AbstractThe effect of nonmuscle actin ADP-ribosylated by botulinum C2 toxin on the polymerization of nonmuscle actin was investigated in order to clarify whether nonmuscle actin is converted into a capping protein by ADP-ribosylation. ADP-ribosylated actin was found to decrease the rate of polymerization of actin filaments which are free at both ends. ADP-ribosylated actin turned out to have no effect on the rate or extent of polymerization at the pointed ends of actin filaments the barbed ends of which were capped by gelsolin. The monomer concentration reached at the final stage of polymerization was similar to the critical concentration of the pointed ends of actin filaments. The results suggest that nonmuscle actin ADP-ribosylated by bot...
The general features of the kinetics of actin polymerization are investigated by mathematical models...
International audienceTc toxins deliver toxic enzymes into host cells by a unique injection mechanis...
AbstractBotulinum C2 toxin was employed as a specific inhibitor of actin polymerization in rat neutr...
AbstractActin ADP-ribosylated at Arg177 was previously shown not to polymerise after increasing the ...
AbstractADP-ribosylation of actin by Clostridium botulinum C2 toxin resulted in a depolymerization o...
The binary botulinum C2 toxin ADP-ribosylated the actin of human neutrophils. Treatment of human neu...
AbstractClostridium perfringens iota toxin ADP-ribosylates actin. Substrates of C. perfringens toxin...
AbstractThe culture medium of certain strains of Clostridium botulinum type C contains two separable...
AbstractActin filament polymerization results primarily from the addition of monomers to pre-existin...
AbstractWe have studied the effect of actin skeleton depolymerisation induced by C2 toxin on protein...
Current theory and experiments describing actin polymerization suggest that site-specific cleavage o...
The gelsolin-actin complex was ADP-ribosylated by Clostridium botulinum C2 toxin and Clostridium per...
AbstractBackground: Actin filaments polymerize in vivo primarily from their fast-growing barbed ends...
<p><i>A.</i> J774A.1 cells were incubated with C3bot1E174Q-C2I (0.5 µg/mL, 2 µg/mL, 4 µg/mL), C3bot1...
AbstractThe hypothesis that inhibition of secretion by botulinum neurotoxin type D occurs by an intr...
The general features of the kinetics of actin polymerization are investigated by mathematical models...
International audienceTc toxins deliver toxic enzymes into host cells by a unique injection mechanis...
AbstractBotulinum C2 toxin was employed as a specific inhibitor of actin polymerization in rat neutr...
AbstractActin ADP-ribosylated at Arg177 was previously shown not to polymerise after increasing the ...
AbstractADP-ribosylation of actin by Clostridium botulinum C2 toxin resulted in a depolymerization o...
The binary botulinum C2 toxin ADP-ribosylated the actin of human neutrophils. Treatment of human neu...
AbstractClostridium perfringens iota toxin ADP-ribosylates actin. Substrates of C. perfringens toxin...
AbstractThe culture medium of certain strains of Clostridium botulinum type C contains two separable...
AbstractActin filament polymerization results primarily from the addition of monomers to pre-existin...
AbstractWe have studied the effect of actin skeleton depolymerisation induced by C2 toxin on protein...
Current theory and experiments describing actin polymerization suggest that site-specific cleavage o...
The gelsolin-actin complex was ADP-ribosylated by Clostridium botulinum C2 toxin and Clostridium per...
AbstractBackground: Actin filaments polymerize in vivo primarily from their fast-growing barbed ends...
<p><i>A.</i> J774A.1 cells were incubated with C3bot1E174Q-C2I (0.5 µg/mL, 2 µg/mL, 4 µg/mL), C3bot1...
AbstractThe hypothesis that inhibition of secretion by botulinum neurotoxin type D occurs by an intr...
The general features of the kinetics of actin polymerization are investigated by mathematical models...
International audienceTc toxins deliver toxic enzymes into host cells by a unique injection mechanis...
AbstractBotulinum C2 toxin was employed as a specific inhibitor of actin polymerization in rat neutr...