Evolution, structural features, and biochemical diversity of snake venom serine proteinases

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Estadual do Norte Fluminense Darcy Ribeiro
dc.contributorUNESC
dc.date.accessioned2018-12-11T17:12:15Z
dc.date.available2018-12-11T17:12:15Z
dc.date.created2018-12-11T17:12:15Z
dc.date.issued2016-01-01
dc.identifierSnake Venoms and Envenomation: Modern Trends and Future Prospects, p. 169-213.
dc.identifierhttp://hdl.handle.net/11449/174650
dc.identifier2-s2.0-85019878643
dc.identifier9162508978945887
dc.identifier0000-0003-2460-1145
dc.description.abstractSnake venom serine proteinases share high sequence homology and are structurally similar to mammalian serine proteinases. Detailed structural comparisons based on highresolution crystal structures highlight structural determinants and indicate the roles of the differences in amino acid sequences, positions and degree of glycosylation and surface charges in modulating and determining their specificity. This makes them especially interesting for a wide range of clinical and diagnostic applications.
dc.languageeng
dc.relationSnake Venoms and Envenomation: Modern Trends and Future Prospects
dc.rightsAcesso restrito
dc.sourceScopus
dc.subjectActivity
dc.subjectEvolution
dc.subjectMolecular mechanisms
dc.subjectSerine proteinase
dc.subjectSnake venom
dc.subjectStructure
dc.titleEvolution, structural features, and biochemical diversity of snake venom serine proteinases
dc.typeCapítulos de libros


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