Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
about
The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyHuman perforin employs different avenues to damage membranesCholesterol-dependent cytolysins, a family of versatile pore-forming toxinsCholesterol 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 domainRedefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysinsPerfringolysin O Theta Toxin as a Tool to Monitor the Distribution and Inhomogeneity of Cholesterol in Cellular MembranesObstructing toxin pathways by targeted pore blockageThe Transition from Closed to Open Conformation of Treponema pallidum Outer Membrane-associated Lipoprotein TP0453 Involves Membrane Sensing and Integration by Two Amphipathic HelicesCrystal structure of listeriolysin O reveals molecular details of oligomerization and pore formationListeriolysin o is strongly immunogenic independently of its cytotoxic activityConsensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAINPerfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsStructural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.Membrane damage by an α-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered stepsDisulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.TprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structureMembrane assembly of the cholesterol-dependent cytolysin pore complex.Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membraneAuto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2Complexin 2 modulates vesicle-associated membrane protein (VAMP) 2-regulated zymogen granule exocytosis in pancreatic acini.Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.Direct injection of functional single-domain antibodies from E. coli into human cells.The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formationThe SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release.Efficient isolation of Pseudomonas aeruginosa type III secretion translocators and assembly of heteromeric transmembrane pores in model membranes.Arcanolysin is a cholesterol-dependent cytolysin of the human pathogen Arcanobacterium haemolyticum.Magnetically immobilized nanoporous giant proteoliposomes as a platform for biosensing.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Membrane damage during Listeria monocytogenes infection triggers a caspase-7 dependent cytoprotective responseSV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release.Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.Expression, localization, and functional role for synaptotagmins in pancreatic acinar cells.Perfringolysin O: The Underrated Clostridium perfringens Toxin?Listeriolysin O: a key protein of Listeria monocytogenes with multiple functions.Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysinProtein arcs may form stable pores in lipid membranes.The influence of natural lipid asymmetry upon the conformation of a membrane-inserted protein (perfringolysin O)
P2860
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P2860
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
@ast
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
@en
type
label
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
@ast
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
@en
prefLabel
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
@ast
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
@en
P2093
P2860
P356
P1476
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
@en
P2093
Alejandro P Heuck
Arthur E Johnson
Rodney K Tweten
P2860
P304
31218-31225
P356
10.1074/JBC.M303151200
P407
P577
2003-05-30T00:00:00Z