ArticleJournal of virology2013
Configuration of viral ribonucleoprotein complexes within the influenza A virion.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 52 citations in OpenAlex.
- Influenza A virus circumvents the innate immune response through the sequestration of double-stranded RNA.Journal of virology · 2025Article
- Concentration-dependent formation of intersegment interactions in the viral inclusions of influenza A virus infected cells.iScience · 2025Article
- High-throughput single-virion DNA-PAINT reveals structural diversity, cooperativity, and flexibility during selective packaging in influenza.Nucleic acids research · 2025Article
- Purification and Ultramicroscopic Observation of the Influenza A Virus Ribonucleoprotein Complex.Methods in molecular biology (Clifton, N.J.) · 2025Article
- ViPal: A framework for virulence prediction of influenza viruses with prior viral knowledge using genomic sequences.Journal of biomedical informatics · 2023Article
- Article
- Role of VP30 Phosphorylation in Ebola Virus Nucleocapsid Assembly and Transport.Journal of virology · 2022Article
- Inferring Protein Function in an Emerging Virus: Detection of the Nucleoprotein in Tilapia Lake Virus.Journal of virology · 2022Article
- Ultrastructure of influenza virus ribonucleoprotein complexes during viral RNA synthesis.Communications biology · 2021Article
- Review
- Selective Genome Packaging Mechanisms of Influenza A Viruses.Cold Spring Harbor perspectives in medicine · 2021Review
- Host factor Rab11a is critical for efficient assembly of influenza A virus genomic segments.PLoS pathogens · 2021Article
- RNA Secondary Structure as a First Step for Rational Design of the Oligonucleotides towards Inhibition of Influenza A Virus Replication.Pathogens (Basel, Switzerland) · 2020Review
- The parts are greater than the whole: the role of semi-infectious particles in influenza A virus biology.Current opinion in virology · 2018Review
- Influenza A virus nucleoprotein is acetylated by histone acetyltransferases PCAF and GCN5.The Journal of biological chemistry · 2018Article
- Importance of the 1+7 configuration of ribonucleoprotein complexes for influenza A virus genome packaging.Nature communications · 2018Article
- A Comprehensive Review on the Interaction Between the Host GTPase Rab11 and Influenza A Virus.Frontiers in cell and developmental biology · 2018Review
- Influenza virus genome reaches the plasma membrane via a modified endoplasmic reticulum and Rab11-dependent vesicles.Nature communications · 2017Article
- Structural studies of influenza virus RNPs by electron microscopy indicate molecular contortions within NP supra-structures.Journal of structural biology · 2017Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The influenza A virus possesses an eight-segmented, negative-sense, single-stranded RNA genome (vRNA). Each vRNA segment binds to multiple copies of viral nucleoproteins and a small number of heterotrimeric polymerase complexes to form a rod-like ribonucleoprotein complex (RNP), which is essential for the transcription and replication of the vRNAs. However, how the RNPs are organized within the progeny virion is not fully understood. Here, by focusing on polymerase complexes, we analyzed the fine structure of purified RNPs and their configuration within virions by using various electron microscopies (EM). We confirmed that the individual RNPs possess a single polymerase complex at one end of the rod-like structure and that, as determined using immune EM, some RNPs are incorporated into budding virions with their polymerase-binding ends at the budding tip, whereas others align with their polymerase-binding ends at the bottom of the virion. These data further our understanding of influenza virus virion morphogenesis.
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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.