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Stress relief during host infection: The phage shock protein response supports bacterial virulence in various waysRecent findings about the Yersinia enterocolitica phage shock protein responseThe Pseudomonas aeruginosa periplasmic protease CtpA can affect systems that impact its ability to mount both acute and chronic infectionsGenome-wide screens to identify genes of human pathogenic Yersinia species that are expressed during host infection.Fnr, NarP, and NarL regulation of Escherichia coli K-12 napF (periplasmic nitrate reductase) operon transcription in vitro.Membrane association of PspA depends on activation of the phage-shock-protein response in Yersinia enterocoliticaPeriplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12Identification of inducers of the Yersinia enterocolitica phage shock protein system and comparison to the regulation of the RpoE and Cpx extracytoplasmic stress responses.YtxR, a conserved LysR-like regulator that induces expression of genes encoding a putative ADP-ribosyltransferase toxin homologue in Yersinia enterocoliticaThe Yersinia enterocolitica phage shock proteins B and C can form homodimers and heterodimers in vivo with the possibility of close association between multiple domainsActivity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners.Expression of the narX, narL, narP, and narQ genes of Escherichia coli K-12: regulation of the regulators.FtsH-dependent degradation of phage shock protein C in Yersinia enterocolitica and Escherichia coliCyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa.PspG, a new member of the Yersinia enterocolitica phage shock protein regulonIdentification of YsaP, the Pilotin of the Yersinia enterocolitica Ysa Type III Secretion System.Regulation of bacterial virulence gene expression by cell envelope stress responses.The phage-shock-protein response.Links between type III secretion and extracytoplasmic stress responses in YersiniaAnalysis of the Yersinia enterocolitica PspBC proteins defines functional domains, essential amino acids and new roles within the phage-shock-protein response.Differential regulation by the homologous response regulators NarL and NarP of Escherichia coli K-12 depends on DNA binding site arrangement.The Phage Shock Protein Response.Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the Yersinia enterocolitica Cytoplasmic Membrane.Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response.Global analysis of tolerance to secretin-induced stress in Yersinia enterocolitica suggests that the phage-shock-protein system may be a remarkably self-contained stress response.Elongation factor-P at the crossroads of the host-endosymbiont interface.Analysis of secretin-induced stress in Pseudomonas aeruginosa suggests prevention rather than response and identifies a novel protein involved in secretin function.Nitrate and nitrite regulation of the Fnr-dependent aeg-46.5 promoter of Escherichia coli K-12 is mediated by competition between homologous response regulators (NarL and NarP) for a common DNA-binding site.A Proteolytic Complex Targets Multiple Cell Wall Hydrolases in Pseudomonas aeruginosa.
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P50
description
researcher
@en
wetenschapper
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հետազոտող
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name
Andrew J Darwin
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Andrew J Darwin
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Andrew J Darwin
@es
Andrew J Darwin
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type
label
Andrew J Darwin
@ast
Andrew J Darwin
@en
Andrew J Darwin
@es
Andrew J Darwin
@nl
prefLabel
Andrew J Darwin
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Andrew J Darwin
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Andrew J Darwin
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Andrew J Darwin
@nl
P106
P31
P496
0000-0002-7751-1293