ReviewCold Spring Harbor perspectives in medicine2021
Hemagglutinin Structure and Activities.
Review in Cold Spring Harbor perspectives in medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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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
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Who cites it
62 citing papers in PubMed.
- Targeting virus-glycan recognition in influenza viruses and coronaviruses: from the molecular principles to glycomimetic antivirals strategies.RSC chemical biology · 2026Review
- Residues Ser83, Arg85, Tyr88, Asn124, and Lys192 of C-Terminal Lipid-Associated Membrane Hemagglutinin AffectMicroorganisms · 2026Article
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Molecular Insights into High-Pathogenicity RNA Viruses.Viruses · 2026Review
- An In Vitro Screen Identifies H1 Influenza Hemagglutinin Substitutions That Alter mRNA-LNP Vaccine Responses Against the Stalk Domain.Vaccines · 2026Article
- Molecular Characterization of Influenza A(H3N2) Hemagglutinin Variants Circulating in Western Mexico, 2022.International journal of molecular sciences · 2026Article
- New determinant of influenza hemagglutinin cleavability identified through random mutagenesis for acid-stabilizing mutations.Microbiology spectrum · 2026Article
- Lymphoid-Tissue-on-Chip Recapitulates Human Antibody Responses In Vitro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Pathogenicity and immune response of turkey A(H1N2) influenza virus of swine-origin on turkeys and mice.Veterinary research · 2026Article
- Evolutionary Rate Variation at Predicted PTM Sites Reveals Localized Host-Associated Patterns in Influenza A Virus.Genome biology and evolution · 2026Article
- A novel entry inhibitor targeting the stalk domain of the hemagglutinin of H1N1.Acta pharmaceutica Sinica. B · 2026Article
- Influenza hemagglutinin subtypes have different sequence constraints despite sharing extremely similar structures.bioRxiv : the preprint server for biology · 2026Article
- Scalable secretory production of influenza A (H1N1) hemagglutinin HA1 in Pichia pastoris through expression and process optimization.Microbial cell factories · 2026Article
- Genomic surveillance of H1N1, H3N2 and influenza B Victoria lineage viruses in Qingyang (2020-2023): phylogenetic and molecular characteristics analysis of HA/NA genes.BMC infectious diseases · 2026Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza haemagglutinin.Nature ecology & evolution · 2026Article
- The Emerging Promise of Pentacyclic Triterpenoid Derivatives as Novel Antiviral Agents Against SARS-CoV-2 Variants.Molecules (Basel, Switzerland) · 2026Review
- Influenza hemagglutinin subtypes have different sequence constraints despite sharing extremely similar structures.Virus evolution · 2026Article
- Increased levels of α2-3- and α2-6-linked sialic acids during airway inflammation govern influenza A binding to peripheral airway mucins in a subtype-dependent manner.Frontiers in immunology · 2026Article
- A primary oseltamivir-resistant mutation in influenza hemagglutinin and its implications for antiviral resistance surveillance.Nature communications · 2025Article
- N-glycosylation at the receptor binding site drives differences in receptor binding specificity between influenza B virus lineages.Journal of virology · 2025Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Hemagglutinins (HAs) are the receptor-binding and membrane fusion glycoproteins of influenza viruses. They recognize sialic acid-containing, cell-surface glycoconjugates as receptors but have limited affinity for them, and, as a consequence, virus attachment to cells requires their interaction with several virus HAs. Receptor-bound virus is transferred into endosomes where membrane fusion by HAs is activated at pH between 5 and 6.5, depending on the strain of virus. Fusion activity requires extensive rearrangements in HA conformation that include extrusion of a buried "fusion peptide" to connect with the endosomal membrane, form a bridge to the virus membrane, and eventually bring both membranes close together. In this review, we give an overview of the structures of the 16 genetically and antigenically distinct subtypes of influenza A HA in relation to these two functions in virus replication and in relation to recognition of HA by antibodies that neutralize infection.
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