(Q35689419)

English

GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus

scientific article published on 28 November 2011

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

9 August 2017

GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus (English)

1 reference

Europe PubMed Central

9 August 2017

Staphylococcus aureus

1 reference

based on heuristic

inferred from title

antimicrobial peptide

1 reference

based on heuristic

inferred from title

author name string

Mélanie Falord

1

1 reference

Europe PubMed Central

9 August 2017

Gouzel Karimova

2

1 reference

Europe PubMed Central

9 August 2017

Aurélia Hiron

3

1 reference

Europe PubMed Central

9 August 2017

Tarek Msadek

4

1 reference

Europe PubMed Central

9 August 2017

language of work or name

0 references

publication date

28 November 2011

1 reference

Europe PubMed Central

9 August 2017

Antimicrobial Agents and Chemotherapy

1 reference

Europe PubMed Central

9 August 2017

56

1 reference

Europe PubMed Central

9 August 2017

1047-1058

1 reference

Europe PubMed Central

9 August 2017

2

1 reference

Europe PubMed Central

9 August 2017

The Staphylococcus aureus two-component regulatory system, GraRS, senses and confers resistance to selected cationic antimicrobial peptides

1 reference

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Investigation of the Staphylococcus aureus GraSR regulon reveals novel links to virulence, stress response and cell wall signal transduction pathways

1 reference

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Coevolution of ABC transporters and two-component regulatory systems as resistance modules against antimicrobial peptides in Firmicutes Bacteria

1 reference

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1 reference

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Three (and more) component regulatory systems - auxiliary regulators of bacterial histidine kinases

1 reference

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Transcriptome analysis of the responses of Staphylococcus aureus to antimicrobial peptides and characterization of the roles of vraDE and vraSR in antimicrobial resistance

1 reference

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Cell envelope stress response in Gram-positive bacteria

1 reference

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Alternative mechanisms of action of cationic antimicrobial peptides on bacteria

1 reference

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Gram-positive three-component antimicrobial peptide-sensing system

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Interaction of the GraRS two-component system with the VraFG ABC transporter to support vancomycin-intermediate resistance in Staphylococcus aureus

1 reference

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Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies

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Stimulus perception in bacterial signal-transducing histidine kinases

1 reference

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Intramembrane-sensing histidine kinases: a new family of cell envelope stress sensors in Firmicutes bacteria

1 reference

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Peptide antimicrobial agents

1 reference

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Antimicrobial peptide resistance mechanisms of human bacterial pathogens.

1 reference

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DNA microarray-based identification of genes associated with glycopeptide resistance in Staphylococcus aureus.

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Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis

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New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria.

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Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems.

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ABC transporters: physiology, structure and mechanism--an overview

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1 reference

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inferred from PubMed ID database lookup

Identifiers

10.1128/AAC.05054-11

1 reference

Europe PubMed Central

9 August 2017

1 reference

Europe PubMed Central

9 August 2017

1 reference

Europe PubMed Central

9 August 2017

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