Lipid phase coexistence favors membrane insertion of equinatoxin-II, a pore-forming toxin from Actinia equina.
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Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O bindingIdentification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of ActinoporinsStructural basis for self-assembly of a cytolytic pore lined by protein and lipidAssembling the puzzle: Oligomerization of α-pore forming proteins in membranesImaging the lipid-phase-dependent pore formation of equinatoxin II in droplet interface bilayers.Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.A Polychaete's powerful punch: venom gland transcriptomics of Glycera reveals a complex cocktail of toxin homologsStructural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics SimulationIn situ scanning probe microscopy studies of tetanus toxin-membrane interactionsInfrared spectroscopy study on the conformational changes leading to pore formation of the toxin sticholysin II.Membranes: a meeting point for lipids, proteins and therapiesMore Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes.Effects of HIV-1 gp41-Derived Virucidal Peptides on Virus-like Lipid Membranes.Oligomerization and pore formation by equinatoxin II inhibit endocytosis and lead to plasma membrane reorganization.Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.Budding Yeast: An Ideal Backdrop for In vivo Lipid Biochemistry.Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistenceA pore-forming toxin requires a specific residue for its activity in membranes with particular physicochemical properties.End-products diacylglycerol and ceramide modulate membrane fusion induced by a phospholipase C/sphingomyelinase from Pseudomonas aeruginosaSpecific RNA binding to ordered phospholipid bilayersSynergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores.The effect of cholesterol on the long-range network of interactions established among sea anemone Sticholysin II residues at the water-membrane interfaceColicin N binds to the periphery of its receptor and translocator, outer membrane protein F.Crystallization and preliminary crystallographic analysis of fragaceatoxin C, a pore-forming toxin from the sea anemone Actinia fragacea.The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition.Insertion of the enteropathogenic Escherichia coli Tir virulence protein into membranes in vitro.Novel Adjuvant Based on the Pore-Forming Protein Sticholysin II Encapsulated into Liposomes Effectively Enhances the Antigen-Specific CTL-Mediated Immune Response.Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone.Alpha-Helical Fragaceatoxin C Nanopore Engineered for Double-Stranded and Single-Stranded Nucleic Acid Analysis.Subcellular localization of sphingomyelin revealed by two toxin-based probes in mammalian cells.Haemolytic actinoporins interact with carbohydrates using their lipid-binding module.Light induced transmembrane proton gradient in artificial lipid vesicles reconstituted with photosynthetic reaction centers.Membrane insertion of Escherichia coli alpha-hemolysin is independent from membrane lysis.
P2860
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P2860
Lipid phase coexistence favors membrane insertion of equinatoxin-II, a pore-forming toxin from Actinia equina.
description
2004 nî lūn-bûn
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2004年の論文
@ja
2004年学术文章
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2004年学术文章
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2004年学术文章
@zh-cn
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@zh-hans
2004年学术文章
@zh-my
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name
Lipid phase coexistence favors ...... ing toxin from Actinia equina.
@en
Lipid phase coexistence favors ...... ing toxin from Actinia equina.
@nl
type
label
Lipid phase coexistence favors ...... ing toxin from Actinia equina.
@en
Lipid phase coexistence favors ...... ing toxin from Actinia equina.
@nl
prefLabel
Lipid phase coexistence favors ...... ing toxin from Actinia equina.
@en
Lipid phase coexistence favors ...... ing toxin from Actinia equina.
@nl
P2093
P2860
P50
P356
P1476
Lipid phase coexistence favors ...... ming toxin from Actinia equina
@en
P2093
Ariana Barlic
Ion Gutiérrez-Aguirre
Maria-Begoña Ruiz-Argüello
P2860
P304
34209-34216
P356
10.1074/JBC.M313817200
P407
P577
2004-06-02T00:00:00Z