Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol. - Wikidata - wikimedia - TriplyDB

Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.

Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.

http://www.wikidata.org/entity/Q34635171

about

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 Obstructing toxin pathways by targeted pore blockage Crucial role of perfringolysin O D1 domain in orchestrating structural transitions leading to membrane-perforating pores: a hydrogen-deuterium exchange study.Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O Perfringolysin O: The Underrated Clostridium perfringens Toxin?Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin O.The influence of natural lipid asymmetry upon the conformation of a membrane-inserted protein (perfringolysin O)Clostridial toxins.Bacterial toxins and the nervous system: neurotoxins and multipotential toxins interacting with neuronal cells.Domain 4 (D4) of Perfringolysin O to Visualize Cholesterol in Cellular Membranes-The Update.Listeriolysin O: from bazooka to Swiss army knife.Mechanistic Insights into the Cholesterol-dependent Binding of Perfringolysin O-based Probes and Cell Membranes.Interaction of Cholesterol with Perfringolysin O: What Have We Learned from Functional Analysis?

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P2860

Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.

http://www.wikidata.org/entity/Q34635171

description

2007 nî lūn-bûn

@nan

2007 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հունիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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name

Conformational changes that ef ...... O upon binding to cholesterol.

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Conformational changes that ef ...... O upon binding to cholesterol.

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Conformational changes that ef ...... O upon binding to cholesterol.

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type

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Conformational changes that ef ...... O upon binding to cholesterol.

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Conformational changes that ef ...... O upon binding to cholesterol.

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Conformational changes that ef ...... O upon binding to cholesterol.

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Conformational changes that ef ...... O upon binding to cholesterol.

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Conformational changes that ef ...... O upon binding to cholesterol.

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Conformational changes that ef ...... O upon binding to cholesterol.

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P1433

Journal of Biological Chemistry

P1476

Conformational changes that ef ...... O upon binding to cholesterol

@en

P2093

Andreas Holzenburg

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

Arthur E Johnson

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

Christos G Savva

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

P2860

Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins

Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form

How to measure and predict the molar absorption coefficient of a protein

From lanosterol to cholesterol: structural evolution and differential effects on lipid bilayers

Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy.

Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane

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.

Pore-forming protein structure analysis in membranes using multiple independent fluorescence techniques.

P304

22629-22637

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scholarly article

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10.1074/JBC.M703207200

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31

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282

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Alejandro P Heuck

P577

2007-06-05T00:00:00Z

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P698

17553799

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