ArticleJournal of virology2025
Ubiquitin-dependent proteasomal degradation of small hepatitis B virus surface antigen mediated by TRIM21 and antagonized by OTUD4.
Article in Journal of virology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Unraveling the Multifaceted Role of TRIM21 in Virus-Triggered Innate Immunity and Diseases.Biomolecules · 2026Review
- PRMT5-mediated symmetric dimethylation of SHBs at Arg169 stabilizes SHBs and promotes angiogenesis and tumor growth.Tumour virus research · 2026Article
- Rewriting the viral script: post-translational modifications orchestrating SARS-CoV-2 pathogenesis and immune evasion.Frontiers in microbiology · 2026Review
- SHBs Mitigates Sorafenib-Induced Apoptosis in Hepatocellular Carcinoma via Activation of RAF1/MEK/ERK Signaling Pathway.Cancer science · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
The small hepatitis B surface antigen (SHBs) is the most abundant hepatitis B virus (HBV) protein in individuals infected with HBV, and clearance of HBV surface antigen, which is primarily composed of SHBs, is considered a surrogate biomarker for achieving a functional cure of chronic HBV. Understanding SHBs degradation is crucial for its elimination and targeted eradication strategies. This study demonstrates that SHBs undergoes degradation via a ubiquitin/proteasome pathway, primarily through K48-linked ubiquitination, with K122 as the critical ubiquitination site. Utilizing immunoprecipitation and mass spectrometry, we identified TRIM21 (an E3 ubiquitin ligase) and OTUD4 (a deubiquitinase) as key regulators of SHBs. We verified the direct interaction between SHBs and TRIM21's coiled-coil domain, as well as the N-terminal amino acids 1-180 of OTUD4, using coimmunoprecipitation and glutathione S-transferase (GST) pull-down assays in both
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Registered trials
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