Evidence map›Paper›PMID 22421137›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyaviruses.

Yu Guo, Wenming Wang, Wei Ji, Maping Deng, Yuna Sun, Honggang Zhou, Cheng Yang, Fei Deng, Hualin Wang, Zhihong Hu and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
6.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

80 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Structural Features of Nucleoproteins from the Recently DiscoveredInternational journal of molecular sciences · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Crimean-Congo haemorrhagic fever virus.Nature reviews. Microbiology · 2023
    Review
  17. Article
  18. Review
  19. Review
  20. Article

20 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 2 countries.

Yu GuoLaboratory of Structural Biology, School of Medicine and Life Sciences, Tsinghua University, Beijing 100084, China.
Wenming Wang
Wei Ji
Maping Deng
Yuna Sun
Honggang Zhou
Cheng Yang
Fei Deng
Hualin Wang
Zhihong Hu
Zhiyong Lou
Zihe Rao
Chinese Academy of Sciences · CNNankai University · CNTianjin International Joint Academy of Biomedicine · CNWuhan Institute of Virology · CNInstitute of Biophysics · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crimean-Congo hemorrhagic fever virus (CCHFV), a virus with high mortality in humans, is a member of the genus Nairovirus in the family Bunyaviridae, and is a causative agent of severe hemorrhagic fever (HF). It is classified as a biosafety level 4 pathogen and a potential bioterrorism agent due to its aerosol infectivity and its ability to cause HF outbreaks with high case fatality (∼30%). However, little is known about the structural features and function of nucleoproteins (NPs) in the Bunyaviridae, especially in CCHFV. Here we report a 2.3-Å resolution crystal structure of the CCHFV nucleoprotein. The protein has a racket-shaped overall structure with distinct "head" and "stalk" domains and differs significantly with NPs reported so far from other negative-sense single-stranded RNA viruses. Furthermore, CCHFV NP shows a distinct metal-dependent DNA-specific endonuclease activity. Single residue mutations in the predicted active site resulted in a significant reduction in the observed endonuclease activity. Our results present a new folding mechanism and function for a negative-strand RNA virus nucleoprotein, extend our structural insight into bunyavirus NPs, and provide a potential target for antiviral drug development to treat CCHFV infection.

Indexed as

Chromatography, GelCrystallography, X-RayDNA, ViralEndonucleasesHemorrhagic Fever Virus, Crimean-CongoHost-Pathogen InteractionsModels, MolecularNucleoproteinsOrthobunyavirusProtein Structure, SecondaryProtein Structure, TertiaryRNA-Binding ProteinsRNA CapsViral ProteinsDNA, ViralEndonucleasesNucleoproteinsRNA-Binding ProteinsRNA CapsViral Proteins

Identifiers

PMID22421137
PMCPMC3324003
OpenAlexW2063046860

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.