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Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin.
Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity.
Crystallization and preliminary X-ray analysis of the human-specific toxin intermedilysin.
Identification of functional domains of Clostridium septicum alpha toxin.
Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.
An Intermolecular p-Stacking Interaction Drives Conformational Changes Necessary to ß-Barrel Formation in a Pore-Forming Toxin.
A Key Motif in the Cholesterol-Dependent Cytolysins Reveals a Large Family of Related Proteins.
Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins.
Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration.
The Structural Basis for a Transition State That Regulates Pore Formation in a Bacterial Toxin.
Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin.
Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.
Conformational changes during pore formation by the perforin-related protein pleurotolysin.
Stonefish toxin defines an ancient branch of the perforin-like superfamily.
Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins.
Crystallography X Ray