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Understanding the in vitro neuromuscular activity of snake venom Lys49 phospholipase A(2) homologues
(Pergamon-Elsevier B.V. Ltd, 2010-01-01)
Phospholipases A(2) (PLA(2)s) with a lysine substituting for the highly conserved aspartate 49, Lys49 PLA(2) homologues, are important myotoxic components in venoms from snakes of Viperidae family. These proteins induce ...
Understanding the in vitro neuromuscular activity of snake venom Lys49 phospholipase A(2) homologues
(Pergamon-Elsevier B.V. Ltd, 2010-01-01)
Phospholipases A(2) (PLA(2)s) with a lysine substituting for the highly conserved aspartate 49, Lys49 PLA(2) homologues, are important myotoxic components in venoms from snakes of Viperidae family. These proteins induce ...
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 ...
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 ...
Comparison between apo and complexed structures of bothropstoxin-I reveals the role of Lys122 and Ca2+-binding loop region for the catalytically inactive Lys49-PLA(2)s
(Academic Press Inc. Elsevier B.V., 2010-07-01)
Phospholipases A(2) (Asp49-PLA(2)s) are enzymes responsible for cellular membrane disruption through Ca2+-dependent hydrolysis of phospholipids. A class of these proteins (Lys49-PLA(2)s) does not show catalytic activity ...
Comparison between apo and complexed structures of bothropstoxin-I reveals the role of Lys122 and Ca2+-binding loop region for the catalytically inactive Lys49-PLA(2)s
(Academic Press Inc. Elsevier B.V., 2010-07-01)
Phospholipases A(2) (Asp49-PLA(2)s) are enzymes responsible for cellular membrane disruption through Ca2+-dependent hydrolysis of phospholipids. A class of these proteins (Lys49-PLA(2)s) does not show catalytic activity ...
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 ...
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 ...
A Lys49 phospholipase A2 homologue from Bothrops asper snake venom induces proliferation, apoptosis and necrosis in a lymphoblastoid cell line
(2005-04)
Lys49 phospholipase A2 homologues are abundant in viperid snake venoms. These proteins have substitutions at the calcium-binding loop and catalytic center which render them enzymatically inactive; however, they display a ...
A Lys49 phospholipase A2 homologue from Bothrops asper snake venom induces proliferation, apoptosis and necrosis in a lymphoblastoid cell line
(2005-04)
Lys49 phospholipase A2 homologues are abundant in viperid snake venoms. These proteins have substitutions at the calcium-binding loop and catalytic center which render them enzymatically inactive; however, they display a ...