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http://purl.uniprot.org/citations/21430051http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21430051http://www.w3.org/2000/01/rdf-schema#comment"Us3, a serine/threonine kinase encoded by all alphaherpesviruses, plays diverse roles during virus infection, including preventing virus-induced apoptosis, facilitating nuclear egress of capsids, stimulating mRNA translation and promoting cell-to-cell spread of virus infection. Given this diversity, the full spectrum of Us3 function may not yet be recognized. We noted, in transiently transfected cells, that herpes simplex virus type 2 (HSV-2) Us3 disrupted promyelocytic leukemia protein nuclear bodies (PML-NBs). However, PML-NB disruption was not observed in cells expressing catalytically inactive HSV-2 Us3. Analysis of PML-NBs in Vero cells transfected with pseudorabies virus (PRV) Us3 and those in Vero cells infected with Us3-null or -repaired PRV strains indicated that PRV Us3 expression also leads to the disruption of PML-NBs. While loss of PML-NBs in response to Us3 expression was prevented by the proteasome inhibitor MG132, Us3-mediated degradation of PML was not observed in infected cells or in transfected cells expressing enhanced green fluorescent protein (EGFP)-tagged PML isoform IV. These findings demonstrate that Us3 orthologues derived from distantly related alphaherpesviruses cause a disruption of PML-NBs in a kinase- and proteasome-dependent manner but, unlike the alphaherpesvirus ICP0 orthologues, do not target PML for degradation."xsd:string
http://purl.uniprot.org/citations/21430051http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00022-11"xsd:string
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/author"Jung M."xsd:string
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/author"Banfield B.W."xsd:string
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/author"Finnen R.L."xsd:string
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/author"Neron C.E."xsd:string
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/name"J Virol"xsd:string
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/pages"5301-5311"xsd:string
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/title"The alphaherpesvirus serine/threonine kinase us3 disrupts promyelocytic leukemia protein nuclear bodies."xsd:string
http://purl.uniprot.org/citations/21430051http://purl.uniprot.org/core/volume"85"xsd:string
http://purl.uniprot.org/citations/21430051http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21430051
http://purl.uniprot.org/citations/21430051http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21430051
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http://purl.uniprot.org/uniprot/#_B4DV67-mappedCitation-21430051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21430051
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http://purl.uniprot.org/uniprot/#_P29590-mappedCitation-21430051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21430051
http://purl.uniprot.org/uniprot/#_Q05835-mappedCitation-21430051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21430051
http://purl.uniprot.org/uniprot/#_Q9BZY1-mappedCitation-21430051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21430051
http://purl.uniprot.org/uniprot/#_Q59GQ8-mappedCitation-21430051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21430051
http://purl.uniprot.org/uniprot/#_Q59H09-mappedCitation-21430051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21430051
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http://purl.uniprot.org/uniprot/P29590http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21430051