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

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

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

http://www.wikidata.org/entity/Q30164706

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The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly Human perforin employs different avenues to damage membranes 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 Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins Perfringolysin O Theta Toxin as a Tool to Monitor the Distribution and Inhomogeneity of Cholesterol in Cellular Membranes Obstructing toxin pathways by targeted pore blockage The Transition from Closed to Open Conformation of Treponema pallidum Outer Membrane-associated Lipoprotein TP0453 Involves Membrane Sensing and Integration by Two Amphipathic Helices Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation Listeriolysin o is strongly immunogenic independently of its cytotoxic activity Consensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAIN Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins Structural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.Membrane damage by an α-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered steps Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.TprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structure Membrane assembly of the cholesterol-dependent cytolysin pore complex.Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2 Complexin 2 modulates vesicle-associated membrane protein (VAMP) 2-regulated zymogen granule exocytosis in pancreatic acini.Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.Direct injection of functional single-domain antibodies from E. coli into human cells.The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation The SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release.Efficient isolation of Pseudomonas aeruginosa type III secretion translocators and assembly of heteromeric transmembrane pores in model membranes.Arcanolysin is a cholesterol-dependent cytolysin of the human pathogen Arcanobacterium haemolyticum.Magnetically immobilized nanoporous giant proteoliposomes as a platform for biosensing.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Membrane damage during Listeria monocytogenes infection triggers a caspase-7 dependent cytoprotective response SV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release.Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.Expression, localization, and functional role for synaptotagmins in pancreatic acinar cells.Perfringolysin O: The Underrated Clostridium perfringens Toxin?Listeriolysin O: a key protein of Listeria monocytogenes with multiple functions.Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin Protein arcs may form stable pores in lipid membranes.The influence of natural lipid asymmetry upon the conformation of a membrane-inserted protein (perfringolysin O)

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P2860

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

http://www.wikidata.org/entity/Q30164706

description

2003 nî lūn-bûn

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2003 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2003 թվականի մայիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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

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

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type

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

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

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prefLabel

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

@ast

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

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P1433

Journal of Biological Chemistry

P1476

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

@en

P2093

Alejandro P Heuck

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

Arthur E Johnson

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

Rodney K Tweten

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

P2860

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

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

How to measure and predict the molar absorption coefficient of a protein

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.

Pore-forming protein structure analysis in membranes using multiple independent fluorescence techniques.

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

Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization.

The family of thiol-activated, cholesterol-binding cytolysins.

Pore-forming toxins.

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31218-31225

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scholarly article

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10.1074/JBC.M303151200

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P433

33

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278

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2003-05-30T00:00:00Z

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12777381

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