Evidence map›Paper›PMID 38982083›Full record

ArticleCell death & disease2024

ZBP1 condensate formation synergizes Z-NAs recognition and signal transduction.

Feiyan Xie, Di Wu, Jing Huang, Xuehe Liu, Yanfang Shen, Jinqing Huang, Zhipeng Su, Jixi Li

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death & disease, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Review
  2. The gasdermin family: from pyroptosis mechanisms to therapeutic targets.Signal transduction and targeted therapy · 2026
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Formation and biological implications of Z-DNA.Trends in genetics : TIG · 2026
    Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
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

8 authors.

Feiyan Xie *Department of Neurology, Huashan Hospital and School of Life Sciences, State Key Laboratory of Genetic Engineering, Fudan University, 200438, Shanghai, China.
Di Wu *Department of Neurology, Huashan Hospital and School of Life Sciences, State Key Laboratory of Genetic Engineering, Fudan University, 200438, Shanghai, China.
Jing HuangDepartment of Parasitology, School of Basic Medical Science, Central South University, Changsha, 410083, Hunan, China.
Xuehe LiuDepartment of Neurology, Huashan Hospital and School of Life Sciences, State Key Laboratory of Genetic Engineering, Fudan University, 200438, Shanghai, China.
Yanfang ShenDepartment of Neurology, Huashan Hospital and School of Life Sciences, State Key Laboratory of Genetic Engineering, Fudan University, 200438, Shanghai, China.
Jinqing HuangDepartment of Chemistry, The Hong Kong University of Science and Technology, Hong Kong, China.ORCID 0000-0001-6865-8528
Zhipeng SuDepartment of Neurosurgery, First Affiliated Hospital of Wenzhou Medical University, Wenzhou, 325000, China. drsuzhipeng@wmu.edu.cn.ORCID 0000-0002-0794-4122
Jixi LiDepartment of Neurology, Huashan Hospital and School of Life Sciences, State Key Laboratory of Genetic Engineering, Fudan University, 200438, Shanghai, China. lijixi@fudan.edu.cn.ORCID 0000-0003-3463-3175

Funding

National Natural Science Foundation of China (National Science Foundation of China) 82071782
6 · The paper itself

Abstract

Z-DNA binding protein 1 (ZBP1) is a crucial player in the intracellular recognition of Z-form nucleic acids (Z-NAs) through its Zαβ domain, initiating downstream interactions with RIPK1 and RIPK3 via RHIM domains. This engagement leads to the assembly of PANoptosomes, ultimately inducing programmed cell death to curb pathogen dissemination. How Zαβ and RHIM domain cooperate to trigger Z-NAs recognition and signal transduction remains unclear. Here, we show that ZBP1 condensate formation facilitates Z-NAs binding and antiviral signal transduction. The ZBP1 Zαβ dimerizes in a concentration-dependent manner, forming characteristic condensates in solutions evidenced by DLS and SAXS methods. ZBP1 exhibits a binding preference for 10-bp length CG (10CG) DNA and Z-RNA ligand, which in turn enhanced Zαβ dimerization, expediting the formation of droplet condensates in vitro and amyloid-like puncta in cells. Subsequent investigations reveal that Zαβ could form condensates with liquid-liquid phase separation property upon HSV and IAV infections, while full-length ZBP1 forms amyloid-like puncta with or without infections. Furthermore, ZBP1 RHIM domains show typical amyloidal fibril characterizations and cross-polymerize with RIPK1 depending on the core motif of

Indexed as

RNA-Binding ProteinsSignal TransductionAnimalsDNA, Z-FormHumansProtein BindingProtein MultimerizationReceptor-Interacting Protein Serine-Threonine KinasesDNA, Z-FormReceptor-Interacting Protein Serine-Threonine KinasesRIPK1 protein, humanRNA-Binding ProteinsZBP1 protein, human

Identifiers

PMID38982083
PMCPMC11233663

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Registered trials

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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.