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

A molecular pin to study the dynamics of beta-barrel formation in pore-forming toxins on erythrocytes: a sliding model.

Cellular and molecular life sciences : CMLS - 1 Jan 2008

Viero G, Gropuzzo A, Joubert O, Keller D, Prévost G, Dalla Serra M

Abstract excerpt

gamma-Hemolysins are pore-forming toxins which develop from water-soluble monomers by combining two different 'albeit homologous' proteins. They form oligomeric pores in both cell and model membranes by undergoing a still poorly understood conformational rearrangement in the stem region. The stem is formed by three beta-strands, folded onto the core of the soluble protein and completely extended in the pore. We...

Read the complete abstract on PubMed

Topics

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

Share to Disulfides
Share to Electrophysiology

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

Share to Erythrocyte Membrane

Share to Erythrocytes

Share to Hemolysin Proteins

Share to Hemolysis

Share to Membranes, Artificial

Share to Mutant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 18080087
DOI: 10.1007/s00018-007-7491-2
PMCID: PMC11131672

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

A molecular pin to study the dynamics of beta-barrel formation in pore-forming toxins on erythrocytes: a sliding model.PMID 18080087Read ↗

Controlling pore assembly of staphylococcal gamma-haemolysin by low temperature and by disulphide bond formation in double-cysteine LukF mutants.Semantic proximity Read ↗

Structural basis for pore-forming mechanism of staphylococcal α-hemolysin.Semantic proximity Read ↗

Disulphide bond restrains the C-terminal region of thermostable direct hemolysin during folding to promote oligomerization.Semantic proximity Read ↗

Engineered covalent leucotoxin heterodimers form functional pores: insights into S-F interactions.Semantic proximity Read ↗

Retrieving biological activity from LukF-PV mutants combined with different S components implies compatibility between the stem domains of these staphylococcal bicomponent leucotoxins.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 ↗

Grafting synthetic transmembrane units to the engineered low-toxicity α-hemolysin to restore its hemolytic activity.Semantic proximity Read ↗

An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Semantic proximity Read ↗

Sequence Diversity in the Pore-Forming Motifs of the Membrane-Damaging Protein Toxins.Semantic proximity Read ↗

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

Burst-phase expansion of native protein prior to global unfolding in SDS.Semantic proximity Read ↗

Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment.Semantic proximity Read ↗

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