ArticleNature2024
Legionella effector LnaB is a phosphoryl-AMPylase that impairs phosphosignalling
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Article in Nature, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.
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0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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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.
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Who cites it
23 citing papers in PubMed.
- Crystal structure of theVirulence · 2026Article
- The Legionella pneumophila effector SidL is an adenylyltransferase that modifies the glycolytic intermediate 3-phosphoglycerate.Molecular cell · 2026Article
- Crystal structure of Legionella pneumophila glycosidase effector LegY.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Molecular basis of host ATP level modulation by actin-dependent secreted bacterial ATPase and its metaeffector.Nature communications · 2026Article
- The toxin-antitoxin complex Fic-1-AntF functions as a deAMPylase that regulates the activity of DNA gyrase.mLife · 2026Article
- Manipulation of nonclassical ubiquitin signaling by pathogenic bacteria.Current opinion in microbiology · 2026Review
- Ubiquitination and autophagy in host-pathogen interactions: from immune surveillance to therapeutic targeting.Nature reviews. Immunology · 2026Review
- A bacterial YopJ-family acetyltransferase suppresses host immune response by Nε-acetylation of JAK1.Nature communications · 2026Article
- Article
- Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase.Nature chemical biology · 2026Article
- Development and Validation of a High-Throughput Screening Assay for the Legionella ADP-Ribosyl Transferase SdeA.Chembiochem : a European journal of chemical biology · 2025Article
- Crystal structure of thebioRxiv : the preprint server for biology · 2025Article
- Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025Article
- Regulation of host immunity by a novel Legionella pneumophila E3 ubiquitin ligase.PLoS pathogens · 2025Article
- Legionella effector LpPIP recruits protein phosphatase 1 to the mitochondria to induce dephosphorylation of outer membrane proteins.PLoS biology · 2025Article
- Modulation of host ATP levels by secreted bacterial effectors.Nature communications · 2025Article
- Cryo-EM Detection of AMPylated Histidine Implies Covalent Catalysis in AMPylation Mediated by a Bacterial Effector.Journal of molecular biology · 2025Article
- Insights into mechanisms of ubiquitin ADP-ribosylation reversal.Biochemical Society transactions · 2024Review
- Review
- Review
Corrections and comments
- Erratum issued
Authors and funding
16 authors.
Ting Wang *Department of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Xiaonan Song *Department of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Jiaxing Tan *Department of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China.ORCID 0000-0003-0638-9048
Wei XianDepartment of Microbiology and Infectious Disease Center, NHC Key Laboratory of Medical Immunology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID 0000-0002-3683-7983
Xingtong ZhouDepartment of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Mingru YuDepartment of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Xiaofei WangDepartment of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China.ORCID 0000-0002-4654-1983
Yan XuDepartment of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China.ORCID 0009-0001-5547-564X
Ting WuMOE Key Laboratory of Biosystems Homeostasis and Protection, and Zhejiang Provincial Key Laboratory of Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Keke YuanDepartment of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Yu RanMOE Key Laboratory of Biosystems Homeostasis and Protection, and Zhejiang Provincial Key Laboratory of Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Bing YangMOE Key Laboratory of Biosystems Homeostasis and Protection, and Zhejiang Provincial Key Laboratory of Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Gaofeng FanSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.ORCID 0000-0002-6729-2867
Xiaoyun LiuDepartment of Microbiology and Infectious Disease Center, NHC Key Laboratory of Medical Immunology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China. xiaoyun.liu@bjmu.edu.cn.ORCID 0000-0001-7083-5263
Yan ZhouDepartment of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China. zhouyanlsi@zju.edu.cn.ORCID 0000-0001-9352-7108
Yongqun ZhuDepartment of Gastroenterology of the Second Affiliated Hospital, School of Medicine and College of Animal Sciences, Life Sciences Institute, Zhejiang University, Hangzhou, China. zhuyongqun@zju.edu.cn.ORCID 0000-0002-4158-5223
Funding
No grant is acknowledged in the PubMed record.
Abstract
AMPylation is a post-translational modification in which AMP is added to the amino acid side chains of proteins
Indexed as
Adenosine MonophosphateBacterial ProteinsLegionella pneumophilaPhosphotyrosineSignal TransductionActinsAdenosine TriphosphateADP-RibosylationDeubiquitinating EnzymesHumansHydrolysisLigandsModels, MolecularN-Glycosyl HydrolasesPhosphorylationProtein FoldingActinsAdenosine MonophosphateAdenosine TriphosphateADP-ribosylarginine hydrolaseBacterial ProteinsDeubiquitinating EnzymesLigandsN-Glycosyl HydrolasesPhosphotyrosineTyrosineUbiquitin
Identifiers
PMID
38776962What OpenQuestion holds
Textmetadata
Read underepoch 390
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.