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• W2093673362 abstract "In this paper we describe reconstructions by electron cryo-microscopy of two oligomeric states of the pore-forming toxin pneumolysin. The results are interpreted by the fitting of atomic models of separated domains to the 3-dimensional electron density maps, revealing two steps in the mechanism of pore formation by the family of cholesterol-binding toxins. We briefly describe the observation of the toxin pore in model membranes and contrast the apparent mechanism of pneumolysin with that of other pore-forming toxins." @default.
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• W2093673362 date "2000-10-01" @default.
• W2093673362 modified "2023-10-16" @default.
• W2093673362 title "Structural basis of pore formation by cholesterol-binding toxins" @default.
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• W2093673362 doi "https://doi.org/10.1016/s1438-4221(00)80049-1" @default.
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