Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane.
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Obstructing toxin pathways by targeted pore blockageClostridium perfringens epsilon toxin: a malevolent molecule for animals and man?Host cell-induced signaling causes Clostridium perfringens to upregulate production of toxins important for intestinal infectionsClostridium perfringens type A-E toxin plasmidsCryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.The Myelin and Lymphocyte Protein MAL Is Required for Binding and Activity of Clostridium perfringens ε-ToxinRecombinant Alpha, Beta, and Epsilon Toxins of Clostridium perfringens: Production Strategies and Applications as Veterinary VaccinesClostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysinGene-trap mutagenesis identifies mammalian genes contributing to intoxication by Clostridium perfringens ε-toxinClostridium perfringens epsilon toxin targets granule cells in the mouse cerebellum and stimulates glutamate releaseSubunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.Immunization with a novel Clostridium perfringens epsilon toxin mutant rETX(Y196E)-C confers strong protection in mice.Identification of Small Molecule Inhibitors of Clostridium perfringens ε-Toxin Cytotoxicity Using a Cell-Based High-Throughput ScreenMapping of the continuous epitopes displayed on the Clostridium perfringens type D epsilon-toxin.Highly sensitive sandwich immunoassay and immunochromatographic test for the detection of Clostridial epsilon toxin in complex matrices.Clostridium perfringens epsilon-toxin increases permeability of single perfused microvessels of rat mesenteryEvidence for a prepore stage in the action of Clostridium perfringens epsilon toxin.Prevention and treatment of Clostridium perfringens epsilon toxin intoxication in mice with a neutralizing monoclonal antibody (c4D7) produced in Nicotiana benthamiana.Polymer partitioning and ion selectivity suggest asymmetrical shape for the membrane pore formed by epsilon toxin.Epsilon-toxin is required for most Clostridium perfringens type D vegetative culture supernatants to cause lethality in the mouse intravenous injection modelProteolytic processing and activation of Clostridium perfringens epsilon toxin by caprine small intestinal contents.Oligomerization of Clostridium perfringens epsilon toxin is dependent upon caveolins 1 and 2.Both epsilon-toxin and beta-toxin are important for the lethal properties of Clostridium perfringens type B isolates in the mouse intravenous injection modelFunctional analysis of neutralizing antibodies against Clostridium perfringens epsilon-toxinVirulence plasmid diversity in Clostridium perfringens type D isolatesClostridium Perfringens Epsilon Toxin Binds to Membrane Lipids and Its Cytotoxic Action Depends on SulfatideAccumulation of Clostridium perfringens epsilon-toxin in the mouse kidney and its possible biological significance.Toxin plasmids of Clostridium perfringens.Diagnosis of Clostridium perfringens intestinal infections in sheep and goats.Dominant-negative inhibitors of the Clostridium perfringens epsilon-toxin.Bacterial toxins and the nervous system: neurotoxins and multipotential toxins interacting with neuronal cells.Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.Clostridium perfringens epsilon-toxin forms a heptameric pore within the detergent-insoluble microdomains of Madin-Darby canine kidney cells and rat synaptosomes.F199E substitution reduced toxicity of Clostridium perfringens epsilon toxin by depriving the receptor binding capability.Identification of a lambda toxin-negative Clostridium perfringens strain that processes and activates epsilon prototoxin intracellularly.Clostridium perfringens epsilon toxin is cytotoxic for human renal tubular epithelial cells.Pore-forming epsilon toxin causes membrane permeabilization and rapid ATP depletion-mediated cell death in renal collecting duct cells.The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless of their aggregation state.Detergent-resistant membrane microdomains facilitate Ib oligomer formation and biological activity of Clostridium perfringens iota-toxin.Effect of epsilon toxin-GFP on MDCK cells and renal tubules in vivo.
P2860
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P2860
Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Cleavage of a C-terminal pepti ...... in the synaptosomal membrane.
@en
type
label
Cleavage of a C-terminal pepti ...... in the synaptosomal membrane.
@en
prefLabel
Cleavage of a C-terminal pepti ...... in the synaptosomal membrane.
@en
P2093
P2860
P356
P1476
Cleavage of a C-terminal pepti ...... in the synaptosomal membrane.
@en
P2093
P2860
P304
13778-13783
P356
10.1074/JBC.M011527200
P407
P577
2001-02-01T00:00:00Z