Mechanistic Insights into the Cholesterol-dependent Binding of Perfringolysin O-based Probes and Cell Membranes.

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Interaction of Cholesterol with Perfringolysin O: What Have We Learned from Functional Analysis?Missing elimination via membrane vesicle shedding contributes to the diminished calcium sensitivity of listeriolysin O

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Mechanistic Insights into the Cholesterol-dependent Binding of Perfringolysin O-based Probes and Cell Membranes.

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http://www.wikidata.org/entity/Q45786843

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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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2017年學術文章

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2017年學術文章

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name

Mechanistic Insights into the ...... sed Probes and Cell Membranes.

@en

Mechanistic Insights into the ...... sed Probes and Cell Membranes.

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type

Item

label

Mechanistic Insights into the ...... sed Probes and Cell Membranes.

@en

Mechanistic Insights into the ...... sed Probes and Cell Membranes.

@nl

prefLabel

Mechanistic Insights into the ...... sed Probes and Cell Membranes.

@en

Mechanistic Insights into the ...... sed Probes and Cell Membranes.

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P1476

Mechanistic Insights into the ...... sed Probes and Cell Membranes.

@en

P2093

Benjamin B Johnson

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

Mariana Breña

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

P2860

The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly

Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding

Perfringolysin O Theta Toxin as a Tool to Monitor the Distribution and Inhomogeneity of Cholesterol in Cellular Membranes

Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis

The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.

Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.

Membrane assembly of the cholesterol-dependent cytolysin pore complex.

Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.

Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin.

Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.

P2888

s41598-017-14002-x

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scholarly article

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10.1038/S41598-017-14002-X

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English

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

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Juan Anguita

Alejandro P Heuck

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2017-10-23T00:00:00Z

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1092262024

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29061991

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5653841

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Mechanistic Insights into the Cholesterol-dependent Binding of Perfringolysin O-based Probes and Cell Membranes.

about

P2860

P2860

Mechanistic Insights into the Cholesterol-dependent Binding of Perfringolysin O-based Probes and Cell Membranes.

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type

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P1476

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