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Cys mutants in functional regions of Sticholysin I clarify the participation of these residues in pore formation
(PERGAMON-ELSEVIER SCIENCE LTD, 2011)
Experimental evidence shows that the mechanism of pore formation by actinoporins is a multistep process, involving binding of the water-soluble monomer to the membrane and subsequent oligomerization on the membrane surface, ...
c-Jun Proto-Oncoprotein Plays a Protective Role in Lung Epithelial Cells Exposed to Staphylococcal α-toxin
(Frontiers Media SA, 2018-05)
c-Jun is a member of the early mammalian transcriptional regulators belonging to the AP-1 family, which participates in a wide range of cellular processes such as proliferation, apoptosis, tumorigenesis, and differentiation. ...
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
(Indian Acad Sciences, 2011-12-01)
The sea anemone Stichodactyla helianthus produces two pore-forming proteins, sticholysins I and II (St I and St II). Despite their high identity (93%), these toxins exhibit differences in hemolytic activity that can be ...
Cys mutants in functional regions of Sticholysin I clarify the participation of these residues in pore formation
(2011)
Experimental evidence shows that the mechanism of pore formation by actinoporins is a multistep process, involving binding of the water-soluble monomer to the membrane and subsequent oligomerization on the membrane surface, ...
Effects of Pore-forming toxins (PFTs) on oxidized model membranes represented by Giant Unilamellar Vesicles (GUVs)
(Sociedade Brasileira de Biof??sica, 2019)
Cloning, purification and characterization of nigrelysin, a novel actinoporin from the sea anemone Anthopleura nigrescens
(2019)
Actinoporins constitute a unique class of pore-forming toxins found in sea anemones that being secreted
as soluble monomers are able to bind and permeabilize membranes leading to cell death. The interest in
these proteins ...
Tertiary structural changes of the alpha-hemolysin from Staphylococcus aureus on association with liposome membranes
(Academic Press Inc., 1998-03-01)
The interaction of alpha-hemolysin (also called alpha-toxin) from Staphylococcus aureus with mixed egg-yolk phosphatidylcholine/cholesterol liposomes has been investigated using the intrinsic tryptophan fluorescence emission ...