| http://purl.uniprot.org/citations/26157134 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26157134 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26157134 | http://www.w3.org/2000/01/rdf-schema#comment | "Herpes simplex virus (HSV) is an important human pathogen. It enters cells through an orchestrated process that requires four essential glycoproteins, gD, gH/gL, and gB, activated in cascade fashion by receptor-binding and signaling. gH/gL heterodimer is conserved across the Herpesviridae family. HSV entry is enabled by gH/gL interaction with αvβ6- or αvβ8-integrin receptors. We report that the interaction of virion gH/gL with integrins resulted in gL dissociation and its release in the medium. gL dissociation occurred if all components of the entry apparatus-receptor-bound gD and gB-were present and was prevented if entry was blocked by a neutralizing monoclonal antibody to gH or by a mutation in gH. We propose that (i) gL dissociation from gH/gL is part of the activation of HSV glycoproteins, critical for HSV entry; and (ii) gL is a functional inhibitor of gH and maintains gH in an inhibited form until receptor-bound gD and integrins signal to gH/gL."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1506846112"xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1506846112"xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/author | "Campadelli-Fiume G."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/author | "Campadelli-Fiume G."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/author | "Gianni T."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/author | "Gianni T."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/author | "Massaro R."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/author | "Massaro R."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/pages | "E3901-3910"xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/pages | "E3901-3910"xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/title | "Dissociation of HSV gL from gH by alphavbeta6- or alphavbeta8-integrin promotes gH activation and virus entry."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/title | "Dissociation of HSV gL from gH by alphavbeta6- or alphavbeta8-integrin promotes gH activation and virus entry."xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/volume | "112"xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://purl.uniprot.org/core/volume | "112"xsd:string |
| http://purl.uniprot.org/citations/26157134 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26157134 |
| http://purl.uniprot.org/citations/26157134 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26157134 |
| http://purl.uniprot.org/citations/26157134 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26157134 |
| http://purl.uniprot.org/citations/26157134 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26157134 |