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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 ...
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, ...
Snake venomics and antivenomics: Proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming
(2009-03-06)
Snakebite envenoming represents a neglected tropical disease that has a heavy public health impact, particularly in Asia, Africa and Latin America. A global initiative, aimed at increasing antivenom production and ...
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 ...
Differential susceptibility of C2C12 myoblasts and myotubes to group II phospholipase A2 myotoxins from crotalid snake venoms
(2005)
Group II phospholipase A2 (PLA2) myotoxins isolated from Viperidae/Crotalidae snake venoms induce a rapid cytolytic
effect upon diverse cell types in vitro. Previous studies suggested that this effect could be more ...
The Phospholipase A2 Homologues of Snake Venoms: Biological Activities and Their Possible Adaptive Roles
(2009)
A particular subgroup of toxins with phospholipase A2 (PLA2) structure, but devoid of this enzymatic activity, is commonly found in the venoms of snakes of the family Viperidae, and known as the PLA2 homologues. Among ...
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 ...
Identification of the myotoxic site of the Lys49 phospholipase A2 from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities
(2001)
Group II phospholipase A2 (PLA2) myotoxins found in the venoms of Crotalidae snakes can be divided into `Asp49' and
`Lys49' isoforms, the latter being considered catalytically-inactive variants. Previous studies on one ...
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 ...
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 ...