PMC:7352545 / 21275-22022 JSON TXT

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LitCovid_Glycan-Motif-Structure

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T60","span":{"begin":18,"end":20},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T61","span":{"begin":199,"end":201},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T62","span":{"begin":418,"end":429},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T63","span":{"begin":544,"end":550},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T64","span":{"begin":677,"end":679},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Biologically, the SA O-acetylation event confers merits to hosts such as protection from pathogenic invasion and maintenance of systemic self-homeostasis. The O-acetylation event of SAs protects the SA-containing glycans from neuraminidase (NA)/sialidase action, because O-acetyl-groups inhibit microbial NA activity. The chemical structure of the O-acetyl group is quite unstable and susceptible to esterase enzymes. Sialic acid cleavage of the di-acetylated Neu5,7,9Ac3 by bacterial NAs decreases two-fold, when compared to mono-O-acetylated Neu5Ac. The O-acetylated glycan modification invites interaction with viruses, antibodies and mammalian lectins [32]. Therefore, the SA O-acetylation modification confers specific functions to organisms."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T254","span":{"begin":182,"end":185},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T255","span":{"begin":308,"end":316},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T256","span":{"begin":614,"end":621},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T257","span":{"begin":737,"end":746},"obj":"http://purl.obolibrary.org/obo/OBI_0100026"},{"id":"T258","span":{"begin":737,"end":746},"obj":"http://purl.obolibrary.org/obo/UBERON_0000468"}],"text":"Biologically, the SA O-acetylation event confers merits to hosts such as protection from pathogenic invasion and maintenance of systemic self-homeostasis. The O-acetylation event of SAs protects the SA-containing glycans from neuraminidase (NA)/sialidase action, because O-acetyl-groups inhibit microbial NA activity. The chemical structure of the O-acetyl group is quite unstable and susceptible to esterase enzymes. Sialic acid cleavage of the di-acetylated Neu5,7,9Ac3 by bacterial NAs decreases two-fold, when compared to mono-O-acetylated Neu5Ac. The O-acetylated glycan modification invites interaction with viruses, antibodies and mammalian lectins [32]. Therefore, the SA O-acetylation modification confers specific functions to organisms."}

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T43","span":{"begin":142,"end":153},"obj":"http://purl.obolibrary.org/obo/GO_0042592"}],"text":"Biologically, the SA O-acetylation event confers merits to hosts such as protection from pathogenic invasion and maintenance of systemic self-homeostasis. The O-acetylation event of SAs protects the SA-containing glycans from neuraminidase (NA)/sialidase action, because O-acetyl-groups inhibit microbial NA activity. The chemical structure of the O-acetyl group is quite unstable and susceptible to esterase enzymes. Sialic acid cleavage of the di-acetylated Neu5,7,9Ac3 by bacterial NAs decreases two-fold, when compared to mono-O-acetylated Neu5Ac. The O-acetylated glycan modification invites interaction with viruses, antibodies and mammalian lectins [32]. Therefore, the SA O-acetylation modification confers specific functions to organisms."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T203","span":{"begin":0,"end":154},"obj":"Sentence"},{"id":"T204","span":{"begin":155,"end":317},"obj":"Sentence"},{"id":"T205","span":{"begin":318,"end":417},"obj":"Sentence"},{"id":"T206","span":{"begin":418,"end":551},"obj":"Sentence"},{"id":"T207","span":{"begin":552,"end":661},"obj":"Sentence"},{"id":"T208","span":{"begin":662,"end":747},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Biologically, the SA O-acetylation event confers merits to hosts such as protection from pathogenic invasion and maintenance of systemic self-homeostasis. The O-acetylation event of SAs protects the SA-containing glycans from neuraminidase (NA)/sialidase action, because O-acetyl-groups inhibit microbial NA activity. The chemical structure of the O-acetyl group is quite unstable and susceptible to esterase enzymes. Sialic acid cleavage of the di-acetylated Neu5,7,9Ac3 by bacterial NAs decreases two-fold, when compared to mono-O-acetylated Neu5Ac. The O-acetylated glycan modification invites interaction with viruses, antibodies and mammalian lectins [32]. Therefore, the SA O-acetylation modification confers specific functions to organisms."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-27936566-51943972","span":{"begin":657,"end":659},"obj":"27936566"},{"id":"T37447","span":{"begin":657,"end":659},"obj":"27936566"}],"text":"Biologically, the SA O-acetylation event confers merits to hosts such as protection from pathogenic invasion and maintenance of systemic self-homeostasis. The O-acetylation event of SAs protects the SA-containing glycans from neuraminidase (NA)/sialidase action, because O-acetyl-groups inhibit microbial NA activity. The chemical structure of the O-acetyl group is quite unstable and susceptible to esterase enzymes. Sialic acid cleavage of the di-acetylated Neu5,7,9Ac3 by bacterial NAs decreases two-fold, when compared to mono-O-acetylated Neu5Ac. The O-acetylated glycan modification invites interaction with viruses, antibodies and mammalian lectins [32]. Therefore, the SA O-acetylation modification confers specific functions to organisms."}