ArticleThe Journal of biological chemistry2014
The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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
53 citing papers in PubMed, 76 citations in OpenAlex.
- Roles of the M2 protein of influenza A virus.Virus genes · 2026Review
- Small molecule inhibition of the mitochondrial lipid transfer protein STARD7 attenuates influenza viral replication.PLoS pathogens · 2026Article
- Live-cell single-vRNP imaging identifies viral gene expression signatures that shape influenza infection heterogeneity.Cell systems · 2026Article
- Regulatory hotspot on the influenza A virus polymerase revealed through the structure of the NEP-polymerase complex.Science advances · 2026Article
- Involvement of a tick-borne orthomyxovirus matrix protein in vRNP nuclear export.Journal of virology · 2025Article
- Matrix protein 1 (M1) of influenza A virus: structural and functional insights.Emerging microbes & infections · 2025Review
- Host Protein Kinase C⍺: The novel Mitogen Activated Protein Kinase (MAPK) specific scaffold regulating nuclear export of influenza virus ribonucleoprotein complexes.PLoS pathogens · 2025Article
- Eukaryotic RNA binding protein hnRNPH1 suppresses influenza A virus replication through interaction with virus NS1 protein.Emerging microbes & infections · 2025Article
- Molecular patterns of matrix protein 1 (M1): A strong predictor of adaptive evolution in H9N2 avian influenza viruses.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Probing the functional constraints of influenza A virus NEP by deep mutational scanning.Cell reports · 2025Article
- Influenza A virus NS2 protein acts on vRNA-resident polymerase to drive the transcription to replication switch.Nucleic acids research · 2025Article
- Review
- The biology of the avian influenza virus: A comprehensive review with insights into novel therapeutic strategies.Open veterinary journal · 2025Review
- Inhibition of RAN attenuates influenza a virus replication and nucleoprotein nuclear export.Emerging microbes & infections · 2024Article
- Incompatible packaging signals and impaired protein functions hinder reassortment of bat H17N10 or H18N11 segment 7 with human H1N1 influenza A viruses.Journal of virology · 2024Article
- Review
- Unveiling the role of host kinases at different steps of influenza A virus life cycle.Journal of virology · 2024Review
- Fine Regulation of Influenza Virus RNA Transcription and Replication by Stoichiometric Changes in Viral NS1 and NS2 Proteins.Journal of virology · 2023Article
- Article
- Strategies of Influenza A Virus to Ensure the Translation of Viral mRNAs.Pathogens (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
In influenza A virus-infected cells, replication and transcription of the viral genome occurs in the nucleus. To be packaged into viral particles at the plasma membrane, encapsidated viral genomes must be exported from the nucleus. Intriguingly, the nuclear export protein (NEP) is involved in both processes. Although NEP stimulates viral RNA synthesis by binding to the viral polymerase, its function during nuclear export implicates interaction with viral ribonucleoprotein (vRNP)-associated M1. The observation that both interactions are mediated by the C-terminal moiety of NEP raised the question whether these two features of NEP are linked functionally. Here we provide evidence that the interaction between M1 and the vRNP depends on the NEP C terminus and its polymerase activity-enhancing property for the nuclear export of vRNPs. This suggests that these features of NEP are linked functionally. Furthermore, our data suggest that the N-terminal domain of NEP interferes with the stability of the vRNP-M1-NEP nuclear export complex, probably mediated by its highly flexible intramolecular interaction with the NEP C terminus. On the basis of our data, we propose a new model for the assembly of the nuclear export complex of Influenza A vRNPs.
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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.