International audienceWe report the detailed chemical, immunological and pharmacological characterization of the α-toxin Bot IX from the Moroccan scorpion Buthus occitanus tunetanus venom. Bot IX, which consists of 70 amino acids, is a highly atypical toxin. It carries a unique N-terminal sequence extension and is highly lethal in mice. Voltage clamp recordings on oocytes expressing rat Nav1.2 or insect BgNav1 reveal that, similar to other α-like toxins, Bot IX inhibits fast inactivation of both variants. Moreover, Bot IX belongs to the same structural/immunological group as the α-like toxin Bot I. Remarkably, radioiodinated Bot IX competes efficiently with the classical α-toxin AaH II from Androctonus australis, and displays one of the hig...
AbstractThe first example of a new sub-family of toxins (α-KTx20.1) from the scorpion Tityus trivitt...
In-depth structure-function studies of voltage-gated Na+ channels and peptide toxins are continuousl...
The venoms of Buthidae scorpions are known to contain basic, single-chain protein -toxins consisting...
International audienceWe report the detailed chemical, immunological and pharmacological characteriz...
International audienceAlpha scorpion toxins bind to receptor site 3 on voltage-dependent sodium chan...
Scorpion venom is a rich source of promising therapeutic compounds, such as highly selective ion cha...
International audienceIn this study, we have characterized the immunological and pharmacological pro...
International audienceThe venom of the North African scorpion Androctonus amoreuxi (Aam) was analyze...
International audienceA new toxin, BotIT2, with a unique mode of action on the isolated giant axon o...
International audienceOn attempts to identify toxins showing original profile of activity among K+ c...
Kbot55 is a 39 amino acid peptide isolated from the venom of the Tunisian scorpion Buthus occitanus ...
AbstractA new neurotoxic component named BmK abT was purified from the venom of Chinese scorpion But...
AbstractBackground: Scorpion neurotoxins, which bind and modulate sodium channels, have been divided...
<正> The neurotoxins from scorpions are one kind of low molecular toxic proteins which can bind...
α-Scorpion toxins are modulators of voltage-gated Na(+) channels (Navs), which bind to the receptor ...
AbstractThe first example of a new sub-family of toxins (α-KTx20.1) from the scorpion Tityus trivitt...
In-depth structure-function studies of voltage-gated Na+ channels and peptide toxins are continuousl...
The venoms of Buthidae scorpions are known to contain basic, single-chain protein -toxins consisting...
International audienceWe report the detailed chemical, immunological and pharmacological characteriz...
International audienceAlpha scorpion toxins bind to receptor site 3 on voltage-dependent sodium chan...
Scorpion venom is a rich source of promising therapeutic compounds, such as highly selective ion cha...
International audienceIn this study, we have characterized the immunological and pharmacological pro...
International audienceThe venom of the North African scorpion Androctonus amoreuxi (Aam) was analyze...
International audienceA new toxin, BotIT2, with a unique mode of action on the isolated giant axon o...
International audienceOn attempts to identify toxins showing original profile of activity among K+ c...
Kbot55 is a 39 amino acid peptide isolated from the venom of the Tunisian scorpion Buthus occitanus ...
AbstractA new neurotoxic component named BmK abT was purified from the venom of Chinese scorpion But...
AbstractBackground: Scorpion neurotoxins, which bind and modulate sodium channels, have been divided...
<正> The neurotoxins from scorpions are one kind of low molecular toxic proteins which can bind...
α-Scorpion toxins are modulators of voltage-gated Na(+) channels (Navs), which bind to the receptor ...
AbstractThe first example of a new sub-family of toxins (α-KTx20.1) from the scorpion Tityus trivitt...
In-depth structure-function studies of voltage-gated Na+ channels and peptide toxins are continuousl...
The venoms of Buthidae scorpions are known to contain basic, single-chain protein -toxins consisting...