ArticleJournal of natural products2024
Facile Halogenation of Antimicrobial Peptides As Demonstrated by Producing Bromotryptophan-Labeled Nisin Variants with Enhanced Antimicrobial Activity.
Article in Journal of natural products, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- A truncated nisin variant, lipidated at its C-terminus, displays improved stability and increased antibacterial activity against methicillin-resistantRSC chemical biology · 2026Article
- Continuous evolution of a halogenase enzyme with improved solubility and activity for sustainable bioproduction.Nature communications · 2026Article
- Synthesis and Antimicrobial Specificities of Halogenated Tryptophan-Containing Nisin Variants.ACS chemical biology · 2025Article
- Functionalizing Nisin with a Sugar Moiety Improves Its Solubility and Results in an Altered Antibacterial Spectrum and Mode of Action.ACS synthetic biology · 2025Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Recent Advances in Augmenting the Therapeutic Efficacy of Peptide-Drug Conjugates.Journal of medicinal chemistry · 2025Review
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
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides (AMPs) have raised significant interest, forming a potential new class of antibiotics in the fight against multi-drug-resistant bacteria. Various AMPs are ribosomally synthesized and post-translationally modified peptides (RiPPs). One post-translational modification found in AMPs is the halogenation of Trp residues. This modification has, for example, been shown to be critical for the activity of the potent AMP NAI-107 from
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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.