AbstractThe interaction between Bacillus thuringiensis insecticidal 5-endotoxin CryIC and phospholipid vesicles was studied by fluorescence spectroscopy. The toxin dissipates the diffusion potential across vesicular membranes, presumably by creating ion permeable channels or pores. This effect is pH-dependent and strongly increases under acidic conditions. The enhanced membrane-perturbing activity of CryIC at low pH correlates with the increased surface hydrophobicity of the toxin molecule. The membrane permeabilizing effect of the toxin is further increased by the presence of acidic phospholipids. These findings are discussed in relation to the mode of insecticidal action of the toxin
AbstractThe luminal membrane of larval midgut cells is the site of action of insecticidal delta-endo...
AbstractThe δ-endotoxin produced by Bacillus thuringiensis ssp. entomocidus induced the release of e...
We have examined the type of inhibition exerted by an activated preparation of the Bacillus thuringi...
AbstractThe interaction between Bacillus thuringiensis insecticidal 5-endotoxin CryIC and phospholip...
AbstractMembrane potential measurements using a fluorescent dye indicated that two specific toxins a...
The effect of pH on the pore-forming ability of two Bacillus thuringiensis toxins, Cry1Ac and Cry1C,...
AbstractA purified, GPI-linked receptor complex isolated from Manduca sexta midgut epithelial cells ...
AbstractMembrane potential measurements using a fluorescent dye indicated that two specific toxins a...
AbstractIn order to determine the mechanism of action of the 27 kDa mosquitocidal δ-endotoxin of Bac...
We have investigated the interaction of Pseudomonas exotoxin A with small unilamellar vesicles compr...
Cyt1A is a cytolytic toxin produced by Bacillus thuringiensis var. israelensis. Due to its toxicity ...
AbstractBacillus thuringiensis Cry toxins are efficient, environment-friendly biological insecticide...
An optical biosensor technology based on surface plasmon resonance was used to determine the kinetic...
The Bacillus thuringiensis Cry1Ac delta-endotoxin was shown to bind in a biphasic manner to Manduca ...
The pores formed by Bacillus thuringiensis insecticidal toxins have been shown to allow the diffusio...
AbstractThe luminal membrane of larval midgut cells is the site of action of insecticidal delta-endo...
AbstractThe δ-endotoxin produced by Bacillus thuringiensis ssp. entomocidus induced the release of e...
We have examined the type of inhibition exerted by an activated preparation of the Bacillus thuringi...
AbstractThe interaction between Bacillus thuringiensis insecticidal 5-endotoxin CryIC and phospholip...
AbstractMembrane potential measurements using a fluorescent dye indicated that two specific toxins a...
The effect of pH on the pore-forming ability of two Bacillus thuringiensis toxins, Cry1Ac and Cry1C,...
AbstractA purified, GPI-linked receptor complex isolated from Manduca sexta midgut epithelial cells ...
AbstractMembrane potential measurements using a fluorescent dye indicated that two specific toxins a...
AbstractIn order to determine the mechanism of action of the 27 kDa mosquitocidal δ-endotoxin of Bac...
We have investigated the interaction of Pseudomonas exotoxin A with small unilamellar vesicles compr...
Cyt1A is a cytolytic toxin produced by Bacillus thuringiensis var. israelensis. Due to its toxicity ...
AbstractBacillus thuringiensis Cry toxins are efficient, environment-friendly biological insecticide...
An optical biosensor technology based on surface plasmon resonance was used to determine the kinetic...
The Bacillus thuringiensis Cry1Ac delta-endotoxin was shown to bind in a biphasic manner to Manduca ...
The pores formed by Bacillus thuringiensis insecticidal toxins have been shown to allow the diffusio...
AbstractThe luminal membrane of larval midgut cells is the site of action of insecticidal delta-endo...
AbstractThe δ-endotoxin produced by Bacillus thuringiensis ssp. entomocidus induced the release of e...
We have examined the type of inhibition exerted by an activated preparation of the Bacillus thuringi...