Tityus kappa (Ts κ), a novel toxin from the venom of the scorpion Tityus serrulatus, is a 35‐
residue polypeptide cross‐linked by three disulphide bridges and acts on small …

Four peptide inhibitors of small-conductance Ca2+-activated, apamin-sensitive K+ channels
(SKCa) have been isolated from the venom of the Chinese scorpion Buthus martensi …

Four peptidyl inhibitors of the small‐conductance Ca2+‐activated K+ channels (SKCa) have
been isolated from the venom of the Chinese scorpion Buthus martensi. These peptides …

Scorpion venoms contain numerous toxic polypeptides displaying various pharmacological
activities. These toxins interact with ion channels of excitable membranes. Long toxins (60 …

Maurotoxin is a toxin isolated from the venom of the Tunisian chactoid scorpion Scorpio
maurus. It is a 34‐amino‐acid peptide cross‐linked by four disulfide bridges. Maurotoxin …

On attempts to identify toxins showing original profile of activity among K+ channels, we
purified Kbot1, a scorpion toxin that blocks Kv1 and SK potassium channels. With 28 amino …

The crystal structures of two group III α-like toxins from the scorpion Buthus martensii Karsch,
BmK M1 and BmK M4, were determined at 1.7 Å and 1.3 Å resolution and refined to R …

Three novel peptide inhibitors of the SKCa channels were purified to homogeneity from the
venom of the scorpion Androctonus mauretanicus mauretanicus using one step of RP …

In the last decade, numerous polypeptide toxins acting on ion channels have been isolated
and characterized from diverse scorpion venoms. These toxins are useful pharmacological …

The primary structure of TsTX-IV, a neurotoxin isolated from Tityus serrulatus scorpion
venom, is reported. Its amino acid sequence was determined by automated Edman …