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

Conserved Salt Bridges Facilitate Assembly of the Helical Core Export Apparatus of a Salmonella enterica Type III Secretion System.

Journal of molecular biology - 17 Sept 2021

Singh Nidhi, Kronenberger Thales, Eipper Andrea, Weichel Felix, Franz-Wachtel Mirita, Macek Boris, Wagner Samuel

Abstract excerpt

Virulence-associated type III secretion systems (T3SS) are utilized by Gram negative bacterial pathogens for injection of effector proteins into eukaryotic host cells. The transmembrane export apparatus at the core of T3SS is composed of a unique helical complex of the hydrophobic proteins SctR, SctS, SctT, and SctU. These components comprise a number of highly conserved charged residues within their hydrophobic...

Topics

Models, Molecular
Multiprotein Complexes
Mutation
Protein Conformation
Protein Domains
Salmonella enterica
Type III Secretion Systems
Virulence

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 34303721
DOI: 10.1016/j.jmb.2021.167175

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conserved Salt Bridges Facilitate Assembly of the Helical Core Export Apparatus of a Salmonella enterica Type III Secretion System.PMID 34303721Read ↗

Role of the alpha-helical linker of the C-terminal translocator in the biogenesis of the serine protease subfamily of autotransporters.Semantic proximity Read ↗

The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa.Semantic proximity Read ↗

Structure of the nonameric bacterial amyloid secretion channelSemantic proximity Read ↗

Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion.Semantic proximity Read ↗

Mutations in the Yersinia pseudotuberculosis type III secretion system needle protein, YscF, that specifically abrogate effector translocation into host cells.Semantic proximity Read ↗

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

Structural and functional characterization of the IpaD π-helix reveals critical roles in DOC interaction, T3SS apparatus maturation, and Shigella virulenceSemantic proximity Read ↗

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

Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion.Semantic proximity Read ↗

Expanded Roles for Multicargo and Class 1B Effector Chaperones in Type III SecretionSemantic proximity Read ↗

Mechanism of loading and translocation of type VI secretion system effector Tse6.Semantic proximity Read ↗

Site-Directed Mutagenesis and Its Application in Studying the Interactions of T3S Components.Semantic proximity Read ↗

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