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http://purl.uniprot.org/citations/19837656http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19837656http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19837656http://www.w3.org/2000/01/rdf-schema#comment"The origin and evolution of venom proteins in helodermatid lizards were investigated by multidisciplinary techniques. Our analyses elucidated novel toxin types resultant from three unique domain-expression processes: 1) The first full-length sequences of lethal toxin isoforms (helofensins) revealed this toxin type to be constructed by an ancestral monodomain, monoproduct gene (beta-defensin) that underwent three tandem domain duplications to encode a tetradomain, monoproduct with a possible novel protein fold; 2) an ancestral monodomain gene (encoding a natriuretic peptide) was medially extended to become a pentadomain, pentaproduct through the additional encoding of four tandemly repeated proline-rich peptides (helokinestatins), with the five discrete peptides liberated from each other by posttranslational proteolysis; and 3) an ancestral multidomain, multiproduct gene belonging to the vasoactive intestinal peptide (VIP)/glucagon family being mutated to encode for a monodomain, monoproduct (exendins) followed by duplication and diversification into two variant classes (exendins 1 and 2 and exendins 3 and 4). Bioactivity characterization of exendin and helokinestatin elucidated variable cardioactivity between isoforms within each class. These results highlight the importance of utilizing evolutionary-based search strategies for biodiscovery and the virtually unexplored potential of lizard venoms in drug design and discovery."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.org/dc/terms/identifier"doi:10.1093/molbev/msp251"xsd:string
http://purl.uniprot.org/citations/19837656http://purl.org/dc/terms/identifier"doi:10.1093/molbev/msp251"xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Fry B.G."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Fry B.G."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Hodgson W.C."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Hodgson W.C."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Norman J.A."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Norman J.A."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Shaw C."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Shaw C."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Winter K."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Winter K."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Wong L."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Wong L."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Scanlon D."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Scanlon D."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Karas J."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Karas J."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Kwok H.F."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Kwok H.F."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Roelants K."xsd:string
http://purl.uniprot.org/citations/19837656http://purl.uniprot.org/core/author"Roelants K."xsd:string