The CroRS two-component regulatory system is required for intrinsic beta-lactam resistance in Enterococcus faecalis. - Wikidata - wikimedia - TriplyDB

The CroRS two-component regulatory system is required for intrinsic beta-lactam resistance in Enterococcus faecalis.

The CroRS two-component regulatory system is required for intrinsic beta-lactam resistance in Enterococcus faecalis.

http://www.wikidata.org/entity/Q34231476

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Restructuring of Enterococcus faecalis biofilm architecture in response to antibiotic-induced stress MurAA is required for intrinsic cephalosporin resistance of Enterococcus faecalis Serine/threonine protein phosphatase-mediated control of the peptidoglycan cross-linking L,D-transpeptidase pathway in Enterococcus faecium SalB inactivation modulates culture supernatant exoproteins and affects autolysis and viability in Enterococcus faecalis OG1RF.Oxidative stress enhances cephalosporin resistance of Enterococcus faecalis through activation of a two-component signaling system.Regulatory circuits controlling enterococcal conjugation: lessons for functional genomics.Reciprocal regulation of cephalosporin resistance in Enterococcus faecalis.Mechanisms of antibiotic resistance in enterococci.Mutations in the β subunit of RNA polymerase alter intrinsic cephalosporin resistance in Enterococci.Mutation landscape of acquired cross-resistance to glycopeptide and β-lactam antibiotics in Enterococcus faecium Competitive Growth Enhances Conditional Growth Mutant Sensitivity to Antibiotics and Exposes a Two-Component System as an Emerging Antibacterial Target in Burkholderia cenocepacia The Two-Component System ChtRS Contributes to Chlorhexidine Tolerance in Enterococcus faecium Modes and modulations of antibiotic resistance gene expression.Involvement of the Eukaryote-Like Kinase-Phosphatase System and a Protein That Interacts with Penicillin-Binding Protein 5 in Emergence of Cephalosporin Resistance in Cephalosporin-Sensitive Class A Penicillin-Binding Protein Mutants in Enterococcus Nutritional control of antibiotic resistance via an interface between the phosphotransferase system and a two-component signaling system.Thymidylate Limitation Potentiates Cephalosporin Activity toward Enterococci via an Exopolysaccharide-Based Mechanism.Systematic inactivation and phenotypic characterization of two-component signal transduction systems of Enterococcus faecalis V583.Bacterial stress responses as determinants of antimicrobial resistance.Functional Dissection of the CroRS Two-Component System Required for Resistance to Cell Wall Stressors in Enterococcus faecalis.Extracellular SalB contributes to intrinsic cephalosporin resistance and cell envelope integrity in Enterococcus faecalis.Requirement of the CroRS Two-Component System for Resistance to Cell Wall-Targeting Antimicrobials in Enterococcus faecium.The response regulator CroR modulates expression of the secreted stress-induced SalB protein in Enterococcus faecalis.New insights into the Enterococcus faecalis CroRS two-component system obtained using a differential-display random arbitrarily primed PCR approach.Influence of two-component signal transduction systems of Lactobacillus casei BL23 on tolerance to stress conditions Comparison of OG1RF and an isogenic fsrB deletion mutant by transcriptional analysis: the Fsr system of Enterococcus faecalis is more than the activator of gelatinase and serine protease.Expression, purification and activities of the entire family of intact membrane sensor kinases from Enterococcus faecalis.The role of the CroR response regulator in resistance of Enterococcus faecalis to D-cycloserine is defined using an inducible receiver domain.Modulators of Enterococcus faecalis Cell Envelope Integrity and Antimicrobial Resistance Influence Stable Colonization of the Mammalian Gastrointestinal Tract.Convergence of PASTA kinase and two-component signaling in response to cell wall stress in Enterococcus faecalis.

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The CroRS two-component regulatory system is required for intrinsic beta-lactam resistance in Enterococcus faecalis.

http://www.wikidata.org/entity/Q34231476

description

2003 nî lūn-bûn

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2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

The CroRS two-component regula ...... ance in Enterococcus faecalis.

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The CroRS two-component regula ...... ance in Enterococcus faecalis.

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The CroRS two-component regula ...... ance in Enterococcus faecalis.

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type

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The CroRS two-component regula ...... ance in Enterococcus faecalis.

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The CroRS two-component regula ...... ance in Enterococcus faecalis.

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The CroRS two-component regula ...... ance in Enterococcus faecalis.

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The CroRS two-component regula ...... ance in Enterococcus faecalis.

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The CroRS two-component regula ...... ance in Enterococcus faecalis.

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The CroRS two-component regula ...... ance in Enterococcus faecalis.

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JB.185.24.7184-7192.2003

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Journal of Bacteriology

P1476

The CroRS two-component regula ...... tance in Enterococcus faecalis

@en

P2093

Jean-Paul Brouard

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Ling Li

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Lionnel Dubost

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Richard Quintiliani

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Yannick Comenge

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P2860

Role of Mobile DNA in the Evolution of Vancomycin-Resistant Enterococcus faecalis

Peptidoglycan types of bacterial cell walls and their taxonomic implications

The life and times of the Enterococcus

The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase

Antibiotic resistance as a stress response: complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin.

Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes.

Overproduction of a low-affinity penicillin-binding protein and high-level ampicillin resistance in Enterococcus faecium.

The unphosphorylated receiver domain of PhoB silences the activity of its output domain

Regulation of VanA- and VanB-type glycopeptide resistance in enterococci

Infection with vancomycin-resistant Staphylococcus aureus containing the vanA resistance gene.

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7184-7192

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10.1128/JB.185.24.7184-7192.2003

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24

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Jean-Emmanuel Hugonnet

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2003-12-01T00:00:00Z

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14645279

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296236

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