ArticleCell2025
Engineering and structures of Crimean-Congo hemorrhagic fever virus glycoprotein complexes.
Article in Cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
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Who cites it
14 citing papers in PubMed.
- The Crimean-Congo haemorrhagic fever virus hijacks the liver lipid metabolic pathway for virion production.Emerging microbes & infections · 2026Article
- Genetic heterogeneity and pathogenic potential of historical Crimean-Congo hemorrhagic fever virus isolates in China.Virologica Sinica · 2026Article
- CCHFV GP38 and GP85 interact with cell-surface glycosaminoglycans.Npj viruses · 2026Article
- Crimean-Congo hemorrhagic fever virus protein GP38 from isolate M18-China confers broad immunological breadth.Research square · 2026Article
- Griffithsin-mediated inhibition of cellular entry of hemorrhagic fever viruses and insights into its mechanisms.Journal of virology · 2026Article
- Human antibody targeting Crimean-Congo hemorrhagic fever virus glycoprotein 38 protects mice against heterologous virus challenge.The Journal of clinical investigation · 2026Article
- Review
- Isolation of Huangpi tick virus 1 and assessment of potential zoonotic relevance.Parasites & vectors · 2026Article
- Structural basis of mpox virus A30/H2 subcomplex formation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- GP38 is a structural component of Crimean-Congo hemorrhagic fever virus particles.Virologica Sinica · 2026Article
- IntelligentFrontiers in cellular and infection microbiology · 2026Article
- Neutralization of Crimean-Congo hemorrhagic fever pseudotyped virions with heavy chain antibodies.Virologica Sinica · 2025Article
- Immunogenicity of NSDV GP38 and the role of furin in GP38 proteolytic processing.Journal of virology · 2025Article
- Antibodies targeting Crimean-Congo hemorrhagic fever virus GP38 limit vascular leak and viral spread.Science translational medicine · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Crimean-Congo hemorrhagic fever virus (CCHFV) is a tickborne virus that can cause severe disease in humans with case fatality rates of 10%-40%. Although structures of CCHFV glycoproteins GP38 and Gc have provided insights into viral entry and defined epitopes of neutralizing and protective antibodies, the structure of glycoprotein Gn and its interactions with GP38 and Gc have remained elusive. Here, we use structure-guided protein engineering to produce a stabilized GP38-Gn-Gc heterotrimeric glycoprotein complex (GP38-Gn
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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.