ReviewArchives of microbiology2025
Exploring thurincin H as a biotechnologically relevant sactipeptide after fifteen years of research.
Review in Archives of microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Production of Multiple Variants of the Antimicrobial Sactipeptide Gnavucin D by the Human Gut Isolate Mediterraneibacter gnavus HB038.MicrobiologyOpen · 2026Article
- Whole genome sequencing and molecular characterization of twoFrontiers in bioinformatics · 2026Article
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.
Funding
Abstract
Thurincin H is an anionic antimicrobial peptide of 31 amino acids with a molecular weight of 3139.51 Da, it belongs to the group of sactipeptides and is produced by the bacterium Bacillus thuringiensis. Its antimicrobial spectrum is mainly directed against Gram-positive bacteria, and it has been shown to have antimicrobial activity against food pathogens and phytopathogens. In addition, it is attributed with the ability to act as a signaling molecule that promotes growth in plants, especially under stress conditions. Therefore, it is considered a peptide with biotechnological potential. One of the main limitations for the biotechnological use of thurincin H is its low production yield, mainly due to the complexity of its biosynthesis, which also hampers heterologous expression. To address this, several studies have investigated the functions of genes within its biosynthetic cluster. This review aims to summarize the key discoveries and research findings on thurincin H and explore its potential applications in biotechnology.
Indexed as
Identifiers
40498112What 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.