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http://purl.uniprot.org/citations/9282826http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9282826http://www.w3.org/2000/01/rdf-schema#comment"The p17 matrix protein of the human immunodeficiency virus type 1 (HIV-1) plays a crucial role in AIDS pathogenesis. It orchestrates viral assembly and directs the preintegration complex to the nucleus of infected cells. Recently, the three-dimensional structure of p17 was shown to resemble that of interferon-gamma (IFN-gamma), suggesting that both proteins might share analogous functions. We demonstrate that in monocytes, p17 shares with IFN-gamma the ability to induce 1alpha-hydroxylase activity and to activate fructose 1,6-bisphosphatase gene expression in the presence of 25-hydroxyvitamin D3. However, p17 does not bind to the IFN-gamma cell membrane receptor and fails to increase expression of IFN-gamma-induced proteins, such as tryptophanyl-tRNA synthetase, Fc gammaRI, and HLA DR or B7/BB1 antigens. Altogether, our results raise the possibility that the structural resemblance between p17 and IFN-gamma causes the selective activation of a common pathway resulting in the production of 1,25-dihydroxyvitamin D3. We also found that unlike IFN-gamma, p17 increases the intracellular ATP content. Since transport of the HIV-1 preintegration complex through the nuclear membrane is an ATP-dependent process, our observation suggests that p17 plays a double role in this active transport, not only by acting as a chaperone molecule but also by recruiting the necessary energy for this process."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.org/dc/terms/identifier"doi:10.1089/jir.1997.17.461"xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/author"Solomon D."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/author"Just J."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/author"Cayre Y.E."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/author"Besancon F."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/author"Van Weyenbergh J."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/author"Wietzerbin J."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/author"Guillozo H."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/author"Bourgeade M.F."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/name"J Interferon Cytokine Res"xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/pages"461-467"xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/title"HIV-1 p17 and IFN-gamma both induce fructose 1,6-bisphosphatase."xsd:string
http://purl.uniprot.org/citations/9282826http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9282826http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9282826
http://purl.uniprot.org/citations/9282826http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9282826
http://purl.uniprot.org/uniprot/O15528#attribution-F66950E02CCB67F98568B0AD2301649Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9282826
http://purl.uniprot.org/uniprot/P01579#attribution-F66950E02CCB67F98568B0AD2301649Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9282826
http://purl.uniprot.org/uniprot/Q77YG1#attribution-98C05C50411A38BD9CB88DF39013F5DEhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9282826
http://purl.uniprot.org/uniprot/Q77YG1#attribution-F66950E02CCB67F98568B0AD2301649Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9282826