Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin.
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The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyCholesterol-dependent cytolysins, a family of versatile pore-forming toxinsInerolysin, a cholesterol-dependent cytolysin produced by Lactobacillus inersCholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O bindingCharacterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domainObstructing toxin pathways by targeted pore blockageMore than a pore: the cellular response to cholesterol-dependent cytolysinsThe pore-forming haemolysins of bacillus cereus: a reviewA new model for pore formation by cholesterol-dependent cytolysinsStructural basis of complement membrane attack complex formation.Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defenseCellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracisManipulating the Lewis antigen specificity of the cholesterol-dependent cytolysin lectinolysinStructure of the Lectin Regulatory Domain of the Cholesterol-Dependent Cytolysin Lectinolysin Reveals the Basis for Its Lewis Antigen SpecificityStructural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59Structure and secretion of CofJ, a putative colonization factor of enterotoxigenic Escherichia coliCrystal structure of listeriolysin O reveals molecular details of oligomerization and pore formationStructural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent CytolysinsThe Bacillus anthracis cholesterol-dependent cytolysin, Anthrolysin O, kills human neutrophils, monocytes and macrophagesListeriolysin o is strongly immunogenic independently of its cytotoxic activityDisentangling the roles of cholesterol and CD59 in intermedilysin pore formation.Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsMembrane assembly of the cholesterol-dependent cytolysin pore complex.The MACPF/CDC family of pore-forming toxins.Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunitStructures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysinsApicomplexan perforin-like proteins.Development of a single-gene, signature-tag-based approach in combination with alanine mutagenesis to identify listeriolysin O residues critical for the in vivo survival of Listeria monocytogenes.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin OIdentification of functional domains of Clostridium septicum alpha toxin.Perforin: structure, function, and role in human immunopathology.Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.Functional and phylogenetic characterization of Vaginolysin, the human-specific cytolysin from Gardnerella vaginalis.Aegerolysins: structure, function, and putative biological role.The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.
P2860
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P2860
Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Insights into the action of th ...... rom studies of intermedilysin.
@ast
Insights into the action of th ...... rom studies of intermedilysin.
@en
type
label
Insights into the action of th ...... rom studies of intermedilysin.
@ast
Insights into the action of th ...... rom studies of intermedilysin.
@en
prefLabel
Insights into the action of th ...... rom studies of intermedilysin.
@ast
Insights into the action of th ...... rom studies of intermedilysin.
@en
P2093
P2860
P356
P1476
Insights into the action of th ...... rom studies of intermedilysin.
@en
P2093
Galina Polekhina
Kara Sue Giddings
Rodney K Tweten
P2860
P304
P356
10.1073/PNAS.0403229101
P407
P577
2005-01-06T00:00:00Z