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Lysine 49 phospholipase A2 proteins.
Structure, Function and Biophysical Aspects of the Myotoxins from Snake Venoms
The purpose of this review is to describe the structure and function of these myotoxins and to evaluate features they might share which could shed light on the function and structure of snake venom toxins.
A Molecular Mechanism for Lys49-Phospholipase A2 Activity Based on Ligand-induced Conformational Change*
An activation mechanism is proposed that relates fatty acid retention at the active site to conformational changes within the C-terminal region, a part of the molecule that has long been associated with Ca2+-independent membrane damaging activity and myotoxicity.
Molecular cloning and sequence analysis of cDNAs for metalloproteinases from broad-banded copperhead Agkistrodon contortrix laticinctus.
The cDNA sequences of two related genes coding for metalloproteinases from a venom gland library of Agkistrodon contortrix laticinctus have been determined, and it is suggested that snake venom fibrinolytic metaloproteinase genes belong to the metalliproteinase/disintegrin gene family.
Citrate inhibition of snake venom proteases.
Hemorrhagic toxins from rattlesnake (Crotalus atrox) venom. Pathogenesis of hemorrhage induced by three purified toxins.
The experimental injection of three purified hemorrhagic toxins induced hemorrhage by the same mechanism as does the crude venom, ie, per rhexis, in addition, one of the toxins, hemorrhagic toxin beta, causes myonecrosis.