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

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

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

http://www.wikidata.org/entity/Q30167667

about

The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins Rapid assembly of a multimeric membrane protein pore Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins Disentangling the roles of cholesterol and CD59 in intermedilysin pore formation.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.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.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Membrane assembly of the cholesterol-dependent cytolysin pore complex.Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.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.Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.The solution structure and oligomerization behavior of two bacterial toxins: pneumolysin and perfringolysin O.Development of a single-gene, signature-tag-based approach in combination with alanine mutagenesis to identify listeriolysin O residues critical for the in vivo survival of Listeria monocytogenes.Construction and immunological characterization of a novel nontoxic protective pneumolysin mutant for use in future pneumococcal vaccines.Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.Perfringolysin O: The Underrated Clostridium perfringens Toxin?Cloning, functional characterization, and mode of action of a novel insecticidal pore-forming toxin, sphaericolysin, produced by Bacillus sphaericus.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Antibody-mediated neutralization of perfringolysin o for intracellular protein delivery.Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity.Use of mutant 125I-perfringolysin O to probe transport and organization of cholesterol in membranes of animal cells.Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin Listeriolysin O as a strong immunogenic molecule for the development of new anti-tumor vaccines The influence of natural lipid asymmetry upon the conformation of a membrane-inserted protein (perfringolysin O)Clostridial toxins.Insights into structure and activity of natural compound inhibitors of pneumolysin.Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: effect of tetracycline and trehalose.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.Listeria monocytogenes impairs SUMOylation for efficient infection.Immunization with genetic toxoids of the Arcanobacterium pyogenes cholesterol-dependent cytolysin, pyolysin, protects mice against infection.Measuring kinetic drivers of pneumolysin pore structure.Incomplete pneumolysin oligomers form membrane pores.

P2860

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P2860

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

http://www.wikidata.org/entity/Q30167667

description

2002 nî lūn-bûn

@nan

2002 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հունվարին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Monomer-monomer interactions d ...... olesterol-dependent cytolysin.

@ast

Monomer-monomer interactions d ...... olesterol-dependent cytolysin.

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type

label

Monomer-monomer interactions d ...... olesterol-dependent cytolysin.

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Monomer-monomer interactions d ...... olesterol-dependent cytolysin.

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prefLabel

Monomer-monomer interactions d ...... olesterol-dependent cytolysin.

@ast

Monomer-monomer interactions d ...... olesterol-dependent cytolysin.

@en

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P1433

Journal of Biological Chemistry

P1476

Monomer-monomer interactions d ...... olesterol-dependent cytolysin.

@en

P2093

Arthur E Johnson

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

Daniel M Czajkowsky

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

Eileen M Hotze

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

Rodney K Tweten

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

Zhifeng Shao

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

P2860

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

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

Crystal structure of the anthrax toxin protective antigen

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

Beta-barrel pore-forming toxins: intriguing dimorphic proteins.

The alpha and the beta: protein translocation across mitochondrial and plastid outer membranes.

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

Anthrax protective antigen: prepore-to-pore conversion.

Identification of residues lining the anthrax protective antigen channel.

The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH.

P304

11597-11605

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scholarly article

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10.1074/JBC.M111039200

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13

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P478

277

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Alejandro P Heuck

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2002-01-17T00:00:00Z

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11799121

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