Snake venom Lys49 myotoxins: From phospholipases A2 to non-enzymatic membrane disruptors
Author:
Funder
International Center of Genetic Engineering and Biotechnology
Vicerrectoría de Investigación
University of Costa Rica
Publisher
Elsevier BV
Subject
Toxicology
Reference113 articles.
1. A molecular mechanism for Lys49-phospholipase A2 activity based on ligand-induced conformational change;Ambrosio;J. Biol. Chem.,2005
2. Differential susceptibility of C2C12 myoblasts and myotubes to group II phospholipase A2 myotoxins from crotalid snake venoms;Angulo;Cell Biochem. Funct.,2005
3. Structural characterization and phylogenetic relationships of myotoxin II from Atropoides (Bothrops) nummifer snake venom, a Lys49 phospholipase A2 homologue;Angulo;Int. J. Biochem. Cell Biol.,2002
4. Myotoxic and cytolytic activities of dimeric Lys49 phospholipase A2 homologues are reduced, but not abolished, by a pH-induced dissociation;Angulo;Toxicon,2005
5. Permeabilization of E. coli K12 inner and outer membranes by bothropstoxin-I, a Lys49 phospholipase A2 from Bothrops jararacussu;Aragão;Toxicon,2008
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