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

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

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

http://www.wikidata.org/entity/Q30163889

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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-dependent cytolysins, a family of versatile pore-forming toxins 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 Obstructing toxin pathways by targeted pore blockage 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 A new model for pore formation by cholesterol-dependent cytolysins Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process.Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis Crystal Structure of Clostridium perfringens Enterotoxin Displays Features of -Pore-forming Toxins Structure of Complement C6 Suggests a Mechanism for Initiation and Unidirectional, Sequential Assembly of Membrane Attack Complex (MAC)Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59 Defining the interaction of perforin with calcium and the phospholipid membrane Structure of the poly-C9 component of the complement membrane attack complex AFM study on the electric-field effects on supported bilayer lipid membranes 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 Apicomplexan CDC/MACPF-like pore-forming proteins.Plasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected].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.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Membrane assembly of the cholesterol-dependent cytolysin pore complex.Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.An in vitro assay for entry into cilia reveals unique properties of the soluble diffusion barrier Large-scale analysis of high-speed atomic force microscopy data sets using adaptive image processing.Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation Efficient isolation of Pseudomonas aeruginosa type III secretion translocators and assembly of heteromeric transmembrane pores in model membranes.Perforin rapidly induces plasma membrane phospholipid flip-flop Computational reconstruction of multidomain proteins using atomic force microscopy data.Effects of MACPF/CDC proteins on lipid membranes.Perforin: structure, function, and role in human immunopathology.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

P2860

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P2860

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

http://www.wikidata.org/entity/Q30163889

description

2004 nî lūn-bûn

@nan

2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի օգոստոսին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

@wuu

name

Vertical collapse of a cytolys ...... beta-hairpins to the membrane

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Vertical collapse of a cytolys ...... beta-hairpins to the membrane

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type

label

Vertical collapse of a cytolys ...... beta-hairpins to the membrane

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Vertical collapse of a cytolys ...... beta-hairpins to the membrane

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prefLabel

Vertical collapse of a cytolys ...... beta-hairpins to the membrane

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Vertical collapse of a cytolys ...... beta-hairpins to the membrane

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P1433

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P356

SJ.EMBOJ.7600350

P1433

The EMBO Journal

P1476

Vertical collapse of a cytolys ...... beta-hairpins to the membrane

@en

P2093

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

Bacillus thuringiensis and its pesticidal crystal proteins

Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation

Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel

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

MOLMOL: a program for display and analysis of macromolecular structures

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.

P304

3206-3215

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scholarly article

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10.1038/SJ.EMBOJ.7600350

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P433

16

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23

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2004-08-05T00:00:00Z

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8412980

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15297878

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transmembrane protein

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514522

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