Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. - Wikidata - awgldk - TriplyDB

Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.

Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.

http://www.wikidata.org/entity/Q33732672

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The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytes The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins Inerolysin, a cholesterol-dependent cytolysin produced by Lactobacillus iners Perfringolysin O Theta Toxin as a Tool to Monitor the Distribution and Inhomogeneity of Cholesterol in Cellular Membranes Multifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes Conformational changes during pore formation by the perforin-related protein pleurotolysin Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins Listeriolysin o is strongly immunogenic independently of its cytotoxic activity Single point mutation in Vibrio cholerae cytolysin compromises the membrane pore-formation mechanism of the toxin CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.Disentangling the roles of cholesterol and CD59 in intermedilysin pore formation.Revisiting the membrane interaction mechanism of a membrane-damaging β-barrel pore-forming toxin Vibrio cholerae cytolysin.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.The Apicomplexan CDC/MACPF-like pore-forming proteins.An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.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.Functional mapping of the lectin activity site on the β-prism domain of vibrio cholerae cytolysin: implications for the membrane pore-formation mechanism of the toxin.Membrane assembly of the cholesterol-dependent cytolysin pore complex.The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.Listeria monocytogenes induces an interferon-enhanced activation of the integrated stress response that is detrimental for resolution of infection in mice Cholesterol selectively activates canonical Wnt signalling over non-canonical Wnt signalling.The impact of pneumolysin on the macrophage response to Streptococcus pneumoniae is strain-dependent.Arcanolysin is a cholesterol-dependent cytolysin of the human pathogen Arcanobacterium haemolyticum.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Streptococcus pneumoniae translocates into the myocardium and forms unique microlesions that disrupt cardiac function.Effects of MACPF/CDC proteins on lipid membranes.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O Anthrolysin O and fermentation products mediate the toxicity of Bacillus anthracis to lung epithelial cells under microaerobic conditions.The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cells The cholesterol-dependent cytolysins pneumolysin and streptolysin O require binding to red blood cell glycans for hemolytic activity Characterization of putative cholesterol recognition/interaction amino acid consensus-like motif of Campylobacter jejuni cytolethal distending toxin C The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.Degradation products of the extracellular pathogen Streptococcus pneumoniae access the cytosol via its pore-forming toxin.Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9 Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration.Reconstitution of cholesterol-dependent vaginolysin into tethered phospholipid bilayers: implications for bioanalysis.Cholesterol depletion reduces entry of Campylobacter jejuni cytolethal distending toxin and attenuates intoxication of host cells

P2860

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P2860

Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.

http://www.wikidata.org/entity/Q33732672

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Only two amino acids are essen ...... terol at the membrane surface.

@ast

Only two amino acids are essen ...... terol at the membrane surface.

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type

label

Only two amino acids are essen ...... terol at the membrane surface.

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Only two amino acids are essen ...... terol at the membrane surface.

@en

prefLabel

Only two amino acids are essen ...... terol at the membrane surface.

@ast

Only two amino acids are essen ...... terol at the membrane surface.

@en

P1433

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PNAS.0911581107

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Only two amino acids are essen ...... terol at the membrane surface.

@en

P2093

Allison J Farrand

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

Arthur E Johnson

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

Eileen M Hotze

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

Rodney K Tweten

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Stephanie LaChapelle

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P2860

Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins

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

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

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

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

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

Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin.

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

The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation

Specific roles for lipids in virus fusion and exit. Examples from the alphaviruses.

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10.1073/PNAS.0911581107

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107

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2010-02-09T00:00:00Z

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41419510

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20145114

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P932

2840085

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