In-depth profiling of the LiaR response of Bacillus subtilis.
about
Mechanisms of drug resistance: daptomycin resistanceStructure, Bioactivity, and Resistance Mechanism of Streptomonomicin, an Unusual Lasso Peptide from an Understudied Halophilic ActinomyceteLantibiotic resistance.SecDF as part of the Sec-translocase facilitates efficient secretion of Bacillus cereus toxins and cell wall-associated proteinsProteomic response of Bacillus subtilis to lantibiotics reflects differences in interaction with the cytoplasmic membrane.Cell envelope stress response in cell wall-deficient L-forms of Bacillus subtilisImmediate and heterogeneous response of the LiaFSR two-component system of Bacillus subtilis to the peptide antibiotic bacitracinThe HtrA-like serine protease PepD interacts with and modulates the Mycobacterium tuberculosis 35-kDa antigen outer envelope protein.Mutational analyses of open reading frames within the vraSR operon and their roles in the cell wall stress response of Staphylococcus aureus.The Bacillus subtilis GntR family repressor YtrA responds to cell wall antibioticsThe Yersinia enterocolitica phage shock proteins B and C can form homodimers and heterodimers in vivo with the possibility of close association between multiple domainsA liaR deletion restores susceptibility to daptomycin and antimicrobial peptides in multidrug-resistant Enterococcus faecalis.Genetic basis for in vivo daptomycin resistance in enterococci.FtsH-dependent degradation of phage shock protein C in Yersinia enterocolitica and Escherichia coliMutations associated with reduced surotomycin susceptibility in Clostridium difficile and Enterococcus speciesA variable DNA recognition site organization establishes the LiaR-mediated cell envelope stress response of enterococci to daptomycinListeria monocytogenes shows temperature-dependent and -independent responses to salt stress, including responses that induce cross-protection against other stresses.Deletion of liaR Reverses Daptomycin Resistance in Enterococcus faecium Independent of the Genetic BackgroundPhage shock protein C (PspC) of Yersinia enterocolitica is a polytopic membrane protein with implications for regulation of the Psp stress responseWhole-genome analysis of a daptomycin-susceptible enterococcus faecium strain and its daptomycin-resistant variant arising during therapyPhysiological and transcriptomic analyses reveal mechanistic insight into the adaption of marine Bacillus subtilis C01 to alumina nanoparticles.Adaptation of Enterococcus faecalis to daptomycin reveals an ordered progression to resistanceDaptomycin inhibits cell envelope synthesis by interfering with fluid membrane microdomains.Small cationic antimicrobial peptides delocalize peripheral membrane proteins.Antibiotic resistance in Enterococcus faecium clinical isolates.The applied side of antimicrobial peptide-inducible promoters from Firmicutes bacteria: expression systems and whole-cell biosensors.Transcription Regulation and Membrane Stress Management in Enterobacterial Pathogens.The cell envelope stress response of Bacillus subtilis: from static signaling devices to dynamic regulatory network.Mechanism of Action and Resistance to Daptomycin in Staphylococcus aureus and EnterococciRegulation of bacterial cell wall growth.Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme.A Novel Phosphodiesterase of the GdpP Family Modulates Cyclic di-AMP Levels in Response to Cell Membrane Stress in Daptomycin-Resistant Enterococci.Evaluating the role of phage-shock protein A in Burkholderia pseudomallei.Contributions of the σ(W) , σ(M) and σ(X) regulons to the lantibiotic resistome of Bacillus subtilis.The LIKE system, a novel protein expression toolbox for Bacillus subtilis based on the liaI promoterComparative transcriptional analysis of Bacillus subtilis cells overproducing either secreted proteins, lipoproteins or membrane proteinsSubcellular localization, interactions and dynamics of the phage-shock protein-like Lia response in Bacillus subtilis.Membrane chaperoning by members of the PspA/IM30 protein family.The Essential UPP Phosphatase Pair BcrC and UppP Connects Cell Wall Homeostasis during Growth and Sporulation with Cell Envelope Stress Response in Bacillus subtilis.The three-component system EsrISR regulates a cell envelope stress response in Corynebacterium glutamicum.
P2860
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P2860
In-depth profiling of the LiaR response of Bacillus subtilis.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
In-depth profiling of the LiaR response of Bacillus subtilis.
@en
In-depth profiling of the LiaR response of Bacillus subtilis.
@nl
type
label
In-depth profiling of the LiaR response of Bacillus subtilis.
@en
In-depth profiling of the LiaR response of Bacillus subtilis.
@nl
prefLabel
In-depth profiling of the LiaR response of Bacillus subtilis.
@en
In-depth profiling of the LiaR response of Bacillus subtilis.
@nl
P2093
P2860
P356
P1476
In-depth profiling of the LiaR response of Bacillus subtilis
@en
P2093
Anna Juszczak
Birgit Voigt
Diana Wolf
Falk Kalamorz
Georg Homuth
Michael Hecker
Michael Hoppert
Sina Jordan
Thorsten Mascher
Tina Wecke
P2860
P304
P356
10.1128/JB.00543-10
P577
2010-07-16T00:00:00Z