Membrane assembly of the cholesterol-dependent cytolysin pore complex. - Test2 - elhamkhani - TriplyDB

Membrane assembly of the cholesterol-dependent cytolysin pore complex.

Membrane assembly of the cholesterol-dependent cytolysin pore complex.

http://www.wikidata.org/entity/Q30155494

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Interactions between Autophagy and Bacterial Toxins: Targets for Therapy?Obstructing toxin pathways by targeted pore blockage Biological effects of listeriolysin O: implications for vaccination Multifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes More than a pore: the cellular response to cholesterol-dependent cytolysins Conformational changes during pore formation by the perforin-related protein pleurotolysin Listeriolysin O Membrane Damaging Activity Involves Arc Formation and Lineaction -- Implication for Listeria monocytogenes Escape from Phagocytic Vacuole Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly A new model for pore formation by cholesterol-dependent cytolysins Manipulating the Lewis antigen specificity of the cholesterol-dependent cytolysin lectinolysin Structure and secretion of CofJ, a putative colonization factor of enterotoxigenic Escherichia coli CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.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.Decreasing Transmembrane Segment Length Greatly Decreases Perfringolysin O Pore Size.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.Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.Cysteine-scanning mutagenesis supports the importance of Clostridium perfringens enterotoxin amino acids 80 to 106 for membrane insertion and pore formation Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes Induction of endoplasmic reticulum stress and unfolded protein response constitutes a pathogenic strategy of group A streptococcus Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Effects of MACPF/CDC proteins on lipid membranes.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cells The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.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.Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin.Protective role of the dynamin inhibitor Dynasore against the cholesterol-dependent cytolysin of Trueperella pyogenes Perfringolysin O: The Underrated Clostridium perfringens Toxin?Listeriolysin O Affects the Permeability of Caco-2 Monolayer in a Pore-Dependent and Ca2+-Independent Manner.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Dual modes of membrane binding direct pore formation by Streptolysin O.Identification and characterization of the first cholesterol-dependent cytolysins from Gram-negative bacteria Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin O.Antibody-mediated neutralization of perfringolysin o for intracellular protein delivery.Vaginolysin drives epithelial ultrastructural responses to Gardnerella vaginalis.Insights into structure and activity of natural compound inhibitors of pneumolysin.

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P2860

Membrane assembly of the cholesterol-dependent cytolysin pore complex.

http://www.wikidata.org/entity/Q30155494

description

2011 nî lūn-bûn

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2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2011 թվականի հուլիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Membrane assembly of the cholesterol-dependent cytolysin pore complex.

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Membrane assembly of the cholesterol-dependent cytolysin pore complex.

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Membrane assembly of the cholesterol-dependent cytolysin pore complex.

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Membrane assembly of the cholesterol-dependent cytolysin pore complex.

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Membrane assembly of the cholesterol-dependent cytolysin pore complex.

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Membrane assembly of the cholesterol-dependent cytolysin pore complex.

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J.BBAMEM.2011.07.036

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Biochimica et Biophysica Acta

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Membrane assembly of the cholesterol-dependent cytolysin pore complex.

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Eileen M Hotze

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Rodney K Tweten

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P2860

Lipid rafts clustering and signalling by listeriolysin O

Purification, characterization, and toxicity of the sulfhydryl-activated hemolysin listeriolysin O from Listeria monocytogenes

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

Characterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domain

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

Histone modifications induced by a family of bacterial toxins

A common fold mediates vertebrate defense and bacterial attack

Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense

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

The structural basis for membrane binding and pore formation by lymphocyte perforin

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1028-1038

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