ArticleNature communications2023
Structural landscape of the respiratory syncytial virus nucleocapsids.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Direct interaction between RSV polymerase L and active Rab11a mediates viral ribonucleoprotein transport to assembly sites.PLoS pathogens · 2026Article
- Structural insights into the Nipah virus nucleocapsid assembly.Communications biology · 2026Article
- Open and closed forms of assembled henipavirus nucleoprotein suggest structural basis of genome access.Science advances · 2026Article
- In vitro liquid-liquid phase separation induced by respiratory syncytial virus proteins and RNA.Science advances · 2026Article
- Structure and assembly of Borna disease virus 1 nucleoprotein-RNA complexes.Science advances · 2026Article
- Assembly of the Linear Viral Nucleocapsid.Microorganisms · 2026Article
- Article
- Compost Tea as a Natural Bioactive Solution: Unlocking the Antimicrobial and Antiviral Potential of Bell Pepper and Citrus Wastes.Environmental microbiology reports · 2026Article
- ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- In silico prediction, molecular docking and simulation of natural flavonoid apigenin and xanthoangelol E against human metapneumovirus.In silico pharmacology · 2026Article
- Construction and validation of a predictive model for severe pneumonia risk using respiratory pathogen nucleic acid Ct values combined with host immune biomarkers.American journal of translational research · 2025Article
- Single-Particle Electron Microscopy Analysis of Respiratory Syncytial Virus Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Introduction to Respiratory Syncytial Virus.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Assembly of respiratory syncytial virus matrix protein lattice and its coordination with fusion glycoprotein trimers.Nature communications · 2024Article
- The cryoEM structure of the Hendra henipavirus nucleoprotein reveals insights into paramyxoviral nucleocapsid architectures.Scientific reports · 2024Article
- From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y.Communications chemistry · 2024Article
- Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus.Nature communications · 2023Article
- Cryo-EM structure of the nucleocapsid-like assembly of respiratory syncytial virus.Signal transduction and targeted therapy · 2023Article
- Clinical Insights and Advancements in Human Metapneumovirus Management and Prognosis.Discoveries (Craiova, Romania)Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human Respiratory Syncytial Virus (HRSV) is a prevalent cause of severe respiratory infections in children and the elderly. The helical HRSV nucleocapsid is a template for the viral RNA synthesis and a scaffold for the virion assembly. This cryo-electron microscopy analysis reveals the non-canonical arrangement of the HRSV nucleocapsid helix, composed of 16 nucleoproteins per asymmetric unit, and the resulting systematic variations in the RNA accessibility. We demonstrate that this unique helical symmetry originates from longitudinal interactions by the C-terminal arm of the HRSV nucleoprotein. We explore the polymorphism of the nucleocapsid-like assemblies, report five structures of the full-length particles and two alternative arrangements formed by a C-terminally truncated nucleoprotein mutant, and demonstrate the functional importance of the identified longitudinal interfaces. We put all these findings in the context of the HRSV RNA synthesis machinery and delineate the structural basis for its further investigation.
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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.