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

Studies on the structure and mechanism of a bacterial protein toxin by analytical ultracentrifugation and small-angle neutron scattering.

Journal of molecular biology - 12 Nov 1999

Gilbert R J, Heenan R K, Timmins P A, Gingles N A, Mitchell T J, Rowe A J, Rossjohn J, Parker M W, Andrew P W, Byron O

Abstract excerpt

Pneumolysin, an important virulence factor of the human pathogen Streptococcus pneumoniae, is a pore-forming toxin which also possesses the ability to activate the complement system directly. Pneumolysin binds to cholesterol in cell membrane surfaces as a prelude to pore formation, which involves the oligomerization of the protein. Two important aspects of the pore-forming activity of pneumolysin are therefore...

Read the complete abstract on PubMed

Topics

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

Share to Cytotoxins
Share to Lipid Bilayers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Liposomes

Share to Neutrons

Share to Scattering, Radiation

Share to Solutions

Share to Streptolysins

Share to Ultracentrifugation

Source

Identifiers

PMID: 10547292
DOI: 10.1006/jmbi.1999.3210

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

Studies on the structure and mechanism of a bacterial protein toxin by analytical ultracentrifugation and small-angle neutron scattering.PMID 10547292Read ↗

Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.Semantic proximity Read ↗

Formation of pre-pore complexes of pneumolysin is accompanied by a decrease in short-range order of lipid molecules throughout vesicle bilayers.Semantic proximity Read ↗

The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae.Semantic proximity Read ↗

Exolysin (ExlA) from Pseudomonas aeruginosa Punctures Holes into Target Membranes Using a Molten Globule Domain.Semantic proximity Read ↗

Assembly of streptolysin O pores assessed by quartz crystal microbalance and atomic force microscopy provides evidence for the formation of anchored but incomplete oligomers.Semantic proximity Read ↗

Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins.Semantic proximity Read ↗

Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins.Semantic proximity Read ↗

Partial oligomerization of pyolysin induced by a disulfide-tethered mutant.Semantic proximity Read ↗

X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form.Semantic proximity Read ↗

Tethered bilayer membranes as a complementary tool for functional and structural studies: The pyolysin case.Semantic proximity Read ↗

Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization.Semantic proximity Read ↗

Helical crystallization on nickel-lipid nanotubes: perfringolysin O as a model protein.Semantic proximity Read ↗

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