Mapping the Intermedilysin-Human CD59 Receptor Interface Reveals a Deep Correspondence with the Binding Site on CD59 for Complement Binding Proteins C8α and C9

The structural basis for membrane binding and pore formation by lymphocyte perforin

(2010) Ruby H. P. Law et al.   NATURE

Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface

(2010) A. J. Farrand et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Intermedilysin-Receptor Interactions during Assembly of the Pore Complex

(2009) Stephanie LaChapelle et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Identification of the high affinity binding site in the Streptococcus intermedius toxin intermedilysin for its membrane receptor, the human complement regulator CD59

(2009) Timothy R. Hughes et al.   MOLECULAR IMMUNOLOGY

Characterization of a Streptococcal Cholesterol-Dependent Cytolysin with a Lewis y and b Specific Lectin Domain†

(2008) Stephen Farrand et al.   BIOCHEMISTRY

The MACPF/CDC family of pore-forming toxins

(2008) Carlos J. Rosado et al.   CELLULAR MICROBIOLOGY

Functional and Phylogenetic Characterization of Vaginolysin, the Human-Specific Cytolysin from Gardnerella vaginalis

(2008) S. E. Gelber et al.   JOURNAL OF BACTERIOLOGY

Crystal Structure of the MACPF Domain of Human Complement Protein C8α in Complex with the C8γ Subunit

(2008) Daniel J. Slade et al.   JOURNAL OF MOLECULAR BIOLOGY