ArticleNature communications2024
Cryo-EM structure of Nipah virus L-P polymerase complex.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed.
- Nipah virus in the era of global connectivity: molecular evolution, transmission risk, and preparedness strategies.Virus genes · 2026Review
- Nipah Virus: A Neurotropic Zoonosis-From Molecular Biology to Clinical Manifestations and Translational Advances.Viruses · 2026Review
- Machine learning-driven drug repurposing and computational validation for Nipah virus.Molecular diversity · 2026Article
- Unreacted RSV Polymerase Structures Expand the Post-Translocation Landscape of the Nucleotide Addition Cycle.Microorganisms · 2026Article
- mRNA cap formation by the human respiratory syncytial virus large protein.Nucleic acids research · 2026Article
- Targeting the RSV and hMPV L Protein: Cryo-EM and Structure-Based Approaches to Antiviral Drug Discovery.Biomolecules · 2026Review
- Structural basis for RNA synthesis and inhibition of the orthobunyavirus polymerase.Nature communications · 2026Article
- Small Molecule Inhibition of Mononegavirales RNA Polymerases.Journal of medical virology · 2026Review
- Orchestrated and dynamic nucleotide addition cycle during respiratory syncytial virus early-stage elongation.Nature communications · 2026Article
- Assembly of the Linear Viral Nucleocapsid.Microorganisms · 2026Article
- Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.Protein & cell · 2025Article
- Cryo-EM structures of Nipah virus polymerases and high-throughput RdRp assay development enable anti-NiV drug discovery.Nature communications · 2025Article
- Construction of Minigenome Replicon of Nipah Virus and Investigation of Biological Activity.Viruses · 2025Article
- A deep learning and molecular modeling approach to repurposing Cangrelor as a potential inhibitor of Nipah virus.Scientific reports · 2025Article
- Structure of the measles virus ternary polymerase complex.Nature communications · 2025Article
- Structural basis of Nipah virus RNA synthesis.Nature communications · 2025Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Nipah virus (NiV) is a non-segmented, negative-strand (NNS) RNA virus, belonging to Paramyxoviridae. The RNA polymerase complex, composed of large (L) protein and tetrameric phosphoprotein (P), is responsible for genome transcription and replication by catalyzing NTP polymerization, mRNA capping and cap methylation. Here, we determine the cryo-electron microscopy (cryo-EM) structure of fully bioactive NiV L-P polymerase complex at a resolution of 3.19 Å. The L-P complex displays a conserved architecture like other NNS RNA virus polymerases and L interacts with the oligomerization domain and the extreme C-terminus region of P tetramer. Moreover, we elucidate that NiV is naturally resistant to the allosteric L-targeting inhibitor GHP-88309 due to the conformational change in the drug binding site. We also find that the non-nucleotide drug suramin can inhibit the NiV L-P polymerase activity at both the enzymatic and cellular levels. Our findings have greatly enhanced the molecular understanding of NiV genome replication and transcription and provided the rationale for broad-spectrum polymerase-targeted drug design.
Indexed as
Identifiers
What Socratic 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 Socratic graph.