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

Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus

5 Jul 2005

Abstract excerpt

Hendra virus (HeV) and Nipah virus (NiV) belong to the genus Henipavirus of the family Paramyxoviridae and are unique in that they exhibit a broad species tropism and cause fatal disease in both animals and humans. They infect cells through a pH-independent membrane fusion process mediated by their fusion and attachment glycoproteins. Previously, we demonstrated identical cell fusion tropisms for HeV and NiV and...

Read the complete abstract on PubMed

Topics

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

Share to Platelet Disorders and Treatments
Share to vaccines and immunoinformatics approaches
Share to Virology and Viral Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15998730
DOI: 10.1073/pnas.0504887102

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virusPMID 15998730Read ↗

Single Amino Acid Changes in the Nipah and Hendra Virus Attachment Glycoproteins Distinguish EphrinB2 from EphrinB3 UsageSemantic proximity Read ↗

EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirusSemantic proximity Read ↗

A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virusSemantic proximity Read ↗

A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virusSemantic proximity Read ↗

The Sequence Basis for Selectivity of Ephrin-B2 Ligand for Eph Receptors and Pathogenic Henipavirus G GlycoproteinsSemantic proximity Read ↗

Structure guided mutagenesis of Henipavirus Receptor Binding Proteins reveals molecular determinants of receptor usage and antibody binding epitopesSemantic proximity Read ↗

Dual microRNA Screens Reveal That the Immune-Responsive miR-181 Promotes Henipavirus Entry and Cell-Cell FusionSemantic proximity Read ↗

Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virusSemantic proximity Read ↗

Ephrin-B2 and ephrin-B3 as functional henipavirus receptorsSemantic proximity Read ↗

Functional studies of host-specific ephrin-B ligands as Henipavirus receptorsSemantic proximity Read ↗

Molecular recognition of human ephrinB2 cell surface receptor by an emergent African henipavirusSemantic proximity Read ↗

Functional Analysis of the Fusion and Attachment Glycoproteins of Mojiang HenipavirusSemantic proximity Read ↗

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