Evidence map›Paper›PMID 40810525›Full record

ArticlemBio2025

Structural insights into distinct filamentation states reveal a regulatory mechanism for bacterial STING activation.

Yuchao Yang, Yueyue Liu, Xue Ma, Xuan Zhao, Jian Cao, Yu Liu, Shanqin Li, Jing Wu, Yuanzhu Gao, Lianwan Chen and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. TIR-like NADases act in bacterial immunity and the RNA vault.bioRxiv : the preprint server for biology · 2026
    Article
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

14 authors.

Yuchao YangShanxi Key Laboratory for Modernization of Traditional Chinese Veterinary Medicine (TCVM), College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong, China.ORCID 0009-0009-6717-6872
Yueyue LiuShanxi Key Laboratory for Modernization of Traditional Chinese Veterinary Medicine (TCVM), College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong, China.
Xue MaCollege of Life Sciences, Shanxi Agricultural University, Taiyuan, China.
Xuan ZhaoCollege of Life Sciences, Shanxi Agricultural University, Taiyuan, China.
Jian CaoInstitute of Pediatrics, Shenzhen Children's Hospital, Shenzhen, China.
Yu LiuCollege of Life Sciences, Shanxi Agricultural University, Taiyuan, China.
Shanqin LiInstitute of Pediatrics, Shenzhen Children's Hospital, Shenzhen, China.
Jing WuCryo-EM Center, Southern University of Science and Technology, Shenzhen, China.
Yuanzhu GaoCryo-EM Center, Southern University of Science and Technology, Shenzhen, China.
Lianwan ChenKey Laboratory of Biomacromolecules (Chinese Academy of Sciences), National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Changxin WuThe Key Laboratory of Medical Molecular Cell Biology of Shanxi Province, Institutes of Biomedical Sciences, Shanxi University, Taiyuan, China.
Guijun ShangShanxi Key Laboratory for Modernization of Traditional Chinese Veterinary Medicine (TCVM), College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong, China.ORCID 0000-0002-0187-7934
Sheng LiuInstitute of Pediatrics, Shenzhen Children's Hospital, Shenzhen, China.ORCID 0000-0002-8109-9772
Defen LuShanxi Key Laboratory for Modernization of Traditional Chinese Veterinary Medicine (TCVM), College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong, China.ORCID 0000-0002-6154-0364

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cyclic oligonucleotide-based antiphage signaling system (CBASS) is a bacterial immune mechanism that was evolutionarily linked to the eukaryotic cGAS-STING pathway, which protects against phage infection through abortive cell death. CBASS operons encode cyclic dinucleotide synthases (CD-NTases) and effector proteins (Caps), such as bacterial STING, which senses cyclic dinucleotides like 3'3'-c-di-GMP to trigger defense. Although bacterial STING oligomerizes into filaments upon ligand binding, the functional roles of distinct filament states remain unclear. Here, we resolve cryo-EM structures of

Indexed as

Bacterial ProteinsMembrane ProteinsCryoelectron MicroscopyCyclic GMPModels, MolecularProtein BindingProtein ConformationProtein MultimerizationSignal TransductionBacterial Proteinsbis(3',5')-cyclic diguanylic acidCyclic GMPMembrane Proteins3′3′-c-di-GMPCap proteinsCBASSCD-NTasesfilamentTIR-STING

Identifiers

PMID40810525
PMCPMC12421889

What OpenQuestion holds

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LicenceCC BY
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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.