ArticleJournal of virology2021
Tetramerization of Phosphoprotein is Essential for Respiratory Syncytial Virus Budding while its N Terminal Region Mediates Direct Interactions with the Matrix Protein.
Article in Journal of virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Reduced expression of human metapneumovirus matrix protein impacts virus assembly and ribonucleoprotein localization.Journal of virology · 2026Article
- A comprehensive look at Respiratory Syncytial Virus (RSV): from pathogenesis to prevention.Tropical diseases, travel medicine and vaccines · 2026Review
- In vitro liquid-liquid phase separation induced by respiratory syncytial virus proteins and RNA.Science advances · 2026Article
- Epidemiological characteristics and whole-genome analysis of respiratory syncytial virus in Jining city from February 2023 to December 2024.Frontiers in microbiology · 2026Article
- Human metapneumovirus: understanding the molecular mechanisms and pathology of infection.Journal of virology · 2025Review
- Exploring Therapeutic Targets From Spreading Patterns Against Respiratory Syncytial Virus.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Review
- Antagonism of BST2/Tetherin, a new restriction factor of respiratory syncytial virus, requires the viral NS1 protein.PLoS pathogens · 2024Article
- Assembly of respiratory syncytial virus matrix protein lattice and its coordination with fusion glycoprotein trimers.Nature communications · 2024Article
- Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus.Nature communications · 2023Article
- Virus-Like Particles Assembled Using Respiratory Syncytial Virus Matrix Protein Elicit Protective Immunity in Mice.Infection and drug resistance · 2023Article
- Respiratory syncytial virus ribonucleoproteins hijack microtubule Rab11 dependent transport for intracellular trafficking.PLoS pathogens · 2022Article
- Review
- A Structural and Dynamic Analysis of the Partially Disordered Polymerase-Binding Domain in RSV Phosphoprotein.Biomolecules · 2021Article
- Tetramerization of Phosphoprotein is Essential for Respiratory Syncytial Virus Budding while its N Terminal Region Mediates Direct Interactions with the Matrix Protein.Journal of virology · 2021Article
- Clinical Insights and Advancements in Human Metapneumovirus Management and Prognosis.Discoveries (Craiova, Romania)Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It was shown previously that the Matrix (M), Phosphoprotein (P), and the Fusion (F) proteins of Respiratory syncytial virus (RSV) are sufficient to produce virus-like particles (VLPs) that resemble the RSV infection-induced virions. However, the exact mechanism and interactions among the three proteins are not known. This work examines the interaction between P and M during RSV assembly and budding. We show that M interacts with P in the absence of other viral proteins in cells using a Split Nano Luciferase assay. By using recombinant proteins, we demonstrate a direct interaction between M and P. By using Nuclear Magnetic Resonance (NMR) we identify three novel M interaction sites on P, namely site I in the α
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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.