Saturation mutagenesis of lysine 12 leads to the identification of derivatives of nisin A with enhanced antimicrobial activity.
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Bioengineering Lantibiotics for Therapeutic SuccessNovel formulations for antimicrobial peptidesAntibiotic alternatives: the substitution of antibiotics in animal husbandry?Bioengineering of the model lantibiotic nisinA bioengineered nisin derivative to control biofilms of Staphylococcus pseudintermediusIn Vitro Activities of Nisin and Nisin Derivatives Alone and In Combination with Antibiotics against Staphylococcus BiofilmsThe presence of modifiable residues in the core peptide part of precursor nisin is not crucial for precursor nisin interactions with NisB- and NisCImprovement of biocatalysts for industrial and environmental purposes by saturation mutagenesisSaturation mutagenesis of TsrA Ala4 unveils a highly mutable residue of thiostrepton A.Engineering unnatural variants of plantazolicin through codon reprogramming.Antibacterial polymeric nanostructures for biomedical applications.Multipronged approach for engineering novel peptide analogues of existing lantibiotics.Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Bacteriocins and bacteriophage; a narrow-minded approach to food and gut microbiology.In Vitro Biosynthesis and Substrate Tolerance of the Plantazolicin Family of Natural Products.A Bioengineered Nisin Derivative, M21A, in Combination with Food Grade Additives Eradicates Biofilms of Listeria monocytogenesEngineering deamidation-susceptible asparagines leads to improved stability to thermal cycling in a lipase.Intensive mutagenesis of the nisin hinge leads to the rational design of enhanced derivatives.Expanding the Genetic Code of Lactococcus lactis and Escherichia coli to Incorporate Non-canonical Amino Acids for Production of Modified Lantibiotics.High-resolution NMR studies of antibiotics in cellular membranesThe potency of the broad spectrum bacteriocin, bactofencin A, against staphylococci is highly dependent on primary structure, N-terminal charge and disulphide formation
P2860
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P2860
Saturation mutagenesis of lysine 12 leads to the identification of derivatives of nisin A with enhanced antimicrobial activity.
description
2013 nî lūn-bûn
@nan
2013 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մարտին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@ast
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@en
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@nl
type
label
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@ast
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@en
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@nl
prefLabel
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@ast
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@en
Saturation mutagenesis of lysi ...... hanced antimicrobial activity.
@nl
P2860
P50
P1433
P1476
Saturation mutagenesis of lysi ...... nhanced antimicrobial activity
@en
P2093
Paula M O' Connor
P2860
P304
P356
10.1371/JOURNAL.PONE.0058530
P407
P577
2013-03-11T00:00:00Z