PMC:7461420 / 12694-13531 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T79","span":{"begin":35,"end":42},"obj":"Body_part"},{"id":"T80","span":{"begin":115,"end":122},"obj":"Body_part"},{"id":"T81","span":{"begin":331,"end":335},"obj":"Body_part"}],"attributes":[{"id":"A79","pred":"fma_id","subj":"T79","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A80","pred":"fma_id","subj":"T80","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A81","pred":"fma_id","subj":"T81","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"The sequence identity of the spike protein between SARS‐CoV‐1 (1273 aa) and SARS‐CoV‐2 (1253 aa) is 76%. The spike protein has two regions, S1 and S2. The S1 region of the SARS‐CoV‐1 has a RBD that forms high‐affinity interactions with ACE2. The prevailing understanding is that SARS‐CoV‐2 employs this RBD to enter its human host cell as well. Aligning the two different RBDs revealed a sequence identity of 73.5%. However, many nonconserved mutations that interact directly with ACE2 are located in the two structural regions. 31 And both crystal and cryo‐EM structures of the SARS‐CoV‐1 spike‐ACE2 complex have shown that merely residues of regions 1 and 2 form hydrogen bonds and hydrophobic interactions with ACE2. The mutations in these two regions of SARS‐CoV‐2 will, therefore, likely reduce the number of those interactions. 32"}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T75","span":{"begin":51,"end":55},"obj":"Disease"},{"id":"T76","span":{"begin":76,"end":80},"obj":"Disease"},{"id":"T77","span":{"begin":172,"end":176},"obj":"Disease"},{"id":"T78","span":{"begin":279,"end":283},"obj":"Disease"},{"id":"T79","span":{"begin":580,"end":584},"obj":"Disease"},{"id":"T80","span":{"begin":759,"end":763},"obj":"Disease"}],"attributes":[{"id":"A75","pred":"mondo_id","subj":"T75","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A76","pred":"mondo_id","subj":"T76","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A77","pred":"mondo_id","subj":"T77","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A78","pred":"mondo_id","subj":"T78","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A79","pred":"mondo_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A80","pred":"mondo_id","subj":"T80","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"The sequence identity of the spike protein between SARS‐CoV‐1 (1273 aa) and SARS‐CoV‐2 (1253 aa) is 76%. The spike protein has two regions, S1 and S2. The S1 region of the SARS‐CoV‐1 has a RBD that forms high‐affinity interactions with ACE2. The prevailing understanding is that SARS‐CoV‐2 employs this RBD to enter its human host cell as well. Aligning the two different RBDs revealed a sequence identity of 73.5%. However, many nonconserved mutations that interact directly with ACE2 are located in the two structural regions. 31 And both crystal and cryo‐EM structures of the SARS‐CoV‐1 spike‐ACE2 complex have shown that merely residues of regions 1 and 2 form hydrogen bonds and hydrophobic interactions with ACE2. The mutations in these two regions of SARS‐CoV‐2 will, therefore, likely reduce the number of those interactions. 32"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T128","span":{"begin":68,"end":70},"obj":"http://purl.obolibrary.org/obo/CLO_0001627"},{"id":"T129","span":{"begin":93,"end":95},"obj":"http://purl.obolibrary.org/obo/CLO_0001627"},{"id":"T130","span":{"begin":123,"end":126},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T131","span":{"begin":140,"end":142},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T132","span":{"begin":147,"end":149},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T133","span":{"begin":147,"end":149},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T134","span":{"begin":155,"end":157},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T135","span":{"begin":183,"end":186},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T136","span":{"begin":187,"end":188},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T137","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T138","span":{"begin":331,"end":335},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T139","span":{"begin":386,"end":387},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"The sequence identity of the spike protein between SARS‐CoV‐1 (1273 aa) and SARS‐CoV‐2 (1253 aa) is 76%. The spike protein has two regions, S1 and S2. The S1 region of the SARS‐CoV‐1 has a RBD that forms high‐affinity interactions with ACE2. The prevailing understanding is that SARS‐CoV‐2 employs this RBD to enter its human host cell as well. Aligning the two different RBDs revealed a sequence identity of 73.5%. However, many nonconserved mutations that interact directly with ACE2 are located in the two structural regions. 31 And both crystal and cryo‐EM structures of the SARS‐CoV‐1 spike‐ACE2 complex have shown that merely residues of regions 1 and 2 form hydrogen bonds and hydrophobic interactions with ACE2. The mutations in these two regions of SARS‐CoV‐2 will, therefore, likely reduce the number of those interactions. 32"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T78","span":{"begin":35,"end":42},"obj":"Chemical"},{"id":"T79","span":{"begin":115,"end":122},"obj":"Chemical"},{"id":"T80","span":{"begin":147,"end":149},"obj":"Chemical"},{"id":"T81","span":{"begin":559,"end":561},"obj":"Chemical"},{"id":"T82","span":{"begin":666,"end":674},"obj":"Chemical"}],"attributes":[{"id":"A78","pred":"chebi_id","subj":"T78","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A79","pred":"chebi_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A80","pred":"chebi_id","subj":"T80","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A81","pred":"chebi_id","subj":"T81","obj":"http://purl.obolibrary.org/obo/CHEBI_73507"},{"id":"A82","pred":"chebi_id","subj":"T82","obj":"http://purl.obolibrary.org/obo/CHEBI_49637"}],"text":"The sequence identity of the spike protein between SARS‐CoV‐1 (1273 aa) and SARS‐CoV‐2 (1253 aa) is 76%. The spike protein has two regions, S1 and S2. The S1 region of the SARS‐CoV‐1 has a RBD that forms high‐affinity interactions with ACE2. The prevailing understanding is that SARS‐CoV‐2 employs this RBD to enter its human host cell as well. Aligning the two different RBDs revealed a sequence identity of 73.5%. However, many nonconserved mutations that interact directly with ACE2 are located in the two structural regions. 31 And both crystal and cryo‐EM structures of the SARS‐CoV‐1 spike‐ACE2 complex have shown that merely residues of regions 1 and 2 form hydrogen bonds and hydrophobic interactions with ACE2. The mutations in these two regions of SARS‐CoV‐2 will, therefore, likely reduce the number of those interactions. 32"}

{"project":"LitCovid-PubTator","denotations":[{"id":"455","span":{"begin":29,"end":34},"obj":"Gene"},{"id":"456","span":{"begin":109,"end":114},"obj":"Gene"},{"id":"457","span":{"begin":236,"end":240},"obj":"Gene"},{"id":"458","span":{"begin":481,"end":485},"obj":"Gene"},{"id":"459","span":{"begin":597,"end":601},"obj":"Gene"},{"id":"460","span":{"begin":715,"end":719},"obj":"Gene"},{"id":"461","span":{"begin":591,"end":596},"obj":"Gene"},{"id":"462","span":{"begin":51,"end":59},"obj":"Species"},{"id":"463","span":{"begin":76,"end":86},"obj":"Species"},{"id":"464","span":{"begin":172,"end":180},"obj":"Species"},{"id":"465","span":{"begin":279,"end":289},"obj":"Species"},{"id":"466","span":{"begin":320,"end":325},"obj":"Species"},{"id":"467","span":{"begin":580,"end":588},"obj":"Species"},{"id":"468","span":{"begin":759,"end":769},"obj":"Species"},{"id":"469","span":{"begin":666,"end":674},"obj":"Chemical"}],"attributes":[{"id":"A455","pred":"tao:has_database_id","subj":"455","obj":"Gene:43740568"},{"id":"A456","pred":"tao:has_database_id","subj":"456","obj":"Gene:43740568"},{"id":"A457","pred":"tao:has_database_id","subj":"457","obj":"Gene:59272"},{"id":"A458","pred":"tao:has_database_id","subj":"458","obj":"Gene:59272"},{"id":"A459","pred":"tao:has_database_id","subj":"459","obj":"Gene:59272"},{"id":"A460","pred":"tao:has_database_id","subj":"460","obj":"Gene:59272"},{"id":"A461","pred":"tao:has_database_id","subj":"461","obj":"Gene:43740568"},{"id":"A462","pred":"tao:has_database_id","subj":"462","obj":"Tax:694009"},{"id":"A463","pred":"tao:has_database_id","subj":"463","obj":"Tax:2697049"},{"id":"A464","pred":"tao:has_database_id","subj":"464","obj":"Tax:694009"},{"id":"A465","pred":"tao:has_database_id","subj":"465","obj":"Tax:2697049"},{"id":"A466","pred":"tao:has_database_id","subj":"466","obj":"Tax:9606"},{"id":"A467","pred":"tao:has_database_id","subj":"467","obj":"Tax:694009"},{"id":"A468","pred":"tao:has_database_id","subj":"468","obj":"Tax:2697049"},{"id":"A469","pred":"tao:has_database_id","subj":"469","obj":"MESH:D006859"}],"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":"The sequence identity of the spike protein between SARS‐CoV‐1 (1273 aa) and SARS‐CoV‐2 (1253 aa) is 76%. The spike protein has two regions, S1 and S2. The S1 region of the SARS‐CoV‐1 has a RBD that forms high‐affinity interactions with ACE2. The prevailing understanding is that SARS‐CoV‐2 employs this RBD to enter its human host cell as well. Aligning the two different RBDs revealed a sequence identity of 73.5%. However, many nonconserved mutations that interact directly with ACE2 are located in the two structural regions. 31 And both crystal and cryo‐EM structures of the SARS‐CoV‐1 spike‐ACE2 complex have shown that merely residues of regions 1 and 2 form hydrogen bonds and hydrophobic interactions with ACE2. The mutations in these two regions of SARS‐CoV‐2 will, therefore, likely reduce the number of those interactions. 32"}

{"project":"LitCovid-sentences","denotations":[{"id":"T134","span":{"begin":0,"end":104},"obj":"Sentence"},{"id":"T135","span":{"begin":105,"end":150},"obj":"Sentence"},{"id":"T136","span":{"begin":151,"end":241},"obj":"Sentence"},{"id":"T137","span":{"begin":242,"end":344},"obj":"Sentence"},{"id":"T138","span":{"begin":345,"end":415},"obj":"Sentence"},{"id":"T139","span":{"begin":416,"end":528},"obj":"Sentence"},{"id":"T140","span":{"begin":529,"end":720},"obj":"Sentence"},{"id":"T141","span":{"begin":721,"end":834},"obj":"Sentence"},{"id":"T142","span":{"begin":835,"end":837},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The sequence identity of the spike protein between SARS‐CoV‐1 (1273 aa) and SARS‐CoV‐2 (1253 aa) is 76%. The spike protein has two regions, S1 and S2. The S1 region of the SARS‐CoV‐1 has a RBD that forms high‐affinity interactions with ACE2. The prevailing understanding is that SARS‐CoV‐2 employs this RBD to enter its human host cell as well. Aligning the two different RBDs revealed a sequence identity of 73.5%. However, many nonconserved mutations that interact directly with ACE2 are located in the two structural regions. 31 And both crystal and cryo‐EM structures of the SARS‐CoV‐1 spike‐ACE2 complex have shown that merely residues of regions 1 and 2 form hydrogen bonds and hydrophobic interactions with ACE2. The mutations in these two regions of SARS‐CoV‐2 will, therefore, likely reduce the number of those interactions. 32"}