ArticlemBio2025
Histone variant H2A.Z cooperates with EBNA1 to maintain Epstein-Barr virus latent epigenome.
Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- EBNA1 inhibitors reveal CDC7 and POU2F1 as direct functional targets in EBV epithelial cancers.mBio · 2026Article
- EBNA1 SUMOylation by PIAS1 suppresses EBV lytic replication and enhances episome maintenance.mBio · 2026Article
- Article
- Human herpesvirus 6B U65 binds to histone proteins and suppresses interferon production.Journal of virology · 2025Article
- EBNA1 SUMOylation by PIAS1 Suppresses EBV Lytic Replication and Enhances Episome Maintenance.bioRxiv : the preprint server for biology · 2025Article
- Expression of EBNA1 and miR-155 in Papillary Thyroid Carcinoma: A Case-Control Study in Iraqi Patients.F1000Research · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Chromatin structure plays a central role in the regulation of Epstein-Barr virus (EBV) latency. The histone variant H2A.Z.1 has been implicated in chromatin structures associated with the initiation of transcription and DNA replication. Here, we investigate the functional role of H2AZ.1 in the regulation of EBV chromatin, gene expression, and copy number during latent infection. We found that H2A.Z.1 is highly enriched near EBNA1-binding sites at the origin of plasmid replication (
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