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

Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ.

Journal of bacteriology - 1 Jun 2003

Sukhan Anand, Kubori Tomoko, Galán Jorge E

Abstract excerpt

An essential component of type III secretion systems (TTSS) is a supramolecular structure termed the needle complex. In Salmonella enterica, at least four proteins make up this structure: InvG, PrgH, PrgK, and PrgI. Another protein, PrgJ, is thought to play a role in the assembly of this structure, but its function is poorly understood. We have analyzed the expression and localization of PrgJ and the needle...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Culture Media

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Salmonella typhimurium

Share to Sequence Alignment

Share to Sequence Homology, Amino Acid

Share to Transcription, Genetic

Share to Virulence

Source

Open in PubMed Open full text

Identifiers

PMID: 12754250
DOI: 10.1128/JB.185.11.3480-3483.2003
PMCID: PMC155383

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ.PMID 12754250Read ↗

A protein secreted by the Salmonella type III secretion system controls needle filament assembly.Semantic proximity Read ↗

Tandem Translation Generates a Chaperone for the Salmonella Type III Secretion System Protein SsaQSemantic proximity Read ↗

Assembly of the inner rod determines needle length in the type III secretion injectisome.Semantic proximity Read ↗

Role of EscF, a putative needle complex protein, in the type III protein translocation system of enteropathogenic Escherichia coli.Semantic proximity Read ↗

The Common Structural Architecture of Shigella flexneri and Salmonella typhimurium Type Three Secretion NeedlesSemantic proximity Read ↗

Structural and functional characterisation of SiiA, an auxiliary protein from the SPI4-encoded type 1 secretion system from <i>Salmonella enterica</i>Semantic proximity Read ↗

The Salmonella FlgA protein, a putativeve periplasmic chaperone essential for flagellar P ring formation.Semantic proximity Read ↗

Genetic and molecular analysis of GogB, a phage-encoded type III-secreted substrate in Salmonella enterica serovar typhimurium with autonomous expression from its associated phage.Semantic proximity Read ↗

Supramolecular structure of the Shigella type III secretion machinery: the needle part is changeable in length and essential for delivery of effectors.Semantic proximity Read ↗

The Staphylococcus aureus Pathogenicity Island 1 Protein gp6 Functions as an Internal Scaffold during Capsid Size DeterminationSemantic proximity Read ↗

IpgD, a protein secreted by the type III secretion machinery of <i>Shigella flexneri</i> , is chaperoned by IpgE and implicated in entry focus formationSemantic proximity Read ↗

Structural control for the coordinated assembly into functional pathogenic type-3 secretion systemsSemantic proximity Read ↗

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