ReviewNature reviews. Microbiology2014
Novel bacterial ADP-ribosylating toxins: structure and function.
Review in Nature reviews. Microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.
What it found
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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
130 citing papers in PubMed, 218 citations in OpenAlex.
- Global identification of Chromobacterium violaceum T6SS effectors reveals an Rhs antibacterial toxin featuring FIX and ADP-ribosyltransferase domains.The Journal of biological chemistry · 2026Article
- Structure and function of a fungal AB toxin-like chimerolectin involved in anti-nematode defense.The EMBO journal · 2026Article
- MAP4Ks drive cell death in response tomBio · 2026Article
- A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Metabolites beyond metabolism: Exploring their atypical roles in protein modification and signaling transduction.Chinese medical journal · 2026Review
- Revisiting lactococcal abortive infection-like antiphage systems: diversity, structures, and mechanisms.FEMS microbiology reviews · 2026Review
- Preparation and Evaluation of Sodium Alginate Nanoparticles Containing Recombinant Diphtheria Toxoid (CRM197) and their Immunogenicity in Mice.Current pharmaceutical design · 2026Article
- Mechanisms of bacterial host-to-host transmission.Microbiology and molecular biology reviews : MMBR · 2025Review
- Genomic profiling of enterotoxigenicMicrobial genomics · 2025Article
- Convergent mechanisms of epithelial cell structure manipulation by intestinal pathogens.PLoS pathogens · 2025Review
- Structure of lymphostatin, a large multi-functional virulence factor of pathogenic Escherichia coli.Nature communications · 2025Article
- Diverse toxin repertoire but limited metabolic capacities inferred from the draft genome assemblies of threeMicrobial genomics · 2025Article
- Venomous Cargo: Diverse Toxin-Related Proteins Are Associated with Extracellular Vesicles in Parasitoid Wasp Venom.Pathogens (Basel, Switzerland) · 2025Article
- RACK1 MARylation regulates translation and stress granules in ovarian cancer cells.The Journal of cell biology · 2025Article
- Comparison of two immunotoxins against DLL3 receptor; as an inhibitor for small cell lung cancer.Frontiers in molecular biosciences · 2025Article
- Mono-ADP-Ribosylation of Peptides: An Overview of Synthetic and Chemoenzymatic Methodologies.Chembiochem : a European journal of chemical biology · 2024Review
- Functional and practical insights into three lactococcal antiphage systems.Applied and environmental microbiology · 2024Article
- Discovery of antiphage systems in the lactococcal plasmidome.Nucleic acids research · 2024Article
- Dissemination of pathogenic bacteria is reinforced by a MARTX toxin effector duet.Nature communications · 2024Article
- A deep learning method to predict bacterial ADP-ribosyltransferase toxins.Bioinformatics (Oxford, England) · 2024Article
70 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial ADP-ribosyltransferase toxins (bARTTs) transfer ADP-ribose to eukaryotic proteins to promote bacterial pathogenesis. In this Review, we use prototype bARTTs, such as diphtheria toxin and pertussis toxin, as references for the characterization of several new bARTTs from human, insect and plant pathogens, which were recently identified by bioinformatic analyses. Several of these toxins, including cholix toxin (ChxA) from Vibrio cholerae, SpyA from Streptococcus pyogenes, HopU1 from Pseudomonas syringae and the Tcc toxins from Photorhabdus luminescens, ADP-ribosylate novel substrates and have unique organizations, which distinguish them from the reference toxins. The characterization of these toxins increases our appreciation of the range of structural and functional properties that are possessed by bARTTs and their roles in bacterial pathogenesis.
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What OpenQuestion holds
Registered trials
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.