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dc.creatorLomonte, Bruno
dc.creatorAngulo Ugalde, Yamileth
dc.creatorSasa Marín, Mahmood
dc.creatorGutiérrez, José María
dc.date.accessioned2016-11-16T17:04:04Z
dc.date.available2016-11-16T17:04:04Z
dc.date.issued2009
dc.identifier.citationhttp://www.eurekaselect.com/84726/article#
dc.identifier.issn1875-5305
dc.identifier.urihttps://hdl.handle.net/10669/29251
dc.description.abstractA 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 these, the most frequent type presents a lysine residue at position 49 (Lys49), in substitution of the otherwise conserved aspartate (Asp49) of catalytically-active PLA2s. A brief and updated overview of these toxic PLA2 homologues is presented, emphasizing their various biological activities, both in vivo and in vitro. The relevance of these bioactivities in relation to their possible adaptive roles for the snakes is discussed. Finally, experiments designed to assess the validity of such hypothetical roles are suggested, to stimulate future studies in this field.es_ES
dc.description.sponsorshipSweden-Central America NeTropicaes_ES
dc.description.sponsorshipUniversidad de Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceProtein & Peptide Letters; Volumen 16, Número 8, 2009es_ES
dc.subjectMyotoxines_ES
dc.subjectPhospholipases A2es_ES
dc.subjectLys49 homologueses_ES
dc.subjectSnake venomes_ES
dc.titleThe Phospholipase A2 Homologues of Snake Venoms: Biological Activities and Their Possible Adaptive Roleses_ES
dc.typeartículo original
dc.identifier.doi10.2174/092986609788923356
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.description.procedenceUCR::Vicerrectoría de Docencia::Salud::Facultad de Medicina::Escuela de Medicinaes_ES


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