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Novel catalytically-inactive PII metalloproteinases from a viperid snake venom with substitutions in the canonical zinc-binding motif
(2016-10-12)
Snake venom metalloproteinases (SVMPs) play key biological roles in prey immobilization
and digestion. The majority of these activities depend on the hydrolysis of relevant protein substrates
in the tissues. Hereby, we ...
Wound exudate as a proteomic window to reveal different mechanisms of tissue damage by snake venom toxins
(2009)
In light of the complexity of wound tissue, proteomic analysis may not clearly reveal the nature of the wound or the processes involved in healing. However, exudate associated with wounds may provide a “window” on cellular ...
Local tissue damage induced by BaP1, a metalloproteinase isolated from Bothrops asper (Terciopelo) snake venom
(1995-12)
The pathogenesis of hemorrhage and other local effects induced by the metalloproteinase BaP1, isolated from Bothrops asper venom, was investigated using various in vivo and in vitro models. Upon intramuscular injection in ...
Understanding structural and functional aspects of PII snake venom metalloproteinases: Characterization of BlatH1, a hemorrhagic dimeric enzyme from the venom of Bothriechis lateralis
(2014-06)
A new homodimeric PII metalloproteinase, named BlatH1, was purified from the venom of the Central American arboreal viperid snake Bothriechis lateralis by a combination of anion-exchange chromatography, hydrophobic interaction ...