Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures.
about
Intrinsic local disorder and a network of charge-charge interactions are key to actinoporin membrane disruption and cytotoxicityA Pore Idea: the ion conduction pathway of TMEM16/ANO proteins is composed partly of lipidMembrane damage by an α-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered stepsChemical Synthesis and Characterization of an Equinatoxin II(1-85) Analogue.Structural basis for self-assembly of a cytolytic pore lined by protein and lipidImaging the lipid-phase-dependent pore formation of equinatoxin II in droplet interface bilayers.Perforin rapidly induces plasma membrane phospholipid flip-flopEffects of MACPF/CDC proteins on lipid membranes.Perforin oligomers form arcs in cellular membranes: a locus for intracellular delivery of granzymes.Functional characterization of sticholysin I and W111C mutant reveals the sequence of the actinoporin's pore assemblyInfrared spectroscopy study on the conformational changes leading to pore formation of the toxin sticholysin II.Current fluctuation analysis of the PopB and PopD translocon components of the Pseudomonas aeruginosa type III secretion system.Role of pore-forming toxins in neonatal sepsisEvolution of the Cytolytic Pore-Forming Proteins (Actinoporins) in Sea Anemones.The perforin pore facilitates the delivery of cationic cargos.Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algaeMechanisms of cytolysin-induced cell damage -- a role for auto- and paracrine signalling.Membrane-active peptides from marine organisms--antimicrobials, cell-penetrating peptides and peptide toxins: applications and prospects.More Than a Pore: The Interplay of Pore-Forming Proteins and 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.Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins.Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistenceIncomplete pneumolysin oligomers form membrane pores.Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteinsToxicity of an α-pore-forming toxin depends on the assembly mechanism on the target membrane as revealed by single molecule imaging.A toxin-based probe reveals cytoplasmic exposure of Golgi sphingomyelinSynergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores.Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F.Membrane binding of zebrafish actinoporin-like protein: AF domains, a novel superfamily of cell membrane binding domains.Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A.Membrane insertion of the N-terminal alpha-helix of equinatoxin II, a sea anemone cytolytic toxin.Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM.Aggregatibacter actinomycetemcomitans leukotoxin cytotoxicity occurs through bilayer destabilization.Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.Crystallization and preliminary crystallographic analysis of fragaceatoxin C, a pore-forming toxin from the sea anemone Actinia fragacea.Functional and topological studies with Trp-containing analogs of the peptide StII(1-30) derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane.Photobleaching reveals heterogeneous stoichiometry for equinatoxin II oligomers.Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich.Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone.
P2860
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P2860
Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Pore formation by equinatoxin ...... nonlamellar lipid structures.
@en
Pore formation by equinatoxin ...... nonlamellar lipid structures.
@nl
type
label
Pore formation by equinatoxin ...... nonlamellar lipid structures.
@en
Pore formation by equinatoxin ...... nonlamellar lipid structures.
@nl
prefLabel
Pore formation by equinatoxin ...... nonlamellar lipid structures.
@en
Pore formation by equinatoxin ...... nonlamellar lipid structures.
@nl
P2860
P50
P356
P1476
Pore formation by equinatoxin ...... nonlamellar lipid structures.
@en
P2093
Gianfranco Menestrina
P2860
P304
45216-45223
P356
10.1074/JBC.M305916200
P407
P577
2003-08-27T00:00:00Z