Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate.
about
The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytesThe cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyCholesterol-dependent cytolysins, a family of versatile pore-forming toxinsCharacterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domainRedefining 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 MembranesMultifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenesConformational changes during pore formation by the perforin-related protein pleurotolysinA new model for pore formation by cholesterol-dependent cytolysinsCrystal structure of listeriolysin O reveals molecular details of oligomerization and pore formationThe 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.Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsDisulfide-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.Vertical 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.Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysinsMapping dominant-negative mutations of anthrax protective antigen by scanning mutagenesis.Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin.Molecular basis of listeriolysin O pH dependence.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Effects of MACPF/CDC proteins on lipid membranes.Identification of invasive serotype 1 pneumococcal isolates that express nonhemolytic pneumolysin.Cardiac myocyte dysfunction induced by streptolysin O is membrane pore and calcium dependent.Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.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 cytolysinDominant-negative inhibitors of the Clostridium perfringens epsilon-toxin.The influence of natural lipid asymmetry upon the conformation of a membrane-inserted protein (perfringolysin O)Insights into structure and activity of natural compound inhibitors of pneumolysin.Intrinsic repair protects cells from pore-forming toxins by microvesicle shedding.Domain 4 (D4) of Perfringolysin O to Visualize Cholesterol in Cellular Membranes-The Update.The mystery behind membrane insertion: a review of the complement membrane attack complexListeriolysin O: from bazooka to Swiss army knife.
P2860
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P2860
Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate.
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին 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
Arresting pore formation of a ...... t from a prepore intermediate.
@ast
Arresting pore formation of a ...... t from a prepore intermediate.
@en
type
label
Arresting pore formation of a ...... t from a prepore intermediate.
@ast
Arresting pore formation of a ...... t from a prepore intermediate.
@en
prefLabel
Arresting pore formation of a ...... t from a prepore intermediate.
@ast
Arresting pore formation of a ...... t from a prepore intermediate.
@en
P2093
P2860
P356
P1476
Arresting pore formation of a ...... t from a prepore intermediate.
@en
P2093
A E Johnson
E M Wilson-Kubalek
M W Parker
R K Tweten
P2860
P304
P356
10.1074/JBC.M009865200
P407
P577
2000-12-01T00:00:00Z