NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
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Focal Targeting of the Bacterial Envelope by Antimicrobial PeptidesABC transporters of antimicrobial peptides in Firmicutes bacteria - phylogeny, function and regulationLantibiotic resistance.A Cationic Amphiphilic Random Copolymer with pH-Responsive Activity against Methicillin-Resistant Staphylococcus aureusThe lone S41 family C-terminal processing protease in Staphylococcus aureus is localized to the cell wall and contributes to virulenceSingle-Molecule Sequencing (PacBio) of the Staphylococcus capitis NRCS-A Clone Reveals the Basis of Multidrug Resistance and Adaptation to the Neonatal Intensive Care Unit Environment.Comparative mechanistic studies of brilacidin, daptomycin, and the antimicrobial peptide LL16.Characterization of SSR42, a novel virulence factor regulatory RNA that contributes to the pathogenesis of a Staphylococcus aureus USA300 representative.Extracellular proteases are key mediators of Staphylococcus aureus virulence via the global modulation of virulence-determinant stability.Transposon library screening for identification of genetic loci participating in intrinsic susceptibility and acquired resistance to antistaphylococcal agents.Microbial interactions in building of communities.Investigating the genetic regulation of the ECF sigma factor σS in Staphylococcus aureus.Small-molecule inhibition of bacterial two-component systems to combat antibiotic resistance and virulence.Mechanisms of resistance to antimicrobial peptides in staphylococci.The extracytoplasmic function sigma factor σS protects against both intracellular and extracytoplasmic stresses in Staphylococcus aureus.Identification of an intracellular M17 family leucine aminopeptidase that is required for virulence in Staphylococcus aureus.The membrane protein PrsS mimics σS in protecting Staphylococcus aureus against cell wall-targeting antibiotics and DNA-damaging agentsThe auxiliary protein complex SaePQ activates the phosphatase activity of sensor kinase SaeS in the SaeRS two-component system of Staphylococcus aureus.Genome-wide Annotation, Identification, and Global Transcriptomic Analysis of Regulatory or Small RNA Gene Expression in Staphylococcus aureus.The impact of CodY on virulence determinant production in community-associated methicillin-resistant Staphylococcus aureus.Bacterial strategies of resistance to antimicrobial peptides.The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucineAn Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor NucleaseThe ω Subunit Governs RNA Polymerase Stability and Transcriptional Specificity in Staphylococcus aureus.Identification and characterization of a bacitracin resistance network in Enterococcus faecalisTranscriptomic analysis of staphylococcal sRNAs: insights into species-specific adaption and the evolution of pathogenesis.The δ subunit of RNA polymerase guides promoter selectivity and virulence in Staphylococcus aureus.Bacterial stress responses as determinants of antimicrobial resistance.The modulation of Staphylococcus aureus mRNA turnoverLoss of membrane-bound lytic transglycosylases increases outer membrane permeability and β-lactam sensitivity in Pseudomonas aeruginosa.Antimicrobial peptide sensing and detoxification modules: unravelling the regulatory circuitry of Staphylococcus aureus.Characterizing the transcriptional adaptation of Staphylococcus aureus to stationary phase growth.Cloning, expression, purification, crystallization and preliminary X-ray diffraction studies of NAD synthetase from methicillin-resistant Staphylococcus aureus.The disruption of prenylation leads to pleiotropic rearrangements in cellular behavior in Staphylococcus aureus.Three distinct two-component systems are involved in resistance to the class I bacteriocins, Nukacin ISK-1 and nisin A, in Staphylococcus aureus.Identification of a unique transcriptional architecture for the sigS operon in Staphylococcus aureus.
P2860
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P2860
NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
@ast
NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
@en
type
label
NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
@ast
NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
@en
prefLabel
NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
@ast
NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
@en
P2093
P2860
P356
P1433
P1476
NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.
@en
P2093
Anna Oszmiana
David S Barber
Frances E Rivera
Halie K Miller
James T Riordan
Jessica E Davenport
Joanna Koziel
Lindsey N Shaw
Mohamed O Elasri
Stacey L Kolar
P2860
P304
P356
10.1099/MIC.0.049692-0
P50
P577
2011-05-12T00:00:00Z