Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy

2005/02/21 by Tuan A. Dang, T DANG, Eileen M. Hotze +7 · 3 citations
Medicine · #Antimicrobial Resistance in Staphylococcus #Clostridium difficile and Clostridium perfringens research #Streptococcal Infections and Treatments

paper · doi:10.1016/j.jsb.2005.02.003

openalex publication_date 2005/02/21 · crossref created 2005/02/21 · crossref issued 2005/04/01 · crossref published 2005/04/01 · crossref published-print 2005/04/01 · crossref deposited 2019/01/28 · openalex created_date 2025/10/10 · crossref indexed 2026/05/10 · openalex updated_date 2026/08/01

Citations

• Structure of a Cholesterol-Binding, Thiol-Activated Cytolysin and a Model of Its Membrane Form
• Identification of a Membrane-Spanning Domain of the Thiol-Activated Pore-Forming Toxin Clostridium perfringens Perfringolysin O: An α-Helical to β-Sheet Transition Identified by Fluorescence Spectroscopy
• Monomer-Monomer Interactions Drive the Prepore to Pore Conversion of a β-Barrel-forming Cholesterol-dependent Cytolysin
• The Mechanism of Membrane Insertion for a Cholesterol-Dependent Cytolysin
• Vertical collapse of a cytolysin prepore moves its transmembrane β‐hairpins to the membrane
• Arresting Pore Formation of a Cholesterol-dependent Cytolysin by Disulfide Trapping Synchronizes the Insertion of the Transmembrane β-Sheet from a Prepore Intermediate

Cited by

• Cholesterol Exposure at the Membrane Surface Is Necessary and Sufficient to Trigger Perfringolysin O Binding
• The Cholesterol-Dependent Cytolysin Family of Gram-Positive Bacterial Toxins
• Cholesterol-dependent cytolysin [wikipedia]