original ) (raw )Interaction of Clostridium perfringensIota-Toxin with Lipid Bilayer Membranes
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Journal of Biological Chemistry, 2001
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Clostridium Perfringens Epsilon Toxin Binds to Membrane Lipids and Its Cytotoxic Action Depends on Sulfatide
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Unexpected wide substrate specificity of C. perfringens α-toxin phospholipase C
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Pore Formation by S. aureus α-toxin in Liposomes and Planar Lipid Bilayers: Effects of Nonelectrolytes
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Effects of bilayer composition and physical properties on the phospholipase C and sphingomyelinase activities of Clostridium perfringens α-toxin
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Biochimica et Biophysica Acta (BBA) - Biomembranes, 2011
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Identification of Residues in the Carboxy-Terminal Domain of Clostridium perfringens α-Toxin (Phospholipase C) Which Are Required for Its Biological Activities
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Cholesterol stimulates the lytic activity of Adenylate Cyclase Toxin on lipid membranes by promoting toxin oligomerization and formation of pores with a greater effective size
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Clostridium perfringens Epsilon Toxin Induces a Rapid Change of Cell Membrane Permeability to Ions and Forms Channels in Artificial Lipid Bilayers
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Different structural requirements for adenylate cyclase toxin interactions with erythrocyte and liposome membranes
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Biochimica et Biophysica Acta (BBA) - Biomembranes, 2004
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Interaction with a lipid membrane: a key step in bacterial toxins virulence
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Interaction of Clostridium perfringens Iota-Toxin with Lipid Bilayer Membranes. DEMONSTRATION OF CHANNEL FORMATION BY THE ACTIVATED BINDING COMPONENT Ib AND CHANNEL BLOCK BY THE ENZYME COMPONENT Ia
Roland Benz
Journal of Biological Chemistry, 2001
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Interaction of Clonixin with EPC Liposomes Used as Membrane Models
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Differences in the Carboxy-Terminal (Putative Phospholipid Binding) Domains of Clostridium perfringens and Clostridium bifermentans Phospholipases C Influence the Hemolytic and Lethal Properties of These Enzymes
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Infection and Immunity, 1999
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Membrane Restructuring by Bordetella pertussis Adenylate Cyclase Toxin, a Member of the RTX Toxin Family
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Clostridium perfringens Beta2 toxin forms highly cation-selective channels in lipid bilayers
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Tyrosine 331 and phenylalanine 334 in Clostridium perfringens α-toxin are essential for cytotoxic activity
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The catalytic domains of clostridium sordellii lethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid
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