Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregates
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RTX proteins: a highly diverse family secreted by a common mechanismIdentification of two porins in Pelobacter venetianus fermenting high-molecular-mass polyethylene glycolsDifferences in purinergic amplification of osmotic cell lysis by the pore-forming RTX toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the role of pore size.Increased leukotoxin production: Characterization of 100 base pairs within the 530 base pair leukotoxin promoter region of Aggregatibacter actinomycetemcomitans.Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranesGenetic conservation of hlyA determinants and serological conservation of HlyA: basis for developing a broadly cross-reactive subunit Escherichia coli alpha-hemolysin vaccine.Electrifying symbiosis.Epitopes of Escherichia coli alpha-hemolysin: identification of monoclonal antibodies that prevent hemolysisParadoxical lipid dependence of pores formed by the Escherichia coli alpha-hemolysin in planar phospholipid bilayer membranes.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Channel-forming activity and channel size of the RTX toxins ApxI, ApxII, and ApxIII of Actinobacillus pleuropneumoniae.Binding of Pasteurella haemolytica leukotoxin to bovine leukocytesPore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members.Regulation of Actinobacillus actinomycetemcomitans leukotoxin expression: analysis of the promoter regions of leukotoxic and minimally leukotoxic strainsAnalysis of toxinogenic functions associated with the RTX repeat region and monoclonal antibody D12 epitope of Escherichia coli hemolysin.The nodulation-signaling protein NodO from Rhizobium leguminosarum biovar viciae forms ion channels in membranesRole of pore-forming toxins in neonatal sepsisActivation of bovine neutrophils by partially purified Pasteurella haemolytica leukotoxinAlpha-hemolysin contributes to the pathogenicity of piliated digalactoside-binding Escherichia coli in the kidney: efficacy of an alpha-hemolysin vaccine in preventing renal injury in the BALB/c mouse model of pyelonephritis.Calcium is required for binding of Escherichia coli hemolysin (HlyA) to erythrocyte membranesDomains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranesAerolysin of Aeromonas sobria: evidence for formation of ion-permeable channels and comparison with alpha-toxin of Staphylococcus aureus.Immunoserological comparison of 104-kilodalton proteins associated with hemolysis and cytolysis in Actinobacillus pleuropneumoniae, Actinobacillus suis, Pasteurella haemolytica, and Escherichia coliMembrane association and destabilization by Aggregatibacter actinomycetemcomitans leukotoxin requires changes in secondary structuresSingle-Walled Carbon Nanotubes: Mimics of Biological Ion Channels.The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives.[Ca2+]i Oscillations and IL-6 Release Induced by α-Hemolysin from Escherichia coli Require P2 Receptor Activation in Renal Epithelia.Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function.The role of specific surface loop regions in determining the function of the imipenem-specific pore protein OprD of Pseudomonas aeruginosa.Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.Porcine CD18 mediates Actinobacillus pleuropneumoniae ApxIII species-specific toxicity.The major outer membrane protein of Acidovorax delafieldii is an anion-selective porin.Characterization of monoclonal antibodies against alpha-hemolysin of Escherichia coli.Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola.Effects of temperature, time, and toxin concentration on lesion formation by the Escherichia coli hemolysin.Pore formation by the Escherichia coli alpha-hemolysin: role for mediator release from human inflammatory cellsAggregatibacter actinomycetemcomitans leukotoxin cytotoxicity occurs through bilayer destabilization.Relevance of fatty acid covalently bound to Escherichia coli alpha-hemolysin and membrane microdomains in the oligomerization process.Enterotoxin: The Toxin Forms Highly Cation-Selective Channels in Lipid Bilayers
P2860
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P2860
Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregates
description
1989 nî lūn-bûn
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1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
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1989年學術文章
@zh
1989年學術文章
@zh-hant
name
Pore formation by the Escheric ...... of the pore-forming aggregates
@en
type
label
Pore formation by the Escheric ...... of the pore-forming aggregates
@en
prefLabel
Pore formation by the Escheric ...... of the pore-forming aggregates
@en
P2093
P2860
P1476
Pore formation by the Escheric ...... of the pore-forming aggregates
@en
P2093
P2860
P304
P407
P577
1989-03-01T00:00:00Z