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Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

http://www.wikidata.org/entity/Q30160079

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Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components Obstructing toxin pathways by targeted pore blockage Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins Identification of a crucial residue required for Staphylococcus aureus LukAB cytotoxicity and receptor recognition.Distinction between pore assembly by staphylococcal alpha-toxin versus leukotoxins.Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.The bicomponent pore-forming leucocidins of Staphylococcus aureus Inhibiting bacterial toxins by channel blockage.Internalization of staphylococcal leukotoxins that bind and divert the C5a receptor is required for intracellular Ca2+mobilization by human neutrophils

P2860

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P2860

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

http://www.wikidata.org/entity/Q30160079

description

2005 nî lūn-bûn

@nan

2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

@ast

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

@en

type

label

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

@ast

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

@en

prefLabel

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

@ast

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

@en

P1433

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P356

P1433

Journal of Biological Chemistry

P1476

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

@en

P2093

George Miles

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

Lakmal Jayasinghe

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

P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

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

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

Involvement of Panton-Valentine leukocidin-producing Staphylococcus aureus in primary skin infections and pneumonia

Bacterial two-component and hetero-heptameric pore-forming cytolytic toxins: structures, pore-forming mechanism, and organization of the genes

Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxins

Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.

The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis.

Beta-barrel membrane protein folding and structure viewed through the lens of alpha-hemolysin.

P304

2205-2214

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P31

scholarly article

P356

10.1074/JBC.M510842200

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4

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281

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2005-11-03T00:00:00Z

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16269405

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