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S. Typhimurium strategies to resist killing by cationic antimicrobial peptides.

S. Typhimurium strategies to resist killing by cationic antimicrobial peptides.

http://www.wikidata.org/entity/Q38341710

about

Focal Targeting of the Bacterial Envelope by Antimicrobial Peptides Antimicrobial peptides in 2014 Stress as a Normal Cue in the Symbiotic Environment.Identification of EnvC and Its Cognate Amidases as Novel Determinants of Intrinsic Resistance to Cationic Antimicrobial Peptides.Antimicrobial Peptides: Insights into Membrane Permeabilization, Lipopolysaccharide Fragmentation and Application in Plant Disease Control.Genetic Regulation of Virulence and Antibiotic Resistance in Acinetobacter baumannii Environmental and genetic modulation of the phenotypic expression of antibiotic resistance.Application of the Subtractive Genomics and Molecular Docking Analysis for the Identification of Novel Putative Drug Targets against Salmonella enterica subsp. enterica serovar Poona.Salmonella Persistence in Tomatoes Requires a Distinct Set of Metabolic Functions Identified by Transposon Insertion Sequencing.Susceptibility of Colistin-Resistant, Gram-Negative Bacteria to Antimicrobial Peptides and Ceragenins.The Biochemistry of Sensing: Enteric Pathogens Regulate Type III Secretion in Response to Environmental and Host Cues.Salmonella Typhimurium PagP- and UgtL-dependent resistance to antimicrobial peptides contributes to the gut colonization.

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S. Typhimurium strategies to resist killing by cationic antimicrobial peptides.

http://www.wikidata.org/entity/Q38341710

description

2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

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2015年學術文章

@zh-hant

name

S. Typhimurium strategies to resist killing by cationic antimicrobial peptides.

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type

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S. Typhimurium strategies to resist killing by cationic antimicrobial peptides.

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S. Typhimurium strategies to resist killing by cationic antimicrobial peptides.

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J.BBAMEM.2015.01.013

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Biochimica et Biophysica Acta

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S. Typhimurium strategies to resist killing by cationic antimicrobial peptides

@en

P2093

Samuel I Miller

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Susana Matamouros

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P2860

Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria

A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides.

Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation.

An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor.

Resistance to host antimicrobial peptides is necessary for Salmonella virulence

Determination of pyrophosphorylated forms of lipid A in Gram-negative bacteria using a multivaried mass spectrometric approach.

Host defence (cationic) peptides: what is their future clinical potential?

The Rcs phosphorelay system is specific to enteric pathogens/commensals and activates ydeI, a gene important for persistent Salmonella infection of mice.

Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides

Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium.

P304

3021-3025

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scholarly article

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10.1016/J.BBAMEM.2015.01.013

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P433

11 Pt B

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1848

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Susana Matamouros

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2015-01-30T00:00:00Z

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25644871

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4520786

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