Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.
about
The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyA very late viral protein triggers the lytic release of SV40Human perforin employs different avenues to damage membranesCholesterol-dependent cytolysins, a family of versatile pore-forming toxinsCholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O bindingRedefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysinsPerfringolysin O Theta Toxin as a Tool to Monitor the Distribution and Inhomogeneity of Cholesterol in Cellular MembranesA new model for pore formation by cholesterol-dependent cytolysinsFunctional characterization of a melittin analog containing a non-natural tryptophan analogCellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracisThe Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.Plasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected].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 cytolysinsMembrane damage by an α-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered stepsDisulfide-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.Identification of a prepore large-complex stage in the mechanism of action of Clostridium perfringens enterotoxinVertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membraneAssembly and topography of the prepore complex in cholesterol-dependent cytolysins.Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin.Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate.Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysinsOnly two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin.Comprehensive measurement of respiratory activity in permeabilized cells using extracellular flux analysisThe domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formationBax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis.Molecular basis of listeriolysin O pH dependence.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.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin OConformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.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.The assembly dynamics of the cytolytic pore toxin ClyA.Interaction of heat shock protein 70 with membranes depends on the lipid environment.Differential sensitivity of types 1 and 2 cholecystokinin receptors to membrane cholesterol.Perfringolysin O: The Underrated Clostridium perfringens Toxin?
P2860
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P2860
Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Mechanism of membrane insertio ...... oupled conformational changes.
@ast
Mechanism of membrane insertio ...... oupled conformational changes.
@en
type
label
Mechanism of membrane insertio ...... oupled conformational changes.
@ast
Mechanism of membrane insertio ...... oupled conformational changes.
@en
prefLabel
Mechanism of membrane insertio ...... oupled conformational changes.
@ast
Mechanism of membrane insertio ...... oupled conformational changes.
@en
P2093
P1433
P1476
Mechanism of membrane insertio ...... oupled conformational changes.
@en
P2093
A E Johnson
R K Tweten
P304
P356
10.1016/S1097-2765(00)00119-2
P577
2000-11-01T00:00:00Z