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Chemical synthesis and characterization of maurotoxin, a short scorpion toxin with four disulfide bridges that acts on K+ channels.
- R. Kharrat, K. Mabrouk, J. Sabatier
- Biology, ChemistryEuropean journal of biochemistry
- 1 December 1996
The physicochemical and pharmacological properties of synthetic maurotoxin were indistinguishable from those of natural mau Rotoxin, which suggests that natural mAUrotoxin adopts the same half-cystine pairing pattern.
Development of an ELISA for the detection of scorpion venoms in sera of humans envenomed by Androctonus australis garzonii (Aag) and Buthus occitanus tunetanus (Bot): correlation with clinical…
Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca2+ release channel/ryanodine receptors
Hemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channels.
Overall, these data identify a new biologically active toxin that belongs to a family of peptides active on the ryanodine-sensitive channel.
Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries: insight into the evolution of the snake venom integrin-inhibition system.
The results highlight the fact that disintegrins have evolved a restricted panel of integrin-blocking sequences that segregate with defined branches of the phylogenetic tree of the integrin alpha-chains, providing novel insights into the evolutionary adaptation of the snake venom antagonists to the ligand-binding sites of their target integrin receptors.
Purification and chemical and biological characterizations of seven toxins from the Mexican scorpion, Centruroides suffusus suffusus.
The antigenic structure of a scorpion toxin.
Snake venomics: Comparative analysis of the venom proteomes of the Tunisian snakes Cerastes cerastes, Cerastes vipera and Macrovipera lebetina
The comparative proteomic analysis of Tunisian snake venoms provides a comprehensible catalogue of secreted proteins, which may contribute to a deeper understanding of the biological effects of the venoms, and may also serve as a starting point for studying structure‐function correlations of individual toxins.
PIVL, a new serine protease inhibitor from Macrovipera lebetina transmediterranea venom, impairs motility of human glioblastoma cells.