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

Topology of the outer-membrane secretin PilQ from Neisseria meningitidis.

Microbiology (Reading, England) - 1 Dec 2006

Frye Stephan A, Assalkhou Reza, Collins Richard F, Ford Robert C, Petersson Christoffer, Derrick Jeremy P, Tønjum Tone

Abstract excerpt

Neisseria meningitidis is the causative agent of epidemic meningococcal meningitis and septicaemia. Type IV pili are surface organelles that mediate a variety of functions, including adhesion, twitching motility, and competence for DNA binding and uptake in transformation. The secretin PilQ is required for type IV pilus expression at the cell surface, and forms a dodecameric cage-like macromolecular complex in...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Outer Membrane Proteins
Share to Fimbriae Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Freeze Fracturing

Share to Microscopy, Immunoelectron

Share to Mutagenesis, Insertional

Share to Neisseria meningitidis

Share to Periplasm

Share to Subcellular Fractions

Source

Identifiers

PMID: 17159226
DOI: 10.1099/mic.0.2006/000315-0

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

Topology of the outer-membrane secretin PilQ from Neisseria meningitidis.PMID 17159226Read ↗

Interactions between the lipoprotein PilP and the secretin PilQ in Neisseria meningitidis.Semantic proximity Read ↗

PilMNOPQ from the Pseudomonas aeruginosa Type IV Pilus System Form a Transenvelope Protein Interaction Network That Interacts with PilASemantic proximity Read ↗

PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin.Semantic proximity Read ↗

A systematic genetic analysis in <i>Neisseria meningitidis</i> defines the Pil proteins required for assembly, functionality, stabilization and export of type IV piliSemantic proximity Read ↗

Large‐scale study of the interactions between proteins involved in type IV pilus biology in Neisseria meningitidis : characterization of a subcomplex involved in pilus assemblySemantic proximity Read ↗

CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.Semantic proximity Read ↗

The number of Neisseria meningitidis type IV pili determines host cell interaction.Semantic proximity Read ↗

PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin.Semantic proximity Read ↗

Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function.Semantic proximity Read ↗

Type IV pilin proteins: versatile molecular modules.Semantic proximity Read ↗

Type IV-like pili formed by the type II secreton: specificity, composition, bundling, polar localization, and surface presentation of peptides.Semantic proximity Read ↗

The Myxococcus xanthus pilQ (sglA) gene encodes a secretin homolog required for type IV pilus biogenesis, social motility, and development.Semantic proximity Read ↗

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