Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxins
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Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxinsCrystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structureStructural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringensStructural Insights into Clostridium perfringens Delta Toxin Pore FormationResidues Essential for Panton-Valentine Leukocidin S Component Binding to Its Cell Receptor Suggest Both Plasticity and Adaptability in Its Interaction SurfaceMolecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxinsStaphylococcus aureus Pore-Forming Toxins.Identification of a crucial residue required for Staphylococcus aureus LukAB cytotoxicity and receptor recognition.Staphylococcal Panton-Valentine leucocidin as a major virulence factor associated to furuncles.Distinction between pore assembly by staphylococcal alpha-toxin versus leukotoxins.Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.Homologous versus heterologous interactions in the bicomponent staphylococcal gamma-haemolysin pore.Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis.The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.Structural model of the pre-pore ring-like structure of Panton-Valentine leukocidin: providing dimensionality to biophysical and mutational data.The bicomponent pore-forming leucocidins of Staphylococcus aureusSimulation of charge transport in ion channels and nanopores with anisotropic permittivity.SIMULATION OF ION CONDUCTION IN α-HEMOLYSIN NANOPORES WITH COVALENTLY ATTACHED β-CYCLODEXTRIN BASED ON BOLTZMANN TRANSPORT MONTE CARLO MODEL.Structurally designed attenuated subunit vaccines for S. aureus LukS-PV and LukF-PV confer protection in a mouse bacteremia model.Molecular modeling reveals the novel inhibition mechanism and binding mode of three natural compounds to staphylococcal α-hemolysin.Five birds, one stone: neutralization of α-hemolysin and 4 bi-component leukocidins of Staphylococcus aureus with a single human monoclonal antibody.Crystallization and preliminary crystallographic studies of both components of the staphylococcal LukE-LukD leukotoxin.Context matters: The importance of dimerization-induced conformation of the LukGH leukocidin of Staphylococcus aureus for the generation of neutralizing antibodies.Staphylococcus aureus hemolysins, bi-component leukocidins, and cytolytic peptides: a redundant arsenal of membrane-damaging virulence factors?Crystal structures of the components of the Staphylococcus aureus leukotoxin ED.Role of pore-forming toxins in neonatal sepsisStaphylococcus aureus leukotoxin ED targets the chemokine receptors CXCR1 and CXCR2 to kill leukocytes and promote infection.Inflammasome Activation Can Mediate Tissue-Specific Pathogenesis or Protection in Staphylococcus aureus Infection.Staphylococcus aureus Leukocidin LukED and HIV-1 gp120 Target Different Sequence Determinants on CCR5.Above and beyond C5a Receptor Targeting by Staphylococcal Leucotoxins: Retrograde Transport of Panton-Valentine Leucocidin and γ-Hemolysin.Computer aided screening and evaluation of herbal therapeutics against MRSA infectionsStructure and Function of the Two-Component Cytotoxins of Staphylococcus aureus - Learnings for Designing Novel Therapeutics.Site-directed mutagenesis to assess the binding capacity of class s protein of Staphylococcus aureus leucotoxins to the surface of polymorphonuclear cells.Engineered covalent leucotoxin heterodimers form functional pores: insights into S-F interactions.Staphylococcus aureus proteins SSL6 and SElX interact with neutrophil receptors as identified using secretome phage display.Prepore for a breakthrough.Assembly of Staphylococcal Leukocidin into a Pore-Forming Oligomer on Detergent-Resistant Membrane Microdomains, Lipid Rafts, in Human Polymorphonuclear Leukocytesp-Sulfonato-calix[n]arenes inhibit staphylococcal bicomponent leukotoxins by supramolecular interactions
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P2860
Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxins
description
2004 nî lūn-bûn
@nan
2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@ast
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@en
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@nl
type
label
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@ast
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@en
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@nl
prefLabel
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@ast
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@en
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@nl
P2093
P2860
P3181
P356
P1476
Crystal structure of leucotoxi ...... eta-barrel pore-forming toxins
@en
P2093
Gianfranco Menestrina
Gilles Prévost
Henri Monteil
Lionel Mourey
Manuela Coraiola
Pierre Roblin
Sandra Werner
Valérie Guillet
P2860
P304
P3181
P356
10.1074/JBC.M406904200
P407
P577
2004-09-24T00:00:00Z