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http://purl.uniprot.org/citations/31435636http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31435636http://www.w3.org/2000/01/rdf-schema#comment"Human immunodeficiency virus (HIV) transcription is closely associated with chromatin remodeling. Retinoblastoma binding protein 4 (RBBP4) is a histone chaperone implicated in chromatin remodeling. However, the role of RBBP4 in HIV-1 infection and the underlying mechanism remain elusive. In the present study, we showed that RBBP4 plays a negative regulatory role during HIV-1 infection. RBBP4 expression was significantly increased in HIV-1-infected T cells. RBBP4 binds to the HIV-1 long terminal repeat (LTR), represses HIV-1 LTR-mediated transcription through recruiting nuclear receptor subfamily 2 group F member 1(NR2F1) and histone deacetylase 1 and 2 (HDAC1/2) to HIV-1 LTR, and further controls local histone 3 (H3) deacetylation and chromatin compaction. Furthermore, the occupancy of RBBP4, HDAC1/2, and NR2F1 on LTR in HIV-latent J-lat cells was significantly higher than that in HIV-1-activated cells. In conclusion, our results establish RBBP4 as a new potent antiretroviral factor, which may provide theoretical basis for the treatment of HIV in the future."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.org/dc/terms/identifier"doi:10.1093/abbs/gmz082"xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/author"Cheng L."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/author"Lu L."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/author"Yang Z."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/author"Wu N."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/author"Pan K."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/name"Acta Biochim Biophys Sin (Shanghai)"xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/pages"934-944"xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/title"Retinoblastoma binding protein 4 represses HIV-1 long terminal repeat-mediated transcription by recruiting NR2F1 and histone deacetylase."xsd:string
http://purl.uniprot.org/citations/31435636http://purl.uniprot.org/core/volume"51"xsd:string
http://purl.uniprot.org/citations/31435636http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31435636
http://purl.uniprot.org/citations/31435636http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31435636
http://purl.uniprot.org/uniprot/#_B4DRT0-mappedCitation-31435636http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31435636
http://purl.uniprot.org/uniprot/#_Q09028-mappedCitation-31435636http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31435636
http://purl.uniprot.org/uniprot/B4DRT0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31435636
http://purl.uniprot.org/uniprot/Q09028http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31435636