ReviewEXS2010
Toxins from bacteria.
Review in EXS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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.
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.
Who cites it
42 citing papers in PubMed, 82 citations in OpenAlex.
- Toxin data quality: a critical examination of bacterial exotoxins and animal toxins.BMC research notes · 2025Article
- Polarization of THP-1-Derived Human M0 to M1 Macrophages Exposed to Flavored E-Liquids.Toxics · 2025Article
- Assessing the relationship between the gut microbiota and growth traits in Chinese indigenous pig breeds.BMC veterinary research · 2025Article
- Infection biology ofEcoSal Plus · 2024Review
- Circumventing the Impossible: Cell-Free Synthesis of Protein Toxins for Medical and Diagnostic Applications.International journal of molecular sciences · 2024Review
- The Comparative Characterization of a HypervirulentInternational journal of molecular sciences · 2024Article
- Synthesis of biologically active Shiga toxins in cell-free systems.Scientific reports · 2024Article
- Special Issue "Bacterial Toxins and Cancer".International journal of molecular sciences · 2024Article
- Defined microbial communities and their soluble products protect mice from Clostridioides difficile infection.Communications biology · 2024Article
- Characterizing a Silver Nanoparticle-Based Electrochemical Biosensor for Shiga Toxin Detection.ACS omega · 2023Article
- GM1a ganglioside-binding domain peptide inhibits host adhesion and inflammatory response of enterotoxigenic Escherichia coli heat-labile enterotoxin-B in HCT-8 cells.Scientific reports · 2023Article
- AB Toxins as High-Affinity Ligands for Cell Targeting in Cancer Therapy.International journal of molecular sciences · 2023Review
- GRP75 as a functional element of cholix transcytosis.Tissue barriers · 2023Article
- Article
- Reliability of the In Silico Prediction Approach to In Vitro Evaluation of Bacterial Toxicity.Sensors (Basel, Switzerland) · 2022Article
- Review
- Bacterial AB toxins and host-microbe interactions.Advances in microbial physiology · 2022Review
- Bacterial Toxins Escape the Endosome by Inducing Vesicle Budding and Collapse.ACS chemical biology · 2021Article
- Resolution of Two Steps in Botulinum Neurotoxin Serotype A1 Light Chain Localization to the Intracellular Plasma Membrane.International journal of molecular sciences · 2021Article
- Pore-forming Esx proteins mediate toxin secretion by Mycobacterium tuberculosis.Nature communications · 2021Article
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 2 institutions in 1 country.
Funding
Abstract
Bacterial toxins damage the host at the site of bacterial infection or distant from the site. Bacterial toxins can be single proteins or oligomeric protein complexes that are organized with distinct AB structure-function properties. The A domain encodes a catalytic activity. ADP ribosylation of host proteins is the earliest post-translational modification determined to be performed by bacterial toxins; other modifications include glucosylation and proteolysis. Bacterial toxins also catalyze the non-covalent modification of host protein function or can modify host cell properties through direct protein-protein interactions. The B domain includes two functional domains: a receptor-binding domain, which defines the tropism of a toxin for a cell and a translocation domain that delivers the A domain across a lipid bilayer, either on the plasma membrane or the endosome. Bacterial toxins are often characterized based upon the secretion mechanism that delivers the toxin out of the bacterium, termed types I-VII. This review summarizes the major families of bacterial toxins and also describes the specific structure-function properties of the botulinum neurotoxins.
Indexed as
Identifiers
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.