ArticlePLoS pathogens2016
Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 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
69 citing papers in PubMed, 99 citations in OpenAlex.
- Towards broader-spectrum direct-acting antivirals against RNA viruses.Nature reviews. Microbiology · 2026Review
- Perspectives for pharmaceutical screening at XFEL sources using the example of Lassa virus endonuclease.Acta crystallographica. Section D, Structural biology · 2026Article
- Evaluation of new adjuvants in enhancing the immune response to a candidate of Severe Fever with Thrombocytopenia Syndrome Virus vaccine.bioRxiv : the preprint server for biology · 2026Article
- Article
- Article
- Comparison of the pathogenicity in type I interferon receptor deficient A129 mice and characterization of amino acid substitutions among severe fever with thrombocytopenia syndrome virus strains.The Journal of veterinary medical science · 2026Article
- Structures of the Crimean-Congo hemorrhagic fever virus RNA-dependent RNA polymerase.Cell discovery · 2026Article
- Review
- Inhibitors of the Machupo Virus L Endonuclease for Bolivian Hemorrhagic Fever Treatments.Microorganisms · 2026Article
- Structure and function of the nairovirus cap-snatching endonuclease.Nucleic acids research · 2026Article
- Pharmacophores of Influenza Virus PA Endonuclease Inhibitors.Advances in experimental medicine and biology · 2026Review
- Orthobunyavirus neurovirulence is a complex trait involving all three genome segments.bioRxiv : the preprint server for biology · 2025Article
- Article
- Structural characterization of the full-length Hantaan virus polymerase.PLoS pathogens · 2024Article
- Structural snapshots of phenuivirus cap-snatching and transcription.Nucleic acids research · 2024Article
- Article
- Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers.Nature communications · 2024Article
- Insight into the Hantaan virus RNA-dependent RNA polymerase inhibition using in-silico approaches.Molecular diversity · 2023Article
- The Arenaviridae Family: Knowledge Gaps, Animal Models, Countermeasures, and Prototype Pathogens.The Journal of infectious diseases · 2023Article
- Coronavirus 2'-O-methyltransferase: A promising therapeutic target.Virus research · 2023Review
9 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
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Segmented negative strand RNA viruses of the arena-, bunya- and orthomyxovirus families uniquely carry out viral mRNA transcription by the cap-snatching mechanism. This involves cleavage of host mRNAs close to their capped 5' end by an endonuclease (EN) domain located in the N-terminal region of the viral polymerase. We present the structure of the cap-snatching EN of Hantaan virus, a bunyavirus belonging to hantavirus genus. Hantaan EN has an active site configuration, including a metal co-ordinating histidine, and nuclease activity similar to the previously reported La Crosse virus and Influenza virus ENs (orthobunyavirus and orthomyxovirus respectively), but is more active in cleaving a double stranded RNA substrate. In contrast, Lassa arenavirus EN has only acidic metal co-ordinating residues. We present three high resolution structures of Lassa virus EN with different bound ion configurations and show in comparative biophysical and biochemical experiments with Hantaan, La Crosse and influenza ENs that the isolated Lassa EN is essentially inactive. The results are discussed in the light of EN activation mechanisms revealed by recent structures of full-length influenza virus polymerase.
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.