ArticleNature communications2020
Cryo-EM structure of the respiratory syncytial virus RNA polymerase.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
What it found
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Who cites it
80 citing papers in PubMed, 109 citations in OpenAlex.
- Unreacted RSV Polymerase Structures Expand the Post-Translocation Landscape of the Nucleotide Addition Cycle.Microorganisms · 2026Article
- Direct interaction between RSV polymerase L and active Rab11a mediates viral ribonucleoprotein transport to assembly sites.PLoS pathogens · 2026Article
- Targeting the RSV and hMPV L Protein: Cryo-EM and Structure-Based Approaches to Antiviral Drug Discovery.Biomolecules · 2026Review
- Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.Microorganisms · 2026Review
- In vitro liquid-liquid phase separation induced by respiratory syncytial virus proteins and RNA.Science advances · 2026Article
- Orchestrated and dynamic nucleotide addition cycle during respiratory syncytial virus early-stage elongation.Nature communications · 2026Article
- Article
- Structural Mapping of Surveillance Data Reveals Conservation of NNI Binding Site in RSV L Protein.Pathogens (Basel, Switzerland) · 2026Article
- Mumps Virus: Replication, Immune Response, and the Changing Landscape of Vaccine Effectiveness.Pathogens (Basel, Switzerland) · 2026Review
- RSV vaccine development: advances and fusion protein-focused strategies.Frontiers in immunology · 2026Review
- The S190R mutation in RSV-A F protein impairs nirsevimab binding and neutralization capacity.Virus evolution · 2026Article
- The structure of the mammalian bornavirus polymerase complex.Nature communications · 2025Article
- Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.Protein & cell · 2025Article
- Discovery of a non-nucleoside inhibitor that binds to a novel site in the palm domain of the respiratory syncytial virus RNA-dependent RNA polymerase.Journal of virology · 2025Article
- Cryo-EM structures of Nipah virus polymerases and high-throughput RdRp assay development enable anti-NiV drug discovery.Nature communications · 2025Article
- Review
- Structure of the measles virus ternary polymerase complex.Nature communications · 2025Article
- Functional dissection of the C-terminal domain of rabies virus RNA polymerase L protein.Journal of virology · 2025Article
- Advances in development of antiviral strategies against respiratory syncytial virus.Acta pharmaceutica Sinica. B · 2025Review
- Structural insights into the RNA-dependent RNA polymerase complexes from highly pathogenic Marburg and Ebola viruses.Nature communications · 2025Article
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 1 institution in 1 country.
Funding
Abstract
The respiratory syncytial virus (RSV) RNA polymerase, constituted of a 250 kDa large (L) protein and tetrameric phosphoprotein (P), catalyzes three distinct enzymatic activities - nucleotide polymerization, cap addition, and cap methylation. How RSV L and P coordinate these activities is poorly understood. Here, we present a 3.67 Å cryo-EM structure of the RSV polymerase (L:P) complex. The structure reveals that the RNA dependent RNA polymerase (RdRp) and capping (Cap) domains of L interact with the oligomerization domain (P
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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.