{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Woods MW"],"funding":["Canadian Institutes of Health Research"],"pagination":["27"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4021598"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["<h4>Background</h4>Type I interferon (IFN) inhibits virus replication by activating multiple antiviral mechanisms and pathways. It has long been recognized that type I IFNs can potently block HIV-1 replication in vitro; as such, HIV-1 has been used as a system to identify and characterize IFN-induced antiviral proteins responsible for this block. IFN-induced HERC5 contains an amino-terminal Regulator of Chromosome Condensation 1 (RCC1)-like domain and a carboxyl-terminal Homologous to the E6-AP Carboxyl Terminus (HECT) domain. HERC5 is the main cellular E3 ligase that conjugates the IFN-induced protein ISG15 to proteins. This E3 ligase activity was previously shown to inhibit the replication of evolutionarily diverse viruses, including HIV-1. The contribution of the RCC1-like domain to the"],"journal":["Retrovirology"],"pubmed_title":["Interferon-induced HERC5 is evolving under positive selection and inhibits HIV-1 particle production by a novel mechanism targeting Rev/RRE-dependent RNA nuclear export."],"pmcid":["PMC4021598"],"funding_grant_id":["MOP 130465","MOP 286719","MOP 317646"],"pubmed_authors":["Haeryfar SM","Tom SK","Tong JG","Cavanagh PC","Woods MW","Szabo PA","Dikeakos JD","Barr SD"],"additional_accession":[]},"is_claimable":false,"name":"Interferon-induced HERC5 is evolving under positive selection and inhibits HIV-1 particle production by a novel mechanism targeting Rev/RRE-dependent RNA nuclear export.","description":"<h4>Background</h4>Type I interferon (IFN) inhibits virus replication by activating multiple antiviral mechanisms and pathways. It has long been recognized that type I IFNs can potently block HIV-1 replication in vitro; as such, HIV-1 has been used as a system to identify and characterize IFN-induced antiviral proteins responsible for this block. IFN-induced HERC5 contains an amino-terminal Regulator of Chromosome Condensation 1 (RCC1)-like domain and a carboxyl-terminal Homologous to the E6-AP Carboxyl Terminus (HECT) domain. HERC5 is the main cellular E3 ligase that conjugates the IFN-induced protein ISG15 to proteins. This E3 ligase activity was previously shown to inhibit the replication of evolutionarily diverse viruses, including HIV-1. The contribution of the RCC1-like domain to the","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Apr","modification":"2025-04-19T02:40:16.616Z","creation":"2019-03-27T01:28:15Z"},"accession":"S-EPMC4021598","cross_references":{"pubmed":["24693865"],"doi":["10.1186/1742-4690-11-27"]}}