The influence of natural lipid asymmetry upon the conformation of a membrane-inserted protein (perfringolysin O). [PDF]
J Biol Chem, 2014 Lin Q, London E.
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Use of mutant 125I-perfringolysin O to probe transport and organization of cholesterol in membranes of animal cells. [PDF]
Proc Natl Acad Sci U S A, 2013 Das A +4 more
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Visualization of cholesterol deposits in lysosomes of Niemann-Pick type C fibroblasts using recombinant perfringolysin O. [PDF]
Orphanet J Rare Dis, 2014 Kwiatkowska K +8 more
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Crucial role of perfringolysin O D1 domain in orchestrating structural transitions leading to membrane-perforating pores: a hydrogen-deuterium exchange study. [PDF]
J Biol Chem, 2014 Kacprzyk-Stokowiec A +5 more
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Transmembrane protein (perfringolysin o) association with ordered membrane domains (rafts) depends upon the raft-associating properties of protein-bound sterol. [PDF]
Biophys J, 2013 Lin Q, London E.
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Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding. [PDF]
Biochemistry, 2009 Flanagan JJ +3 more
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Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin O. [PDF]
J Biol Chem, 2013 Lin Q, London E.
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