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

Structure of the measles virus H glycoprotein sheds light on an efficient vaccine.

Proceedings of the National Academy of Sciences of the United States of America - 26 Dec 2007

Ruigrok Rob W H, Gerlier Denis

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Antiviral Agents
Share to Carbohydrates
Share to Crystallography, X-Ray
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Design

Share to Measles Vaccine

Share to Receptors, Virus

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 18087048
DOI: 10.1073/pnas.0709995105
PMCID: PMC2409202

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of the measles virus H glycoprotein sheds light on an efficient vaccine.PMID 18087048Read ↗

Functional and Structural Characterization of Neutralizing Epitopes of Measles Virus Hemagglutinin ProteinSemantic proximity Read ↗

Stabilized Full-Length Measles Fusion Protein Elicits Potent Immunity and Protection In VivoSemantic proximity Read ↗

Molecular Characterization of Epitopes on the Measles Virus Hemagglutinin ProteinSemantic proximity Read ↗

A basis for vaccine development: Comparative characterization of Haemophilus influenzae outer membrane vesiclesSemantic proximity Read ↗

Identification of two amino acids in the hemagglutinin glycoprotein of measles virus (MV) that govern hemadsorption, HeLa cell fusion, and CD46 downregulation: phenotypic markers that differentiate vaccine and wild-type MV strains.Semantic proximity Read ↗

Measles Virus Fusion Protein: Structure, Function and InhibitionSemantic proximity Read ↗

In Vivo Efficacy of Measles Virus Fusion Protein-Derived Peptides Is Modulated by the Properties of Self-Assembly and Membrane ResidenceSemantic proximity Read ↗

Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk.Semantic proximity Read ↗

Structure-based design of chimeric antigens for multivalent protein vaccinesSemantic proximity Read ↗

Epitope dampening monotypic measles virus hemagglutinin glycoprotein results in resistance to cocktail of monoclonal antibodies.Semantic proximity Read ↗

A Stabilized Headless Measles Virus Attachment Protein Stalk Efficiently Triggers Membrane FusionSemantic proximity Read ↗

Structure of the measles virus hemagglutinin bound to the CD46 receptorSemantic proximity Read ↗

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