuraminidase (NA) in promoting the release of progeny virus is well-known, its role in the virus entry process remains poorly understood. Studies have suggested that certain subtypes of NA can act as receptor-binding proteins, either alone or in conjunction with haemagglutinin (HA). An important distinction is that NA from the avian influenza virus have a second sialic acid-binding site (2SBS) that is preserved in avian strains but missing in human or swine strains. Those observations suggest that the 2SBS may play a key role in the adaptation of the avian influenza virus to mammalian hosts. In this review, we provide an update of the recent research advances in the receptor-binding role of NA and highlight its underestimated importance during the early stages of the IAV life cycle. By doing so, we aim to provide new insights into the mechanisms underlying IAV host adaptation and pathogenesis.
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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 Socratic graph.