Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147. - Wikidata - wikimedia - TriplyDB

Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

http://www.wikidata.org/entity/Q37332509

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Lantibiotic resistance.Investigating the importance of charged residues in lantibiotics.Non-proteinogenic amino acids in lacticin 481 analogues result in more potent inhibition of peptidoglycan transglycosylation.A general method for fluorescent labeling of the N-termini of lanthipeptides and its application to visualize their cellular localization.Saturation mutagenesis of selected residues of the α-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity The dawning of a 'Golden era' in lantibiotic bioengineering.Recent derivatives from smaller classes of fermentation-derived antibacterials.Increasing the success rate of lantibiotic drug discovery by Synthetic Biology.Bioengineering: a bacteriocin perspective.Metabolic engineering, new antibiotics and biofilm viscoelasticity.

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Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

http://www.wikidata.org/entity/Q37332509

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

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scientific article published on 23 August 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

@en

Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

@nl

type

label

Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

@en

Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

@nl

prefLabel

Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

@en

Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

@nl

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J.1751-7915.2009.00145.X

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Microbial Biotechnology

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Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147.

@en

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Andreas Peschel

http://www.w3.org/2001/XMLSchema#string

Colin Hill

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Elaine M Lawton

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Lorraine A Draper

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Lucy H Deegan

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Paul D Cotter

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R Paul Ross

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Srinivas Suda

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P2860

Structure-activity relationship studies of the two-component lantibiotic haloduracin

Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics.

Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci.

Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity.

Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity.

Two-component anti-Staphylococcus aureus lantibiotic activity produced by Staphylococcus aureus C55

Streptococcus rattus strain BHT produces both a class I two-component lantibiotic and a class II bacteriocin.

Discovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic.

Relatedness between the two-component lantibiotics lacticin 3147 and staphylococcin C55 based on structure, genetics and biological activity.

Genetic analysis of a unique bacteriocin, Smb, produced by Streptococcus mutans GS5

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222-234

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scholarly article

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10.1111/J.1751-7915.2009.00145.X

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2

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3

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Floor Hugenholtz

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2009-08-23T00:00:00Z

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