The behavior of sea anemone actinoporins at the water-membrane interface.
about
Sea anemone (Cnidaria, Anthozoa, Actiniaria) toxins: an overviewThe venomous cocktail of the vampire snail Colubraria reticulata (Mollusca, Gastropoda)Ancient Venom Systems: A Review on Cnidaria ToxinsMembrane damage by an α-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered stepsStructural basis for self-assembly of a cytolytic pore lined by protein and lipidSolution NMR analysis of the interaction between the actinoporin sticholysin I and DHPC micelles--correlation with backbone dynamics.Assembling the puzzle: Oligomerization of α-pore forming proteins in membranesImaging the lipid-phase-dependent pore formation of equinatoxin II in droplet interface bilayers.A Polychaete's powerful punch: venom gland transcriptomics of Glycera reveals a complex cocktail of toxin homologsMolecular Diversity and Gene Evolution of the Venom Arsenal of Terebridae Predatory Marine Snails.Listeriolysin O Affects the Permeability of Caco-2 Monolayer in a Pore-Dependent and Ca2+-Independent Manner.More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes.α-sarcin and RNase T1 based immunoconjugates: the role of intracellular trafficking in cytotoxic efficiency.Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.A pore-forming toxin requires a specific residue for its activity in membranes with particular physicochemical properties.Multiomics analysis of the giant triton snail salivary gland, a crown-of-thorns starfish predator.Evolution of an ancient venom: recognition of a novel family of cnidarian toxins and the common evolutionary origin of sodium and potassium neurotoxins in sea anemone.Toxicity of an α-pore-forming toxin depends on the assembly mechanism on the target membrane as revealed by single molecule imaging.Synergistic 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 interfaceEffect of human serum albumin upon the permeabilizing activity of sticholysin II, a pore forming toxin from Stichodactyla heliantus.Haemolytic actinoporins interact with carbohydrates using their lipid-binding module.Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation.Multigene Family of Pore-Forming Toxins from Sea Anemone Heteractis crispa.
P2860
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P2860
The behavior of sea anemone actinoporins at the water-membrane interface.
description
2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
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2011年學術文章
@yue
2011年學術文章
@zh-hant
name
The behavior of sea anemone actinoporins at the water-membrane interface.
@en
The behavior of sea anemone actinoporins at the water-membrane interface.
@nl
type
label
The behavior of sea anemone actinoporins at the water-membrane interface.
@en
The behavior of sea anemone actinoporins at the water-membrane interface.
@nl
prefLabel
The behavior of sea anemone actinoporins at the water-membrane interface.
@en
The behavior of sea anemone actinoporins at the water-membrane interface.
@nl
P50
P1476
The behavior of sea anemone actinoporins at the water-membrane interface.
@en
P2093
Sara García-Linares
P304
P356
10.1016/J.BBAMEM.2011.05.012
P577
2011-05-20T00:00:00Z