ArticleNature2010
Cap binding and immune evasion revealed by Lassa nucleoprotein structure.
Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 184 papers, 1 of them a synthesis that pooled it.
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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Who cites it
184 citing papers in PubMed, 1 synthesis or guideline pooled it, 262 citations in OpenAlex.
- Ribavirin for treating Lassa fever: A systematic review of pre-clinical studies and implications for human dosing.PLoS neglected tropical diseases · 2022Pooled it
- Akabane virus reprograms the PKR‑eIF2α‑SGs/PBs axis to fine-tune cap-snatching efficiency.Virulence · 2026Article
- Lassa Virus-A Persistent and Evolving Threat.Microorganisms · 2026Review
- Distinct modes of RNA degradation by the structurally related coronavirus and arenavirus exoribonucleases.Journal of virology · 2026Article
- Selective targeting of human TREX1 exonuclease by small molecule inhibitors is mediated by a conformational switch.NAR molecular medicine · 2026Article
- Lassa and Mopeia viruses produce different RIG-I-activating RNA in the absence of a functional viral exoribonuclease domain.Journal of virology · 2026Article
- Molecular characterization of arenavirus defective viral genomes reveals sequence features associated with their formation.Journal of virology · 2026Article
- Inhibitory effects of molnupiravir on Crimean-Congo hemorrhagic fever virus polymerase.NAR molecular medicine · 2026Article
- Article
- In-silico investigations of bioactive compounds from ginger against Lassa fever virus nucleoprotein.Scientific reports · 2025Article
- In-silico screening of small compounds against Lassa fever haemorrhagic virus nucleoprotein.Scientific reports · 2025Article
- Lassa virus protein-protein interactions as mediators of Lassa fever pathogenesis.Virology journal · 2025Review
- Article
- Architectural organization andJournal of virology · 2024Article
- High-Affinity-Mediated Viral Entry Triggers Innate Affinity Escape Resulting in Type I IFN Resistance and Impaired T Cell Immunity.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Alternative translation contributes to the generation of a cytoplasmic subpopulation of the Junín virus nucleoprotein that inhibits caspase activation and innate immunity.Journal of virology · 2024Article
- The Phlebovirus Ribonucleoprotein: An Overview.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Lassa virus NP DEDDh 3'-5' exoribonuclease activity is required for optimal viral RNA replication and mutation control.bioRxiv : the preprint server for biology · 2023Article
- RNA to Rule Them All: Critical Steps in Lassa Virus Ribonucleoparticle Assembly and Recruitment.Journal of the American Chemical Society · 2023Article
- The Arenaviridae Family: Knowledge Gaps, Animal Models, Countermeasures, and Prototype Pathogens.The Journal of infectious diseases · 2023Article
124 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Lassa virus, the causative agent of Lassa fever, causes thousands of deaths annually and is a biological threat agent, for which there is no vaccine and limited therapy. The nucleoprotein (NP) of Lassa virus has essential roles in viral RNA synthesis and immune suppression, the molecular mechanisms of which are poorly understood. Here we report the crystal structure of Lassa virus NP at 1.80 Å resolution, which reveals amino (N)- and carboxy (C)-terminal domains with structures unlike any of the reported viral NPs. The N domain folds into a novel structure with a deep cavity for binding the m7GpppN cap structure that is required for viral RNA transcription, whereas the C domain contains 3'-5' exoribonuclease activity involved in suppressing interferon induction. To our knowledge this is the first X-ray crystal structure solved for an arenaviral NP, which reveals its unexpected functions and indicates unique mechanisms in cap binding and immune evasion. These findings provide great potential for vaccine and drug development.
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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.