ReviewBriefings in functional genomics2018
The structural variability of the influenza A hemagglutinin receptor-binding site.
Review in Briefings in functional genomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 37 citations in OpenAlex.
- Substitutions affecting the HA-NA-receptor balance preceded the emergence of the pandemic 2009 H1N1 virus.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Optimizing an avian influenza vaccine using a novel Bacterial Enzymatic Combinatorial Chemistry (BECC) TLR4 adjuvant.mSphere · 2026Article
- Predicting host tropism in influenza a viruses: insights from multi-segment nucleotide signatures.Journal of translational medicine · 2025Article
- A single mutation at position 214 of influenza B hemagglutinin enhances cross-neutralization.Emerging microbes & infections · 2025Article
- Nanobodies: a new frontier in influenza virus neutralization.Folia microbiologica · 2025Review
- Article
- Structural basis of receptor-binding adaptation of human-infecting H3N8 influenza A virus.Journal of virology · 2025Article
- Influenza Virus Genomic Mutations, Host Barrier and Cross-species Transmission.Current genomics · 2025Review
- Analysis of the Monophyletic Lineage of Avian Influenza H5N1 Which Circulated in Venezuelan Birds During the 2022-2023 Outbreak.Microorganisms · 2024Article
- A Comparison of Host Responses to Infection with Wild-Type Avian Influenza Viruses in Chickens and Tufted Ducks.Microbiology spectrum · 2023Article
- Review
- Avian Influenza Virus Tropism in Humans.Viruses · 2023Review
- Evolution of Indian Influenza A (H1N1) Hemagglutinin Strains: A Comparative Analysis of the Pandemic Californian HA Strain.Frontiers in molecular biosciences · 2023Article
- Phylodynamics and Molecular Mutations of the Hemagglutinin Affecting Global Transmission and Host Adaptation of H5Nx Viruses.Transboundary and emerging diseases · 2023Article
- Passive antifouling and active self-disinfecting antiviral surfaces.Chemical engineering journal (Lausanne, Switzerland : 1996) · 2022Review
- Small Molecule Inhibitors of Influenza Virus Entry.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Modeling theBiomolecules · 2021Article
- Comparison of Clinical Features and Outcomes of Medically Attended COVID-19 and Influenza Patients in a Defined Population in the 2020 Respiratory Virus Season.Frontiers in public health · 2021Article
- Article
- Broadly Neutralizing Bovine Antibodies: Highly Effective New Tools against Evasive Pathogens?Viruses · 2020Review
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
Abstract
Hemagglutinin (HA) is a transmembrane protein of the influenza A virus and a key component in its life cycle. The protein allows the virus to enter a host cell by recognizing specific glycans attached to transmembrane proteins of the host, which leads to viral endocytosis. In recent years, significant progress has been made in understanding the structural relationship between changes in the HA receptor-binding site (RBS) and the sialylated glycans that bind them. Several mutations were identified in the HA RBS that allows the virus to change host tropism. Their impact on binding the analogs of human and avian receptors was determined with X-ray crystallography. In this article, we provide a short overview of the HA protein structure and briefly discuss the adaptive mutations introduced to different HA subtypes.
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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.