ArticleMicrobiology (Reading, England)2022
Bacterial pore-forming toxins.
Article in Microbiology (Reading, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed, 83 citations in OpenAlex.
- NheABC is a pH-dependent cytotoxin that targets mitochondria and contributes to the virulence of Bacillus cereus in wound infections.Cell communication and signaling : CCS · 2026Article
- Cryo-EM structure of detergent-boundbioRxiv : the preprint server for biology · 2026Article
- Exploitation of cholesterol-dependent cytolysins for targeted biosensing and therapeutic systems.Drug delivery and translational research · 2026Review
- Three Decades of China's Bt Cotton: Achievements and Insights.Plant biotechnology journal · 2026Review
- Current Status and Future Challenges in the Use of Bacteriocins to Modulate Ruminant Gut Microbiota.Probiotics and antimicrobial proteins · 2026Review
- Bacterial pore-forming toxins: mechanisms and implications for host immunity.Bioscience reports · 2026Review
- Cytotoxic CD4 T Cells: Dual Agents in HIV-1 Pathogenesis and Persistence.Current HIV/AIDS reports · 2026Review
- Through the holes: the biotechnological potential of actinoporins (and other PFPs).Biophysical reviews · 2026Review
- Salmonella typhimurium co-expressing cytolysin A and hyaluronidase suppresses tumor growth and metastasis.Cell death discovery · 2026Article
- High resolution immunoinformatic profiling of Zonula occludens toxin reveals a conserved multiepitope vaccine candidate inFrontiers in immunology · 2026Article
- Stimuli-responsive nanocarriers for precision targeted and controlled antimicrobial drug delivery in drug-resistant infections.Frontiers in microbiology · 2026Review
- An electron transport complex required in the gut sensitizesProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A widely-occurring family of pore-forming effectors broadens the impact of the Serratia Type VI secretion system.The EMBO journal · 2025Article
- The yxiD gene from Bacillus subtilis 6633 encodes a polymorphic toxin with tRNase activity and is neutralized by the cognate immunity protein YxxD.Nucleic acids research · 2025Article
- Distinct immunity protein families mediate compartment-specific neutralization of a bacterial toxin.Cell reports · 2025Article
- Polyphenol-Mediated Peptide Assembly Modulates Melittin Toxicity: A Structure-Activity Strategy for Neutralizing the Interface Affinity of Pore-Forming Toxins to Cell Membranes.ACS applied materials & interfaces · 2025Article
- Vibrio cholerae cytolysin induces pro-inflammatory and death signals through novel TLR assembly.PLoS pathogens · 2025Article
- Novel Insights into the Therapeutic Effect of Amentoflavone AgainstInternational journal of molecular sciences · 2025Article
- A new understanding of Acanthamoeba castellanii: dispelling the role of bacterial pore-forming toxins in cyst formation and amoebicidal actions.Cell death discovery · 2025Article
- Circumventing the Impossible: Cell-Free Synthesis of Protein Toxins for Medical and Diagnostic Applications.International journal of molecular sciences · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Pore-forming toxins (PFTs) are widely distributed in both Gram-negative and Gram-positive bacteria. PFTs can act as virulence factors that bacteria utilise in dissemination and host colonisation or, alternatively, they can be employed to compete with rival microbes in polymicrobial niches. PFTs transition from a soluble form to become membrane-embedded by undergoing large conformational changes. Once inserted, they perforate the membrane, causing uncontrolled efflux of ions and/or nutrients and dissipating the protonmotive force (PMF). In some instances, target cells intoxicated by PFTs display additional effects as part of the cellular response to pore formation. Significant progress has been made in the mechanistic description of pore formation for the different PFTs families, but in several cases a complete understanding of pore structure remains lacking. PFTs have evolved recognition mechanisms to bind specific receptors that define their host tropism, although this can be remarkably diverse even within the same family. Here we summarise the salient features of PFTs and highlight where additional research is necessary to fully understand the mechanism of pore formation by members of this diverse group of protein toxins.
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.