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Molecular biology of the pore-forming cytolysins from Staphylococcus aureus, α- and γ-hemolysin and leykocidin
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Essential binding of LukF of staphylococcal y-hemolysin followed by the binding of Hyll for the hemolysis of human erythrocytes
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Sequential binding of staphylococcal y-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface
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Assembly of Staphylococcus aureus y-hemolysin into pore-forming ring-shaped complex on the surface of human erythrocytes
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Identification of the minimum segment in which the threonine246 residue is a potential phosphorylated site by protein kinase A for the LukS-specific function of staphylococcal leukocidin
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Identification of the essential region for LukS- and Hyll-specific function of staphylococcal leukocidin and y-hemolysin
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Gamma-hemolysin genes in the same family with lukF and lukS genes in methicillin resistant
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Rahman, A., Izaki, K., and Kamio, Y., Gamma-hemolysin genes in the same family with lukF and lukS genes in methicillin resistant. Staphylococcus aureus, Biosci. Biotechnol. Biochem., 57, 1234-1236 (1993).
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Existence of a new protein component with the same function as the LukF component of leukocidin or y-hemolysin and its gene in Staphylococcus aureus P83
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