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LitCovid-PD-FMA-UBERON

LitCovid-PD-MONDO

LitCovid-PD-CLO

LitCovid-PD-CHEBI

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T33","span":{"begin":109,"end":121},"obj":"Chemical"},{"id":"T34","span":{"begin":220,"end":227},"obj":"Chemical"},{"id":"T35","span":{"begin":388,"end":390},"obj":"Chemical"},{"id":"T36","span":{"begin":601,"end":608},"obj":"Chemical"},{"id":"T37","span":{"begin":1809,"end":1811},"obj":"Chemical"},{"id":"T38","span":{"begin":1927,"end":1935},"obj":"Chemical"},{"id":"T39","span":{"begin":2029,"end":2036},"obj":"Chemical"},{"id":"T40","span":{"begin":2064,"end":2066},"obj":"Chemical"},{"id":"T41","span":{"begin":2282,"end":2289},"obj":"Chemical"},{"id":"T42","span":{"begin":2337,"end":2343},"obj":"Chemical"}],"attributes":[{"id":"A33","pred":"chebi_id","subj":"T33","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A34","pred":"chebi_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A35","pred":"chebi_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A36","pred":"chebi_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A37","pred":"chebi_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A38","pred":"chebi_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/CHEBI_15356"},{"id":"A39","pred":"chebi_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A40","pred":"chebi_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A41","pred":"chebi_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A42","pred":"chebi_id","subj":"T42","obj":"http://purl.obolibrary.org/obo/CHEBI_17115"},{"id":"A43","pred":"chebi_id","subj":"T42","obj":"http://purl.obolibrary.org/obo/CHEBI_17822"}],"text":"Upon analysis of the SARS-CoV-2-ACE-2 interaction, there was confirmation that this occurs through the spike glycoprotein expressed on the viral envelope, being the same for all coronaviruses [35]. The coronavirus spike protein is composed of an intracellular segment, a transmembrane segment and a large ectodomain formed by an S1 subunit for interaction with the target receptor and an S2 subunit for fusion between the viral and cell membrane [57]. Subunit S1 consists of four domains, one N terminal domain (NTD) and three C-terminal domains (CTD1, CTD2 and CTD3). The cell receptor and the viral protein bind through the receptor-binding domain (RBD), located in the CTD1 domain in the case of SARS-CoV [58]. Experiments undertaken to investigate virus-receptor interaction with resolution at the atomic level showed that SARS-CoV and SARS-CoV-2 had a high sequence similarity (89.2%) and sequence identity (73.7%) [14,22]. However, a more targeted evaluation of SARS-CoV-2 RBD revealed peculiar characteristics that are probably responsible for the greater diffusion compared with SARS-CoV. Wan et al. found that the SARS-CoV-2 RBD has a single mutation that improves its binding affinity with ACE-2 [59]. Heet al. have shown that the characteristics of SARS-CoV-2 RBD make the virus more soluble, therefore capable of binding ACE-2 more easily, but also more stable, therefore able to survive at high temperatures [42]. At the same time, the SARS-CoV-2 RBD has greater flexibility than the SARS-CoV RBD, especially near the binding site. For this reason, SARS-CoV-2 is much more sensitive to temperature than SARS-CoV in terms of the RBD-ACE-2 bond and this would cause the decrease in infectivity with increasing temperatures [42]. The SARS-CoV RBD-ACE-2 binding induces conformational changes in the S2 subunit, such as to induce the fusion between the viral membrane and the cell. A low pH and pH-dependent endosomal cysteine proteases called cathepsins facilitate endosomal cell entry of the virus. Furthermore, the S protein is cleaved into the S1 and S2 subunits by the host transmembrane cell proteases [60], which are necessary for the entry of the virus through the cell surface non-endosomal pathway [61]. Hoffmann et al. have shown that in particular SARS-CoV-2 S protein depends on the cellular protease Transmembrane Serine Protease 2 (TMPRSS2) for priming [62]."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T116","span":{"begin":0,"end":197},"obj":"Sentence"},{"id":"T117","span":{"begin":198,"end":451},"obj":"Sentence"},{"id":"T118","span":{"begin":452,"end":568},"obj":"Sentence"},{"id":"T119","span":{"begin":569,"end":713},"obj":"Sentence"},{"id":"T120","span":{"begin":714,"end":928},"obj":"Sentence"},{"id":"T121","span":{"begin":929,"end":1096},"obj":"Sentence"},{"id":"T122","span":{"begin":1097,"end":1211},"obj":"Sentence"},{"id":"T123","span":{"begin":1212,"end":1426},"obj":"Sentence"},{"id":"T124","span":{"begin":1427,"end":1544},"obj":"Sentence"},{"id":"T125","span":{"begin":1545,"end":1739},"obj":"Sentence"},{"id":"T126","span":{"begin":1740,"end":1890},"obj":"Sentence"},{"id":"T127","span":{"begin":1891,"end":2009},"obj":"Sentence"},{"id":"T128","span":{"begin":2010,"end":2222},"obj":"Sentence"},{"id":"T129","span":{"begin":2223,"end":2382},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Upon analysis of the SARS-CoV-2-ACE-2 interaction, there was confirmation that this occurs through the spike glycoprotein expressed on the viral envelope, being the same for all coronaviruses [35]. The coronavirus spike protein is composed of an intracellular segment, a transmembrane segment and a large ectodomain formed by an S1 subunit for interaction with the target receptor and an S2 subunit for fusion between the viral and cell membrane [57]. Subunit S1 consists of four domains, one N terminal domain (NTD) and three C-terminal domains (CTD1, CTD2 and CTD3). The cell receptor and the viral protein bind through the receptor-binding domain (RBD), located in the CTD1 domain in the case of SARS-CoV [58]. Experiments undertaken to investigate virus-receptor interaction with resolution at the atomic level showed that SARS-CoV and SARS-CoV-2 had a high sequence similarity (89.2%) and sequence identity (73.7%) [14,22]. However, a more targeted evaluation of SARS-CoV-2 RBD revealed peculiar characteristics that are probably responsible for the greater diffusion compared with SARS-CoV. Wan et al. found that the SARS-CoV-2 RBD has a single mutation that improves its binding affinity with ACE-2 [59]. Heet al. have shown that the characteristics of SARS-CoV-2 RBD make the virus more soluble, therefore capable of binding ACE-2 more easily, but also more stable, therefore able to survive at high temperatures [42]. At the same time, the SARS-CoV-2 RBD has greater flexibility than the SARS-CoV RBD, especially near the binding site. For this reason, SARS-CoV-2 is much more sensitive to temperature than SARS-CoV in terms of the RBD-ACE-2 bond and this would cause the decrease in infectivity with increasing temperatures [42]. The SARS-CoV RBD-ACE-2 binding induces conformational changes in the S2 subunit, such as to induce the fusion between the viral membrane and the cell. A low pH and pH-dependent endosomal cysteine proteases called cathepsins facilitate endosomal cell entry of the virus. Furthermore, the S protein is cleaved into the S1 and S2 subunits by the host transmembrane cell proteases [60], which are necessary for the entry of the virus through the cell surface non-endosomal pathway [61]. Hoffmann et al. have shown that in particular SARS-CoV-2 S protein depends on the cellular protease Transmembrane Serine Protease 2 (TMPRSS2) for priming [62]."}

LitCovid-PubTator

2_test

{"project":"2_test","denotations":[{"id":"32759645-27578435-58096178","span":{"begin":447,"end":449},"obj":"27578435"},{"id":"32759645-30102747-58096179","span":{"begin":709,"end":711},"obj":"30102747"},{"id":"32759645-32064853-58096180","span":{"begin":924,"end":926},"obj":"32064853"},{"id":"32759645-26868298-58096181","span":{"begin":2118,"end":2120},"obj":"26868298"},{"id":"32759645-22558251-58096182","span":{"begin":2218,"end":2220},"obj":"22558251"}],"text":"Upon analysis of the SARS-CoV-2-ACE-2 interaction, there was confirmation that this occurs through the spike glycoprotein expressed on the viral envelope, being the same for all coronaviruses [35]. The coronavirus spike protein is composed of an intracellular segment, a transmembrane segment and a large ectodomain formed by an S1 subunit for interaction with the target receptor and an S2 subunit for fusion between the viral and cell membrane [57]. Subunit S1 consists of four domains, one N terminal domain (NTD) and three C-terminal domains (CTD1, CTD2 and CTD3). The cell receptor and the viral protein bind through the receptor-binding domain (RBD), located in the CTD1 domain in the case of SARS-CoV [58]. Experiments undertaken to investigate virus-receptor interaction with resolution at the atomic level showed that SARS-CoV and SARS-CoV-2 had a high sequence similarity (89.2%) and sequence identity (73.7%) [14,22]. However, a more targeted evaluation of SARS-CoV-2 RBD revealed peculiar characteristics that are probably responsible for the greater diffusion compared with SARS-CoV. Wan et al. found that the SARS-CoV-2 RBD has a single mutation that improves its binding affinity with ACE-2 [59]. Heet al. have shown that the characteristics of SARS-CoV-2 RBD make the virus more soluble, therefore capable of binding ACE-2 more easily, but also more stable, therefore able to survive at high temperatures [42]. At the same time, the SARS-CoV-2 RBD has greater flexibility than the SARS-CoV RBD, especially near the binding site. For this reason, SARS-CoV-2 is much more sensitive to temperature than SARS-CoV in terms of the RBD-ACE-2 bond and this would cause the decrease in infectivity with increasing temperatures [42]. The SARS-CoV RBD-ACE-2 binding induces conformational changes in the S2 subunit, such as to induce the fusion between the viral membrane and the cell. A low pH and pH-dependent endosomal cysteine proteases called cathepsins facilitate endosomal cell entry of the virus. Furthermore, the S protein is cleaved into the S1 and S2 subunits by the host transmembrane cell proteases [60], which are necessary for the entry of the virus through the cell surface non-endosomal pathway [61]. Hoffmann et al. have shown that in particular SARS-CoV-2 S protein depends on the cellular protease Transmembrane Serine Protease 2 (TMPRSS2) for priming [62]."}