ReviewToxins2019
Cytolethal Distending Toxin Subunit B: A Review of Structure-Function Relationship.
Review in Toxins, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed, 63 citations in OpenAlex.
- Structure and function of a fungal AB toxin-like chimerolectin involved in anti-nematode defense.The EMBO journal · 2026Article
- Integrated Immune-Gut Profiling Identifies an Exploratory Pediatric Inflammatory Intestinal Profile Associated with Food-Specific IgG Reactivity.Biomolecules · 2026Article
- Field evaluation of maize genotypes for resistance to pre-harvestFrontiers in plant science · 2026Article
- Review
- Protein-centric mechanisms of typhoidalFrontiers in cellular and infection microbiology · 2026Review
- Virulence gene profile (Open veterinary journal · 2025Article
- Helicobacter hepaticus promotes hepatic steatosis through CdtB-induced mitochondrial stress and lipid metabolism reprogramming.Nature communications · 2025Article
- Identification and Characterization of the Two Glycosyltransferases Required for the Polymerization of the HS:1 Serotype Capsular Polysaccharide ofBiochemistry · 2025Article
- Article
- Host factor Rab4b mediates internalization and intoxication of 3D4/21 cells by the active subunit of theFrontiers in microbiology · 2025Article
- Rab4b Promotes Cytolethal Distending Toxin fromToxins · 2024Article
- Article
- Phylogenetic analysis ofOpen veterinary journal · 2024Article
- A Synthetic Small Molecule, LGM2605: A Promising Modulator of Increased Pro-Inflammatory Cytokine and Osteoclast Differentiation byDentistry journal · 2024Article
- Unravelling bacterial virulence factors in yeast: From identification to the elucidation of their mechanisms of action.Archives of microbiology · 2024Review
- Campylobacter jejuni virulence factors: update on emerging issues and trends.Journal of biomedical science · 2024Review
- Predisposition factors and control strategies of avian pathogenicFrontiers in veterinary science · 2024Review
- Genetic Diversity and Expression of Intimin inMicroorganisms · 2023Article
- GSK3 as a Master Regulator of Cellular Processes.International journal of molecular sciences · 2023Article
- Article
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
No grant is acknowledged in the PubMed record.
Abstract
The Cytolethal Distending Toxin (CDT) is a bacterial virulence factor produced by several Gram-negative pathogenic bacteria. These bacteria, found in distinct niches, cause diverse infectious diseases and produce CDTs differing in sequence and structure. CDTs have been involved in the pathogenicity of the associated bacteria by promoting persistent infection. At the host-cell level, CDTs cause cell distension, cell cycle block and DNA damage, eventually leading to cell death. All these effects are attributable to the catalytic CdtB subunit, but its exact mode of action is only beginning to be unraveled. Sequence and 3D structure analyses revealed similarities with better characterized proteins, such as nucleases or phosphatases, and it has been hypothesized that CdtB exerts a biochemical activity close to those enzymes. Here, we review the relationships that have been established between CdtB structure and function, particularly by mutation experiments on predicted key residues in different experimental systems. We discuss the relevance of these approaches and underline the importance of further study in the molecular mechanisms of CDT toxicity, particularly in the context of different pathological conditions.
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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.