ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structural basis of the hepatitis B virus X protein in complex with DDB1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Synthesis of Nitazoxanide Derivatives as Potent and Orally Available HBx-DDB1 Inhibitors against Hepatitis B Virus.ACS medicinal chemistry letters · 2026Article
- Landscape and biogenesis of piRNAs in HBV-associated hepatocarcinogenesis: from repetitive elements to oncogenic circuits.Discover oncology · 2026Review
- HBV HBx protein masks epigenetic reader Spindlin1 via an inter-molecular zinc finger to subvert transcriptional control.Nature communications · 2026Article
- Design, synthesis, characterization and exploration of anti-HBV activity of matrine-adenine hybrids.Molecular diversity · 2026Article
- Transcription factor HOXA4 promotes HBV replication and hepatocellular carcinoma proliferation by activating KIF11 transcription.In vitro cellular & developmental biology. Animal · 2026Article
- [Analysis of the Advantages and Clinical Validation of Real-Time Fluorescence Nucleic Acid Isothermal Amplification Detection Technology in Detecting Low Viral Load Samples From HBV-Infected Patients].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2026Article
- Novel C-terminal HBx truncation (G135) in genotype D1 HBV: predicted effects on oncogenic signaling.Infectious agents and cancer · 2026Article
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
A cure for chronic hepatitis B requires eliminating or permanently silencing covalently closed circular DNA (cccDNA). A pivotal target of this approach is the hepatitis B virus (HBV) X protein (HBx), which is a key factor that promotes transcription from cccDNA. However, the HBx structure remains unsolved. Here, we present the cryoelectron microscopy structure of HBx in complex with DDB1, which is an essential complex for cccDNA transcription. In this structure, hydrophobic interactions within HBx were identified, and mutational analysis highlighted their importance in the HBV life cycle. Our biochemical analysis revealed that the HBx-DDB1 complex directly interacts simultaneously with NSE3, which is a component of the SMC5/6 complex, and Spindlin1. Additionally, HBx-DDB1 complex dynamics were explored via high-speed atomic force microscopy. These findings provide comprehensive insights into the structure and function of HBx in HBV replication.
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Registered trials
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