ArticleNature communications2019
Atomic structure of the Epstein-Barr virus portal.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 38 citations in OpenAlex.
- Cryogenic electron tomography reveals herpesvirus capsid assembly intermediates inside the cell nucleus.Nature communications · 2026Article
- Epstein-Barr virus-associated tumors: commonalities in pathogenesis and the tumor immune microenvironment.Frontiers in immunology · 2026Review
- Relationship between Epstein-Barr virus and inflammatory bowel disease.World journal of gastroenterology · 2025Review
- A comprehensive overview on the crosstalk between microRNAs and viral pathogenesis and infection.Medicinal research reviews · 2025Review
- Research landmarks on the 60th anniversary of Epstein-Barr virus.Science China. Life sciences · 2025Review
- Viral contamination in cell culture: analyzing the impact of Epstein Barr virus and Ovine Herpesvirus 2.Frontiers in microbiology · 2025Review
- Mutagenesis and functional analysis of the varicella-zoster virus portal protein.Journal of virology · 2024Article
- Epstein-Barr virus infection: the micro and macro worlds.Virology journal · 2023Review
- Worldwide Prevalence of Epstein-Barr Virus in Patients with Burkitt Lymphoma: A Systematic Review and Meta-Analysis.Diagnostics (Basel, Switzerland) · 2023Review
- Structural insights into a spindle-shaped archaeal virus with a sevenfold symmetrical tail.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22.Viruses · 2022Article
- Cryo-EM Structure of a Kinetically Trapped Dodecameric Portal Protein from the Pseudomonas-phage PaP3.Journal of molecular biology · 2022Article
- Immunosuppressive Tumor Microenvironment and Immunotherapy of Epstein-Barr Virus-Associated Malignancies.Viruses · 2022Review
- The remarkable viral portal vertex: structure and a plausible model for mechanism.Current opinion in virology · 2021Review
- Assembly of infectious Kaposi's sarcoma-associated herpesvirus progeny requires formation of a pORF19 pentamer.PLoS biology · 2021Article
- Review
- Stress-Induced Epstein-Barr Virus Reactivation.Biomolecules · 2021Review
- Structural changes in bacteriophage T7 upon receptor-induced genome ejection.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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- Article
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 3 institutions in 2 countries.
Funding
Abstract
Herpesviridae is a vast family of enveloped DNA viruses that includes eight distinct human pathogens, responsible for diseases that range from almost asymptomatic to severe and life-threatening. Epstein-Barr virus infects B-cells and epithelial cells, causing infectious mononucleosis, as well as a number of cancers. Epstein-Barr infection cannot be cured since neither vaccine nor antiviral drug treatments are available. All herpesviruses contain a linear double-stranded DNA genome, enclosed within an icosahedral capsid. Viral portal protein plays a key role in the procapsid assembly and DNA packaging. The portal is the entrance and exit pore for the viral genome, making it an attractive pharmacological target for the development of new antivirals. Here we present the atomic structure of the portal protein of Epstein-Barr virus, solved by cryo-electron microscopy at 3.5 Å resolution. The detailed architecture of this protein suggests that it plays a functional role in DNA retention during packaging.
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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.