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http://purl.uniprot.org/citations/15218184http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15218184http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15218184http://www.w3.org/2000/01/rdf-schema#comment"The human cytomegalovirus UL37 gene encodes at least three isoforms, which share N-terminal UL37 exon 1 (UL37x1) sequences. UL37 proteins traffic dually into the endoplasmic reticulum (ER) and to mitochondria. Trafficking of the UL37 glycoprotein (gpUL37) in relation to its post-translational processing was investigated. gpUL37 is internally cleaved in the ER and its products traffic differentially. Its C-terminal fragment (UL37(COOH)) is ER-localized and N-glycosylated. Unlike conventional ER signal sequences, its N-terminal fragment is stable and traffics to mitochondria. Inhibition of N-glycosylation did not block pUL37 cleavage and dramatically decreased the levels of but not of UL37(COOH). pUL37(M), which differs from gpUL37 by the lack of residues 178-262 and hence the UL37x3 consensus signal peptidase cleavage site, traffics into the ER and mitochondria, but is neither cleaved nor N-glycosylated. This finding of a relationship between ER processing and mitochondrial importation of UL37 proteins is unique for herpesvirus proteins."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.org/dc/terms/identifier"doi:10.1099/vir.0.80094-0"xsd:string
http://purl.uniprot.org/citations/15218184http://purl.org/dc/terms/identifier"doi:10.1099/vir.0.80094-0"xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/author"Colberg-Poley A.M."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/author"Colberg-Poley A.M."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/author"Mavinakere M.S."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/author"Mavinakere M.S."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/name"J. Gen. Virol."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/name"J. Gen. Virol."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/pages"1989-1994"xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/pages"1989-1994"xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/title"Internal cleavage of the human cytomegalovirus UL37 immediate-early glycoprotein and divergent trafficking of its proteolytic fragments."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/title"Internal cleavage of the human cytomegalovirus UL37 immediate-early glycoprotein and divergent trafficking of its proteolytic fragments."xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/volume"85"xsd:string
http://purl.uniprot.org/citations/15218184http://purl.uniprot.org/core/volume"85"xsd:string
http://purl.uniprot.org/citations/15218184http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15218184
http://purl.uniprot.org/citations/15218184http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15218184
http://purl.uniprot.org/citations/15218184http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15218184
http://purl.uniprot.org/citations/15218184http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15218184
http://purl.uniprot.org/uniprot/P16778http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15218184
http://purl.uniprot.org/uniprot/P16778#attribution-E2AB3C4D14127E58F41A07C0FBB8CFB6http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15218184