Structure and Function of the Two-Component Cytotoxins of Staphylococcus aureus - Learnings for Designing Novel Therapeutics.

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Structure and Function of the Two-Component Cytotoxins of Staphylococcus aureus - Learnings for Designing Novel Therapeutics.

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2017 nî lūn-bûn

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2017年学术文章

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Structure and Function of the ...... Designing Novel Therapeutics.

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Structure and Function of the ...... Designing Novel Therapeutics.

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Structure and Function of the ...... Designing Novel Therapeutics.

@en

Structure and Function of the ...... Designing Novel Therapeutics.

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Structure and Function of the ...... Designing Novel Therapeutics.

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Structure and Function of the ...... Designing Novel Therapeutics.

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P1476

Structure and Function of the ...... Designing Novel Therapeutics.

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Adriana Badarau

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Eszter Nagy

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Nikolina Trstenjak

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P2860

Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components

Staphylococcus aureus α-toxin: nearly a century of intrigue

The pore-forming haemolysins of bacillus cereus: a review

The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins

Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel

A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins

2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structure

Residues Essential for Panton-Valentine Leukocidin S Component Binding to Its Cell Receptor Suggest Both Plasticity and Adaptability in Its Interaction Surface

Mechanism of action and in vivo efficacy of a human-derived antibody against Staphylococcus aureus α-hemolysin

Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins

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scholarly article

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10.1007/5584_2016_200

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English

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2017-04-29T00:00:00Z

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28455832

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