Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
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Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxinsOMPdb: a database of {beta}-barrel outer membrane proteins from Gram-negative bacteriaCrystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two componentsTargeting Staphylococcus aureus Toxins: A Potential form of Anti-Virulence TherapyCryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil foldsX-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structureStructures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins And Its Mode of Sphingomyelin RecognitionMolecular Architecture and Functional Analysis of NetB, a Pore-forming Toxin from Clostridium perfringensStructural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringensStructural Insights into Clostridium perfringens Delta Toxin Pore FormationStructure of the NheA Component of the Nhe Toxin from Bacillus cereus: Implications for FunctionCrystal Structures of CusC Review Conformational Changes Accompanying Folding and Transmembrane Channel 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 toxinsCrystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxinsStaphylococcus aureus Pore-Forming Toxins.Revisiting the membrane interaction mechanism of a membrane-damaging β-barrel pore-forming toxin Vibrio cholerae cytolysin.X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form.Trapping of Vibrio cholerae cytolysin in the membrane-bound monomeric state blocks membrane insertion and functional pore formation by the toxinIdentification of a crucial residue required for Staphylococcus aureus LukAB cytotoxicity and receptor recognition.Functional mapping of the lectin activity site on the β-prism domain of vibrio cholerae cytolysin: implications for the membrane pore-formation mechanism of the toxin.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.Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membraneIon 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.Membrane insertion of the heptameric staphylococcal alpha-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane.Point mutations in anthrax protective antigen that block translocation.A new cytotoxin from Bacillus cereus that may cause necrotic enteritis.A functional protein pore with a "retro" transmembrane domain.The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.Structural basis for self-assembly of a cytolytic pore lined by protein and lipidStochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3.Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore.The bicomponent pore-forming leucocidins of Staphylococcus aureus
P2860
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P2860
Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Crystal structure of staphyloc ...... ion of a transmembrane channel
@ast
Crystal structure of staphyloc ...... ion of a transmembrane channel
@en
Crystal structure of staphyloc ...... ion of a transmembrane channel
@nl
type
label
Crystal structure of staphyloc ...... ion of a transmembrane channel
@ast
Crystal structure of staphyloc ...... ion of a transmembrane channel
@en
Crystal structure of staphyloc ...... ion of a transmembrane channel
@nl
prefLabel
Crystal structure of staphyloc ...... ion of a transmembrane channel
@ast
Crystal structure of staphyloc ...... ion of a transmembrane channel
@en
Crystal structure of staphyloc ...... ion of a transmembrane channel
@nl
P2093
P3181
P356
P1476
Crystal structure of staphyloc ...... ion of a transmembrane channel
@en
P2093
P304
P3181
P356
10.1038/5821
P577
1999-02-01T00:00:00Z