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Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.
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Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.
Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes. Mol Cell. 2000 Nov; 6(5):1233-42.
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PubMed
subject areas
Bacterial Toxins
Bacterial Toxins
Cell Membrane
Cell Membrane
Cholesterol
Cholesterol
Clostridium perfringens
Clostridium perfringens
Hemolysin Proteins
Hemolysin Proteins
Kinetics
Kinetics
Lipid Bilayers
Lipid Bilayers
Liposomes
Liposomes
Microscopy, Fluorescence
Microscopy, Fluorescence
Models, Biological
Models, Biological
Phospholipids
Phospholipids
Protein Binding
Protein Binding
Protein Structure, Secondary
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Structure, Tertiary
Protein Transport
Protein Transport
Time Factors
Time Factors
authors with profiles
Rodney Kim Tweten