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

Structural model of the pre-pore ring-like structure of Panton-Valentine leukocidin: providing dimensionality to biophysical and mutational data.

Journal of biomolecular structure & dynamics - 1 Aug 2010

Aman M Javad, Karauzum Hatice, Bowden M Gabriela, Nguyen Tam Luong

Abstract excerpt

Panton-Valentine leukocidin (PVL) is a bipartite toxin that plays an important role in the pathogenesis of methicillin-resistant Staphylococcus aureus. Recent clinical data suggest a correlation between PVL and severe cases of S. aureus pneumonia. A clear understanding of the structure and functi...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Toxins
Share to Crystallography, X-Ray
Share to Exotoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Leukocidins

Share to Methicillin-Resistant Staphylococcus aureus

Share to Models, Molecular

Share to Protein Conformation

Source

Identifiers

PMID: 20476791
DOI: 10.1080/073911010010524952

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-20476791-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural model of the pre-pore ring-like structure of Panton-Valentine leukocidin: providing dimensionality to biophysical and mutational data.PMID 20476791Read ↗

Residues essential for Panton-Valentine leukocidin S component binding to its cell receptor suggest both plasticity and adaptability in its interaction surface.Semantic proximity Read ↗

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureusSemantic proximity Read ↗

Studying Staphylococcal Leukocidins: A Challenging EndeavorSemantic proximity Read ↗

Unlatching of the stem domains in the Staphylococcus aureus pore-forming leukocidin LukAB influences toxin oligomerization.Semantic proximity Read ↗

The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Semantic proximity Read ↗

Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxins.Semantic proximity Read ↗

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

Structural Basis of the Pore-Forming Toxin/Membrane InteractionSemantic proximity Read ↗

Host-Receptor Post-Translational Modifications Refine Staphylococcal Leukocidin Cytotoxicity.Semantic proximity Read ↗

Structure-function analysis of heterodimer formation, oligomerization, and receptor binding of the Staphylococcus aureus bi-component toxin LukGH.Semantic proximity Read ↗

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

Structural insights into loss of function of a pore forming toxin and its role in pneumococcal adaptation to an intracellular lifestyleSemantic proximity Read ↗

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