| http://purl.uniprot.org/citations/24189547 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24189547 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24189547 | http://www.w3.org/2000/01/rdf-schema#comment | "Viroporins are small integral membrane proteins functional in viral assembly and egress by promoting permeabilization. Blocking of viroporin function therefore constitutes a target for antiviral development. Classical swine fever virus (CSFV) protein p7 has been recently regarded as a class II viroporin. Here, we sought to establish the determinants of the CSFV p7 permeabilizing activity in a minimal model system. Assessment of an overlapping peptide library mapped the porating domain to the C-terminal hydrophobic stretch (residues 39-67). Pore-opening dependence on pH or sensitivity to channel blockers observed for the full protein required the inclusion of a preceding polar sequence (residues 33-38). Effects of lipid composition and structural data further support that the resulting peptide (residues 33-67), may comprise a bona fide surrogate to assay p7 activity in model membranes. Our observations imply that CSFV p7 relies on genus-specific structures-mechanisms to perform its viroporin function."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.antiviral.2013.10.015"xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.antiviral.2013.10.015"xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Borca M.V."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Borca M.V."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Gladue D.P."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Gladue D.P."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Nieva J.L."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Nieva J.L."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Huarte N."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Huarte N."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Largo E."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/author | "Largo E."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/name | "Antiviral Res."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/name | "Antiviral Res."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/pages | "30-36"xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/pages | "30-36"xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/title | "Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/title | "Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function."xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/volume | "101"xsd:string |
| http://purl.uniprot.org/citations/24189547 | http://purl.uniprot.org/core/volume | "101"xsd:string |