AbstractUsing phase-separated droplet interface bilayers, we observe membrane binding and pore formation of a eukaryotic cytolysin, Equinatoxin II (EqtII). EqtII activity is known to depend on the presence of sphingomyelin in the target membrane and is enhanced by lipid phase separation. By imaging the ionic flux through individual pores in vitro, we observe that EqtII pores form predominantly within the liquid-disordered phase. We observe preferential binding of labeled EqtII at liquid-ordered/liquid-disordered domain boundaries before it accumulates in the liquid-disordered phase
Observing dynamic pore-forming processes in lipid bilayers is a challenging task. It requires a bila...
AbstractSynchrotron radiation circular dichroism (SRCD) spectroscopy studies of the eukaryotic pore-...
Pore-forming toxins have evolved to induce membrane injury by formation of pores in the target cell ...
AbstractUsing phase-separated droplet interface bilayers, we observe membrane binding and pore forma...
Using phase-separated droplet interface bilayers, we observe membrane binding and pore formation of ...
AbstractEquinatoxin II is a pore-forming protein of the actinoporin family. After membrane binding, ...
AbstractEquinatoxin II (EqtII), a protein toxin from the sea anemone Actinia equina, readily creates...
AbstractEquinatoxin II (EqtII) is a pore-forming protein from Actinia equina that lyses red blood ce...
Equinatoxin II (EqtII), a eukaryotic pore-forming toxin, lyses cell membranes through a mechanism in...
AbstractEquinatoxin II is a 179-amino-acid pore-forming protein isolated from the venom of the sea a...
Pore formation in the target cell membranes is a common mechanism used by many toxins in order to ki...
AbstractEquinatoxin II (EqtII) is a soluble, 20 kDa pore-forming protein toxin isolated from the sea...
Phase segregation of multicomponent lipid bilayers leads to, under phase-coexistence conditions, dom...
Equinatoxin II (EqtII), a eukaryotic pore-forming toxin, lyses cell membranes through a mechanism in...
ABSTRACT Equinatoxin II is a 179-amino-acid pore-forming protein isolated from the venom of the sea ...
Observing dynamic pore-forming processes in lipid bilayers is a challenging task. It requires a bila...
AbstractSynchrotron radiation circular dichroism (SRCD) spectroscopy studies of the eukaryotic pore-...
Pore-forming toxins have evolved to induce membrane injury by formation of pores in the target cell ...
AbstractUsing phase-separated droplet interface bilayers, we observe membrane binding and pore forma...
Using phase-separated droplet interface bilayers, we observe membrane binding and pore formation of ...
AbstractEquinatoxin II is a pore-forming protein of the actinoporin family. After membrane binding, ...
AbstractEquinatoxin II (EqtII), a protein toxin from the sea anemone Actinia equina, readily creates...
AbstractEquinatoxin II (EqtII) is a pore-forming protein from Actinia equina that lyses red blood ce...
Equinatoxin II (EqtII), a eukaryotic pore-forming toxin, lyses cell membranes through a mechanism in...
AbstractEquinatoxin II is a 179-amino-acid pore-forming protein isolated from the venom of the sea a...
Pore formation in the target cell membranes is a common mechanism used by many toxins in order to ki...
AbstractEquinatoxin II (EqtII) is a soluble, 20 kDa pore-forming protein toxin isolated from the sea...
Phase segregation of multicomponent lipid bilayers leads to, under phase-coexistence conditions, dom...
Equinatoxin II (EqtII), a eukaryotic pore-forming toxin, lyses cell membranes through a mechanism in...
ABSTRACT Equinatoxin II is a 179-amino-acid pore-forming protein isolated from the venom of the sea ...
Observing dynamic pore-forming processes in lipid bilayers is a challenging task. It requires a bila...
AbstractSynchrotron radiation circular dichroism (SRCD) spectroscopy studies of the eukaryotic pore-...
Pore-forming toxins have evolved to induce membrane injury by formation of pores in the target cell ...