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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 ...
Structural bases for a complete myotoxic mechanism: Crystal structures of two non-catalytic phospholipases A(2)-like from Bothrops brazili venom
(Elsevier Science BvAmsterdamHolanda, 2013)
Crystal structure of a novel myotoxic Arg49 phospholipase A(2) homolog (zhaoermiatoxin) from Zhaoermia mangshanensis snake venom: Insights into Arg49 coordination and the role of Lys122 in the polarization of the C-terminus
(Pergamon-Elsevier B.V. Ltd, 2008-04-01)
The venom of Zhaoermia mangshanensis, encountered solely in Mt Mang in China's Hunan Province, exhibits coagulant, phosphodiesterase, L-amino acid oxidase, kallikrein, phospholipase A(2) and myotoxic activities. The ...
Crystal structure of a novel myotoxic Arg49 phospholipase A(2) homolog (zhaoermiatoxin) from Zhaoermia mangshanensis snake venom: Insights into Arg49 coordination and the role of Lys122 in the polarization of the C-terminus
(Pergamon-Elsevier B.V. Ltd, 2008-04-01)
The venom of Zhaoermia mangshanensis, encountered solely in Mt Mang in China's Hunan Province, exhibits coagulant, phosphodiesterase, L-amino acid oxidase, kallikrein, phospholipase A(2) and myotoxic activities. The ...
Lys-49 phospholipases A2 as active enzymes for beta-arachidonoyl phospholipid bilayer membranes
(1997)
Phospholipases A2 containing Lys-49 have been reported to be extremely weak or
inactive as enzyme. We have recently shown that basic proteins I and II (BP-I and BP-II), Lys-
49-PLA2s isolated from the venom of Trimeresurus ...
Lys-49 phospholipases A2 as active enzymes for beta-arachidonoyl phospholipid bilayer membranes
(1997)
Phospholipases A2 containing Lys-49 have been reported to be extremely weak or
inactive as enzyme. We have recently shown that basic proteins I and II (BP-I and BP-II), Lys-
49-PLA2s isolated from the venom of Trimeresurus ...
Crystal structure of myotoxin II, a monomeric Lys49-Phospholipase A(2) homologue isolated from the venom of Cerrophidion (Bothrops) godmani
(Academic Press Inc., 1999-06-15)
Lys49-Phospholipase A(2) (Lys49-PLA(2)) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we ...
Crystal structure of myotoxin II, a monomeric Lys49-Phospholipase A(2) homologue isolated from the venom of Cerrophidion (Bothrops) godmani
(Academic Press Inc., 1999-06-15)
Lys49-Phospholipase A(2) (Lys49-PLA(2)) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we ...
Snake venom Lys49 myotoxins: from phospholipases A2 to non-enzymatic membrane disruptors
(2012-09)
Snake venoms often contain toxins that cause a rapid necrosis of skeletal muscle fibers,
referred to as myotoxins. The most common among them are phospholipases A2 (PLA2s),
enzymes that have two independent evolutionary ...