Search
Now showing items 1-10 of 19
Structure of myotoxin-II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
(2006)
Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic
proteins which, although lacking catalytic activity, possess the ability to disrupt
biological membranes, inducing significant muscle-tissue loss ...
Isolation, characterization and molecular cloning of AnMIP, a new α-type phospholipase A2 myotoxin inhibitor from the plasma of the snake Atropoides nummifer (Viperidae: Crotalinae)
(2007)
A new phospholipase A2 (PLA2)-inhibitory protein was isolated from the plasma of Atropoides nummifer, a crotaline snake from Central
America. This inhibitor was named AnMIP, given its ability to neutralize the activity ...
Inhibitory effect of fucoidan on the activities of crotaline snake venom myotoxic phospholipases A2
(2003)
Myotoxic phospholipases A2 account for most of the muscle necrosis that results from envenenomation by crotaline snakes. In this study,
we investigated the protective effect of fucoidan, a natural sulfated polysaccharide ...
Tyr→Trp-substituted peptide 115-129 of a Lys49 phospholipase A2 expresses enhanced membrane-damaging activities and reproduces its in vivo myotoxic effect
(1999)
Myotoxin II is a group II Lys49 phospholipase A2 (PLA2) isolated from the venom of the snake Bothrops asper. Previous
studies on a synthetic peptide derived from its heparin-binding, cationic/hydrophobic sequence 115^129 ...
Crystallization of the Lys49 PLA2 homologue, myotoxin II from the venom of Atropoides nummifer
(2004-12)
Myotoxin II, a Lys49 catalytically inactive phospholipase A2 homologue from Atropoides nummifer venom, was purified, characterized
and crystallized. The crystals belongs to the tetragonal system, space group P43212, with ...
Biochemistry and toxicology of toxins purified from the venom of the snake Bothrops asper
(2009-12-01)
The isolation and study of individual snake venom components paves the way for a deeper
understanding of the pathophysiology of envenomings – thus potentially contributing to
improved therapeutic modalities in the clinical ...
Cytotoxicity induced in myotubes by a Lys49 phospholipase A2 homologue from the venom of the snake Bothrops asper: Evidence of rapid plasma membrane damage and a dual role for extracellular calcium
(2007-12)
Acute muscle tissue damage, myonecrosis, is a typical consequence of envenomations by snakes of the family Viperidae. Catalytically-inactive Lys49 phospholipase A2 homologues are abundant myotoxic components in viperid ...
Comparative study of synthetic peptides corresponding to region 115-129 in Lys49 myotoxic phospholipases A2 from snake venoms
(2003)
Lys49 phospholipase A2 homologues constitute a group of catalytically-inactive proteins, present in the venoms of many
crotalid snakes, which induce myonecrosis. Current evidence supports the mapping of their toxic site ...
Neutralization of Bothrops asper venom by antibodies, natural products, and synthetic drugs: contributions to understanding snakebite envenomings and their treatment
(2009)
Interest in studies on the neutralization of snake venoms and toxins by diverse types of
inhibitors is two-fold. From an applied perspective, results enclose the potential to be
translated into useful therapeutic products ...
Immunochemical properties of the N-terminal helix of myotoxin II, a lysine-49 phospholipase A2 from Bothrops asper snake venom
(2001)
Myotoxic class II phospholipases A2 from snake venoms can be divided into Asp49 and Lys49 types. The latter, including
Bothrops asper myotoxin II, exert membrane damage despite lacking catalytic activity. A heparin-binding, ...