ArticleJournal of virology2023
Sequence basis for selectivity of ephrin-B2 ligand for Eph receptors and pathogenic henipavirus G glycoproteins.
Article in Journal of virology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed, 5 citations in OpenAlex.
- Computational design of potent, broadly neutralizing anti-Nipah virus and Hendra virus miniproteins.bioRxiv : the preprint server for biology · 2026Article
- Slap restricts oncogenic Src-family kinase signaling to maintain colonic epithelial homeostasis.eLife · 2026Article
- Molecular prevalence, genomic characterization, and zoonotic potential of novel paramyxovirus and hepacivirus in Alexandromys fortis, Republic of Korea.Veterinary research · 2026Article
- Article
- Nipah and chandipura viruses: Emerging neurotropic zoonotic viruses in south asia - a comparative review.Molecular biology reports · 2026Review
- Engineered ACE2 decoy in dry powder form for inhalation: A novel therapy for SARS-CoV-2 variants.Molecular therapy. Methods & clinical development · 2025Article
- Structure-guided mutagenesis of Henipavirus receptor-binding proteins reveals molecular determinants of receptor usage and antibody-binding epitopes.Journal of virology · 2024Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
importanceEphrin-B2 (EFNB2) is a ligand for six Eph receptors in humans and regulates multiple cell developmental and signaling processes. It also functions as the cell entry receptor for Nipah virus and Hendra virus, zoonotic viruses that can cause respiratory and/or neurological symptoms in humans with high mortality. Here, we investigate the sequence basis of EFNB2 specificity for binding the Nipah virus attachment G glycoprotein over Eph receptors. We then use this information to engineer EFNB2 as a soluble decoy receptor that specifically binds the attachment glycoproteins of the Nipah virus and other related henipaviruses to neutralize infection. These findings further mechanistic understanding of protein selectivity and may facilitate the development of diagnostics or therapeutics against henipavirus infection.
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