ArticlemSystems2024
Protein aggregation is a consequence of the dormancy-inducing membrane toxin TisB in
Article in mSystems, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Spontaneous TisB toxin expression modulatesFEMS microbes · 2026Article
- Protein aggregation as a bistable switch in bacterial cell fate: from adaptive dormancy to cytotoxic death.Frontiers in microbiology · 2026Review
- Phage-quinolone synergy: mechanisms, clinical strategies, and translational prospects.Frontiers in microbiology · 2026Review
- Article
- TisB enables antibiotic tolerance in Salmonella by preventing prophage induction through ATP depletion.PLoS pathogens · 2025Article
- Article
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- Type I toxin-antitoxin systems in bacteria: from regulation to biological functions.EcoSal Plus · 2024Review
- Relevance of charged and polar amino acids for functionality of membrane toxin TisB.Scientific reports · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
Bacterial dormancy is a valuable strategy to survive stressful conditions. Toxins from chromosomal toxin-antitoxin systems have the potential to halt cell growth, induce dormancy, and eventually promote a stress-tolerant persister state. Due to their potential toxicity when overexpressed, sophisticated expression systems are needed when studying toxin genes. Here, we present a moderate expression system for toxin genes based on an artificial 5' untranslated region. We applied the system to induce expression of the toxin gene IMPORTANCE: Protein aggregates occur in all living cells due to misfolding of proteins. In bacteria, protein aggregation is associated with cellular inactivity, which is related to dormancy and tolerance to stressful conditions, including exposure to antibiotics. In
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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.