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Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect

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Last updated 16 mai 2024
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
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Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
γ-Hemolysin oligomeric structure and effect of its formation on supported lipid bilayers: An AFM Investigation - ScienceDirect
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
Assemblies of pore-forming toxins visualized by atomic force microscopy - ScienceDirect
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
Cryo-EM-based structural insights into supramolecular assemblies of γ- hemolysin from S. aureus reveal the pore formation mechanism - ScienceDirect
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
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Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
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Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes - ScienceDirect
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
Molecular Architecture and Functional Analysis of NetB, a Pore-forming Toxin from Clostridium perfringens - ScienceDirect
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
α-Hemolysin pore formation into a supported phospholipid bilayer using cell-free expression - ScienceDirect
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
α-Hemolysin pore formation into a supported phospholipid bilayer using cell-free expression - ScienceDirect
Membrane binding of pore-forming γ-hemolysin components studied at different lipid compositions - ScienceDirect
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