ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 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
94 citing papers in PubMed, 134 citations in OpenAlex.
- Review
- Microbial pigments as potential anti-rift valley fever virus drugs.BMC chemistry · 2026Article
- Article
- Recent advances in treatment and detection of Rift Valley fever virus: a comprehensive overview.Virus genes · 2025Review
- Novel replication-competent reporter-expressing Rift Valley fever viruses for molecular studies.Journal of virology · 2025Article
- Identification of critical residues for RNA binding of nairovirus nucleoprotein.Journal of virology · 2024Article
- Nucleocapsids of the Rift Valley fever virus ambisense S segment contain an exposed RNA element in the center that overlaps with the intergenic region.Nature communications · 2024Article
- Structural flexibility of Toscana virus nucleoprotein in the presence of a single-chain camelid antibody.Acta crystallographica. Section D, Structural biology · 2024Article
- The Phlebovirus Ribonucleoprotein: An Overview.Methods in molecular biology (Clifton, N.J.) · 2024Review
- RNA to Rule Them All: Critical Steps in Lassa Virus Ribonucleoparticle Assembly and Recruitment.Journal of the American Chemical Society · 2023Article
- Negative and ambisense RNA virus ribonucleocapsids: more than protective armor.Microbiology and molecular biology reviews : MMBR · 2023Review
- Rift Valley Fever Virus-Infection, Pathogenesis and Host Immune Responses.Pathogens (Basel, Switzerland) · 2023Review
- RNA Encapsulation Mode and Evolutionary Insights from the Crystal Structure of Emaravirus Nucleoprotein.Microbiology spectrum · 2023Article
- The molecular interplay of known phytochemicals asSaudi journal of biological sciences · 2023Article
- New Isolation of Ponticelli III Virus (Viruses · 2023Article
- Mechanistic insight into the efficient packaging of antigenomic S RNA into Rift Valley fever virus particles.Frontiers in cellular and infection microbiology · 2023Article
- The mechanism of genome replication and transcription in bunyaviruses.PLoS pathogens · 2023Review
- Article
- Discovery of Rift Valley fever virus natural pan-inhibitors by targeting its multiple key proteins through computational approaches.Scientific reports · 2022Article
- The Role of Nucleoprotein in Immunity to Human Negative-Stranded RNA Viruses-Not Just Another Brick in the Viral Nucleocapsid.Viruses · 2022Review
34 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
4 authors at 1 institution in 1 country.
Funding
Abstract
Rift Valley fever virus (RVFV) is a negative-sense RNA virus (genus Phlebovirus, family Bunyaviridae) that infects livestock and humans and is endemic to sub-Saharan Africa. Like all negative-sense viruses, the segmented RNA genome of RVFV is encapsidated by a nucleocapsid protein (N). The 1.93-A crystal structure of RVFV N and electron micrographs of ribonucleoprotein (RNP) reveal an encapsidated genome of substantially different organization than in other negative-sense RNA virus families. The RNP polymer, viewed in electron micrographs of both virus RNP and RNP reconstituted from purified N with a defined RNA, has an extended structure without helical symmetry. N-RNA species of approximately 100-kDa apparent molecular weight and heterogeneous composition were obtained by exhaustive ribonuclease treatment of virus RNP, by recombinant expression of N, and by reconstitution from purified N and an RNA oligomer. RNA-free N, obtained by denaturation and refolding, has a novel all-helical fold that is compact and well ordered at both the N and C termini. Unlike N of other negative-sense RNA viruses, RVFV N has no positively charged surface cleft for RNA binding and no protruding termini or loops to stabilize a defined N-RNA oligomer or RNP helix. A potential protein interaction site was identified in a conserved hydrophobic pocket. The nonhelical appearance of phlebovirus RNP, the heterogeneous approximately 100-kDa N-RNA multimer, and the N fold differ substantially from the RNP and N of other negative-sense RNA virus families and provide valuable insights into the structure of the encapsidated phlebovirus genome.
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.