Abstract The present study investigates the electrophysiologi-cal actions of BmK M1, an K-like toxin purified from the venom of the scorpion Buthus martensi Karsch, on voltage-gated Na+ channels. Using the voltage clamp technique, we assessed the BmK M1 activity on the cardiac Na+ channel (hH1) functionally expressed in Xenopus oocytes. The main actions of the toxin are a concentration-dependent slowing of the inactivation process and a hyperpolarizing shift of the steady-state inactivation. This work is the first electrophysiological characterization of BmK M1 on a cloned Na+ channel, demonstrating that this toxin belongs to the class of scorpion K-toxins. Our results also show that BmK M1 can be considered as a cardiotoxin. ß 200
AbstractThe two insecticidal peptides Bm32-VI and Bm33-I, isolated from the venom of the Chinese sco...
AbstractThe very first member of K+ channels toxins from the venom of the Iranian scorpion Odonthobu...
International audienceK(+) channels selectively transport K(+) ions across cell membranes and play a...
AbstractThe present study investigates the electrophysiological actions of BmK M1, an α-like toxin p...
In-depth structure-function studies of voltage-gated Na+ channels and peptide toxins are continuousl...
A novel "long chain" toxin BmP09 has been purified and characterized from the venom of the...
In-depth structure-function studies of voltage-gated Na+ channels and peptide toxins are continuousl...
AbstractIn this study, we isolated and pharmacologically characterized the first α-like toxin from t...
BmP02, a short-chain peptide with 28 residues from the venom of Chinese scorpion Buthus martensi Kar...
In this study, we isolated and pharmacologically characterized the first alpha-like toxin from the v...
A peptide toxin was isolated from the venom of Palamneus gravimanus, the Indian black scorpion, to b...
International audienceOn attempts to identify toxins showing original profile of activity among K+ c...
Voltage-gated sodium channels (VGSCs) are responsible for the action potential generation in excitab...
Toxins isolated from scorpion, snake, and spider venoms are valuable tools to probe the physiologic ...
Scorpion beta-toxins represent a particular pharmacological group of voltage-gated sodium channel (V...
AbstractThe two insecticidal peptides Bm32-VI and Bm33-I, isolated from the venom of the Chinese sco...
AbstractThe very first member of K+ channels toxins from the venom of the Iranian scorpion Odonthobu...
International audienceK(+) channels selectively transport K(+) ions across cell membranes and play a...
AbstractThe present study investigates the electrophysiological actions of BmK M1, an α-like toxin p...
In-depth structure-function studies of voltage-gated Na+ channels and peptide toxins are continuousl...
A novel "long chain" toxin BmP09 has been purified and characterized from the venom of the...
In-depth structure-function studies of voltage-gated Na+ channels and peptide toxins are continuousl...
AbstractIn this study, we isolated and pharmacologically characterized the first α-like toxin from t...
BmP02, a short-chain peptide with 28 residues from the venom of Chinese scorpion Buthus martensi Kar...
In this study, we isolated and pharmacologically characterized the first alpha-like toxin from the v...
A peptide toxin was isolated from the venom of Palamneus gravimanus, the Indian black scorpion, to b...
International audienceOn attempts to identify toxins showing original profile of activity among K+ c...
Voltage-gated sodium channels (VGSCs) are responsible for the action potential generation in excitab...
Toxins isolated from scorpion, snake, and spider venoms are valuable tools to probe the physiologic ...
Scorpion beta-toxins represent a particular pharmacological group of voltage-gated sodium channel (V...
AbstractThe two insecticidal peptides Bm32-VI and Bm33-I, isolated from the venom of the Chinese sco...
AbstractThe very first member of K+ channels toxins from the venom of the Iranian scorpion Odonthobu...
International audienceK(+) channels selectively transport K(+) ions across cell membranes and play a...