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Inhibiting bacterial toxins by channel blockage.

Inhibiting bacterial toxins by channel blockage.

http://www.wikidata.org/entity/Q36794160

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Chloroquine derivatives block the translocation pores and inhibit cellular entry of Clostridium botulinum C2 toxin and Bacillus anthracis lethal toxin.

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Inhibiting bacterial toxins by channel blockage.

http://www.wikidata.org/entity/Q36794160

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Inhibiting bacterial toxins by channel blockage.

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Inhibiting bacterial toxins by channel blockage.

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type

label

Inhibiting bacterial toxins by channel blockage.

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Inhibiting bacterial toxins by channel blockage.

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prefLabel

Inhibiting bacterial toxins by channel blockage.

@ast

Inhibiting bacterial toxins by channel blockage.

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Pathogens and disease

P1476

Inhibiting bacterial toxins by channel blockage.

@en

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Ekaterina M Nestorovich

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Sergey M Bezrukov

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

P2860

Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins

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

Anti-alpha-hemolysin monoclonal antibodies mediate protection against Staphylococcus aureus pneumonia

Staphylococcus aureus α-toxin: nearly a century of intrigue

Obstructing toxin pathways by targeted pore blockage

Clostridium perfringens epsilon toxin: a malevolent molecule for animals and man?

Ratcheting up protein translocation with anthrax toxin

Atomic structure of anthrax protective antigen pore elucidates toxin translocation

The Protective Antigen Component of Anthrax Toxin Forms Functional Octameric Complexes

Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

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scholarly article

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10.1093/FEMSPD/FTV113

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2

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74

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2015-12-09T00:00:00Z

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26656888

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4830228

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