PMC:7600245 / 32291-32955 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T127","span":{"begin":84,"end":87},"obj":"Body_part"},{"id":"T128","span":{"begin":640,"end":643},"obj":"Body_part"}],"attributes":[{"id":"A127","pred":"fma_id","subj":"T127","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A128","pred":"fma_id","subj":"T128","obj":"http://purl.org/sig/ont/fma/fma278683"}],"text":"Darunavir (Figure 6) is another antiretroviral drug that competitively inhibits the HIV-1 aspartate protease [101,102]. In addition to the active site, it has been reported that the flexible darunavir binds to another site on the surface of the enzyme, which accounts for its resilience against potential mutations in the targeted protease [103]. Darunavir was approved in 2015 by the U.S. FDA and usually prescribed in combination with the pharmacokinetic booster cobicistat. Although structurally similar to ritonavir, cobicistat lacks antiviral activity due to the lack of the central phenyl-propanol moiety, a key structural feature of HIV protease inhibitors."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T294","span":{"begin":139,"end":145},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T295","span":{"begin":155,"end":158},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T296","span":{"begin":548,"end":556},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T297","span":{"begin":612,"end":613},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"Darunavir (Figure 6) is another antiretroviral drug that competitively inhibits the HIV-1 aspartate protease [101,102]. In addition to the active site, it has been reported that the flexible darunavir binds to another site on the surface of the enzyme, which accounts for its resilience against potential mutations in the targeted protease [103]. Darunavir was approved in 2015 by the U.S. FDA and usually prescribed in combination with the pharmacokinetic booster cobicistat. Although structurally similar to ritonavir, cobicistat lacks antiviral activity due to the lack of the central phenyl-propanol moiety, a key structural feature of HIV protease inhibitors."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T475","span":{"begin":0,"end":9},"obj":"Chemical"},{"id":"T476","span":{"begin":47,"end":51},"obj":"Chemical"},{"id":"T477","span":{"begin":90,"end":99},"obj":"Chemical"},{"id":"T480","span":{"begin":191,"end":200},"obj":"Chemical"},{"id":"T481","span":{"begin":347,"end":356},"obj":"Chemical"},{"id":"T482","span":{"begin":465,"end":475},"obj":"Chemical"},{"id":"T483","span":{"begin":510,"end":519},"obj":"Chemical"},{"id":"T484","span":{"begin":521,"end":531},"obj":"Chemical"},{"id":"T485","span":{"begin":538,"end":547},"obj":"Chemical"},{"id":"T486","span":{"begin":588,"end":594},"obj":"Chemical"},{"id":"T487","span":{"begin":640,"end":663},"obj":"Chemical"},{"id":"T488","span":{"begin":644,"end":663},"obj":"Chemical"},{"id":"T490","span":{"begin":653,"end":663},"obj":"Chemical"}],"attributes":[{"id":"A475","pred":"chebi_id","subj":"T475","obj":"http://purl.obolibrary.org/obo/CHEBI_367163"},{"id":"A476","pred":"chebi_id","subj":"T476","obj":"http://purl.obolibrary.org/obo/CHEBI_23888"},{"id":"A477","pred":"chebi_id","subj":"T477","obj":"http://purl.obolibrary.org/obo/CHEBI_132943"},{"id":"A478","pred":"chebi_id","subj":"T477","obj":"http://purl.obolibrary.org/obo/CHEBI_29995"},{"id":"A479","pred":"chebi_id","subj":"T477","obj":"http://purl.obolibrary.org/obo/CHEBI_72314"},{"id":"A480","pred":"chebi_id","subj":"T480","obj":"http://purl.obolibrary.org/obo/CHEBI_367163"},{"id":"A481","pred":"chebi_id","subj":"T481","obj":"http://purl.obolibrary.org/obo/CHEBI_367163"},{"id":"A482","pred":"chebi_id","subj":"T482","obj":"http://purl.obolibrary.org/obo/CHEBI_72291"},{"id":"A483","pred":"chebi_id","subj":"T483","obj":"http://purl.obolibrary.org/obo/CHEBI_45409"},{"id":"A484","pred":"chebi_id","subj":"T484","obj":"http://purl.obolibrary.org/obo/CHEBI_72291"},{"id":"A485","pred":"chebi_id","subj":"T485","obj":"http://purl.obolibrary.org/obo/CHEBI_22587"},{"id":"A486","pred":"chebi_id","subj":"T486","obj":"http://purl.obolibrary.org/obo/CHEBI_30396"},{"id":"A487","pred":"chebi_id","subj":"T487","obj":"http://purl.obolibrary.org/obo/CHEBI_35660"},{"id":"A488","pred":"chebi_id","subj":"T488","obj":"http://purl.obolibrary.org/obo/CHEBI_37670"},{"id":"A489","pred":"chebi_id","subj":"T488","obj":"http://purl.obolibrary.org/obo/CHEBI_60258"},{"id":"A490","pred":"chebi_id","subj":"T490","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"}],"text":"Darunavir (Figure 6) is another antiretroviral drug that competitively inhibits the HIV-1 aspartate protease [101,102]. In addition to the active site, it has been reported that the flexible darunavir binds to another site on the surface of the enzyme, which accounts for its resilience against potential mutations in the targeted protease [103]. Darunavir was approved in 2015 by the U.S. FDA and usually prescribed in combination with the pharmacokinetic booster cobicistat. Although structurally similar to ritonavir, cobicistat lacks antiviral activity due to the lack of the central phenyl-propanol moiety, a key structural feature of HIV protease inhibitors."}

{"project":"LitCovid-sentences","denotations":[{"id":"T235","span":{"begin":0,"end":119},"obj":"Sentence"},{"id":"T236","span":{"begin":120,"end":346},"obj":"Sentence"},{"id":"T237","span":{"begin":347,"end":389},"obj":"Sentence"},{"id":"T238","span":{"begin":390,"end":476},"obj":"Sentence"},{"id":"T239","span":{"begin":477,"end":664},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Darunavir (Figure 6) is another antiretroviral drug that competitively inhibits the HIV-1 aspartate protease [101,102]. In addition to the active site, it has been reported that the flexible darunavir binds to another site on the surface of the enzyme, which accounts for its resilience against potential mutations in the targeted protease [103]. Darunavir was approved in 2015 by the U.S. FDA and usually prescribed in combination with the pharmacokinetic booster cobicistat. Although structurally similar to ritonavir, cobicistat lacks antiviral activity due to the lack of the central phenyl-propanol moiety, a key structural feature of HIV protease inhibitors."}

{"project":"LitCovid-PubTator","denotations":[{"id":"934","span":{"begin":84,"end":89},"obj":"Species"},{"id":"935","span":{"begin":0,"end":9},"obj":"Chemical"},{"id":"936","span":{"begin":191,"end":200},"obj":"Chemical"},{"id":"937","span":{"begin":347,"end":356},"obj":"Chemical"},{"id":"938","span":{"begin":465,"end":475},"obj":"Chemical"},{"id":"939","span":{"begin":510,"end":519},"obj":"Chemical"},{"id":"940","span":{"begin":521,"end":531},"obj":"Chemical"},{"id":"941","span":{"begin":588,"end":603},"obj":"Chemical"}],"attributes":[{"id":"A934","pred":"tao:has_database_id","subj":"934","obj":"Tax:11676"},{"id":"A935","pred":"tao:has_database_id","subj":"935","obj":"MESH:D000069454"},{"id":"A936","pred":"tao:has_database_id","subj":"936","obj":"MESH:D000069454"},{"id":"A937","pred":"tao:has_database_id","subj":"937","obj":"MESH:D000069454"},{"id":"A938","pred":"tao:has_database_id","subj":"938","obj":"MESH:D000069547"},{"id":"A939","pred":"tao:has_database_id","subj":"939","obj":"MESH:D019438"},{"id":"A940","pred":"tao:has_database_id","subj":"940","obj":"MESH:D000069547"},{"id":"A941","pred":"tao:has_database_id","subj":"941","obj":"MESH:C439395"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"Darunavir (Figure 6) is another antiretroviral drug that competitively inhibits the HIV-1 aspartate protease [101,102]. In addition to the active site, it has been reported that the flexible darunavir binds to another site on the surface of the enzyme, which accounts for its resilience against potential mutations in the targeted protease [103]. Darunavir was approved in 2015 by the U.S. FDA and usually prescribed in combination with the pharmacokinetic booster cobicistat. Although structurally similar to ritonavir, cobicistat lacks antiviral activity due to the lack of the central phenyl-propanol moiety, a key structural feature of HIV protease inhibitors."}