BmP02, a short-chain peptide with 28 residues from the venom of Chinese scorpion Buthus martensi Karsch, has been reported to inhibit the transient outward potassium currents (Ito) in rat ventricular muscle cells. However, it remains unclear whether BmP02 modulates the Kv4.2 channel, one of the main contributors to Ito. The present study investigated the effects of BmP02 on Kv4.2 kinetics and its underlying molecular mechanism. The electrophysiological recordings showed that the inactivation of Kv4.2 expressed in HEK293T cells was significantly delayed by BmP02 in a dose-response manner with EC50 of ~850 nM while the peak current, activation and voltage-dependent inactivation of Kv4.2 were not affected. Meanwhile, the recovery from inactiva...
A novel inhibitor of voltage-gated potassium channel was isolated and purified to homogeneity from t...
International audienceOn attempts to identify toxins showing original profile of activity among K+ c...
Abstract The present study investigates the electrophysiologi-cal actions of BmK M1, an K-like toxin...
BmP02, a short-chain peptide with 28 residues from the venom of Chinese scorpion Buthus martensi Kar...
A novel "long chain" toxin BmP09 has been purified and characterized from the venom of the...
International audienceThe voltage-gated K+ channels Kv3.1 display fast activation and deactivation k...
The voltage-gated K+ channels Kv3.1 display fast activation and deactivation kinetics and are known ...
ABSTRACT: Four peptide inhibitors of small-conductance Ca2+-activated, apamin-sensitive K+ channels ...
Scorpion toxins are important pharmacological tools for probing the physiological roles of ion chann...
International audienceK(+) channels selectively transport K(+) ions across cell membranes and play a...
AbstractA number of invertebrate venoms have been tested for effects on M-type K+ currents (IK(M)) i...
A novel peptide, Cm39, was identified in the venom of the scorpion Centruroides margaritatus. Its pr...
A peptide toxin was isolated from the venom of Palamneus gravimanus, the Indian black scorpion, to b...
Scorpion venom is an unmatched source of selective high-affinity ligands of potassium channels. Ther...
The Kv1.2 channel plays an important role in the maintenance of resting membrane potential and the r...
A novel inhibitor of voltage-gated potassium channel was isolated and purified to homogeneity from t...
International audienceOn attempts to identify toxins showing original profile of activity among K+ c...
Abstract The present study investigates the electrophysiologi-cal actions of BmK M1, an K-like toxin...
BmP02, a short-chain peptide with 28 residues from the venom of Chinese scorpion Buthus martensi Kar...
A novel "long chain" toxin BmP09 has been purified and characterized from the venom of the...
International audienceThe voltage-gated K+ channels Kv3.1 display fast activation and deactivation k...
The voltage-gated K+ channels Kv3.1 display fast activation and deactivation kinetics and are known ...
ABSTRACT: Four peptide inhibitors of small-conductance Ca2+-activated, apamin-sensitive K+ channels ...
Scorpion toxins are important pharmacological tools for probing the physiological roles of ion chann...
International audienceK(+) channels selectively transport K(+) ions across cell membranes and play a...
AbstractA number of invertebrate venoms have been tested for effects on M-type K+ currents (IK(M)) i...
A novel peptide, Cm39, was identified in the venom of the scorpion Centruroides margaritatus. Its pr...
A peptide toxin was isolated from the venom of Palamneus gravimanus, the Indian black scorpion, to b...
Scorpion venom is an unmatched source of selective high-affinity ligands of potassium channels. Ther...
The Kv1.2 channel plays an important role in the maintenance of resting membrane potential and the r...
A novel inhibitor of voltage-gated potassium channel was isolated and purified to homogeneity from t...
International audienceOn attempts to identify toxins showing original profile of activity among K+ c...
Abstract The present study investigates the electrophysiologi-cal actions of BmK M1, an K-like toxin...