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

Role of DegP for two-partner secretion in Bordetella.

Molecular microbiology - 1 Oct 2009

Baud C, Hodak H, Willery E, Drobecq H, Locht C, Jamin M, Jacob-Dubuisson F

Abstract excerpt

Sorting of proteins destined to the surface or the extracellular milieu is mediated by specific machineries, which guide the protein substrates towards the proper route of secretion and determine the compartment in which folding occurs. In gram-negative bacteria, the two-partner secretion (TPS) pathway is dedicated to the secretion of large proteins rich in beta-helical structure. The secretion of the filamentous...

Read the complete abstract on PubMed

Topics

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

Share to Adhesins, Bacterial
Share to Bordetella pertussis
Share to Gene Knockout Techniques

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

Share to Heat-Shock Proteins

Share to Periplasmic Proteins

Share to Serine Endopeptidases

Share to Surface Plasmon Resonance

Share to Virulence Factors, Bordetella

Source

Identifiers

PMID: 19703106
DOI: 10.1111/j.1365-2958.2009.06860.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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of DegP for two-partner secretion in Bordetella.PMID 19703106Read ↗

Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate.Semantic proximity Read ↗

Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis.Semantic proximity Read ↗

Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis.Semantic proximity Read ↗

New Insight into Filamentous Hemagglutinin Secretion Reveals a Role for Full-Length FhaB in Bordetella Virulence.Semantic proximity Read ↗

Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background.Semantic proximity Read ↗

The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes.Semantic proximity Read ↗

Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture.Semantic proximity Read ↗

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

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

Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli.Semantic proximity Read ↗

Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.Semantic proximity Read ↗

Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.Semantic proximity Read ↗

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