Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin - Wikidata - awgldk - TriplyDB

Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin

Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin

http://www.wikidata.org/entity/Q37102350

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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 Characterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domain Multifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes The pore-forming haemolysins of bacillus cereus: a review Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59 Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.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.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.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Membrane assembly of the cholesterol-dependent cytolysin pore complex.Imaging enzyme-triggered self-assembly of small molecules inside live cells Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.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.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cells Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9 Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Crystal structure of cytotoxin protein suilysin from Streptococcus suis.The helix-loop-helix motif at the N terminus of HalI is essential for its immunity function against halocin C8.Clostridial toxins.Bacterial toxins and the nervous system: neurotoxins and multipotential toxins interacting with neuronal cells.Identification of the high affinity binding site in the Streptococcus intermedius toxin intermedilysin for its membrane receptor, the human complement regulator CD59.Taurine Boosts Cellular Uptake of Small D-Peptides for Enzyme-Instructed Intracellular Molecular Self-Assembly Intermedilysin-receptor interactions during assembly of the pore complex: assembly intermediates increase host cell susceptibility to complement-mediated lysis GILT is a critical host factor for Listeria monocytogenes infection.The diversity of receptor recognition in cholesterol-dependent cytolysins.Genetic and biochemical diversity of Gardnerella vaginalis strains isolated from women with bacterial vaginosis.

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P2860

Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin

http://www.wikidata.org/entity/Q37102350

description

article científic

@ca

article scientifique

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articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 05 April 2007

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Specific protein-membrane cont ...... holesterol-dependent cytolysin

@en

Specific protein-membrane cont ...... olesterol-dependent cytolysin.

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type

label

Specific protein-membrane cont ...... holesterol-dependent cytolysin

@en

Specific protein-membrane cont ...... olesterol-dependent cytolysin.

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prefLabel

Specific protein-membrane cont ...... holesterol-dependent cytolysin

@en

Specific protein-membrane cont ...... olesterol-dependent cytolysin.

@nl

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Journal of Biological Chemistry

P1476

Specific protein-membrane cont ...... holesterol-dependent cytolysin

@en

P2093

Arthur E Johnson

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

Casie E Soltani

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

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

VMD: visual molecular dynamics

Structural basis of pore formation by the bacterial toxin pneumolysin

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.

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

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.

Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate.

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15709-15716

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scholarly article

P356

10.1074/JBC.M701173200

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P407

P433

21

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282

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2007-04-05T00:00:00Z

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17412689

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3746338

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