Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.

Nature structural & molecular biology - 1 Mar 2013

Xu Rui, Krause Jens C, McBride Ryan, Paulson James C, Crowe James E, Wilson Ian A

Abstract excerpt

Influenza virus hemagglutinin (HA) mediates receptor binding and viral entry during influenza infection. The development of receptor analogs as viral-entry blockers has not been successful, which suggests that sialic acid may not be an ideal scaffold to obtain broad, potent HA inhibitors. Here, w...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antibodies, Neutralizing
Share to Antibodies, Viral
Share to Antigen-Antibody Complex

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epitopes

Share to Hemagglutinin Glycoproteins, Influenza Virus

Share to Immunoglobulin Fab Fragments

Share to Tryptophan

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 23396351
DOI: 10.1038/nsmb.2500
PMCID: PMC3594569

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23396351-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.PMID 23396351Read ↗

Antibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding SiteSemantic proximity Read ↗

Identification of a cross-neutralizing antibody that targets the receptor binding site of H1N1 and H5N1 influenza virusesSemantic proximity Read ↗

A Broadly Neutralizing Human Monoclonal Antibody That Recognizes a Conserved, Novel Epitope on the Globular Head of the Influenza H1N1 Virus HemagglutininSemantic proximity Read ↗

Structural Insight into a Human Neutralizing Antibody against Influenza Virus H7N9.Semantic proximity Read ↗

Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin.Semantic proximity Read ↗

Antibody 27F3 Broadly Targets Influenza A Group 1 and 2 Hemagglutinins through a Further Variation in VH1-69 Antibody Orientation on the HA Stem.Semantic proximity Read ↗

Immunization by avian H5 influenza hemagglutinin mutants with altered receptor binding specificity.Semantic proximity Read ↗

Complementary recognition of the receptor-binding site of highly pathogenic H5N1 influenza viruses by two human neutralizing antibodiesSemantic proximity Read ↗

A highly conserved neutralizing epitope on group 2 influenza A viruses.Semantic proximity Read ↗

The structural variability of the influenza A hemagglutinin receptor-binding site.Semantic proximity Read ↗

Structural basis of broad protection against influenza virus by human antibodies targeting the neuraminidase active site via a recurring motif in CDR H3Semantic proximity Read ↗

Structural characterisation of hemagglutinin from seven Influenza A H1N1 strains reveal diversity in the C05 antibody recognition siteSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.