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

The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes.

Molecular microbiology - 1 Nov 2005

Rosch Jason W, Caparon Michael G

Abstract excerpt

The Gram-positive pathogen Streptococcus pyogenes secretes proteins through the ExPortal, a unique single microdomain of the cellular membrane specialized to contain the Sec translocons. It has been proposed that the ExPortal functions as an organelle to promote the biogenesis of secreted proteins by coordinating interactions between nascent unfolded secretory proteins and membrane-associated chaperones. In this...

Read the complete abstract on PubMed

Topics

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

Share to Exotoxins
Share to Heat-Shock Proteins
Share to Microscopy, Immunoelectron

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

Share to Organelles

Share to Periplasmic Proteins

Share to Protein Processing, Post-Translational

Share to Serine Endopeptidases

Share to Streptococcus pyogenes

Source

Identifiers

PMID: 16262783
DOI: 10.1111/j.1365-2958.2005.04887.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

The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes.PMID 16262783Read ↗

Anionic lipids enriched at the ExPortal of Streptococcus pyogenes.Semantic proximity Read ↗

A Microdomain for Protein Secretion in Gram-Positive BacteriaSemantic proximity Read ↗

Haemolysin coregulated protein is an exported receptor and chaperone of type VI secretion substrates.Semantic proximity Read ↗

Type V Protein Secretion Pathway: the Autotransporter StorySemantic proximity Read ↗

Streptococcus pyogenes polymyxin B-resistant mutants display enhanced ExPortal integrity.Semantic proximity Read ↗

Three small partner proteins facilitate the type VII-dependent secretion of an antibacterial nucleaseSemantic proximity Read ↗

ESX‐1 secreted virulence factors are recognized by multiple cytosolic AAA ATPases in pathogenic mycobacteriaSemantic proximity Read ↗

Protein Export Systems of <i>Mycobacterium Tuberculosis</i> : Novel Targets for Drug Development?Semantic proximity Read ↗

Demarcating SurA activities required for outer membrane targeting of Yersinia pseudotuberculosis adhesins.Semantic proximity Read ↗

Dynamic action of the Sec machinery during initiation, protein translocation and termination.Semantic proximity Read ↗

Trigger Factor-Mediated Prolyl Isomerization Influences Maturation of the Streptococcus pyogenes Cysteine ProteaseSemantic proximity Read ↗

A sorting platform determines the order of protein secretion in bacterial type III systems.Semantic proximity Read ↗

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