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Isolation and Functional Characterization of an Acidic Myotoxic Phospholipase A₂ from Colombian Bothrops asper Venom
(2017-10-26)
Myotoxic phospholipases A₂ (PLA₂) are responsible for many clinical manifestations in envenomation by Bothrops snakes. A new myotoxic acidic Asp49 PLA₂ (BaCol PLA₂) was isolated from Colombian Bothrops asper venom using ...
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from colombian Bothrops asper venom
(2017-11-01)
Myotoxic phospholipases A2 (PLA2) are responsible for many clinical manifestations in envenomation by Bothrops snakes. A new myotoxic acidic Asp49 PLA2 (BaCol PLA2) was isolated from Colombian Bothrops asper venom using ...
The Intriguing Phospholipases A(2) Homologues: Relevant Structural Features on Myotoxicity and Catalytic Inactivity
(Bentham Science Publ Ltd, 2009-08-01)
Phospholipases A(2) homologues are found in the venom of Crotalinae snakes, being their main action related to myonecrosis induction. Although many studies on these toxins had already been performed, their mechanism of ...
The Intriguing Phospholipases A(2) Homologues: Relevant Structural Features on Myotoxicity and Catalytic Inactivity
(Bentham Science Publ Ltd, 2009-08-01)
Phospholipases A(2) homologues are found in the venom of Crotalinae snakes, being their main action related to myonecrosis induction. Although many studies on these toxins had already been performed, their mechanism of ...
The intriguing phospholipases A2 homologues: Relevant structural features on myotoxicity and catalytic inactivity
(2009-08-01)
Phospholipases A2 homologues are found in the venom of Crotalinae snakes, being their main action related to myonecrosis induction. Although many studies on these toxins had already been performed, their mechanism of action ...
Structural basis for a novel model for myotoxic activity on phospholipases A2
(Int Union Crystallography, 2014-08-01)
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 ...
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 ...
Structural basis of phospholipase A2-like myotoxin inhibition by chicoric acid, a novel potent inhibitor of ophidian toxins
(2018-12-01)
Background: Specific compounds found in vegetal species have been demonstrated to be efficient inhibitors of snake toxins, such as phospholipase A2-like (PLA2-like) proteins. These particular proteins, present in several ...
Comparative structural studies on Lys49-phospholipases A(2) from Bothrops genus reveal their myotoxic site
(Academic Press Inc. Elsevier B.V., 2014)