Results 121 to 130 of about 2,586 (178)

Staphylococcus epidermidis bacteriocin A37 kills natural competitors with a unique mechanism of action. [PDF]

open access: yesISME J
Puls JS   +14 more
europepmc   +1 more source

Small Natural Cyclic Peptides from DBAASP Database. [PDF]

open access: yesPharmaceuticals (Basel)
Alimbarashvili E   +3 more
europepmc   +1 more source

Exploring the lipoproteome of Parageobacillus thermoglucosidasius. [PDF]

open access: yesAccess Microbiol
Jackson M   +4 more
europepmc   +1 more source

Reconstruction of the Reaction of Andalusicin Lantibiotic Modification by Lanthionine Synthetase AncKC in a Heterologous Escherichia coli System. [PDF]

open access: yesActa Naturae
Mirzoeva NZ   +7 more
europepmc   +1 more source

Biomimetic Synthesis of Lantibiotics

Chemistry - A European Journal, 2000
The lantibiotics are a class of highly posttranslationally modified small peptide antibiotics containing numerous lanthionine and dehydroamino acid residues. We have prepared peptides containing multiple dehydroamino acids and cysteine residues in order to probe the biomimetic synthesis of the lantibiotics from their precursor peptides.
Mark Bradley   +2 more
exaly   +3 more sources

Pinensins: The First Antifungal Lantibiotics

Angewandte Chemie - International Edition, 2015
AbstractLantibiotics (lanthionine‐containing antibiotics) from Gram‐positive bacteria typically exhibit activity against Gram‐positive bacteria. The activity and structure of pinensin A (1) and B (2), lantibiotics isolated from a native Gram‐negative producer Chitinophaga pinensis are described.
Rolf Müller   +2 more
exaly   +3 more sources

Posttranslationally modified bacteriocins—the lantibiotics

Biopolymers, 2000
Lantibiotics are a subgroup of bacteriocins that are characterized by the presence of the unusual thioether amino acids lanthionine and 3-methyllanthionine generated through posttranslational modification. The biosynthesis of lantibiotics follows a defined pathway comprising modifications of the prepeptide, proteolytic activation, and export. The genes
H G Sahl
exaly   +3 more sources

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