ReviewCurrent opinion in structural biology2017
New insights into influenza A specificity: an evolution of paradigms.
Review in Current opinion in structural biology, 2017. 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, 39 citations in OpenAlex.
- Standing HA phenotypic breadth shapes H5N1 cross-host potential.Research square · 2026Article
- Structural and immunological characterization of the H3 influenza hemagglutinin during antigenic drift.Nature communications · 2025Article
- Cell-based sialoglycan arrays for directly comparing influenza A virus receptor requirements for binding and infection.iScience · 2025Article
- ComplexJournal of virology · 2024Article
- Viral envelope proteins fused to multiple distinct fluorescent reporters to probe receptor binding.Protein science : a publication of the Protein Society · 2024Article
- Evolution of human H3N2 influenza virus receptor specificity has substantially expanded the receptor-binding domain site.Cell host & microbe · 2024Article
- H3N2 influenza A virus gradually adapts to human-type receptor binding and entry specificity after the start of the 1968 pandemic.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Influence of Host Sialic Acid Receptors Structure on the Host Specificity of Influenza Viruses.Viruses · 2022Review
- Preventing Influenza A Virus Infection by Mixed Inhibition of Neuraminidase and Hemagglutinin by Divalent Inhibitors.Journal of medicinal chemistry · 2022Article
- Article
- A cell free biomembrane platform for multimodal study of influenza virus hemagglutinin and for evaluation of entry-inhibitors against hemagglutinin.Frontiers in molecular biosciences · 2022Article
- Strategies for Glycoengineering Therapeutic Proteins.Frontiers in chemistry · 2022Review
- Characterization of Influenza Virus Binding to Receptors on Isolated Cell Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Hierarchical Multivalent Effects Control Influenza Host Specificity.ACS central science · 2020Article
- Structural Basis and Evolution of Glycan Receptor Specificities within the Polyomavirus Family.mBio · 2020Article
- Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships.Mass spectrometry reviews · 2020Review
- Influenza A Virus Hemagglutinin-Neuraminidase-Receptor Balance: Preserving Virus Motility.Trends in microbiology · 2020Review
- Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors.Journal of medicinal chemistry · 2019Article
- NMR Resonance Assignment Methodology: Characterizing Large Sparsely Labeled Glycoproteins.Journal of molecular biology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Understanding the molecular origin of influenza receptor specificity is complicated by the paucity of quantitative affinity measurements, and the qualitative and variable nature of glycan array data. Further obstacles arise from the varied impact of viral glycosylation and the relatively narrow spectrum of biologically relevant receptors present on glycan arrays. A survey of receptor conformational properties is presented, leading to the conclusion that conformational entropy plays a key role in defining specificity, as does the newly reported ability of biantennary receptors that terminate in Siaα2-6Gal sequences to form bidentate interactions to two binding sites in a hemagglutinin trimer. Bidentate binding provides a functional explanation for the observation that Siaα2-6 receptors adopt an open-umbrella topology when bound to hemagglutinins from human-infective viruses, and calls for a reassessment of virus avidity and tissue tropism.
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.