ArticleNature communications2023
Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus.
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 14 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Circular RNA-mediated regulation of key signaling pathways in cardiovascular diseases: a review.Journal of advanced research · 2026Review
- Differences in RNA Binding Between Segmented and Non-Segmented Negative-Strand Virus Nucleocapsids.Microorganisms · 2026Article
- Open and closed forms of assembled henipavirus nucleoprotein suggest structural basis of genome access.Science advances · 2026Article
- Avian Metapneumovirus: Virology, Epidemiology, and Insights from a Comparative Analysis with Human Metapneumovirus-A Review.Biomolecules · 2026Review
- Genetic and epidemiological characteristics of the spread of human metapneumovirus in Bulgaria, 2023-2025.Frontiers in public health · 2026Article
- In silico prediction, molecular docking and simulation of natural flavonoid apigenin and xanthoangelol E against human metapneumovirus.In silico pharmacology · 2026Article
- COCOMAPS 2.0: a web server for identifying, analyzing, and visualizing atomic interactions at the interface of biomolecular complexes.Bioinformatics (Oxford, England) · 2025Article
- Human metapneumovirus: pathogenesis, epidemiology, diagnostic technologies, and potential intervention strategies.Virology journal · 2025Review
- Human metapneumovirus: understanding the molecular mechanisms and pathology of infection.Journal of virology · 2025Review
- In silico drug repurposing targeting fusion and nucleoprotein of human metapneumovirus: A step toward pandemic preparedness.Indian journal of pharmacology · 2025Article
- Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.Protein & cell · 2025Article
- Recent advancements in the diverse roles of polymerase-associated proteins in the replication and pathogenesis of Newcastle disease virus.Veterinary research · 2025Review
- Cryo-EM structure of Nipah virus L-P polymerase complex.Nature communications · 2024Article
- The Phlebovirus Ribonucleoprotein: An Overview.Methods in molecular biology (Clifton, N.J.) · 2024Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Human metapneumovirus (HMPV) is a major cause of respiratory illness in young children. The HMPV polymerase (L) binds an obligate cofactor, the phosphoprotein (P). During replication and transcription, the L/P complex traverses the viral RNA genome, which is encapsidated within nucleoproteins (N). An essential interaction between N and a C-terminal region of P tethers the L/P polymerase to the template. This N-P interaction is also involved in the formation of cytoplasmic viral factories in infected cells, called inclusion bodies. To define how the polymerase component P recognizes N-encapsidated RNA (N-RNA) we employed cryogenic electron microscopy (cryo-EM) and molecular dynamics simulations, coupled to activity assays and imaging of inclusion bodies in cells. We report a 2.9 Å resolution structure of a triple-complex between multimeric N, bound to both RNA and the C-terminal region of P. Furthermore, we also present cryo-EM structures of assembled N in different oligomeric states, highlighting the plasticity of N. Combined with our functional assays, these structural data delineate in molecular detail how P attaches to N-RNA whilst retaining substantial conformational dynamics. Moreover, the N-RNA-P triple complex structure provides a molecular blueprint for the design of therapeutics to potentially disrupt the attachment of L/P to its template.
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Registered trials
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 Socratic graph.