Article in Nature microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
5.1field-weighted citation impact, top 4% 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
10 citing papers in PubMed, 21 citations in OpenAlex.
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
18 authors at 5 institutions in 3 countries.
Yan Yan *Key Laboratory of Molecular Biophysics, the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.ORCID http://orcid.org/0009-0003-9931-3145
Jun Xiao *Department of Cardiovascular Surgery, Taikang Center for Life and Medical Sciences Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.ORCID http://orcid.org/0000-0003-3589-7076
Fengtao Huang *Key Laboratory of Molecular Biophysics, the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China. huang_fengtao@126.com.ORCID http://orcid.org/0000-0002-9543-2994
Wei Xian *Microbiology and Infectious Disease Center, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID http://orcid.org/0000-0002-3683-7983
Bingbing YuKey Laboratory of Molecular Biophysics, the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.
Rui ChengKey Laboratory of Molecular Biophysics, the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.ORCID http://orcid.org/0000-0003-4348-0350
Hui WuKey Laboratory of Molecular Biophysics, the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.
Xueling LuKey Laboratory of Molecular Biophysics, the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.
Xionglue WangKey Laboratory of Molecular Biophysics, the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.
Wenjing HuangDepartment of Cardiovascular Surgery, Taikang Center for Life and Medical Sciences Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Jing LiDepartment of Cardiovascular Surgery, Taikang Center for Life and Medical Sciences Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.ORCID http://orcid.org/0009-0003-2593-829X
Greater Kayode OyejobiDepartment of Cardiovascular Surgery, Taikang Center for Life and Medical Sciences Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.ORCID http://orcid.org/0000-0001-9202-2028
Xiaoyun LiuMicrobiology and Infectious Disease Center, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China. xiaoyun.liu@bjmu.edu.cn.ORCID http://orcid.org/0000-0001-7083-5263
Longfei WangDepartment of Cardiovascular Surgery, Taikang Center for Life and Medical Sciences Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China. wanglf@whu.edu.cn.ORCID http://orcid.org/0000-0002-7788-2123
Bin ZhuKey Laboratory of Molecular Biophysics, the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China. bin_zhu@hust.edu.cn.ORCID http://orcid.org/0000-0002-9120-8434
Huazhong University of Science and Technology · CNWuhan University · CNBoston Children's Hospital · USPeking University · CNUniversity of Oxford · GB
Funding
National Natural Science Foundation of China (National Science Foundation of China) 21974002National Natural Science Foundation of China (National Science Foundation of China) 22174003National Natural Science Foundation of China (National Science Foundation of China) 31870165National Natural Science Foundation of China (National Science Foundation of China) 31900032National Natural Science Foundation of China (National Science Foundation of China) 32150009
6 · The paper itself
Abstract
The cyclic-oligonucleotide-based anti-phage signalling system (CBASS) is a type of innate prokaryotic immune system. Composed of a cyclic GMP-AMP synthase (cGAS) and CBASS-associated proteins, CBASS uses cyclic oligonucleotides to activate antiviral immunity. One major class of CBASS contains a homologue of eukaryotic ubiquitin-conjugating enzymes, which is either an E1-E2 fusion or a single E2. However, the functions of single E2s in CBASS remain elusive. Here, using biochemical, genetic, cryo-electron microscopy and mass spectrometry investigations, we discover that the E2 enzyme from Serratia marcescens regulates cGAS by imitating the ubiquitination cascade. This includes the processing of the cGAS C terminus, conjugation of cGAS to a cysteine residue, ligation of cGAS to a lysine residue, cleavage of the isopeptide bond and poly-cGASylation. The poly-cGASylation activates cGAS to produce cGAMP, which acts as an antiviral signal and leads to cell death. Thus, our findings reveal a unique regulatory role of E2 in CBASS.
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 Socratic graph.
Phage defence system CBASS is regulated by a prokaryotic E2 enzyme that imitates the ubiquitin pathway. · full record | Socratic