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LitCovid-PubTator

LitCovid-PMC-OGER-BB

LitCovid-PD-FMA-UBERON

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T87","span":{"begin":48,"end":56},"obj":"Disease"},{"id":"T88","span":{"begin":235,"end":243},"obj":"Disease"},{"id":"T89","span":{"begin":321,"end":324},"obj":"Disease"},{"id":"T91","span":{"begin":489,"end":497},"obj":"Disease"},{"id":"T92","span":{"begin":815,"end":823},"obj":"Disease"},{"id":"T93","span":{"begin":1046,"end":1049},"obj":"Disease"},{"id":"T95","span":{"begin":1327,"end":1336},"obj":"Disease"},{"id":"T96","span":{"begin":1443,"end":1446},"obj":"Disease"}],"attributes":[{"id":"A87","pred":"mondo_id","subj":"T87","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A88","pred":"mondo_id","subj":"T88","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A89","pred":"mondo_id","subj":"T89","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A90","pred":"mondo_id","subj":"T89","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A91","pred":"mondo_id","subj":"T91","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A92","pred":"mondo_id","subj":"T92","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A93","pred":"mondo_id","subj":"T93","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A94","pred":"mondo_id","subj":"T93","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A95","pred":"mondo_id","subj":"T95","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A96","pred":"mondo_id","subj":"T96","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A97","pred":"mondo_id","subj":"T96","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"}],"text":"3.6 Potential coordinated interactions between SARS-CoV-2 and the plasma membrane of a host cell: key role of gangliosides in lipid rafts\nTaken together, these data strongly support the concept of a dual receptor/attachment model for SARS-CoV-2, with the RBD domain being involved in ACE-2 receptor recognition, and the NTD interface responsible for finding a ganglioside-rich landing area (lipid raft) at the cell surface.\nSuch a dual receptor model, consistent with the topology of the SARS-CoV-2 S protein, is proposed in Fig. 8 . With this model in mind, the potential effects of CLQ and CLQ-OH were studied, both of which, according to the molecular modelling data, have a high affinity for sialic acids and gangliosides.\nFig. 8 Dual recognition of gangliosides and angiotensin-converting enzyme-2 (ACE-2) by SARS-CoV-2 spike (S) protein. The viral protein displays two distinct domains, the tips of which are available for distinct types of interactions. The receptor-binding domain binds to the ACE-2 receptor, and the N-terminal domain (NTD) binds to the ganglioside-rich domain of the plasma membrane. Lipid rafts, which are membrane domains enriched in gangliosides (in yellow) and cholesterol (in blue), provide a perfect attractive interface for adequately positioning the viral S protein at the first step of the infection process. These structural and molecular modelling studies suggest that amino acid residues 111–162 of the NTD form a functional ganglioside-binding domain, the interaction of which with lipid rafts can be efficiently prevented by chloroquine and hydroxychloroquine."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T158","span":{"begin":67,"end":73},"obj":"http://purl.obolibrary.org/obo/UBERON_0001969"},{"id":"T159","span":{"begin":74,"end":82},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T160","span":{"begin":86,"end":87},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T161","span":{"begin":93,"end":97},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T162","span":{"begin":198,"end":199},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T163","span":{"begin":359,"end":360},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T164","span":{"begin":411,"end":415},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T165","span":{"begin":430,"end":431},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T166","span":{"begin":677,"end":678},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T167","span":{"begin":1095,"end":1101},"obj":"http://purl.obolibrary.org/obo/UBERON_0001969"},{"id":"T168","span":{"begin":1102,"end":1110},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T169","span":{"begin":1135,"end":1143},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T170","span":{"begin":1224,"end":1225},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T171","span":{"begin":1408,"end":1427},"obj":"http://purl.obolibrary.org/obo/CHEBI_33708"},{"id":"T172","span":{"begin":1408,"end":1427},"obj":"http://purl.obolibrary.org/obo/PR_000036907"},{"id":"T173","span":{"begin":1432,"end":1435},"obj":"http://purl.obolibrary.org/obo/CLO_0001002"},{"id":"T174","span":{"begin":1452,"end":1453},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"3.6 Potential coordinated interactions between SARS-CoV-2 and the plasma membrane of a host cell: key role of gangliosides in lipid rafts\nTaken together, these data strongly support the concept of a dual receptor/attachment model for SARS-CoV-2, with the RBD domain being involved in ACE-2 receptor recognition, and the NTD interface responsible for finding a ganglioside-rich landing area (lipid raft) at the cell surface.\nSuch a dual receptor model, consistent with the topology of the SARS-CoV-2 S protein, is proposed in Fig. 8 . With this model in mind, the potential effects of CLQ and CLQ-OH were studied, both of which, according to the molecular modelling data, have a high affinity for sialic acids and gangliosides.\nFig. 8 Dual recognition of gangliosides and angiotensin-converting enzyme-2 (ACE-2) by SARS-CoV-2 spike (S) protein. The viral protein displays two distinct domains, the tips of which are available for distinct types of interactions. The receptor-binding domain binds to the ACE-2 receptor, and the N-terminal domain (NTD) binds to the ganglioside-rich domain of the plasma membrane. Lipid rafts, which are membrane domains enriched in gangliosides (in yellow) and cholesterol (in blue), provide a perfect attractive interface for adequately positioning the viral S protein at the first step of the infection process. These structural and molecular modelling studies suggest that amino acid residues 111–162 of the NTD form a functional ganglioside-binding domain, the interaction of which with lipid rafts can be efficiently prevented by chloroquine and hydroxychloroquine."}

LitCovid-PD-CHEBI

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T175","span":{"begin":0,"end":138},"obj":"Sentence"},{"id":"T176","span":{"begin":139,"end":424},"obj":"Sentence"},{"id":"T177","span":{"begin":425,"end":534},"obj":"Sentence"},{"id":"T178","span":{"begin":535,"end":727},"obj":"Sentence"},{"id":"T179","span":{"begin":728,"end":844},"obj":"Sentence"},{"id":"T180","span":{"begin":845,"end":961},"obj":"Sentence"},{"id":"T181","span":{"begin":962,"end":1111},"obj":"Sentence"},{"id":"T182","span":{"begin":1112,"end":1345},"obj":"Sentence"},{"id":"T183","span":{"begin":1346,"end":1602},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"3.6 Potential coordinated interactions between SARS-CoV-2 and the plasma membrane of a host cell: key role of gangliosides in lipid rafts\nTaken together, these data strongly support the concept of a dual receptor/attachment model for SARS-CoV-2, with the RBD domain being involved in ACE-2 receptor recognition, and the NTD interface responsible for finding a ganglioside-rich landing area (lipid raft) at the cell surface.\nSuch a dual receptor model, consistent with the topology of the SARS-CoV-2 S protein, is proposed in Fig. 8 . With this model in mind, the potential effects of CLQ and CLQ-OH were studied, both of which, according to the molecular modelling data, have a high affinity for sialic acids and gangliosides.\nFig. 8 Dual recognition of gangliosides and angiotensin-converting enzyme-2 (ACE-2) by SARS-CoV-2 spike (S) protein. The viral protein displays two distinct domains, the tips of which are available for distinct types of interactions. The receptor-binding domain binds to the ACE-2 receptor, and the N-terminal domain (NTD) binds to the ganglioside-rich domain of the plasma membrane. Lipid rafts, which are membrane domains enriched in gangliosides (in yellow) and cholesterol (in blue), provide a perfect attractive interface for adequately positioning the viral S protein at the first step of the infection process. These structural and molecular modelling studies suggest that amino acid residues 111–162 of the NTD form a functional ganglioside-binding domain, the interaction of which with lipid rafts can be efficiently prevented by chloroquine and hydroxychloroquine."}