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Activation and mechanism of Clostridium septicum alpha toxin.
Clostridium septicum alpha-toxin is proteolytically activated by furin.
Disulfide-bond scanning reveals assembly state and ß-strand tilt angle of the PFO ß-barrel.
Isolation of a tryptic fragment from Clostridium perfringens theta-toxin that contains sites for membrane binding and self-aggregation.
Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin.