Lys49 phospholipase A2 (Lys49-PLA2) homologues are catalytically inactive snake venom toxins with diverse biological activities, but their functional characterization requires recombinant production strategies to overcome the limitations inherent to native venom-derived proteins. Here, we produced recombinant BaMtx (rB...
D. Torrejón, A. Regalado, Alex Proleón et al.· Toxins· 0 citations
Overall, the available evidence indicates that Bothrops venom proteins represent promising sources of bioactive anticancer scaffolds; however, significant translational challenges remain.
Ana Gabriela Amado-Argüelles, A. Yarlequé, Dan E. Vivas-Ruiz et al.· International Journal of Bio...· 0 citations
Snake venom metalloproteinases are major determinants of viperid venom pathology, but the specific contribution of their metalloprotease domain to toxin function remains insufficiently defined. Here, we produced and characterized the metalloprotease domain of Pictolysin-III, a P-III metalloproteinase from Bothrops pict...
A. Roque, D. Torrejón, Alex Proleón et al.· Biomedicine & pharmacotherap...· 0 citations
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