http://purl.uniprot.org/citations/24118933 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/24118933 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/24118933 | http://www.w3.org/2000/01/rdf-schema#comment | "In addition to the conventional neurotoxins and cytotoxins, venom of the lynx spider Oxyopes takobius was found to contain two-domain modular toxins named spiderines: OtTx1a, 1b, 2a and 2b. These toxins show both insecticidal activity (a median lethal dose against flesh fly larvae of 75 μg·g(-1)) and potent antimicrobial effects (minimal inhibitory concentrations in the range 0.1-10 μm). Full sequences of the purified spiderines were established by a combination of Edman degradation, mass spectrometry and cDNA cloning. They are relatively large molecules (~ 110 residues, 12.0-12.5 kDa) and consist of two distinct modules separated by a short linker. The N-terminal part (~ 40 residues) contains no cysteine residues, is highly cationic, forms amphipathic α-helical structures in a membrane-mimicking environment, and shows potent cytolytic effects on cells of various origins. The C-terminal part (~ 60 residues) is disulfide-rich (five S-S bonds), and contains the inhibitor cystine knot (ICK/knottin) signature. The N-terminal part of spiderines is very similar to linear cytotoxic peptides found in various organisms, whereas the C-terminal part corresponds to the usual spider neurotoxins. We synthesized the modules of OtTx1a and compared their activity to that of full-length mature toxin produced recombinantly, highlighting the importance of the N-terminal part, which retained full-length toxin activity in both insecticidal and antimicrobial assays. The unique structure of spiderines completes the range of two-domain spider toxins."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.org/dc/terms/identifier | "doi:10.1111/febs.12547"xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.org/dc/terms/identifier | "doi:10.1111/febs.12547"xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Grishin E.V."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Grishin E.V."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Kozlov S.A."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Kozlov S.A."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Feofanov A.V."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Feofanov A.V."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Vassilevski A.A."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Vassilevski A.A."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Sachkova M.Y."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Sachkova M.Y."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Ignatova A.A."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/author | "Ignatova A.A."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/name | "FEBS J."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/name | "FEBS J."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/pages | "6247-6261"xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/pages | "6247-6261"xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/title | "Spider toxins comprising disulfide-rich and linear amphipathic domains: A new class of molecules identified in the lynx spider Oxyopes takobius."xsd:string |
http://purl.uniprot.org/citations/24118933 | http://purl.uniprot.org/core/title | "Spider toxins comprising disulfide-rich and linear amphipathic domains: A new class of molecules identified in the lynx spider Oxyopes takobius."xsd:string |