Evidence map›Paper›PMID 37537164›Full record

ArticleNature communications2023

Molecular insights into Spindlin1-HBx interplay and its impact on HBV transcription from cccDNA minichromosome.

Wei Liu, Qiyan Yao, Xiaonan Su, Yafang Deng, Mo Yang, Bo Peng, Fan Zhao, Chao Du, Xiulan Zhang, Jinsong Zhu and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
7.3field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. [The E3 ubiquitin ligase KLHL8 degrades HBx protein via the ubiquitin-proteasome pathway and inhibits HBV cccDNA transcription].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2026
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  9. Microbiota in cancer: current understandings and future perspectives.Signal transduction and targeted therapy · 2026
    Review
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  12. Structural basis of the hepatitis B virus X protein in complex with DDB1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Viral oncogenesis in cancer: from mechanisms to therapeutics.Signal transduction and targeted therapy · 2025
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 7 institutions in 2 countries.

Wei Liu *State Key Laboratory of Molecular Oncology, MOE Key Laboratory of Protein Sciences, Beijing Frontier Research Center for Biological Structure, SXMU-Tsinghua Collaborative Innovation Center for Frontier Medicine, School of Medicine, Tsinghua University, Beijing, 100084, China.ORCID http://orcid.org/0000-0003-4818-581X
Qiyan Yao *National Institute of Biological Sciences, Beijing, 102206, China.
Xiaonan SuState Key Laboratory of Molecular Oncology, MOE Key Laboratory of Protein Sciences, Beijing Frontier Research Center for Biological Structure, SXMU-Tsinghua Collaborative Innovation Center for Frontier Medicine, School of Medicine, Tsinghua University, Beijing, 100084, China.
Yafang DengState Key Laboratory of Molecular Oncology, MOE Key Laboratory of Protein Sciences, Beijing Frontier Research Center for Biological Structure, SXMU-Tsinghua Collaborative Innovation Center for Frontier Medicine, School of Medicine, Tsinghua University, Beijing, 100084, China.
Mo YangNational Center for Nanoscience and Technology, Beijing, 100190, China.
Bo PengNational Institute of Biological Sciences, Beijing, 102206, China.
Fan ZhaoState Key Laboratory of Molecular Oncology, MOE Key Laboratory of Protein Sciences, Beijing Frontier Research Center for Biological Structure, SXMU-Tsinghua Collaborative Innovation Center for Frontier Medicine, School of Medicine, Tsinghua University, Beijing, 100084, China.ORCID http://orcid.org/0000-0002-5745-5271
Chao DuState Key Laboratory of Molecular Oncology, MOE Key Laboratory of Protein Sciences, Beijing Frontier Research Center for Biological Structure, SXMU-Tsinghua Collaborative Innovation Center for Frontier Medicine, School of Medicine, Tsinghua University, Beijing, 100084, China.
Xiulan ZhangState Key Laboratory of Molecular Oncology, MOE Key Laboratory of Protein Sciences, Beijing Frontier Research Center for Biological Structure, SXMU-Tsinghua Collaborative Innovation Center for Frontier Medicine, School of Medicine, Tsinghua University, Beijing, 100084, China.
Jinsong ZhuNational Center for Nanoscience and Technology, Beijing, 100190, China.
Daliang WangState Key Laboratory of Molecular Oncology, MOE Key Laboratory of Protein Sciences, Beijing Frontier Research Center for Biological Structure, SXMU-Tsinghua Collaborative Innovation Center for Frontier Medicine, School of Medicine, Tsinghua University, Beijing, 100084, China. wangdaliang@tsinghua.edu.cn.ORCID http://orcid.org/0000-0002-6063-1897
Wenhui LiNational Institute of Biological Sciences, Beijing, 102206, China. liwenhui@nibs.ac.cn.ORCID http://orcid.org/0000-0003-1305-7404
Haitao LiState Key Laboratory of Molecular Oncology, MOE Key Laboratory of Protein Sciences, Beijing Frontier Research Center for Biological Structure, SXMU-Tsinghua Collaborative Innovation Center for Frontier Medicine, School of Medicine, Tsinghua University, Beijing, 100084, China. lht@tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-6741-293X
Center for Life Sciences · CNTsinghua University · CNNational Institute of Biological Sciences, Beijing · CNChinese Academy of Medical Sciences & Peking Union Medical College · CNFrederick National Laboratory for Cancer Research · USKing Center · USSuzhou University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular interplay between host epigenetic factors and viral proteins constitutes an intriguing mechanism for sustaining hepatitis B virus (HBV) life cycle and its chronic infection. HBV encodes a regulatory protein, HBx, which activates transcription and replication of HBV genome organized as covalently closed circular (ccc) DNA minichromosome. Here we illustrate how HBx accomplishes its task by hijacking Spindlin1, an epigenetic reader comprising three consecutive Tudor domains. Our biochemical and structural studies have revealed that the highly conserved N-terminal 2-21 segment of HBx (HBx

Indexed as

Hepatitis B virusTrans-ActivatorsViral Regulatory and Accessory ProteinsCell Cycle ProteinsDNA, CircularDNA, ViralMicrotubule-Associated ProteinsPhosphoproteinsVirus ReplicationCell Cycle ProteinsDNA, CircularDNA, Viralhepatitis B virus X proteinMicrotubule-Associated ProteinsPhosphoproteinsspindlinTrans-ActivatorsViral Regulatory and Accessory Proteins

Identifiers

PMID37537164
PMCPMC10400593
OpenAlexW4385554457

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.