ArticleeLife2017
Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments.
Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 34 citations in OpenAlex.
- Live-cell 3D-SIM of Rift Valley fever virus NSs filaments reveals a polygon web architecture.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Rift Valley fever virus activates multiple cell death pathways in neurons.Journal of virology · 2026Article
- Oropouche virus NSs protein suppresses host transcription by targeting the RNA polymerase II RPB1 protein.Journal of virology · 2025Article
- Review
- Kaposi's sarcoma-associated herpesvirus ORF61 protein sequesters APOBEC3B in filamentous aggregates.Journal of virology · 2025Article
- Review
- Alphavirus nsP3 organizes into tubular scaffolds essential for infection and the cytoplasmic granule architecture.Nature communications · 2024Article
- Suppression of Interferon Response and Antiviral Strategies of Bunyaviruses.Tropical medicine and infectious disease · 2024Review
- Cell-Free Synthesis of Bunyavirales Proteins in View of Their Structural Characterization by Nuclear Magnetic Resonance.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Development and Validation of Rapid Colorimetric Reverse Transcription Loop-Mediated Isothermal Amplification for Detection of Rift Valley Fever Virus.Advances in virology · 2023Article
- Viral evasion of the integrated stress response through antagonism of eIF2-P binding to eIF2B.Nature communications · 2021Article
- eIF2B-capturing viral protein NSs suppresses the integrated stress response.Nature communications · 2021Article
- The Change P82L in the Rift Valley Fever Virus NSs Protein Confers Attenuation in Mice.Viruses · 2021Article
- NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice.Nature communications · 2020Article
- Nuclear pore protein Nup98 is involved in replication of Rift Valley fever virus and nuclear import of virulence factor NSs.The Journal of general virology · 2020Article
- ULK1/2 Restricts the Formation of Inducible SINT-Speckles, Membraneless Organelles Controlling the Threshold of TBK1 Activation.iScience · 2019Article
- Article
- Structural and functional similarities in bunyaviruses: Perspectives for pan-bunya antivirals.Reviews in medical virology · 2019Review
- BASILIScan: a tool for high-throughput analysis of intrinsic disorder patterns in homologous proteins.BMC genomics · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Rift Valley fever phlebovirus (RVFV) is a clinically and economically important pathogen increasingly likely to cause widespread epidemics. RVFV virulence depends on the interferon antagonist non-structural protein (NSs), which remains poorly characterized. We identified a stable core domain of RVFV NSs (residues 83-248), and solved its crystal structure, a novel all-helical fold organized into highly ordered fibrils. A hallmark of RVFV pathology is NSs filament formation in infected cell nuclei. Recombinant virus encoding the NSs core domain induced intranuclear filaments, suggesting it contains all essential determinants for nuclear translocation and filament formation. Mutations of key crystal fibril interface residues in viruses encoding full-length NSs completely abrogated intranuclear filament formation in infected cells. We propose the fibrillar arrangement of the NSs core domain in crystals reveals the molecular basis of assembly of this key virulence factor in cell nuclei. Our findings have important implications for fundamental understanding of RVFV virulence.
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.