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LitCovid-PubTator

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T77","span":{"begin":1136,"end":1141},"obj":"Body_part"},{"id":"T78","span":{"begin":1334,"end":1341},"obj":"Body_part"}],"attributes":[{"id":"A77","pred":"fma_id","subj":"T77","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A78","pred":"fma_id","subj":"T78","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"MERS-CoV RBD shares a structure similar to that of the homology domain of SARS-CoV (Wang et al., 2013). However, antibodies induced by SARS-CoV RBD have no cross-reactivity and/or cross-neutralizing activity to MERS-CoV (Du et al., 2013b). Moreover, MERS-CoV utilizes dipeptidyl peptidase 4 (DPP4) as a receptor through the RBD (CTD) region (Raj et al., 2013), which is distinct from the SARS-CoV receptor ACE2. Although the core regions of SARS-CoV and MERS-CoV RBDs are similar, their RBM regions are significantly different, which explains why they recognize different receptors (Li, 2015). MERS-CoV S trimer also maintains a structure similar to that of SARS-CoV S trimer. Both standing and lying states can be detected in the MERS-CoV RBDs, whereas DPP4 only binds to the standing RBD (Pallesen et al., 2017; Yuan et al., 2017). MERS-CoV is clustered with Ty-BatCoV HKU4 and Pi-BatCoV HKU5 in the subgenus Merbecovirus. Ty-BatCoV HKU4, but not Pi-BatCoV HKU5, could use human DPP4 as a receptor (Yang et al., 2014b). Recently, some MERS-related CoVs (MERSr-CoVs) have been discovered from bats that can enter human DPP4-expressing cells (Lau et al., 2018; Luo et al., 2018a). These findings suggest that the emergence of MERSr-CoV may threaten human health owing to their potential for cross-species transmission. The MERS-CoV S protein and RBD and their complexes, along with the DPP4 receptor, are shown in Supplementary Figures S1C,D."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T59","span":{"begin":74,"end":82},"obj":"Disease"},{"id":"T60","span":{"begin":135,"end":143},"obj":"Disease"},{"id":"T61","span":{"begin":388,"end":396},"obj":"Disease"},{"id":"T62","span":{"begin":441,"end":449},"obj":"Disease"},{"id":"T63","span":{"begin":658,"end":666},"obj":"Disease"}],"attributes":[{"id":"A59","pred":"mondo_id","subj":"T59","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A60","pred":"mondo_id","subj":"T60","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A61","pred":"mondo_id","subj":"T61","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A62","pred":"mondo_id","subj":"T62","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A63","pred":"mondo_id","subj":"T63","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"MERS-CoV RBD shares a structure similar to that of the homology domain of SARS-CoV (Wang et al., 2013). However, antibodies induced by SARS-CoV RBD have no cross-reactivity and/or cross-neutralizing activity to MERS-CoV (Du et al., 2013b). Moreover, MERS-CoV utilizes dipeptidyl peptidase 4 (DPP4) as a receptor through the RBD (CTD) region (Raj et al., 2013), which is distinct from the SARS-CoV receptor ACE2. Although the core regions of SARS-CoV and MERS-CoV RBDs are similar, their RBM regions are significantly different, which explains why they recognize different receptors (Li, 2015). MERS-CoV S trimer also maintains a structure similar to that of SARS-CoV S trimer. Both standing and lying states can be detected in the MERS-CoV RBDs, whereas DPP4 only binds to the standing RBD (Pallesen et al., 2017; Yuan et al., 2017). MERS-CoV is clustered with Ty-BatCoV HKU4 and Pi-BatCoV HKU5 in the subgenus Merbecovirus. Ty-BatCoV HKU4, but not Pi-BatCoV HKU5, could use human DPP4 as a receptor (Yang et al., 2014b). Recently, some MERS-related CoVs (MERSr-CoVs) have been discovered from bats that can enter human DPP4-expressing cells (Lau et al., 2018; Luo et al., 2018a). These findings suggest that the emergence of MERSr-CoV may threaten human health owing to their potential for cross-species transmission. The MERS-CoV S protein and RBD and their complexes, along with the DPP4 receptor, are shown in Supplementary Figures S1C,D."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T193","span":{"begin":20,"end":21},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T194","span":{"begin":199,"end":207},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T195","span":{"begin":301,"end":302},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T196","span":{"begin":583,"end":585},"obj":"http://purl.obolibrary.org/obo/CLO_0001022"},{"id":"T197","span":{"begin":583,"end":585},"obj":"http://purl.obolibrary.org/obo/CLO_0007314"},{"id":"T198","span":{"begin":627,"end":628},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T199","span":{"begin":975,"end":980},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T200","span":{"begin":989,"end":990},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T201","span":{"begin":1094,"end":1098},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"},{"id":"T202","span":{"begin":1114,"end":1119},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T203","span":{"begin":1136,"end":1141},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T204","span":{"begin":1155,"end":1159},"obj":"http://purl.obolibrary.org/obo/CLO_0001185"},{"id":"T205","span":{"begin":1249,"end":1254},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"}],"text":"MERS-CoV RBD shares a structure similar to that of the homology domain of SARS-CoV (Wang et al., 2013). However, antibodies induced by SARS-CoV RBD have no cross-reactivity and/or cross-neutralizing activity to MERS-CoV (Du et al., 2013b). Moreover, MERS-CoV utilizes dipeptidyl peptidase 4 (DPP4) as a receptor through the RBD (CTD) region (Raj et al., 2013), which is distinct from the SARS-CoV receptor ACE2. Although the core regions of SARS-CoV and MERS-CoV RBDs are similar, their RBM regions are significantly different, which explains why they recognize different receptors (Li, 2015). MERS-CoV S trimer also maintains a structure similar to that of SARS-CoV S trimer. Both standing and lying states can be detected in the MERS-CoV RBDs, whereas DPP4 only binds to the standing RBD (Pallesen et al., 2017; Yuan et al., 2017). MERS-CoV is clustered with Ty-BatCoV HKU4 and Pi-BatCoV HKU5 in the subgenus Merbecovirus. Ty-BatCoV HKU4, but not Pi-BatCoV HKU5, could use human DPP4 as a receptor (Yang et al., 2014b). Recently, some MERS-related CoVs (MERSr-CoVs) have been discovered from bats that can enter human DPP4-expressing cells (Lau et al., 2018; Luo et al., 2018a). These findings suggest that the emergence of MERSr-CoV may threaten human health owing to their potential for cross-species transmission. The MERS-CoV S protein and RBD and their complexes, along with the DPP4 receptor, are shown in Supplementary Figures S1C,D."}

LitCovid-PD-CHEBI

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T74","span":{"begin":583,"end":585},"obj":"Chemical"},{"id":"T75","span":{"begin":880,"end":882},"obj":"Chemical"},{"id":"T76","span":{"begin":949,"end":951},"obj":"Chemical"},{"id":"T77","span":{"begin":1143,"end":1146},"obj":"Chemical"},{"id":"T78","span":{"begin":1334,"end":1341},"obj":"Chemical"}],"attributes":[{"id":"A74","pred":"chebi_id","subj":"T74","obj":"http://purl.obolibrary.org/obo/CHEBI_30145"},{"id":"A75","pred":"chebi_id","subj":"T75","obj":"http://purl.obolibrary.org/obo/CHEBI_35780"},{"id":"A76","pred":"chebi_id","subj":"T76","obj":"http://purl.obolibrary.org/obo/CHEBI_35780"},{"id":"A77","pred":"chebi_id","subj":"T77","obj":"http://purl.obolibrary.org/obo/CHEBI_32359"},{"id":"A78","pred":"chebi_id","subj":"T78","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"MERS-CoV RBD shares a structure similar to that of the homology domain of SARS-CoV (Wang et al., 2013). However, antibodies induced by SARS-CoV RBD have no cross-reactivity and/or cross-neutralizing activity to MERS-CoV (Du et al., 2013b). Moreover, MERS-CoV utilizes dipeptidyl peptidase 4 (DPP4) as a receptor through the RBD (CTD) region (Raj et al., 2013), which is distinct from the SARS-CoV receptor ACE2. Although the core regions of SARS-CoV and MERS-CoV RBDs are similar, their RBM regions are significantly different, which explains why they recognize different receptors (Li, 2015). MERS-CoV S trimer also maintains a structure similar to that of SARS-CoV S trimer. Both standing and lying states can be detected in the MERS-CoV RBDs, whereas DPP4 only binds to the standing RBD (Pallesen et al., 2017; Yuan et al., 2017). MERS-CoV is clustered with Ty-BatCoV HKU4 and Pi-BatCoV HKU5 in the subgenus Merbecovirus. Ty-BatCoV HKU4, but not Pi-BatCoV HKU5, could use human DPP4 as a receptor (Yang et al., 2014b). Recently, some MERS-related CoVs (MERSr-CoVs) have been discovered from bats that can enter human DPP4-expressing cells (Lau et al., 2018; Luo et al., 2018a). These findings suggest that the emergence of MERSr-CoV may threaten human health owing to their potential for cross-species transmission. The MERS-CoV S protein and RBD and their complexes, along with the DPP4 receptor, are shown in Supplementary Figures S1C,D."}

2_test

{"project":"2_test","denotations":[{"id":"32265848-23835475-36511060","span":{"begin":97,"end":101},"obj":"23835475"},{"id":"32265848-23486063-36511062","span":{"begin":354,"end":358},"obj":"23486063"},{"id":"32265848-25428871-36511063","span":{"begin":587,"end":591},"obj":"25428871"},{"id":"32265848-28807998-36511064","span":{"begin":808,"end":812},"obj":"28807998"},{"id":"32265848-28393837-36511065","span":{"begin":827,"end":831},"obj":"28393837"},{"id":"32265848-29346682-36511067","span":{"begin":1155,"end":1159},"obj":"29346682"}],"text":"MERS-CoV RBD shares a structure similar to that of the homology domain of SARS-CoV (Wang et al., 2013). However, antibodies induced by SARS-CoV RBD have no cross-reactivity and/or cross-neutralizing activity to MERS-CoV (Du et al., 2013b). Moreover, MERS-CoV utilizes dipeptidyl peptidase 4 (DPP4) as a receptor through the RBD (CTD) region (Raj et al., 2013), which is distinct from the SARS-CoV receptor ACE2. Although the core regions of SARS-CoV and MERS-CoV RBDs are similar, their RBM regions are significantly different, which explains why they recognize different receptors (Li, 2015). MERS-CoV S trimer also maintains a structure similar to that of SARS-CoV S trimer. Both standing and lying states can be detected in the MERS-CoV RBDs, whereas DPP4 only binds to the standing RBD (Pallesen et al., 2017; Yuan et al., 2017). MERS-CoV is clustered with Ty-BatCoV HKU4 and Pi-BatCoV HKU5 in the subgenus Merbecovirus. Ty-BatCoV HKU4, but not Pi-BatCoV HKU5, could use human DPP4 as a receptor (Yang et al., 2014b). Recently, some MERS-related CoVs (MERSr-CoVs) have been discovered from bats that can enter human DPP4-expressing cells (Lau et al., 2018; Luo et al., 2018a). These findings suggest that the emergence of MERSr-CoV may threaten human health owing to their potential for cross-species transmission. The MERS-CoV S protein and RBD and their complexes, along with the DPP4 receptor, are shown in Supplementary Figures S1C,D."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T99","span":{"begin":0,"end":103},"obj":"Sentence"},{"id":"T100","span":{"begin":104,"end":239},"obj":"Sentence"},{"id":"T101","span":{"begin":240,"end":411},"obj":"Sentence"},{"id":"T102","span":{"begin":412,"end":593},"obj":"Sentence"},{"id":"T103","span":{"begin":594,"end":676},"obj":"Sentence"},{"id":"T104","span":{"begin":677,"end":833},"obj":"Sentence"},{"id":"T105","span":{"begin":834,"end":924},"obj":"Sentence"},{"id":"T106","span":{"begin":925,"end":1021},"obj":"Sentence"},{"id":"T107","span":{"begin":1022,"end":1180},"obj":"Sentence"},{"id":"T108","span":{"begin":1181,"end":1318},"obj":"Sentence"},{"id":"T109","span":{"begin":1319,"end":1442},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"MERS-CoV RBD shares a structure similar to that of the homology domain of SARS-CoV (Wang et al., 2013). However, antibodies induced by SARS-CoV RBD have no cross-reactivity and/or cross-neutralizing activity to MERS-CoV (Du et al., 2013b). Moreover, MERS-CoV utilizes dipeptidyl peptidase 4 (DPP4) as a receptor through the RBD (CTD) region (Raj et al., 2013), which is distinct from the SARS-CoV receptor ACE2. Although the core regions of SARS-CoV and MERS-CoV RBDs are similar, their RBM regions are significantly different, which explains why they recognize different receptors (Li, 2015). MERS-CoV S trimer also maintains a structure similar to that of SARS-CoV S trimer. Both standing and lying states can be detected in the MERS-CoV RBDs, whereas DPP4 only binds to the standing RBD (Pallesen et al., 2017; Yuan et al., 2017). MERS-CoV is clustered with Ty-BatCoV HKU4 and Pi-BatCoV HKU5 in the subgenus Merbecovirus. Ty-BatCoV HKU4, but not Pi-BatCoV HKU5, could use human DPP4 as a receptor (Yang et al., 2014b). Recently, some MERS-related CoVs (MERSr-CoVs) have been discovered from bats that can enter human DPP4-expressing cells (Lau et al., 2018; Luo et al., 2018a). These findings suggest that the emergence of MERSr-CoV may threaten human health owing to their potential for cross-species transmission. The MERS-CoV S protein and RBD and their complexes, along with the DPP4 receptor, are shown in Supplementary Figures S1C,D."}

LitCovid-PMC-OGER-BB

PMC:7105881 / 16155-17597 JSONTXT

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PMC:7105881 / 16155-17597 JSON TXT