Trapping ofVibrio choleraeCytolysin in the Membrane-bound Monomeric State Blocks Membrane Insertion and Functional Pore Formation by the Toxin

Incomplete pneumolysin oligomers form membrane pores

(2014) A. F.- P. Sonnen et al.   Open Biology

Pre-pore oligomer formation by Vibrio cholerae cytolysin: Insights from a truncated variant lacking the pore-forming pre-stem loop

(2013) Karan Paul et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Single point mutation inVibrio choleraecytolysin compromises the membrane pore-formation mechanism of the toxin

(2012) Karan Paul et al.   FEBS Journal

Functional Mapping of the Lectin Activity Site on the β-Prism Domain ofVibrio choleraeCytolysin

(2012) Anand Kumar Rai et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Unfolding Distinguishes theVibrio choleraeCytolysin Precursor from the Mature Form of the Toxin

(2011) Karan Paul et al.   BIOCHEMISTRY

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

Structure and assembly of pore-forming proteins

(2010) Ioan Iacovache et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as β-barrel toxins from gram-positive organisms

(2009) Sabine Löhner et al.   FASEB JOURNAL