| http://purl.uniprot.org/citations/20385552 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20385552 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20385552 | http://www.w3.org/2000/01/rdf-schema#comment | "Spider venoms provide a highly valuable source of peptide toxins that act on a wide diversity of membrane-bound receptors and ion channels. In this work, we report isolation, biochemical analysis, and pharmacological characterization of a novel family of spider peptide toxins, designated beta/delta-agatoxins. These toxins consist of 36-38 amino acid residues and originate from the venom of the agelenid funnel-web spider Agelena orientalis. The presented toxins show considerable amino acid sequence similarity to other known toxins such as mu-agatoxins, curtatoxins, and delta-palutoxins-IT from the related spiders Agelenopsis aperta, Hololena curta, and Paracoelotes luctuosus. beta/delta-Agatoxins modulate the insect Na(V) channel (DmNa(V)1/tipE) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non-inactivating persistent Na(+) current is induced (site 3-like action). Interestingly, both effects take place in a voltage-dependent manner, producing a bell-shaped curve between -80 and 0 mV, and they are absent in mammalian Na(V) channels. To the best of our knowledge, this is the first detailed report of peptide toxins with such a peculiar pharmacological behavior, clearly indicating that traditional classification of toxins according to their binding sites may not be as exclusive as previously assumed."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.125211"xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.125211"xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Tytgat J."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Tytgat J."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Grishin E."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Grishin E."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Debaveye S."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Debaveye S."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Vassilevski A."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Vassilevski A."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Billen B."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Billen B."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Nikolsky A."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/author | "Nikolsky A."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/pages | "18545-18554"xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/pages | "18545-18554"xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/title | "Unique bell-shaped voltage-dependent modulation of Na+ channel gating by novel insect-selective toxins from the spider Agelena orientalis."xsd:string |
| http://purl.uniprot.org/citations/20385552 | http://purl.uniprot.org/core/title | "Unique bell-shaped voltage-dependent modulation of Na+ channel gating by novel insect-selective toxins from the spider Agelena orientalis."xsd:string |