PubMed:24996823 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":71},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":72,"end":160},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":161,"end":346},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":347,"end":504},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":505,"end":573},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":574,"end":803},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":804,"end":932},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":933,"end":1149},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1150,"end":1320},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1321,"end":1420},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1421,"end":1551},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":71},"obj":"Sentence"},{"id":"T2","span":{"begin":72,"end":160},"obj":"Sentence"},{"id":"T3","span":{"begin":161,"end":346},"obj":"Sentence"},{"id":"T4","span":{"begin":347,"end":504},"obj":"Sentence"},{"id":"T5","span":{"begin":505,"end":573},"obj":"Sentence"},{"id":"T6","span":{"begin":574,"end":803},"obj":"Sentence"},{"id":"T7","span":{"begin":804,"end":932},"obj":"Sentence"},{"id":"T8","span":{"begin":933,"end":1320},"obj":"Sentence"},{"id":"T9","span":{"begin":1321,"end":1551},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":71},"obj":"Sentence"},{"id":"T2","span":{"begin":72,"end":160},"obj":"Sentence"},{"id":"T3","span":{"begin":161,"end":346},"obj":"Sentence"},{"id":"T4","span":{"begin":347,"end":504},"obj":"Sentence"},{"id":"T5","span":{"begin":505,"end":573},"obj":"Sentence"},{"id":"T6","span":{"begin":574,"end":803},"obj":"Sentence"},{"id":"T7","span":{"begin":804,"end":932},"obj":"Sentence"},{"id":"T8","span":{"begin":933,"end":1149},"obj":"Sentence"},{"id":"T9","span":{"begin":1150,"end":1320},"obj":"Sentence"},{"id":"T10","span":{"begin":1321,"end":1420},"obj":"Sentence"},{"id":"T11","span":{"begin":1421,"end":1551},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":458,"end":474},"obj":"HP_0002721"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":452,"end":485},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC512"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"ICD10","denotations":[{"id":"T1","span":{"begin":452,"end":485},"obj":"http://purl.bioontology.org/ontology/ICD10/B24"},{"id":"T2","span":{"begin":452,"end":485},"obj":"http://purl.bioontology.org/ontology/ICD10/Z71.7"},{"id":"T3","span":{"begin":452,"end":485},"obj":"http://purl.bioontology.org/ontology/ICD10/B20-B24.9"},{"id":"T4","span":{"begin":458,"end":474},"obj":"http://purl.bioontology.org/ontology/ICD10/D84.9"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":64,"end":67},"obj":"FMAID:167404"},{"id":"_T2","span":{"begin":233,"end":241},"obj":"FMAID:67408"},{"id":"_T3","span":{"begin":233,"end":241},"obj":"FMAID:165330"},{"id":"_T4","span":{"begin":247,"end":252},"obj":"FMAID:68646"},{"id":"_T5","span":{"begin":247,"end":252},"obj":"FMAID:169002"},{"id":"_T6","span":{"begin":329,"end":336},"obj":"FMAID:165447"},{"id":"_T7","span":{"begin":329,"end":336},"obj":"FMAID:67257"},{"id":"_T8","span":{"begin":384,"end":393},"obj":"FMAID:165070"},{"id":"_T9","span":{"begin":384,"end":393},"obj":"FMAID:67180"},{"id":"_T10","span":{"begin":592,"end":597},"obj":"FMAID:169002"},{"id":"_T11","span":{"begin":592,"end":597},"obj":"FMAID:68646"},{"id":"_T12","span":{"begin":768,"end":773},"obj":"FMAID:68646"},{"id":"_T13","span":{"begin":768,"end":773},"obj":"FMAID:169002"},{"id":"_T14","span":{"begin":904,"end":907},"obj":"FMAID:167404"},{"id":"_T15","span":{"begin":926,"end":931},"obj":"FMAID:68646"},{"id":"_T16","span":{"begin":926,"end":931},"obj":"FMAID:169002"},{"id":"_T17","span":{"begin":1031,"end":1034},"obj":"FMAID:167404"},{"id":"_T18","span":{"begin":1202,"end":1207},"obj":"FMAID:68646"},{"id":"_T19","span":{"begin":1202,"end":1207},"obj":"FMAID:169002"},{"id":"_T20","span":{"begin":1231,"end":1238},"obj":"FMAID:165447"},{"id":"_T21","span":{"begin":1231,"end":1238},"obj":"FMAID:67257"},{"id":"_T22","span":{"begin":1273,"end":1281},"obj":"FMAID:165447"},{"id":"_T23","span":{"begin":1273,"end":1281},"obj":"FMAID:67257"},{"id":"_T24","span":{"begin":1392,"end":1399},"obj":"FMAID:196750"},{"id":"_T25","span":{"begin":1392,"end":1399},"obj":"FMAID:82761"},{"id":"_T26","span":{"begin":1532,"end":1535},"obj":"FMAID:167404"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T2","span":{"begin":72,"end":82},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T3","span":{"begin":189,"end":199},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T4","span":{"begin":526,"end":536},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T5","span":{"begin":624,"end":634},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T6","span":{"begin":710,"end":720},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T7","span":{"begin":883,"end":893},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T8","span":{"begin":995,"end":1005},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T9","span":{"begin":1102,"end":1112},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T10","span":{"begin":1180,"end":1190},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T11","span":{"begin":1220,"end":1230},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T12","span":{"begin":1344,"end":1354},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T13","span":{"begin":1473,"end":1483},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T14","span":{"begin":68,"end":70},"obj":"http://www.uniprot.org/uniprot/P80511"},{"id":"T15","span":{"begin":1035,"end":1037},"obj":"http://www.uniprot.org/uniprot/P80511"},{"id":"T16","span":{"begin":1536,"end":1538},"obj":"http://www.uniprot.org/uniprot/P80511"},{"id":"T17","span":{"begin":311,"end":328},"obj":"http://www.uniprot.org/uniprot/Q8WUM4"},{"id":"T18","span":{"begin":315,"end":336},"obj":"http://www.uniprot.org/uniprot/Q9BWK7"},{"id":"T19","span":{"begin":761,"end":764},"obj":"http://www.uniprot.org/uniprot/P01730"},{"id":"T20","span":{"begin":1220,"end":1238},"obj":"http://www.uniprot.org/uniprot/Q08380"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T2","span":{"begin":72,"end":82},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T3","span":{"begin":189,"end":199},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T4","span":{"begin":526,"end":536},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T5","span":{"begin":624,"end":634},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T6","span":{"begin":710,"end":720},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T7","span":{"begin":883,"end":893},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T8","span":{"begin":995,"end":1005},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T9","span":{"begin":1102,"end":1112},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T10","span":{"begin":1180,"end":1190},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T11","span":{"begin":1220,"end":1230},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T12","span":{"begin":1344,"end":1354},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T13","span":{"begin":1473,"end":1483},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T14","span":{"begin":55,"end":59},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T15","span":{"begin":340,"end":344},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T16","span":{"begin":347,"end":351},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T17","span":{"begin":895,"end":899},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T18","span":{"begin":1026,"end":1030},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T19","span":{"begin":1074,"end":1078},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T20","span":{"begin":1144,"end":1148},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T21","span":{"begin":1245,"end":1249},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T22","span":{"begin":1415,"end":1419},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T23","span":{"begin":1527,"end":1531},"obj":"http://www.uniprot.org/uniprot/Q9WU78"},{"id":"T24","span":{"begin":761,"end":764},"obj":"http://www.uniprot.org/uniprot/P06332"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":247,"end":252},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":452,"end":480},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11709"},{"id":"T3","span":{"begin":452,"end":480},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11723"},{"id":"T4","span":{"begin":452,"end":480},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11676"},{"id":"T5","span":{"begin":452,"end":480},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/12721"},{"id":"T6","span":{"begin":458,"end":480},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11673"},{"id":"T7","span":{"begin":475,"end":480},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/184751"},{"id":"T8","span":{"begin":592,"end":597},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T9","span":{"begin":768,"end":773},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T10","span":{"begin":926,"end":931},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T11","span":{"begin":946,"end":948},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/13893"},{"id":"T12","span":{"begin":1202,"end":1207},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":26,"end":33},"obj":"http://purl.obolibrary.org/obo/GO_0007114"},{"id":"T2","span":{"begin":565,"end":572},"obj":"http://purl.obolibrary.org/obo/GO_0007114"},{"id":"T3","span":{"begin":682,"end":689},"obj":"http://purl.obolibrary.org/obo/GO_0007114"},{"id":"T4","span":{"begin":795,"end":802},"obj":"http://purl.obolibrary.org/obo/GO_0007114"},{"id":"T5","span":{"begin":1128,"end":1135},"obj":"http://purl.obolibrary.org/obo/GO_0007114"},{"id":"T6","span":{"begin":1502,"end":1509},"obj":"http://purl.obolibrary.org/obo/GO_0007114"},{"id":"T7","span":{"begin":104,"end":112},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T8","span":{"begin":258,"end":273},"obj":"http://purl.obolibrary.org/obo/GO_0032393"},{"id":"T9","span":{"begin":258,"end":273},"obj":"http://purl.obolibrary.org/obo/GO_0032394"},{"id":"T10","span":{"begin":258,"end":273},"obj":"http://purl.obolibrary.org/obo/GO_0032395"},{"id":"T11","span":{"begin":423,"end":432},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T12","span":{"begin":559,"end":572},"obj":"http://purl.obolibrary.org/obo/GO_0046755"},{"id":"T13","span":{"begin":735,"end":739},"obj":"http://purl.obolibrary.org/obo/GO_0016246"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":149,"end":153},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":247,"end":252},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":592,"end":597},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":768,"end":773},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":926,"end":931},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":1202,"end":1207},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":219,"end":241},"obj":"http://purl.obolibrary.org/obo/GO_0001772"},{"id":"T8","span":{"begin":233,"end":241},"obj":"http://purl.obolibrary.org/obo/GO_0045202"},{"id":"T9","span":{"begin":384,"end":393},"obj":"http://purl.obolibrary.org/obo/GO_0005768"},{"id":"T10","span":{"begin":384,"end":401},"obj":"http://purl.obolibrary.org/obo/GO_0097443"},{"id":"T11","span":{"begin":489,"end":495},"obj":"http://purl.obolibrary.org/obo/GO_0019012"},{"id":"T12","span":{"begin":1312,"end":1319},"obj":"http://purl.obolibrary.org/obo/GO_0019012"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":11,"end":19},"obj":"http://edamontology.org/topic_0749"},{"id":"T2","span":{"begin":11,"end":19},"obj":"http://edamontology.org/topic_0111"},{"id":"T3","span":{"begin":11,"end":19},"obj":"http://edamontology.org/topic_1312"},{"id":"T4","span":{"begin":219,"end":232},"obj":"http://edamontology.org/topic_0804"},{"id":"T5","span":{"begin":317,"end":328},"obj":"http://edamontology.org/topic_0602"},{"id":"T6","span":{"begin":329,"end":336},"obj":"http://edamontology.org/topic_0078"},{"id":"T7","span":{"begin":444,"end":451},"obj":"http://edamontology.org/topic_1312"},{"id":"T8","span":{"begin":444,"end":451},"obj":"http://edamontology.org/topic_0111"},{"id":"T9","span":{"begin":444,"end":451},"obj":"http://edamontology.org/topic_0749"},{"id":"T10","span":{"begin":452,"end":457},"obj":"http://edamontology.org/topic_2815"},{"id":"T11","span":{"begin":831,"end":841},"obj":"http://edamontology.org/topic_3382"},{"id":"T12","span":{"begin":949,"end":980},"obj":"http://edamontology.org/topic_3656"},{"id":"T13","span":{"begin":1017,"end":1025},"obj":"http://edamontology.org/topic_1312"},{"id":"T14","span":{"begin":1017,"end":1025},"obj":"http://edamontology.org/topic_0111"},{"id":"T15","span":{"begin":1017,"end":1025},"obj":"http://edamontology.org/topic_0749"},{"id":"T16","span":{"begin":1113,"end":1121},"obj":"http://edamontology.org/topic_0749"},{"id":"T17","span":{"begin":1113,"end":1121},"obj":"http://edamontology.org/topic_1312"},{"id":"T18","span":{"begin":1113,"end":1121},"obj":"http://edamontology.org/topic_0111"},{"id":"T19","span":{"begin":1231,"end":1238},"obj":"http://edamontology.org/topic_0078"},{"id":"T20","span":{"begin":1273,"end":1281},"obj":"http://edamontology.org/topic_0078"},{"id":"T21","span":{"begin":1357,"end":1365},"obj":"http://edamontology.org/topic_0749"},{"id":"T22","span":{"begin":1373,"end":1382},"obj":"http://edamontology.org/topic_0602"},{"id":"T23","span":{"begin":1513,"end":1522},"obj":"http://edamontology.org/topic_0749"},{"id":"T24","span":{"begin":1513,"end":1522},"obj":"http://edamontology.org/topic_1312"},{"id":"T25","span":{"begin":1513,"end":1522},"obj":"http://edamontology.org/topic_0111"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":92,"end":100},"obj":"http://edamontology.org/data_2048"},{"id":"T2","span":{"begin":117,"end":126},"obj":"http://edamontology.org/operation_0004"},{"id":"T3","span":{"begin":154,"end":159},"obj":"http://edamontology.org/data_2100"},{"id":"T4","span":{"begin":175,"end":183},"obj":"http://edamontology.org/data_2048"},{"id":"T5","span":{"begin":329,"end":336},"obj":"http://edamontology.org/format_1208"},{"id":"T6","span":{"begin":329,"end":336},"obj":"http://edamontology.org/data_1467"},{"id":"T7","span":{"begin":1231,"end":1238},"obj":"http://edamontology.org/format_1208"},{"id":"T8","span":{"begin":1231,"end":1238},"obj":"http://edamontology.org/data_1467"},{"id":"T9","span":{"begin":1273,"end":1281},"obj":"http://edamontology.org/data_1467"},{"id":"T10","span":{"begin":1273,"end":1281},"obj":"http://edamontology.org/format_1208"},{"id":"T11","span":{"begin":1292,"end":1300},"obj":"http://edamontology.org/data_2619"},{"id":"T12","span":{"begin":1366,"end":1382},"obj":"http://edamontology.org/data_2359"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T2","span":{"begin":72,"end":80},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T3","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0272"},{"id":"Lectin_T4","span":{"begin":72,"end":80},"obj":"https://acgg.asia/db/lfdb/LfDB0272"},{"id":"Lectin_T5","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0274"},{"id":"Lectin_T6","span":{"begin":72,"end":80},"obj":"https://acgg.asia/db/lfdb/LfDB0274"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":458,"end":474},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0021094"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":458,"end":474},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002721"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":452,"end":488},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"11676"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":142,"end":153},"obj":"Body_part"},{"id":"T2","span":{"begin":233,"end":241},"obj":"Body_part"},{"id":"T3","span":{"begin":258,"end":264},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0045202"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000084"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":142,"end":153},"obj":"Cell"},{"id":"T2","span":{"begin":245,"end":252},"obj":"Cell"},{"id":"T3","span":{"begin":258,"end":264},"obj":"Cell"},{"id":"T4","span":{"begin":766,"end":773},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000738"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000084"}],"text":"Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.\nGalectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association."}