Analysis of the Yersinia enterocolitica PspBC proteins defines functional domains, essential amino acids and new roles within the phage-shock-protein response.
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Recent findings about the Yersinia enterocolitica phage shock protein response'Big things in small packages: the genetics of filamentous phage and effects on fitness of their host'Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein responseMembrane association of PspA depends on activation of the phage-shock-protein response in Yersinia enterocoliticaThe evolution of the phage shock protein response system: interplay between protein function, genomic organization, and system function.The 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.FtsH-dependent degradation of phage shock protein C in Yersinia enterocolitica and Escherichia coliIdentification of YsaP, the Pilotin of the Yersinia enterocolitica Ysa Type III Secretion System.Phage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica.Links between type III secretion and extracytoplasmic stress responses in YersiniaPhage shock protein C (PspC) of Yersinia enterocolitica is a polytopic membrane protein with implications for regulation of the Psp stress responseTranscription Regulation and Membrane Stress Management in Enterobacterial Pathogens.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.Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli.The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.Subcellular localization, interactions and dynamics of the phage-shock protein-like Lia response in Bacillus subtilis.Contribution of YthA, a PspC family transcriptional regulator to Lactococcus lactis F44 acid tolerance and nisin yield: a transcriptomic approach.
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P2860
Analysis of the Yersinia enterocolitica PspBC proteins defines functional domains, essential amino acids and new roles within the phage-shock-protein response.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 22 September 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Analysis of the Yersinia enter ...... phage-shock-protein response.
@en
Analysis of the Yersinia enter ...... phage-shock-protein response.
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type
label
Analysis of the Yersinia enter ...... phage-shock-protein response.
@en
Analysis of the Yersinia enter ...... phage-shock-protein response.
@nl
prefLabel
Analysis of the Yersinia enter ...... phage-shock-protein response.
@en
Analysis of the Yersinia enter ...... phage-shock-protein response.
@nl
P2860
P1476
Analysis of the Yersinia enter ...... e phage-shock-protein response
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P2093
Diana C Savitzky
P2860
P304
P356
10.1111/J.1365-2958.2009.06885.X
P407
P577
2009-09-22T00:00:00Z