Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides. - Wikidata - awgldk - TriplyDB

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

http://www.wikidata.org/entity/Q34328258

about

Design and Application of Antimicrobial Peptide Conjugates Click chemistry in peptide-based drug design Density-biased sampling: a robust computational method for studying pore formation in membranes Pro-moieties of antimicrobial peptide prodrugs.Challenges and future prospects of antibiotic therapy: from peptides to phages utilization.Covalent modification of a ten-residue cationic antimicrobial peptide with levofloxacin.Bifunctional antimicrobial conjugates and hybrid antimicrobials.Evaluation of the antibacterial and antibiofilm activities of novel CRAMP-vancomycin conjugates with diverse linkers.Targeted antimicrobial peptides.Potential of host defense peptide prodrugs as neutrophil elastase-dependent anti-infective agents for cystic fibrosis.Highly active antibacterial ferrocenoylated or ruthenocenoylated Arg-Trp peptides can be discovered by an l-to-d substitution scan

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P2860

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

http://www.wikidata.org/entity/Q34328258

description

2012 nî lūn-bûn

@nan

2012 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@ast

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@en

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@nl

type

label

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@ast

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@en

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@nl

prefLabel

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@ast

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@en

Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

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JOURNAL.PONE.0039768

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Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides.

@en

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Christopher J Arnusch

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

Roland J Pieters

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P2860

Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor

Studies on anticancer activities of antimicrobial peptides

Antimicrobial peptides of multicellular organisms

Mode of action of linear amphipathic alpha-helical antimicrobial peptides.

Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes.

Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.

The lantibiotic nisin, a special case or not?

The expanding scope of antimicrobial peptide structures and their modes of action.

The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics.

Cu-catalyzed azide-alkyne cycloaddition

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Eefjan Breukink

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