ArticleThe FEBS journal2006
Crystal structures of Nipah and Hendra virus fusion core proteins.
Article in The FEBS journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Hyperfusogenic Mutations Destabilize the Postfusion Six-Helix Bundle of the Measles Virus Fusion Glycoprotein.Biochemistry · 2026Article
- FromImmune network · 2026Review
- Hendra virus: research progress on a bat-borne threat lurking at the human-animal interface.Frontiers in veterinary science · 2026Review
- Structural Studies of Henipavirus Glycoproteins.Viruses · 2024Review
- A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential.Nature communications · 2024Article
- Structure and antigenicity of divergent Henipavirus fusion glycoproteins.Nature communications · 2023Article
- Heptad stereotypy, S/Q layering, and remote origin of the SARS-CoV-2 fusion core.Virus evolution · 2022Article
- Antivirals targeting paramyxovirus membrane fusion.Current opinion in virology · 2021Review
- EphrinB2 clustering by Nipah virus G is required to activate and trap F intermediates at supported lipid bilayer-cell interfaces.Science advances · 2021Article
- Differential Features of Fusion Activation within theViruses · 2020Review
- Phylogeography, Transmission, and Viral Proteins of Nipah Virus.Virologica Sinica · 2018Review
- Malaria parasite CelTOS targets the inner leaflet of cell membranes for pore-dependent disruption.eLife · 2016Article
- Paramyxovirus Glycoproteins and the Membrane Fusion Process.Current clinical microbiology reports · 2016Article
- Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.PLoS pathogens · 2013Article
- Review
- Modes of paramyxovirus fusion: a Henipavirus perspective.Trends in microbiology · 2011Review
- Cells under siege: viral glycoprotein interactions at the cell surface.Journal of structural biology · 2011Review
- Hendra and nipah infection: pathology, models and potential therapies.Infectious disorders drug targets · 2011Review
- Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus.The Journal of biological chemistry · 2011Article
- Inhibition of Nipah virus infection in vivo: targeting an early stage of paramyxovirus fusion activation during viral entry.PLoS pathogens · 2010Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Nipah and Hendra viruses are highly pathogenic paramyxoviruses that recently emerged from flying foxes to cause serious disease outbreaks in humans and livestock in Australia, Malaysia, Singapore and Bangladesh. Their unique genetic constitution, high virulence and wide host range set them apart from other paramyxoviruses. These characteristics have led to their classification into the new genus Henpavirus within the family Paramyxoviridae and to their designation as Biosafety Level 4 pathogens. The fusion protein, an enveloped glycoprotein essential for viral entry, belongs to the family of class I fusion proteins and is characterized by the presence of two heptad repeat (HR) regions, HR1 and HR2. These two regions associate to form a fusion-active hairpin conformation that juxtaposes the viral and cellular membranes to facilitate membrane fusion and enable subsequent viral entry. The Hendra and Nipah virus fusion core proteins were crystallized and their structures determined to 2.2 A resolution. The Nipah and Hendra fusion core structures are six-helix bundles with three HR2 helices packed against the hydrophobic grooves on the surface of a central coiled coil formed by three parallel HR1 helices in an oblique antiparallel manner. Because of the high level of conservation in core regions, it is proposed that the Nipah and Hendra virus fusion cores can provide a model for membrane fusion in all paramyxoviruses. The relatively deep grooves on the surface of the central coiled coil represent a good target site for drug discovery strategies aimed at inhibiting viral entry by blocking hairpin formation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.