Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family.
about
Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two componentsThe pore-forming haemolysins of bacillus cereus: a reviewStructural Insights into Clostridium perfringens Delta Toxin Pore FormationMolecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxinsHow do microbes evade neutrophil killing?Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxinsGrafting synthetic transmembrane units to the engineered low-toxicity α-hemolysin to restore its hemolytic activity.Distinction between pore assembly by staphylococcal alpha-toxin versus leukotoxins.Homologous versus heterologous interactions in the bicomponent staphylococcal gamma-haemolysin pore.The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis.Interactions of peptides with a protein pore.Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus.Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.Bacterial survival amidst an immune onslaught: the contribution of the Staphylococcus aureus leukotoxins.The bicomponent pore-forming leucocidins of Staphylococcus aureusStaphylococcus aureus induces eosinophil cell death mediated by α-hemolysinIon permeation through the alpha-hemolysin channel: theoretical studies based on Brownian dynamics and Poisson-Nernst-Plank electrodiffusion theoryRole of pore-forming toxins in bacterial infectious diseases.Cyclodextrin derivatives as anti-infectives.Characterization of a new cytotoxin that contributes to Staphylococcus aureus pathogenesis.High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: implication for understanding protein-lipid interactions.Vibrio cholerae cytolysin is composed of an alpha-hemolysin-like core.Infectious keratitis: secreted bacterial proteins that mediate corneal damage.Proteomics Analysis Reveals Previously Uncharacterized Virulence Factors in Vibrio proteolyticus.Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity.The rise and rise of Staphylococcus aureus: laughing in the face of granulocytes.Protein conducting channels-mechanisms, structures and applications.Cell targeting by the Staphylococcus aureus pore-forming toxins: it's not just about lipidsProperties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.Retrieving biological activity from LukF-PV mutants combined with different S components implies compatibility between the stem domains of these staphylococcal bicomponent leucotoxins.NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold.Using Quantitative Spectrometry to Understand the Influence of Genetics and Nutritional Perturbations On the Virulence Potential of Staphylococcus aureus.Adaptive processes of Staphylococcus aureus isolates during the progression from acute to chronic bone and joint infections in patients.Association between avian necrotic enteritis and Clostridium perfringens strains expressing NetB toxin.Characterization of Virulence Factors of Staphylococcus aureus: Novel Function of Known Virulence Factors That Are Implicated in Activation of Airway Epithelial Proinflammatory Response.Arresting and releasing Staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds.Purification, cloning and characterization of variant LukE-LukD with strong leukocidal activity of staphylococcal bi-component leukotoxin family.Resistin-like molecule β is a bactericidal protein that promotes spatial segregation of the microbiota and the colonic epithelium.Protein engineering modulates the transport properties and ion selectivity of the pores formed by staphylococcal gamma-haemolysins in lipid membranes.Molecular dynamics simulation of water permeation through the alpha-hemolysin channel.
P2860
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P2860
Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family.
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
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
name
Mode of action of beta-barrel ...... coccal alpha-hemolysin family.
@ast
Mode of action of beta-barrel ...... coccal alpha-hemolysin family.
@en
type
label
Mode of action of beta-barrel ...... coccal alpha-hemolysin family.
@ast
Mode of action of beta-barrel ...... coccal alpha-hemolysin family.
@en
prefLabel
Mode of action of beta-barrel ...... coccal alpha-hemolysin family.
@ast
Mode of action of beta-barrel ...... coccal alpha-hemolysin family.
@en
P2093
P1433
P1476
Mode of action of beta-barrel ...... coccal alpha-hemolysin family.
@en
P2093
P304
P356
10.1016/S0041-0101(01)00153-2
P577
2001-11-01T00:00:00Z