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LitCovid_Glycan-Motif-Structure

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T136","span":{"begin":78,"end":80},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T137","span":{"begin":129,"end":131},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T138","span":{"begin":349,"end":351},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T139","span":{"begin":714,"end":716},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T140","span":{"begin":796,"end":798},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T141","span":{"begin":858,"end":860},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T142","span":{"begin":1050,"end":1052},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T143","span":{"begin":1106,"end":1108},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T144","span":{"begin":1284,"end":1286},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T145","span":{"begin":1362,"end":1364},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T146","span":{"begin":1476,"end":1478},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"6.1.1. α-Coronavirus\nIn α-CoVs such as TGEV, HA-activity is attributed to the SA-recognizing activity to α2,3-NeuGc [61,62]. The SA-binding site is present on the N-terminal region of the S-glycoprotein of TGEV. TGEV has two types with enteric and respiratory tropism. The respiratory TGEV has the porcine aminopeptidase N (pAPN)-binding domain and SA-binding domain. Nucleotide 655 of the S gene is essential for enteric tropism and the S219A mutation of the S glycoprotein confers the enteric to respiratory tropism shift. In addition, a 6-nucleotide insertional mutation at nucleotide 1124, which yields the Y374-T375insND shift of the S glycoprotein, causes enhanced enteric tract tropism. TGEV interacts with SA species on mucin-like glycoprotein (MGP), a highly glycosylated protein, in an SA-dependent manner, on mucin-secreting goblet cells [6]. MGP SA-binding allows virus entry via the mucus layer to the intestinal enterocytes. Different from TGEV, the S glycoprotein of porcine CoV has no hemagglutination activity due to deletion of the SA-binding site of the S glycoprotein [61]. The loss of SA-binding activity is correlated to the non-enteropathogenicity. SAs function as HA-mediated entry determinants for TGEV, causing the enteropathogenic outcome of the virus, and SA-recognition activity is also responsible for virus amplification in cells. SA-binding activity-deficient TGEV can propagate in cells through pAPN, known as CD13, as a receptor [62,63]. The SA-binding activity potentiates infection and is crucial for intestinal infection."}

LitCovid-PD-FMA-UBERON

LitCovid-PD-UBERON

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T7","span":{"begin":896,"end":901},"obj":"Body_part"}],"attributes":[{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0000912"}],"text":"6.1.1. α-Coronavirus\nIn α-CoVs such as TGEV, HA-activity is attributed to the SA-recognizing activity to α2,3-NeuGc [61,62]. The SA-binding site is present on the N-terminal region of the S-glycoprotein of TGEV. TGEV has two types with enteric and respiratory tropism. The respiratory TGEV has the porcine aminopeptidase N (pAPN)-binding domain and SA-binding domain. Nucleotide 655 of the S gene is essential for enteric tropism and the S219A mutation of the S glycoprotein confers the enteric to respiratory tropism shift. In addition, a 6-nucleotide insertional mutation at nucleotide 1124, which yields the Y374-T375insND shift of the S glycoprotein, causes enhanced enteric tract tropism. TGEV interacts with SA species on mucin-like glycoprotein (MGP), a highly glycosylated protein, in an SA-dependent manner, on mucin-secreting goblet cells [6]. MGP SA-binding allows virus entry via the mucus layer to the intestinal enterocytes. Different from TGEV, the S glycoprotein of porcine CoV has no hemagglutination activity due to deletion of the SA-binding site of the S glycoprotein [61]. The loss of SA-binding activity is correlated to the non-enteropathogenicity. SAs function as HA-mediated entry determinants for TGEV, causing the enteropathogenic outcome of the virus, and SA-recognition activity is also responsible for virus amplification in cells. SA-binding activity-deficient TGEV can propagate in cells through pAPN, known as CD13, as a receptor [62,63]. The SA-binding activity potentiates infection and is crucial for intestinal infection."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T123","span":{"begin":1508,"end":1517},"obj":"Disease"},{"id":"T124","span":{"begin":1548,"end":1557},"obj":"Disease"}],"attributes":[{"id":"A123","pred":"mondo_id","subj":"T123","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A124","pred":"mondo_id","subj":"T124","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"6.1.1. α-Coronavirus\nIn α-CoVs such as TGEV, HA-activity is attributed to the SA-recognizing activity to α2,3-NeuGc [61,62]. The SA-binding site is present on the N-terminal region of the S-glycoprotein of TGEV. TGEV has two types with enteric and respiratory tropism. The respiratory TGEV has the porcine aminopeptidase N (pAPN)-binding domain and SA-binding domain. Nucleotide 655 of the S gene is essential for enteric tropism and the S219A mutation of the S glycoprotein confers the enteric to respiratory tropism shift. In addition, a 6-nucleotide insertional mutation at nucleotide 1124, which yields the Y374-T375insND shift of the S glycoprotein, causes enhanced enteric tract tropism. TGEV interacts with SA species on mucin-like glycoprotein (MGP), a highly glycosylated protein, in an SA-dependent manner, on mucin-secreting goblet cells [6]. MGP SA-binding allows virus entry via the mucus layer to the intestinal enterocytes. Different from TGEV, the S glycoprotein of porcine CoV has no hemagglutination activity due to deletion of the SA-binding site of the S glycoprotein [61]. The loss of SA-binding activity is correlated to the non-enteropathogenicity. SAs function as HA-mediated entry determinants for TGEV, causing the enteropathogenic outcome of the virus, and SA-recognition activity is also responsible for virus amplification in cells. SA-binding activity-deficient TGEV can propagate in cells through pAPN, known as CD13, as a receptor [62,63]. The SA-binding activity potentiates infection and is crucial for intestinal infection."}

LitCovid-PD-CLO

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T53","span":{"begin":260,"end":267},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T54","span":{"begin":422,"end":429},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T55","span":{"begin":510,"end":517},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T56","span":{"begin":685,"end":692},"obj":"http://purl.obolibrary.org/obo/GO_0009606"}],"text":"6.1.1. α-Coronavirus\nIn α-CoVs such as TGEV, HA-activity is attributed to the SA-recognizing activity to α2,3-NeuGc [61,62]. The SA-binding site is present on the N-terminal region of the S-glycoprotein of TGEV. TGEV has two types with enteric and respiratory tropism. The respiratory TGEV has the porcine aminopeptidase N (pAPN)-binding domain and SA-binding domain. Nucleotide 655 of the S gene is essential for enteric tropism and the S219A mutation of the S glycoprotein confers the enteric to respiratory tropism shift. In addition, a 6-nucleotide insertional mutation at nucleotide 1124, which yields the Y374-T375insND shift of the S glycoprotein, causes enhanced enteric tract tropism. TGEV interacts with SA species on mucin-like glycoprotein (MGP), a highly glycosylated protein, in an SA-dependent manner, on mucin-secreting goblet cells [6]. MGP SA-binding allows virus entry via the mucus layer to the intestinal enterocytes. Different from TGEV, the S glycoprotein of porcine CoV has no hemagglutination activity due to deletion of the SA-binding site of the S glycoprotein [61]. The loss of SA-binding activity is correlated to the non-enteropathogenicity. SAs function as HA-mediated entry determinants for TGEV, causing the enteropathogenic outcome of the virus, and SA-recognition activity is also responsible for virus amplification in cells. SA-binding activity-deficient TGEV can propagate in cells through pAPN, known as CD13, as a receptor [62,63]. The SA-binding activity potentiates infection and is crucial for intestinal infection."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T327","span":{"begin":0,"end":20},"obj":"Sentence"},{"id":"T328","span":{"begin":21,"end":124},"obj":"Sentence"},{"id":"T329","span":{"begin":125,"end":211},"obj":"Sentence"},{"id":"T330","span":{"begin":212,"end":268},"obj":"Sentence"},{"id":"T331","span":{"begin":269,"end":367},"obj":"Sentence"},{"id":"T332","span":{"begin":368,"end":524},"obj":"Sentence"},{"id":"T333","span":{"begin":525,"end":693},"obj":"Sentence"},{"id":"T334","span":{"begin":694,"end":853},"obj":"Sentence"},{"id":"T335","span":{"begin":854,"end":938},"obj":"Sentence"},{"id":"T336","span":{"begin":939,"end":1093},"obj":"Sentence"},{"id":"T337","span":{"begin":1094,"end":1171},"obj":"Sentence"},{"id":"T338","span":{"begin":1172,"end":1361},"obj":"Sentence"},{"id":"T339","span":{"begin":1362,"end":1471},"obj":"Sentence"},{"id":"T340","span":{"begin":1472,"end":1558},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"6.1.1. α-Coronavirus\nIn α-CoVs such as TGEV, HA-activity is attributed to the SA-recognizing activity to α2,3-NeuGc [61,62]. The SA-binding site is present on the N-terminal region of the S-glycoprotein of TGEV. TGEV has two types with enteric and respiratory tropism. The respiratory TGEV has the porcine aminopeptidase N (pAPN)-binding domain and SA-binding domain. Nucleotide 655 of the S gene is essential for enteric tropism and the S219A mutation of the S glycoprotein confers the enteric to respiratory tropism shift. In addition, a 6-nucleotide insertional mutation at nucleotide 1124, which yields the Y374-T375insND shift of the S glycoprotein, causes enhanced enteric tract tropism. TGEV interacts with SA species on mucin-like glycoprotein (MGP), a highly glycosylated protein, in an SA-dependent manner, on mucin-secreting goblet cells [6]. MGP SA-binding allows virus entry via the mucus layer to the intestinal enterocytes. Different from TGEV, the S glycoprotein of porcine CoV has no hemagglutination activity due to deletion of the SA-binding site of the S glycoprotein [61]. The loss of SA-binding activity is correlated to the non-enteropathogenicity. SAs function as HA-mediated entry determinants for TGEV, causing the enteropathogenic outcome of the virus, and SA-recognition activity is also responsible for virus amplification in cells. SA-binding activity-deficient TGEV can propagate in cells through pAPN, known as CD13, as a receptor [62,63]. The SA-binding activity potentiates infection and is crucial for intestinal infection."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-8764078-51944005","span":{"begin":117,"end":119},"obj":"8764078"},{"id":"32604730-9060696-51944006","span":{"begin":120,"end":122},"obj":"9060696"},{"id":"32604730-14557669-51944007","span":{"begin":850,"end":851},"obj":"14557669"},{"id":"32604730-8764078-51944008","span":{"begin":1089,"end":1091},"obj":"8764078"},{"id":"32604730-9060696-51944009","span":{"begin":1464,"end":1466},"obj":"9060696"},{"id":"32604730-10644848-51944010","span":{"begin":1467,"end":1469},"obj":"10644848"},{"id":"T88722","span":{"begin":117,"end":119},"obj":"8764078"},{"id":"T67423","span":{"begin":120,"end":122},"obj":"9060696"},{"id":"T29243","span":{"begin":850,"end":851},"obj":"14557669"},{"id":"T8143","span":{"begin":1089,"end":1091},"obj":"8764078"},{"id":"T44658","span":{"begin":1464,"end":1466},"obj":"9060696"},{"id":"T73054","span":{"begin":1467,"end":1469},"obj":"10644848"}],"text":"6.1.1. α-Coronavirus\nIn α-CoVs such as TGEV, HA-activity is attributed to the SA-recognizing activity to α2,3-NeuGc [61,62]. The SA-binding site is present on the N-terminal region of the S-glycoprotein of TGEV. TGEV has two types with enteric and respiratory tropism. The respiratory TGEV has the porcine aminopeptidase N (pAPN)-binding domain and SA-binding domain. Nucleotide 655 of the S gene is essential for enteric tropism and the S219A mutation of the S glycoprotein confers the enteric to respiratory tropism shift. In addition, a 6-nucleotide insertional mutation at nucleotide 1124, which yields the Y374-T375insND shift of the S glycoprotein, causes enhanced enteric tract tropism. TGEV interacts with SA species on mucin-like glycoprotein (MGP), a highly glycosylated protein, in an SA-dependent manner, on mucin-secreting goblet cells [6]. MGP SA-binding allows virus entry via the mucus layer to the intestinal enterocytes. Different from TGEV, the S glycoprotein of porcine CoV has no hemagglutination activity due to deletion of the SA-binding site of the S glycoprotein [61]. The loss of SA-binding activity is correlated to the non-enteropathogenicity. SAs function as HA-mediated entry determinants for TGEV, causing the enteropathogenic outcome of the virus, and SA-recognition activity is also responsible for virus amplification in cells. SA-binding activity-deficient TGEV can propagate in cells through pAPN, known as CD13, as a receptor [62,63]. The SA-binding activity potentiates infection and is crucial for intestinal infection."}

PMC:7352545 / 33312-34870 JSONTXT

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PMC:7352545 / 33312-34870 JSON TXT