Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.
about
The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyInerolysin, a cholesterol-dependent cytolysin produced by Lactobacillus inersCholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O bindingPerfringolysin O Theta Toxin as a Tool to Monitor the Distribution and Inhomogeneity of Cholesterol in Cellular MembranesMore than a pore: the cellular response to cholesterol-dependent cytolysinsA new model for pore formation by cholesterol-dependent cytolysinsDifferential Cholesterol Binding by Class II Fusion Proteins Determines Membrane Fusion PropertiesCellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracisStructural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59Listeriolysin o is strongly immunogenic independently of its cytotoxic activityCryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsTrapping of Vibrio cholerae cytolysin in the membrane-bound monomeric state blocks membrane insertion and functional pore formation by the toxinDisulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Membrane assembly of the cholesterol-dependent cytolysin pore complex.The MACPF/CDC family of pore-forming toxins.Specific lipids supply critical negative spontaneous curvature--an essential component of native Ca2+-triggered membrane fusion.Mechanisms underlying the micron-scale segregation of sterols and GM1 in live mammalian spermStatins protect against fulminant pneumococcal infection and cytolysin toxicity in a mouse model of sickle cell diseaseOnly two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin OPerforin: structure, function, and role in human immunopathology.The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cellsSimvastatin enhances protection against Listeria monocytogenes infection in mice by counteracting Listeria-induced phagosomal escape.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.Clostridium sordellii genome analysis reveals plasmid localized toxin genes encoded within pathogenicity lociPerfringolysin O: The Underrated Clostridium perfringens Toxin?Toxin-neutralizing antibodies protect against Clostridium perfringens-induced necrosis in an intestinal loop model for bovine necrohemorrhagic enteritisDual modes of membrane binding direct pore formation by Streptolysin O.Red Blood Cell Susceptibility to Pneumolysin: CORRELATION WITH MEMBRANE BIOCHEMICAL AND PHYSICAL PROPERTIES.Crystal structure of cytotoxin protein suilysin from Streptococcus suis.Mini-review: novel therapeutic strategies to blunt actions of pneumolysin in the lungsBiochemical characterization of membrane fractions in murine sperm: identification of three distinct sub-types of membrane rafts.Listeriolysin O as a strong immunogenic molecule for the development of new anti-tumor vaccinesClostridial toxins.
P2860
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P2860
Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.
description
2007 nî lūn-bûn
@nan
2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Structural elements of the cho ...... nsitive membrane interactions.
@ast
Structural elements of the cho ...... nsitive membrane interactions.
@en
Structural elements of the cho ...... nsitive membrane interactions.
@nl
type
label
Structural elements of the cho ...... nsitive membrane interactions.
@ast
Structural elements of the cho ...... nsitive membrane interactions.
@en
Structural elements of the cho ...... nsitive membrane interactions.
@nl
prefLabel
Structural elements of the cho ...... nsitive membrane interactions.
@ast
Structural elements of the cho ...... nsitive membrane interactions.
@en
Structural elements of the cho ...... nsitive membrane interactions.
@nl
P2093
P2860
P356
P1476
Structural elements of the cho ...... nsitive membrane interactions.
@en
P2093
Arthur E Johnson
Casie E Soltani
Eileen M Hotze
Rodney K Tweten
P2860
P304
20226-20231
P356
10.1073/PNAS.0708104105
P407
P577
2007-12-12T00:00:00Z