Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

PspB and PspC of Yersinia enterocolitica are dual function proteins: regulators and effectors of the phage-shock-protein response.

Molecular microbiology - 1 Mar 2006

Maxson Michelle E, Darwin Andrew J

Abstract excerpt

The phage-shock-protein (Psp) stress-response system is conserved in many bacteria and has been linked to important phenotypes in Escherichia coli, Salmonella enterica and also Yersinia enterocolitica, where it is essential for virulence. It is activated by specific extracytoplasmic stress events such as the mislocalization of secretin proteins. From studies of the Psp system in E. coli, the cytoplasmic membrane...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Proliferation
Share to Dimerization
Share to Gene Expression Regulation, Bacterial

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genetic Complementation Test

Share to Heat-Shock Proteins

Share to Operon

Share to Two-Hybrid System Techniques

Share to Yersinia enterocolitica

Source

Identifiers

PMID: 16468999
DOI: 10.1111/j.1365-2958.2006.05047.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PspB and PspC of Yersinia enterocolitica are dual function proteins: regulators and effectors of the phage-shock-protein response.PMID 16468999Read ↗

Analysis of the Yersinia enterocolitica PspBC proteins defines functional domains, essential amino acids and new roles within the phage-shock-protein response.Semantic proximity Read ↗

Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the Yersinia enterocolitica Cytoplasmic Membrane.Semantic proximity Read ↗

Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response.Semantic proximity Read ↗

PspG, a new member of the Yersinia enterocolitica phage shock protein regulon.Semantic proximity Read ↗

The psp locus of Yersinia enterocolitica is required for virulence and for growth in vitro when the Ysc type III secretion system is produced.Semantic proximity Read ↗

Identification of a new member of the phage shock protein response in Escherichia coli, the phage shock protein G (PspG).Semantic proximity Read ↗

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.Semantic proximity Read ↗

Phage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica.Semantic proximity Read ↗

Secretion defects that activate the phage shock response of Escherichia coli.Semantic proximity Read ↗

Analysis of secretin-induced stress in Pseudomonas aeruginosa suggests prevention rather than response and identifies a novel protein involved in secretin function.Semantic proximity Read ↗

Variations on a theme: evolution of the phage-shock-protein system in Actinobacteria.Semantic proximity Read ↗

Membrane association of PspA depends on activation of the phage-shock-protein response in Yersinia enterocolitica.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.