RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/36827123http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36827123http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36827123http://www.w3.org/2000/01/rdf-schema#comment"Elevenins are peptides found in a range of organisms, including arthropods, annelids, nematodes, and molluscs. They consist of 17 to 19 amino acid residues with a single conserved disulfide bond. The subject of this study, elevenin-Vc1, was first identified in the venom of the cone snail Conus victoriae (Gen. Comp. Endocrinol. 2017, 244, 11-18). Although numerous elevenin sequences have been reported, their physiological function is unclear, and no structural information is available. Upon intracranial injection in mice, elevenin-Vc1 induced hyperactivity at doses of 5 or 10 nmol. The structure of elevenin-Vc1, determined using nuclear magnetic resonance spectroscopy, consists of a short helix and a bend region stabilised by the single disulfide bond. The elevenin-Vc1 structural fold is similar to that of α-conotoxins such as α-RgIA and α-ImI, which are also found in the venoms of cone snails and are antagonists at specific subtypes of nicotinic acetylcholine receptors (nAChRs). In an attempt to mimic the functional motif, Asp-Pro-Arg, of α-RgIA and α-ImI, we synthesised an analogue, designated elevenin-Vc1-DPR. However, neither elevenin-Vc1 nor the analogue was active at six different human nAChR subtypes (α1β1εδ, α3β2, α3β4, α4β2, α7, and α9α10) at 1 µM concentrations."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.org/dc/terms/identifier"doi:10.3390/md21020081"xsd:string
http://purl.uniprot.org/citations/36827123http://purl.org/dc/terms/identifier"doi:10.3390/md21020081"xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Adams D.J."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Adams D.J."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Norton R.S."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Norton R.S."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Robinson A.J."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Robinson A.J."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Krishnarjuna B."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Krishnarjuna B."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Seow J."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Seow J."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Sunanda P."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Sunanda P."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Robinson S.D."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Robinson S.D."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Belgi A."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Belgi A."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Safavi-Hemami H."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Safavi-Hemami H."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Tae H.-S."xsd:string
http://purl.uniprot.org/citations/36827123http://purl.uniprot.org/core/author"Tae H.-S."xsd:string