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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 ...
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 ...
Interfacial surface charge and free accessibility to the PLA(2)-active site-like region are essential requirements for the activity of Lys49 PLA(2) homologues
(Elsevier B.V., 2007-03-01)
Lys49 phospholipase A(2) homologues are highly myotoxic and cause extensive tissue damage but do not display hydrolytic activity towards natural phospholipids. The binding of heparin, heparin derivatives and polyanionic ...
Interfacial surface charge and free accessibility to the PLA(2)-active site-like region are essential requirements for the activity of Lys49 PLA(2) homologues
(Elsevier B.V., 2007-03-01)
Lys49 phospholipase A(2) homologues are highly myotoxic and cause extensive tissue damage but do not display hydrolytic activity towards natural phospholipids. The binding of heparin, heparin derivatives and polyanionic ...
Understanding the in vitro neuromuscular activity of snake venom Lys49 phospholipase A(2) homologues
(Pergamon-Elsevier B.V. Ltd, 2014)
Comparative structural studies on Lys49-phospholipases A(2) from Bothrops genus reveal their myotoxic site
(Academic Press Inc. Elsevier B.V., 2009-08-01)
Phospholipases A(2) (PLA(2)s) are membrane-associated enzymes that hydrolyze phospholipids at the sn-2 position, releasing lysophospholipids and free fatty acids. Phospholipase A(2) homologues (Lys49-PLA(2)s) are highly ...