PMC:7352545 / 24580-26133 JSON TXT

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LitCovid_Glycan-Motif-Structure

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T82","span":{"begin":7,"end":9},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T83","span":{"begin":39,"end":41},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T84","span":{"begin":450,"end":473},"obj":"https://glytoucan.org/Structures/Glycans/G50850NI"},{"id":"T85","span":{"begin":450,"end":473},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T86","span":{"begin":587,"end":589},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T87","span":{"begin":654,"end":656},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T88","span":{"begin":741,"end":743},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T89","span":{"begin":873,"end":875},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T90","span":{"begin":963,"end":965},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T91","span":{"begin":1296,"end":1298},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"4.2.2. SA C9-O-Acetyl Modification\nThe SA 9-O-acetylation in hosts allows hosts to evade influenza A virus hemagglutinin (HA) recognition and some lectins of factor H (FH), CD22/Siglec-2 and sialoadhesin/Siglec-1. Instead, the influenza C virus HA recognizes the hosts. β-elimination and permethylation eliminate the 9-O-acetyl group from SAs. Chemical modification of the C-9 position of Neu5,9Ac2 generates a 9-N-acetyl analog, 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc), a mimic of Neu5,9Ac2 with influenza C virus-binding capacity, which is not cleaved by the HE [42]. SA O-acetylesterase regulates the presence of 7,9-O-Ac and 9-O-Ac. SA O-acetylation and deacetylation are involved in development, cancer and immunology. SA O-acetylation alters host lectin bindings such as siglecs [29]. The presence of 9-O-Ac can also reduce the activity of NAs [43]. SA modifications regulate pathogen binding or pathogen NAs. Influenza A/B/C/D viruses use SA as their entry receptors. Influenza A and B subtypes bind to SAs via HA and NA to allow endocytosis of the virus and fusion of the viral envelope with endosomes. In contrast, influenza C and D subtypes bear only one coated glycoprotein, termed the HE fusion protein (HEF). The HEF acts as the HA and NA. HEF recognizes 9-O-acetyl SA for entry into cells, while the esterase domain removes 9-O-acetyl-groups and liberates the virus from mucus and mis-assembled virus aggregates after budding. The 9-O-Ac on cells prevents the NA activity and HA binding of the influenza A type virus [44]."}

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T217","span":{"begin":450,"end":473},"obj":"Body_part"},{"id":"T218","span":{"begin":1117,"end":1126},"obj":"Body_part"},{"id":"T219","span":{"begin":1189,"end":1201},"obj":"Body_part"},{"id":"T220","span":{"begin":1224,"end":1231},"obj":"Body_part"},{"id":"T221","span":{"begin":1314,"end":1319},"obj":"Body_part"},{"id":"T222","span":{"begin":1402,"end":1407},"obj":"Body_part"},{"id":"T223","span":{"begin":1472,"end":1477},"obj":"Body_part"}],"attributes":[{"id":"A217","pred":"fma_id","subj":"T217","obj":"http://purl.org/sig/ont/fma/fma82788"},{"id":"A218","pred":"fma_id","subj":"T218","obj":"http://purl.org/sig/ont/fma/fma67180"},{"id":"A219","pred":"fma_id","subj":"T219","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A220","pred":"fma_id","subj":"T220","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A221","pred":"fma_id","subj":"T221","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A222","pred":"fma_id","subj":"T222","obj":"http://purl.org/sig/ont/fma/fma66938"},{"id":"A223","pred":"fma_id","subj":"T223","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"4.2.2. SA C9-O-Acetyl Modification\nThe SA 9-O-acetylation in hosts allows hosts to evade influenza A virus hemagglutinin (HA) recognition and some lectins of factor H (FH), CD22/Siglec-2 and sialoadhesin/Siglec-1. Instead, the influenza C virus HA recognizes the hosts. β-elimination and permethylation eliminate the 9-O-acetyl group from SAs. Chemical modification of the C-9 position of Neu5,9Ac2 generates a 9-N-acetyl analog, 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc), a mimic of Neu5,9Ac2 with influenza C virus-binding capacity, which is not cleaved by the HE [42]. SA O-acetylesterase regulates the presence of 7,9-O-Ac and 9-O-Ac. SA O-acetylation and deacetylation are involved in development, cancer and immunology. SA O-acetylation alters host lectin bindings such as siglecs [29]. The presence of 9-O-Ac can also reduce the activity of NAs [43]. SA modifications regulate pathogen binding or pathogen NAs. Influenza A/B/C/D viruses use SA as their entry receptors. Influenza A and B subtypes bind to SAs via HA and NA to allow endocytosis of the virus and fusion of the viral envelope with endosomes. In contrast, influenza C and D subtypes bear only one coated glycoprotein, termed the HE fusion protein (HEF). The HEF acts as the HA and NA. HEF recognizes 9-O-acetyl SA for entry into cells, while the esterase domain removes 9-O-acetyl-groups and liberates the virus from mucus and mis-assembled virus aggregates after budding. The 9-O-Ac on cells prevents the NA activity and HA binding of the influenza A type virus [44]."}

LitCovid-PD-UBERON

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T5","span":{"begin":1402,"end":1407},"obj":"Body_part"}],"attributes":[{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000912"}],"text":"4.2.2. SA C9-O-Acetyl Modification\nThe SA 9-O-acetylation in hosts allows hosts to evade influenza A virus hemagglutinin (HA) recognition and some lectins of factor H (FH), CD22/Siglec-2 and sialoadhesin/Siglec-1. Instead, the influenza C virus HA recognizes the hosts. β-elimination and permethylation eliminate the 9-O-acetyl group from SAs. Chemical modification of the C-9 position of Neu5,9Ac2 generates a 9-N-acetyl analog, 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc), a mimic of Neu5,9Ac2 with influenza C virus-binding capacity, which is not cleaved by the HE [42]. SA O-acetylesterase regulates the presence of 7,9-O-Ac and 9-O-Ac. SA O-acetylation and deacetylation are involved in development, cancer and immunology. SA O-acetylation alters host lectin bindings such as siglecs [29]. The presence of 9-O-Ac can also reduce the activity of NAs [43]. SA modifications regulate pathogen binding or pathogen NAs. Influenza A/B/C/D viruses use SA as their entry receptors. Influenza A and B subtypes bind to SAs via HA and NA to allow endocytosis of the virus and fusion of the viral envelope with endosomes. In contrast, influenza C and D subtypes bear only one coated glycoprotein, termed the HE fusion protein (HEF). The HEF acts as the HA and NA. HEF recognizes 9-O-acetyl SA for entry into cells, while the esterase domain removes 9-O-acetyl-groups and liberates the virus from mucus and mis-assembled virus aggregates after budding. The 9-O-Ac on cells prevents the NA activity and HA binding of the influenza A type virus [44]."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T92","span":{"begin":89,"end":98},"obj":"Disease"},{"id":"T93","span":{"begin":168,"end":170},"obj":"Disease"},{"id":"T94","span":{"begin":227,"end":236},"obj":"Disease"},{"id":"T95","span":{"begin":514,"end":523},"obj":"Disease"},{"id":"T96","span":{"begin":718,"end":724},"obj":"Disease"},{"id":"T97","span":{"begin":933,"end":942},"obj":"Disease"},{"id":"T98","span":{"begin":992,"end":1001},"obj":"Disease"},{"id":"T99","span":{"begin":1141,"end":1150},"obj":"Disease"},{"id":"T100","span":{"begin":1525,"end":1534},"obj":"Disease"}],"attributes":[{"id":"A92","pred":"mondo_id","subj":"T92","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A93","pred":"mondo_id","subj":"T93","obj":"http://purl.obolibrary.org/obo/MONDO_0016525"},{"id":"A94","pred":"mondo_id","subj":"T94","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A95","pred":"mondo_id","subj":"T95","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A96","pred":"mondo_id","subj":"T96","obj":"http://purl.obolibrary.org/obo/MONDO_0004992"},{"id":"A97","pred":"mondo_id","subj":"T97","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A98","pred":"mondo_id","subj":"T98","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A99","pred":"mondo_id","subj":"T99","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A100","pred":"mondo_id","subj":"T100","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"4.2.2. SA C9-O-Acetyl Modification\nThe SA 9-O-acetylation in hosts allows hosts to evade influenza A virus hemagglutinin (HA) recognition and some lectins of factor H (FH), CD22/Siglec-2 and sialoadhesin/Siglec-1. Instead, the influenza C virus HA recognizes the hosts. β-elimination and permethylation eliminate the 9-O-acetyl group from SAs. Chemical modification of the C-9 position of Neu5,9Ac2 generates a 9-N-acetyl analog, 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc), a mimic of Neu5,9Ac2 with influenza C virus-binding capacity, which is not cleaved by the HE [42]. SA O-acetylesterase regulates the presence of 7,9-O-Ac and 9-O-Ac. SA O-acetylation and deacetylation are involved in development, cancer and immunology. SA O-acetylation alters host lectin bindings such as siglecs [29]. The presence of 9-O-Ac can also reduce the activity of NAs [43]. SA modifications regulate pathogen binding or pathogen NAs. Influenza A/B/C/D viruses use SA as their entry receptors. Influenza A and B subtypes bind to SAs via HA and NA to allow endocytosis of the virus and fusion of the viral envelope with endosomes. In contrast, influenza C and D subtypes bear only one coated glycoprotein, termed the HE fusion protein (HEF). The HEF acts as the HA and NA. HEF recognizes 9-O-acetyl SA for entry into cells, while the esterase domain removes 9-O-acetyl-groups and liberates the virus from mucus and mis-assembled virus aggregates after budding. The 9-O-Ac on cells prevents the NA activity and HA binding of the influenza A type virus [44]."}

LitCovid-PD-CLO

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T44","span":{"begin":1054,"end":1065},"obj":"http://purl.obolibrary.org/obo/GO_0006897"},{"id":"T45","span":{"begin":1449,"end":1456},"obj":"http://purl.obolibrary.org/obo/GO_0007114"}],"text":"4.2.2. SA C9-O-Acetyl Modification\nThe SA 9-O-acetylation in hosts allows hosts to evade influenza A virus hemagglutinin (HA) recognition and some lectins of factor H (FH), CD22/Siglec-2 and sialoadhesin/Siglec-1. Instead, the influenza C virus HA recognizes the hosts. β-elimination and permethylation eliminate the 9-O-acetyl group from SAs. Chemical modification of the C-9 position of Neu5,9Ac2 generates a 9-N-acetyl analog, 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc), a mimic of Neu5,9Ac2 with influenza C virus-binding capacity, which is not cleaved by the HE [42]. SA O-acetylesterase regulates the presence of 7,9-O-Ac and 9-O-Ac. SA O-acetylation and deacetylation are involved in development, cancer and immunology. SA O-acetylation alters host lectin bindings such as siglecs [29]. The presence of 9-O-Ac can also reduce the activity of NAs [43]. SA modifications regulate pathogen binding or pathogen NAs. Influenza A/B/C/D viruses use SA as their entry receptors. Influenza A and B subtypes bind to SAs via HA and NA to allow endocytosis of the virus and fusion of the viral envelope with endosomes. In contrast, influenza C and D subtypes bear only one coated glycoprotein, termed the HE fusion protein (HEF). The HEF acts as the HA and NA. HEF recognizes 9-O-acetyl SA for entry into cells, while the esterase domain removes 9-O-acetyl-groups and liberates the virus from mucus and mis-assembled virus aggregates after budding. The 9-O-Ac on cells prevents the NA activity and HA binding of the influenza A type virus [44]."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T233","span":{"begin":0,"end":6},"obj":"Sentence"},{"id":"T234","span":{"begin":7,"end":34},"obj":"Sentence"},{"id":"T235","span":{"begin":35,"end":213},"obj":"Sentence"},{"id":"T236","span":{"begin":214,"end":343},"obj":"Sentence"},{"id":"T237","span":{"begin":344,"end":586},"obj":"Sentence"},{"id":"T238","span":{"begin":587,"end":653},"obj":"Sentence"},{"id":"T239","span":{"begin":654,"end":740},"obj":"Sentence"},{"id":"T240","span":{"begin":741,"end":807},"obj":"Sentence"},{"id":"T241","span":{"begin":808,"end":872},"obj":"Sentence"},{"id":"T242","span":{"begin":873,"end":932},"obj":"Sentence"},{"id":"T243","span":{"begin":933,"end":991},"obj":"Sentence"},{"id":"T244","span":{"begin":992,"end":1127},"obj":"Sentence"},{"id":"T245","span":{"begin":1128,"end":1238},"obj":"Sentence"},{"id":"T246","span":{"begin":1239,"end":1269},"obj":"Sentence"},{"id":"T247","span":{"begin":1270,"end":1457},"obj":"Sentence"},{"id":"T248","span":{"begin":1458,"end":1553},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"4.2.2. SA C9-O-Acetyl Modification\nThe SA 9-O-acetylation in hosts allows hosts to evade influenza A virus hemagglutinin (HA) recognition and some lectins of factor H (FH), CD22/Siglec-2 and sialoadhesin/Siglec-1. Instead, the influenza C virus HA recognizes the hosts. β-elimination and permethylation eliminate the 9-O-acetyl group from SAs. Chemical modification of the C-9 position of Neu5,9Ac2 generates a 9-N-acetyl analog, 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc), a mimic of Neu5,9Ac2 with influenza C virus-binding capacity, which is not cleaved by the HE [42]. SA O-acetylesterase regulates the presence of 7,9-O-Ac and 9-O-Ac. SA O-acetylation and deacetylation are involved in development, cancer and immunology. SA O-acetylation alters host lectin bindings such as siglecs [29]. The presence of 9-O-Ac can also reduce the activity of NAs [43]. SA modifications regulate pathogen binding or pathogen NAs. Influenza A/B/C/D viruses use SA as their entry receptors. Influenza A and B subtypes bind to SAs via HA and NA to allow endocytosis of the virus and fusion of the viral envelope with endosomes. In contrast, influenza C and D subtypes bear only one coated glycoprotein, termed the HE fusion protein (HEF). The HEF acts as the HA and NA. HEF recognizes 9-O-acetyl SA for entry into cells, while the esterase domain removes 9-O-acetyl-groups and liberates the virus from mucus and mis-assembled virus aggregates after budding. The 9-O-Ac on cells prevents the NA activity and HA binding of the influenza A type virus [44]."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-29341588-51943984","span":{"begin":868,"end":870},"obj":"29341588"},{"id":"32604730-31796537-51943985","span":{"begin":1549,"end":1551},"obj":"31796537"},{"id":"T17811","span":{"begin":868,"end":870},"obj":"29341588"},{"id":"T51599","span":{"begin":1549,"end":1551},"obj":"31796537"}],"text":"4.2.2. SA C9-O-Acetyl Modification\nThe SA 9-O-acetylation in hosts allows hosts to evade influenza A virus hemagglutinin (HA) recognition and some lectins of factor H (FH), CD22/Siglec-2 and sialoadhesin/Siglec-1. Instead, the influenza C virus HA recognizes the hosts. β-elimination and permethylation eliminate the 9-O-acetyl group from SAs. Chemical modification of the C-9 position of Neu5,9Ac2 generates a 9-N-acetyl analog, 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc), a mimic of Neu5,9Ac2 with influenza C virus-binding capacity, which is not cleaved by the HE [42]. SA O-acetylesterase regulates the presence of 7,9-O-Ac and 9-O-Ac. SA O-acetylation and deacetylation are involved in development, cancer and immunology. SA O-acetylation alters host lectin bindings such as siglecs [29]. The presence of 9-O-Ac can also reduce the activity of NAs [43]. SA modifications regulate pathogen binding or pathogen NAs. Influenza A/B/C/D viruses use SA as their entry receptors. Influenza A and B subtypes bind to SAs via HA and NA to allow endocytosis of the virus and fusion of the viral envelope with endosomes. In contrast, influenza C and D subtypes bear only one coated glycoprotein, termed the HE fusion protein (HEF). The HEF acts as the HA and NA. HEF recognizes 9-O-acetyl SA for entry into cells, while the esterase domain removes 9-O-acetyl-groups and liberates the virus from mucus and mis-assembled virus aggregates after budding. The 9-O-Ac on cells prevents the NA activity and HA binding of the influenza A type virus [44]."}

LitCovid-PD-HP

{"project":"LitCovid-PD-HP","denotations":[{"id":"T8","span":{"begin":718,"end":724},"obj":"Phenotype"}],"attributes":[{"id":"A8","pred":"hp_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/HP_0002664"}],"text":"4.2.2. SA C9-O-Acetyl Modification\nThe SA 9-O-acetylation in hosts allows hosts to evade influenza A virus hemagglutinin (HA) recognition and some lectins of factor H (FH), CD22/Siglec-2 and sialoadhesin/Siglec-1. Instead, the influenza C virus HA recognizes the hosts. β-elimination and permethylation eliminate the 9-O-acetyl group from SAs. Chemical modification of the C-9 position of Neu5,9Ac2 generates a 9-N-acetyl analog, 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc), a mimic of Neu5,9Ac2 with influenza C virus-binding capacity, which is not cleaved by the HE [42]. SA O-acetylesterase regulates the presence of 7,9-O-Ac and 9-O-Ac. SA O-acetylation and deacetylation are involved in development, cancer and immunology. SA O-acetylation alters host lectin bindings such as siglecs [29]. The presence of 9-O-Ac can also reduce the activity of NAs [43]. SA modifications regulate pathogen binding or pathogen NAs. Influenza A/B/C/D viruses use SA as their entry receptors. Influenza A and B subtypes bind to SAs via HA and NA to allow endocytosis of the virus and fusion of the viral envelope with endosomes. In contrast, influenza C and D subtypes bear only one coated glycoprotein, termed the HE fusion protein (HEF). The HEF acts as the HA and NA. HEF recognizes 9-O-acetyl SA for entry into cells, while the esterase domain removes 9-O-acetyl-groups and liberates the virus from mucus and mis-assembled virus aggregates after budding. The 9-O-Ac on cells prevents the NA activity and HA binding of the influenza A type virus [44]."}

PMC:7352545 / 24580-26133 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7352545 / 24580-26133 JSON TXT