ArticleScience (New York, N.Y.)2025
Molecular basis of influenza ribonucleoprotein complex assembly and processive RNA synthesis.
Article in Science (New York, N.Y.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
18 citing papers in PubMed.
- Nucleocapsid-like cryo-EM structure of influenza B virus.PLoS pathogens · 2026Article
- A Structural View of Influenza Virus Ribonucleoprotein Complex and Its Functions.Microorganisms · 2026Review
- UsingbioRxiv : the preprint server for biology · 2026Article
- Differences in RNA Binding Between Segmented and Non-Segmented Negative-Strand Virus Nucleocapsids.Microorganisms · 2026Article
- Structure and assembly of Borna disease virus 1 nucleoprotein-RNA complexes.Science advances · 2026Article
- Assembly of the Linear Viral Nucleocapsid.Microorganisms · 2026Article
- Molecular architecture of Influenza A virions.bioRxiv : the preprint server for biology · 2026Article
- Secondary analysis of influenza a virus-infected cells at single-cell resolution reveals host BANF1 response to individual and combinations of detected segments.Virology journal · 2026Article
- Polymerase trapping as the mechanism of H5 highly pathogenic avian influenza virus genesis.Science (New York, N.Y.) · 2026Article
- Enolase 1 suppresses influenza A virus replication by blocking the nuclear import of the viral ribonucleoprotein complex.Cellular and molecular life sciences : CMLS · 2026Article
- Anti-influenza drugs targeting trimeric RNA polymerase complex: From development to clinics.Acta pharmaceutica Sinica. B · 2026Review
- Resolving structural heterogeneity in situ through cryogenic electron tomography.Current opinion in structural biology · 2026Review
- Febrile temperature activates the innate immune response by promoting aberrant influenza A virus RNA synthesis.Science advances · 2026Article
- PB1 mutations as key drivers of influenza A virus evolution.Frontiers in microbiology · 2026Review
- Decoding helical dynamics in viral replication: Cryo-EM unveils conserved assembly mechanisms and broad-spectrum antiviral targets.Acta pharmaceutica Sinica. B · 2025Article
- Coupling of polymerase-nucleoprotein-RNA in an influenza virus mini ribonucleoprotein complex.Nature communications · 2025Article
- Identifying a Marine-Derived Small-Molecule Nucleoprotein Inhibitor Against Influenza A Virus.Marine drugs · 2025Article
- Febrile temperature activates the innate immune response by promoting aberrant influenza A virus RNA synthesis.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
Influenza viruses replicate and transcribe their genome in the context of a conserved ribonucleoprotein (RNP) complex. By integrating cryo-electron microscopy single-particle analysis and cryo-electron tomography, we define the influenza RNP as a right-handed, antiparallel double helix with the viral RNA encapsidated in the minor groove. Individual nucleoprotein subunits are connected by a flexible tail loop that inserts into a conserved pocket in its neighbor. We visualize the viral polymerase in RNP at different functional states, revealing how it accesses the RNA template while maintaining the double-helical architecture of RNP by strand sliding. Targeting the tail loop binding interface, we identify lead compounds as potential anti-influenza inhibitors. These findings elucidate the molecular determinants underpinning influenza virus replication and highlight a promising target for antiviral development.
Indexed as
Identifiers
What OpenQuestion holds
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.