Evidence map›Paper›PMID 41767953›Full record

ArticlemLife2026

Structures and mechanism of E2-CBASS anti-phage system.

Jun Xiao, Yan Yan, Jing Li, Greater Kayode Oyejobi, Dongyang Lan, Bin Zhu, Zhiming Wang, Longfei Wang

Abstract read
In one paragraph

Article in mLife, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Jun XiaoSchool of Pharmaceutical Sciences Wuhan University Wuhan China.
Yan YanCollege of Life Science and Technology Huazhong University of Science and Technology Wuhan China.
Jing LiSchool of Pharmaceutical Sciences Wuhan University Wuhan China.
Greater Kayode OyejobiSchool of Pharmaceutical Sciences Wuhan University Wuhan China.
Dongyang LanSchool of Pharmaceutical Sciences Wuhan University Wuhan China.
Bin ZhuCollege of Life Science and Technology Huazhong University of Science and Technology Wuhan China.
Zhiming WangSchool of Pharmaceutical Sciences Wuhan University Wuhan China.
Longfei WangSchool of Pharmaceutical Sciences Wuhan University Wuhan China.ORCID https://orcid.org/0000-0002-7788-2123

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria deploy diverse innate immune systems to combat bacteriophage infections. The cyclic-oligonucleotide-based anti-phage signaling system (CBASS) is a type of innate prokaryotic immune system. CBASS synthesizes cyclic-oligonucleotide through cGAS/DncV-like nucleotidyltransferases (CD-NTases) to activate downstream effectors, which kill bacteriophage-infected bacteria, thereby stopping phage spread. One major class of CBASS contains a homolog of eukaryotic ubiquitin-conjugating enzymes, either as an E1-E2 fusion or a single E2 enzyme. Both enzymes function by regulating CD-NTase activity. Currently, many structures of CD-NTases have been reported, but there are only a few reports of structures where CD-NTases form complexes with the associated E2. In this study, we analyzed the length and classification of the CD-NTase in two types of type II CBASS-E1E2/JAB-CBASS and E2-CBASS. We found that the CD-NTase in E2-CBASS is longer and predominantly belongs to clade G. We also present the structure of the

Indexed as

anti‐phage defense systemCBASSCD‐NTasecryo‐EM structureubiquitin

Identifiers

PMID41767953
PMCPMC12948482

What OpenQuestion holds

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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.