P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

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P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

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P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

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P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

@en

P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

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P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

@en

P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

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P1476

P2X-Receptor Antagonists Inhibit the Interaction of S. aureus Hemolysin A with Membranes.

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P2093

Markus Schwiering

http://www.w3.org/2001/XMLSchema#string

Matthias Husmann

http://www.w3.org/2001/XMLSchema#string

Nadja Hellmann

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P2860

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Differences in purinergic amplification of osmotic cell lysis by the pore-forming RTX toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the role of pore size.

Alpha-hemolysin from Escherichia coli uses endogenous amplification through P2X receptor activation to induce hemolysis.

Staphylococcus aureus alpha-hemolysin activates the NLRP3-inflammasome in human and mouse monocytic cells.

Bacterial RTX toxins allow acute ATP release from human erythrocytes directly through the toxin pore.

Oxidized ATP (oATP) attenuates proinflammatory signaling via P2 receptor-independent mechanisms.

P31

scholarly article

P356

10.3390/TOXINS9100332

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2017-10-19T00:00:00Z

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P698

29048353

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P932

5666378

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