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dc.creatorGutiérrez, José María
dc.creatorLomonte, Bruno
dc.date.accessioned2017-06-08T20:10:50Z
dc.date.available2017-06-08T20:10:50Z
dc.date.issued2013-02
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0041010112007490
dc.identifier.issn0041-0101
dc.identifier.urihttps://hdl.handle.net/10669/30071
dc.description.abstractPhospholipases A2 (PLA2s) are abundant components of snake venoms, where they play toxic and digestive roles. Despite having a similar three-dimensional structure, venom PLA2s exert an amazing variety of toxic and pharmacological effects, which include neurotoxic, myotoxic, hemolytic, edematogenic, hyperalgesic, pro-inflammatory, hypotensive, platelet-aggregation inhibitory, anticoagulant, cytotoxic, and bactericidal activities. Toxinologists have made significant contributions to deciphering the structure, molecular evolution, mechanisms of action, receptors, role of enzymatic activity for toxicity, structural determinants of toxicity and selectivity, and the impact of these enzymes in the overall pathophysiology of snakebite envenoming. The present work highlights some of the most relevant contributions in the study of venom PLA2s, including the personal accounts of the authors of these studies.es_ES
dc.language.isoen_USes_ES
dc.sourceToxicon; Volumen 62. 2013es_ES
dc.subjectPhospholipase A2es_ES
dc.subjectSnake venomes_ES
dc.subjectToxicityes_ES
dc.subjectNeurotoxicityes_ES
dc.subjectMyotoxicityes_ES
dc.subjectMolecular evolutiones_ES
dc.subjectReceptorses_ES
dc.subjectEnzymatic activityes_ES
dc.titlePhospholipases A2: Unveiling the secrets of a functionally versatile group of snake venom toxinses_ES
dc.typeartículo original
dc.identifier.doi10.1016/j.toxicon.2012.09.006
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid23025922


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