ArticleMolecules and cells2012
Structural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus.
Article in Molecules and cells, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 41 citations in OpenAlex.
- Promiscuous Metal Site in Hepatitis B Virus X Protein Binds an Fe-S Cluster.bioRxiv : the preprint server for biology · 2026Article
- Sequential backbone chemical shift assignments of a cancer-associated isoform of the HBx protein from human hepatitis B virus.Biomolecular NMR assignments · 2025Article
- Insights of HIV-1 and HBV transcriptional regulation by viral transactivator Tat and HBx.Virus genes · 2025Review
- Review
- SEC-SAXS/MC Ensemble Structural Studies of the Microtubule Binding Protein Cdt1 Show Monomeric, Folded-Over Conformations.Cytoskeleton (Hoboken, N.J.) · 2025Article
- The Intrinsically Disordered Region of HBx and Virus-Host Interactions: Uncovering New Therapeutic Approaches for HBV and Cancer.International journal of molecular sciences · 2025Review
- Iron‑sulfur clusters in viral proteins: Exploring their elusive nature, roles and new avenues for targeting infections.Biochimica et biophysica acta. Molecular cell research · 2024Review
- SAXS/MC studies of the mixed-folded protein Cdt1 reveal monomeric, folded over conformations.bioRxiv : the preprint server for biology · 2024Article
- Pre- and Post-Transcriptional Control of HBV Gene Expression: The Road Traveled towards the New Paradigm of HBx, Its Isoforms, and Their Diverse Functions.Biomedicines · 2023Review
- Relevance of HBx for Hepatitis B Virus-Associated Pathogenesis.International journal of molecular sciences · 2023Review
- The HBx protein from hepatitis B virus coordinates a redox-active Fe-S cluster.The Journal of biological chemistry · 2022Article
- HBx inhibits DNA sensing signaling pathway via ubiquitination and autophagy of cGAS.Virology journal · 2022Article
- Review
- Canonical and Divergent N-Terminal HBx Isoform Proteins Unveiled: Characteristics and Roles during HBV Replication.Biomedicines · 2021Article
- Hepatitis B: Current Status of Therapy and Future Therapies.Gastroenterology clinics of North America · 2020Review
- Targeting Hepatitis B Virus Covalently Closed Circular DNA and Hepatitis B Virus X Protein: Recent Advances and New Approaches.ACS infectious diseases · 2019Article
- Anti-Hepatitis B Virus Activity of Esculetin fromMolecules (Basel, Switzerland) · 2019Article
- Spatiotemporal Analysis of Hepatitis B Virus X Protein in Primary Human Hepatocytes.Journal of virology · 2019Article
- Hepatitis B Virus X Protein Function Requires Zinc Binding.Journal of virology · 2019Article
- NMR Spectroscopy for Metabolomics Research.Metabolites · 2019Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hepatitis B virus x protein (HBX) is expressed in HBV-infected liver cells and can interact with a wide range of cellular proteins. In order to understand such promiscuous behavior of HBX we expressed a truncated mini-HBX protein (named Tr-HBX) (residues 18-142) with 5 Cys → Ser mutations and characterized its structural features using circular dichroism (CD) spectropolarimetry, NMR spectroscopy as well as bioinformatics tools for predicting disorder in intrinsically unstructured proteins (IUPs). The secondary structural content of Tr-HBX from CD data suggests that Tr-HBX is only partially folded. The protein disorder prediction by IUPred reveals that the unstructured region encompasses its N-terminal ~30 residues of Tr-HBX. A two-dimensional (1)H-(15)N HSQC NMR spectrum exhibits fewer number of resonances than expected, suggesting that Tr-HBX is a hybrid type IUP where its folded C-terminal half coexists with a disordered N-terminal region. Many IUPs are known to be capable of having promiscuous interactions with a multitude of target proteins. Therefore the intrinsically disordered nature of Tr-HBX revealed in this study provides a partial structural basis for the promiscuous structure-function behavior of HBX.
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