ArticleNature communications2018
Promotion of virus assembly and organization by the measles virus matrix protein.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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.
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Who cites it
42 citing papers in PubMed, 119 citations in OpenAlex.
- Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.Nature communications · 2026Article
- Nipah virus matrix protein uses cortical actin to stabilize the virus assembly sites and promote budding.Science advances · 2025Article
- The measles virus matrix F50S mutation from a lethal case of subacute sclerosing panencephalitis promotes receptor-independent neuronal spread.Journal of virology · 2025Article
- The nanoscale organization of the Nipah virus fusion protein informs new membrane fusion mechanisms.eLife · 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
- Prevention and Potential Treatment Strategies for Respiratory Syncytial Virus.Molecules (Basel, Switzerland) · 2024Review
- Methyltransferase K-D-K-E motif influences the intercellular transmission of Newcastle disease virus.Virulence · 2023Article
- Cryo-electron tomography to study viral infection.Biochemical Society transactions · 2023Review
- Article
- Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms.Science advances · 2023Article
- In Situ Imaging of Virus-Infected Cells by Cryo-Electron Tomography: An Overview.Sub-cellular biochemistry · 2023Review
- Atomic model of vesicular stomatitis virus and mechanism of assembly.Nature communications · 2022Article
- Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization.Science advances · 2022Article
- Three-dimensional insights into human enveloped viruses in vitro and in situ.Biochemical Society transactions · 2022Review
- Ubiquitination on Lysine 247 of Newcastle Disease Virus Matrix Protein Enhances Viral Replication and Virulence by Driving Nuclear-Cytoplasmic Trafficking.Journal of virology · 2022Article
- Entropy-regularized deconvolution of cellular cryotransmission electron tomograms.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- The Nucleocapsid of Paramyxoviruses: Structure and Function of an Encapsidated Template.Viruses · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Measles virus (MeV) remains a major human pathogen, but there are presently no licensed antivirals to treat MeV or other paramyxoviruses. Here, we use cryo-electron tomography (cryo-ET) to elucidate the principles governing paramyxovirus assembly in MeV-infected human cells. The three-dimensional (3D) arrangement of the MeV structural proteins including the surface glycoproteins (F and H), matrix protein (M), and the ribonucleoprotein complex (RNP) are characterized at stages of virus assembly and budding, and in released virus particles. The M protein is observed as an organized two-dimensional (2D) paracrystalline array associated with the membrane. A two-layered F-M lattice is revealed suggesting that interactions between F and M may coordinate processes essential for MeV assembly. The RNP complex remains associated with and in close proximity to the M lattice. In this model, the M lattice facilitates the well-ordered incorporation and concentration of the surface glycoproteins and the RNP at sites of virus assembly.
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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 OpenQuestion graph.