PMC:7443692 / 3255-4429
Annnotations
LitCovid-sample-MedDRA
{"project":"LitCovid-sample-MedDRA","denotations":[{"id":"T2","span":{"begin":47,"end":76},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T3","span":{"begin":544,"end":567},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T4","span":{"begin":798,"end":810},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"}],"attributes":[{"id":"A2","pred":"meddra_id","subj":"T2","obj":"http://purl.bioontology.org/ontology/MEDDRA/10050289"},{"id":"A3","pred":"meddra_id","subj":"T3","obj":"http://purl.bioontology.org/ontology/MEDDRA/10058063"},{"id":"A4","pred":"meddra_id","subj":"T4","obj":"http://purl.bioontology.org/ontology/MEDDRA/10062026"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-CHEBI
{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T15","span":{"begin":47,"end":58},"obj":"Chemical"},{"id":"T16","span":{"begin":213,"end":225},"obj":"Chemical"},{"id":"T17","span":{"begin":378,"end":386},"obj":"Chemical"},{"id":"T18","span":{"begin":481,"end":489},"obj":"Chemical"}],"attributes":[{"id":"A15","pred":"chebi_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A16","pred":"chebi_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A17","pred":"chebi_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A18","pred":"chebi_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-PD-NCBITaxon
{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T21","span":{"begin":0,"end":10},"obj":"Species"},{"id":"T22","span":{"begin":17,"end":25},"obj":"Species"},{"id":"T23","span":{"begin":176,"end":183},"obj":"Species"},{"id":"T24","span":{"begin":185,"end":195},"obj":"Species"},{"id":"T25","span":{"begin":1001,"end":1011},"obj":"Species"}],"attributes":[{"id":"A21","pred":"ncbi_taxonomy_id","subj":"T21","obj":"NCBItxid:2697049"},{"id":"A22","pred":"ncbi_taxonomy_id","subj":"T22","obj":"NCBItxid:694009"},{"id":"A23","pred":"ncbi_taxonomy_id","subj":"T23","obj":"NCBItxid:10239"},{"id":"A24","pred":"ncbi_taxonomy_id","subj":"T24","obj":"NCBItxid:2697049"},{"id":"A25","pred":"ncbi_taxonomy_id","subj":"T25","obj":"NCBItxid:2697049"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-sentences
{"project":"LitCovid-sample-sentences","denotations":[{"id":"T22","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"T23","span":{"begin":166,"end":341},"obj":"Sentence"},{"id":"T24","span":{"begin":342,"end":722},"obj":"Sentence"},{"id":"T25","span":{"begin":723,"end":966},"obj":"Sentence"},{"id":"T26","span":{"begin":967,"end":1174},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-PD-MONDO
{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T14","span":{"begin":0,"end":10},"obj":"Disease"},{"id":"T15","span":{"begin":17,"end":25},"obj":"Disease"},{"id":"T16","span":{"begin":185,"end":195},"obj":"Disease"},{"id":"T17","span":{"begin":877,"end":886},"obj":"Disease"},{"id":"T18","span":{"begin":1001,"end":1011},"obj":"Disease"}],"attributes":[{"id":"A14","pred":"mondo_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A15","pred":"mondo_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A16","pred":"mondo_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A17","pred":"mondo_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A18","pred":"mondo_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-UniProt
{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T281","span":{"begin":47,"end":78},"obj":"Protein"},{"id":"T296","span":{"begin":80,"end":84},"obj":"Protein"},{"id":"T297","span":{"begin":207,"end":225},"obj":"Protein"},{"id":"T401","span":{"begin":372,"end":386},"obj":"Protein"},{"id":"T402","span":{"begin":475,"end":489},"obj":"Protein"},{"id":"T403","span":{"begin":779,"end":783},"obj":"Protein"},{"id":"T404","span":{"begin":896,"end":900},"obj":"Protein"},{"id":"T405","span":{"begin":1029,"end":1033},"obj":"Protein"}],"attributes":[{"id":"A281","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A282","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q9NRA7"},{"id":"A283","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q9BYF1"},{"id":"A284","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q99N71"},{"id":"A285","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q99N70"},{"id":"A286","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q8R0I0"},{"id":"A287","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q86WT0"},{"id":"A288","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q6UWP0"},{"id":"A289","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q5RFN1"},{"id":"A290","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q5EGZ1"},{"id":"A291","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q58DD0"},{"id":"A292","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q56NL1"},{"id":"A293","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q56H28"},{"id":"A294","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/Q2PGE2"},{"id":"A295","pred":"uniprot_id","subj":"T281","obj":"https://www.uniprot.org/uniprot/C7ECU1"},{"id":"A296","pred":"uniprot_id","subj":"T296","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A297","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q9QAS2"},{"id":"A298","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q9QAR5"},{"id":"A299","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q9QAQ8"},{"id":"A300","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q9IW04"},{"id":"A301","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q9IKD1"},{"id":"A302","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q990M4"},{"id":"A303","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q990M3"},{"id":"A304","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q990M2"},{"id":"A305","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q990M1"},{"id":"A306","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q91AV1"},{"id":"A307","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q91A26"},{"id":"A308","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q8V436"},{"id":"A309","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q8JSP8"},{"id":"A310","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q8BB25"},{"id":"A311","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q86623"},{"id":"A312","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q85088"},{"id":"A313","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q85087"},{"id":"A314","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q82706"},{"id":"A315","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q82683"},{"id":"A316","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q80BV6"},{"id":"A317","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q7TFB1"},{"id":"A318","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q7TFA2"},{"id":"A319","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q7TA19"},{"id":"A320","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q7T6T3"},{"id":"A321","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q7T696"},{"id":"A322","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q77NC4"},{"id":"A323","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q6TNF9"},{"id":"A324","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q6R1L7"},{"id":"A325","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q6QU82"},{"id":"A326","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q6Q1S2"},{"id":"A327","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q696Q6"},{"id":"A328","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q66291"},{"id":"A329","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q66290"},{"id":"A330","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q66199"},{"id":"A331","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q66177"},{"id":"A332","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q66176"},{"id":"A333","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q66174"},{"id":"A334","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q65984"},{"id":"A335","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q5MQD0"},{"id":"A336","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q5I5X9"},{"id":"A337","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q5DIY0"},{"id":"A338","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q5DIX9"},{"id":"A339","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q5DIX8"},{"id":"A340","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q5DIX7"},{"id":"A341","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q52PA3"},{"id":"A342","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q4ZJS1"},{"id":"A343","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q4U5G0"},{"id":"A344","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q3T8J0"},{"id":"A345","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q3LZX1"},{"id":"A346","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q3I5J5"},{"id":"A347","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q14EB0"},{"id":"A348","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q0ZME7"},{"id":"A349","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q0Q4F2"},{"id":"A350","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q0Q475"},{"id":"A351","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q0Q466"},{"id":"A352","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q0GNB8"},{"id":"A353","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q02385"},{"id":"A354","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q02167"},{"id":"A355","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q01977"},{"id":"A356","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/Q008X4"},{"id":"A357","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P89344"},{"id":"A358","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P89343"},{"id":"A359","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P89342"},{"id":"A360","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P59594"},{"id":"A361","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P36334"},{"id":"A362","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P36300"},{"id":"A363","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P33470"},{"id":"A364","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P30208"},{"id":"A365","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P30207"},{"id":"A366","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P30206"},{"id":"A367","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P27662"},{"id":"A368","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P27655"},{"id":"A369","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P27277"},{"id":"A370","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P25194"},{"id":"A371","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P25193"},{"id":"A372","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P25192"},{"id":"A373","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P25191"},{"id":"A374","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P25190"},{"id":"A375","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P24413"},{"id":"A376","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P23052"},{"id":"A377","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P22432"},{"id":"A378","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P18450"},{"id":"A379","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P17662"},{"id":"A380","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P15777"},{"id":"A381","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P15423"},{"id":"A382","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P12722"},{"id":"A383","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P12651"},{"id":"A384","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P12650"},{"id":"A385","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P12647"},{"id":"A386","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P11225"},{"id":"A387","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P11224"},{"id":"A388","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P11223"},{"id":"A389","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P10033"},{"id":"A390","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P0DTC2"},{"id":"A391","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P07946"},{"id":"A392","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P07923"},{"id":"A393","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P05135"},{"id":"A394","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/P05134"},{"id":"A395","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/O90304"},{"id":"A396","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/O39227"},{"id":"A397","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/K9N5Q8"},{"id":"A398","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/A3EXG6"},{"id":"A399","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/A3EXD0"},{"id":"A400","pred":"uniprot_id","subj":"T297","obj":"https://www.uniprot.org/uniprot/A3EX94"},{"id":"A401","pred":"uniprot_id","subj":"T401","obj":"https://www.uniprot.org/uniprot/P31340"},{"id":"A402","pred":"uniprot_id","subj":"T402","obj":"https://www.uniprot.org/uniprot/P31340"},{"id":"A403","pred":"uniprot_id","subj":"T403","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A404","pred":"uniprot_id","subj":"T404","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A405","pred":"uniprot_id","subj":"T405","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-PD-IDO
{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T15","span":{"begin":42,"end":46},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T16","span":{"begin":102,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0044409"},{"id":"T17","span":{"begin":113,"end":117},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T18","span":{"begin":118,"end":123},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T19","span":{"begin":176,"end":183},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T20","span":{"begin":268,"end":272},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T21","span":{"begin":273,"end":277},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T22","span":{"begin":405,"end":420},"obj":"http://purl.obolibrary.org/obo/GO_0044409"},{"id":"T23","span":{"begin":416,"end":420},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T24","span":{"begin":421,"end":426},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T25","span":{"begin":643,"end":647},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T26","span":{"begin":877,"end":886},"obj":"http://purl.obolibrary.org/obo/IDO_0000586"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-PD-FMA
{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T15","span":{"begin":118,"end":123},"obj":"Body_part"},{"id":"T16","span":{"begin":213,"end":225},"obj":"Body_part"},{"id":"T17","span":{"begin":273,"end":277},"obj":"Body_part"},{"id":"T18","span":{"begin":378,"end":386},"obj":"Body_part"},{"id":"T19","span":{"begin":421,"end":426},"obj":"Body_part"},{"id":"T20","span":{"begin":481,"end":489},"obj":"Body_part"}],"attributes":[{"id":"A15","pred":"fma_id","subj":"T15","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A17","pred":"fma_id","subj":"T17","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A18","pred":"fma_id","subj":"T18","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A19","pred":"fma_id","subj":"T19","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A20","pred":"fma_id","subj":"T20","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-PD-GO-BP-0
{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T6","span":{"begin":102,"end":123},"obj":"http://purl.obolibrary.org/obo/GO_0030260"},{"id":"T7","span":{"begin":102,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0044409"},{"id":"T8","span":{"begin":301,"end":316},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T9","span":{"begin":405,"end":426},"obj":"http://purl.obolibrary.org/obo/GO_0030260"},{"id":"T10","span":{"begin":405,"end":420},"obj":"http://purl.obolibrary.org/obo/GO_0044409"},{"id":"T11","span":{"begin":672,"end":687},"obj":"http://purl.obolibrary.org/obo/GO_0061025"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
LitCovid-sample-GO-BP
{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T6","span":{"begin":102,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0044409"},{"id":"T7","span":{"begin":301,"end":316},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T8","span":{"begin":378,"end":400},"obj":"http://purl.obolibrary.org/obo/GO_0006605"},{"id":"T9","span":{"begin":405,"end":420},"obj":"http://purl.obolibrary.org/obo/GO_0044409"},{"id":"T10","span":{"begin":672,"end":687},"obj":"http://purl.obolibrary.org/obo/GO_0061025"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}
2_test
{"project":"2_test","denotations":[{"id":"32841605-32142651-19659466","span":{"begin":142,"end":146},"obj":"32142651"},{"id":"32841605-14647384-19659467","span":{"begin":159,"end":163},"obj":"14647384"},{"id":"32841605-31121217-19659468","span":{"begin":335,"end":339},"obj":"31121217"},{"id":"32841605-27578435-19659469","span":{"begin":693,"end":697},"obj":"27578435"},{"id":"32841605-31121217-19659470","span":{"begin":716,"end":720},"obj":"31121217"},{"id":"32841605-32332765-19659471","span":{"begin":938,"end":942},"obj":"32332765"},{"id":"32841605-32333836-19659472","span":{"begin":960,"end":964},"obj":"32333836"}],"text":"SARS-CoV-2, like SARS-CoV-1, utilizes the host angiotensin-converting enzyme 2 (ACE2) for binding and entry into host cells (Hoffmann et al., 2020; Li et al., 2003). Like many viruses, SARS-CoV-2 utilizes a Spike glycoprotein trimer for recognition and binding to the host cell entry receptor and for membrane fusion (Watanabe et al., 2019). Given the importance of viral Spike proteins for targeting and entry into host cells along with their location on the viral surface, Spike proteins are often used as immunogens for vaccines to generate neutralizing antibodies and frequently targeted for inhibition by small molecules that might block host receptor binding and/or membrane fusion (Li, 2016; Watanabe et al., 2019). In similar fashion, wild-type or catalytically impaired ACE2 has also been investigated as a potential therapeutic biologic that might interfere with the infection cycle of ACE2-targeting coronaviruses (Lei et al., 2020; Monteil et al., 2020). Thus, a detailed understanding of SARS-CoV-2 Spike binding to ACE2 is critical for elucidating mechanisms of viral binding and entry, as well as for undertaking the rational design of effective therapeutics."}