PMC:7219429 / 18330-18566 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T107","span":{"begin":49,"end":59},"obj":"Body_part"},{"id":"T108","span":{"begin":82,"end":89},"obj":"Body_part"},{"id":"T109","span":{"begin":191,"end":196},"obj":"Body_part"}],"attributes":[{"id":"A107","pred":"fma_id","subj":"T107","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A108","pred":"fma_id","subj":"T108","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A109","pred":"fma_id","subj":"T109","obj":"http://purl.org/sig/ont/fma/fma67264"}],"text":"Moreover, the histograms of Fig. 5 show that all amino acid residues of the spike protein that are involved in ATM binding, including the QFN triad, are also essential for GM1 binding in the lipid raft environment (Table S1 and Fig. 5)."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T181","span":{"begin":49,"end":68},"obj":"http://purl.obolibrary.org/obo/CHEBI_33708"},{"id":"T182","span":{"begin":49,"end":68},"obj":"http://purl.obolibrary.org/obo/PR_000036907"},{"id":"T183","span":{"begin":221,"end":223},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"}],"text":"Moreover, the histograms of Fig. 5 show that all amino acid residues of the spike protein that are involved in ATM binding, including the QFN triad, are also essential for GM1 binding in the lipid raft environment (Table S1 and Fig. 5)."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T332","span":{"begin":49,"end":59},"obj":"Chemical"},{"id":"T333","span":{"begin":49,"end":54},"obj":"Chemical"},{"id":"T334","span":{"begin":55,"end":59},"obj":"Chemical"},{"id":"T335","span":{"begin":82,"end":89},"obj":"Chemical"},{"id":"T336","span":{"begin":111,"end":114},"obj":"Chemical"},{"id":"T337","span":{"begin":172,"end":175},"obj":"Chemical"},{"id":"T340","span":{"begin":191,"end":196},"obj":"Chemical"}],"attributes":[{"id":"A332","pred":"chebi_id","subj":"T332","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A333","pred":"chebi_id","subj":"T333","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A334","pred":"chebi_id","subj":"T334","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"id":"A335","pred":"chebi_id","subj":"T335","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A336","pred":"chebi_id","subj":"T336","obj":"http://purl.obolibrary.org/obo/CHEBI_2955"},{"id":"A337","pred":"chebi_id","subj":"T337","obj":"http://purl.obolibrary.org/obo/CHEBI_18216"},{"id":"A338","pred":"chebi_id","subj":"T337","obj":"http://purl.obolibrary.org/obo/CHEBI_61048"},{"id":"A339","pred":"chebi_id","subj":"T337","obj":"http://purl.obolibrary.org/obo/CHEBI_73110"},{"id":"A340","pred":"chebi_id","subj":"T340","obj":"http://purl.obolibrary.org/obo/CHEBI_18059"}],"text":"Moreover, the histograms of Fig. 5 show that all amino acid residues of the spike protein that are involved in ATM binding, including the QFN triad, are also essential for GM1 binding in the lipid raft environment (Table S1 and Fig. 5)."}

{"project":"LitCovid-PD-GlycoEpitope","denotations":[{"id":"T20","span":{"begin":172,"end":175},"obj":"GlycoEpitope"}],"attributes":[{"id":"A20","pred":"glyco_epitope_db_id","subj":"T20","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Moreover, the histograms of Fig. 5 show that all amino acid residues of the spike protein that are involved in ATM binding, including the QFN triad, are also essential for GM1 binding in the lipid raft environment (Table S1 and Fig. 5)."}

{"project":"LitCovid-sentences","denotations":[{"id":"T137","span":{"begin":0,"end":236},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Moreover, the histograms of Fig. 5 show that all amino acid residues of the spike protein that are involved in ATM binding, including the QFN triad, are also essential for GM1 binding in the lipid raft environment (Table S1 and Fig. 5)."}

{"project":"LitCovid-PubTator","denotations":[{"id":"511","span":{"begin":76,"end":81},"obj":"Gene"},{"id":"532","span":{"begin":172,"end":175},"obj":"Chemical"},{"id":"533","span":{"begin":191,"end":196},"obj":"Chemical"}],"attributes":[{"id":"A511","pred":"tao:has_database_id","subj":"511","obj":"Gene:43740568"},{"id":"A532","pred":"tao:has_database_id","subj":"532","obj":"MESH:D005677"},{"id":"A533","pred":"tao:has_database_id","subj":"533","obj":"MESH:D008055"}],"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":"Moreover, the histograms of Fig. 5 show that all amino acid residues of the spike protein that are involved in ATM binding, including the QFN triad, are also essential for GM1 binding in the lipid raft environment (Table S1 and Fig. 5)."}