ReviewCold Spring Harbor perspectives in medicine2021
Structure and Function of Influenza Polymerase.
Review in Cold Spring Harbor perspectives in medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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
55 citing papers in PubMed, 87 citations in OpenAlex.
- The mouse-lethal H5N1 influenza virus carrying the PB2-384L/443R/460M characteristics acquired in avian hosts can effectively utilize human ANP32A/B proteins.Emerging microbes & infections · 2026Article
- Nucleocapsid-like cryo-EM structure of influenza B virus.PLoS pathogens · 2026Article
- Genetic Determinants Analysis of PB1 and PB2 Genes in H5N1 Avian Influenza Strains from Romania.Pathogens (Basel, Switzerland) · 2026Article
- A Structural View of Influenza Virus Ribonucleoprotein Complex and Its Functions.Microorganisms · 2026Review
- Cellular hnRNP D promotes influenza A virus replication by inhibiting TBK1-IRF3-mediated innate immune response.Journal of virology · 2026Article
- Streamlined Synthesis and Structure-Activity Relationship Analysis of 2-Amidothiophene-3-Carboxamides Targeting Influenza Polymerase PA-PB1 Heterodimerization.ChemMedChem · 2026Article
- Historical Pandemic and Contemporary Influenza A Viruses Reveal PB2 M631L as a Convergent Adaptation to Human ANP32.Microorganisms · 2026Article
- Anti-influenza drugs targeting trimeric RNA polymerase complex: From development to clinics.Acta pharmaceutica Sinica. B · 2026Review
- Regulatory hotspot on the influenza A virus polymerase revealed through the structure of the NEP-polymerase complex.Science advances · 2026Article
- Computational Structural Analysis Predicts Host-Range Promiscuity and Antiviral Resistance in North American H5N1 Lineages.Computational and structural biotechnology journal · 2026Article
- PB1 mutations as key drivers of influenza A virus evolution.Frontiers in microbiology · 2026Review
- Cryo-EM structure of influenza polymerase bound to the cRNA promoter provides insights into the mechanism of viral replication.Communications biology · 2025Article
- Live-attenuated influenza virus vaccine strain with an engineered temperature-sensitive and genetically stable viral polymerase variant.Journal of virology · 2025Article
- Live-attenuated influenza virus vaccine strain with an engineered temperature-sensitive and genetically stable viral polymerase variant.Journal of virology · 2025Article
- Visualizing influenza A virus assembly by in situ cryo-electron tomography.Nature communications · 2025Article
- Influenza A virus circumvents the innate immune response through the sequestration of double-stranded RNA.Journal of virology · 2025Article
- H5N1 2.3.4.4b: a review of mammalian adaptations and risk of pandemic emergence.The Journal of general virology · 2025Review
- Molecular basis of influenza ribonucleoprotein complex assembly and processive RNA synthesis.Science (New York, N.Y.) · 2025Article
- Article
- An evolutionarily unique viral RdRP suggests a common dual-function feature of the priming element.Science advances · 2025Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza polymerase (FluPol) plays a key role in the viral infection cycle by transcribing and replicating the viral genome. FluPol is a multifunctional, heterotrimeric enzyme with cap-binding, endonuclease, RNA-dependent RNA polymerase and polyadenylation activities. It performs its functions in the context of the viral ribonucleoprotein particle (RNP), wherein the template viral RNA is coated by multiple copies of viral nucleoprotein. Moreover, it interacts with a number of host proteins that are essential cofactors and, consequently, adaptive mutations in the polymerase are required for crossing the avian-human species barrier. In this review, we show how mechanistic understanding of how FluPol performs its multiple functions has greatly advanced over the last decade through determination of high-resolution structures by X-ray crystallography and cryo-electron microscopy. These have revealed not only the detailed architecture of FluPol but highlighted the remarkably conformational flexibility that is inherent to its functioning as a dynamic RNA synthesis machine. Structural studies are also underpinning current attempts to develop next-generation anti-influenza drugs that directly target FluPol.
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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.