Crystal structure of the octameric pore of staphylococcal  -hemolysin reveals the  -barrel pore formation mechanism by two components

Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins

(2011) S. De et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structure

(2011) Yoshikazu Tanaka et al.   PROTEIN SCIENCE

Uni-molecular detection and quantification of selected β-lactam antibiotics with a hybrid α-hemolysin protein pore

(2010) Alina Asandei et al.   JOURNAL OF MOLECULAR RECOGNITION

Piercing insights

(2009) Hagan Bayley   NATURE

Pore formation: An ancient yet complex form of attack

(2008) Ioan Iacovache et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Analysis of the Specificity of Panton-Valentine Leucocidin and Gamma-Hemolysin F Component Binding

(2008) F. Meyer et al.   INFECTION AND IMMUNITY

The Influence of Membrane Lipids in Staphylococcus aureus Gamma-Hemolysins Pore Formation

(2008) C. Potrich et al.   JOURNAL OF MEMBRANE BIOLOGY

A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of β-barrel pore-forming toxins

(2008) Pierre Roblin et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS