PMC:7443692 / 29556-30919 JSONTXT

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T183","span":{"begin":316,"end":319},"obj":"Chemical"},{"id":"T184","span":{"begin":373,"end":381},"obj":"Chemical"},{"id":"T185","span":{"begin":439,"end":446},"obj":"Chemical"},{"id":"T186","span":{"begin":536,"end":544},"obj":"Chemical"},{"id":"T187","span":{"begin":1027,"end":1034},"obj":"Chemical"}],"attributes":[{"id":"A186","pred":"chebi_id","subj":"T186","obj":"http://purl.obolibrary.org/obo/CHEBI_59520"},{"id":"A187","pred":"chebi_id","subj":"T187","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A185","pred":"chebi_id","subj":"T185","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A183","pred":"chebi_id","subj":"T183","obj":"http://purl.obolibrary.org/obo/CHEBI_24870"},{"id":"A184","pred":"chebi_id","subj":"T184","obj":"http://purl.obolibrary.org/obo/CHEBI_59520"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T79","span":{"begin":55,"end":60},"obj":"Species"},{"id":"T80","span":{"begin":678,"end":683},"obj":"Species"},{"id":"T81","span":{"begin":1174,"end":1184},"obj":"Species"}],"attributes":[{"id":"A81","pred":"ncbi_taxonomy_id","subj":"T81","obj":"NCBItxid:2697049"},{"id":"A79","pred":"ncbi_taxonomy_id","subj":"T79","obj":"NCBItxid:9606"},{"id":"A80","pred":"ncbi_taxonomy_id","subj":"T80","obj":"NCBItxid:9606"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T166","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"T167","span":{"begin":121,"end":209},"obj":"Sentence"},{"id":"T168","span":{"begin":210,"end":328},"obj":"Sentence"},{"id":"T169","span":{"begin":329,"end":387},"obj":"Sentence"},{"id":"T170","span":{"begin":388,"end":456},"obj":"Sentence"},{"id":"T171","span":{"begin":457,"end":630},"obj":"Sentence"},{"id":"T172","span":{"begin":631,"end":836},"obj":"Sentence"},{"id":"T173","span":{"begin":837,"end":896},"obj":"Sentence"},{"id":"T174","span":{"begin":897,"end":1011},"obj":"Sentence"},{"id":"T175","span":{"begin":1012,"end":1132},"obj":"Sentence"},{"id":"T176","span":{"begin":1133,"end":1249},"obj":"Sentence"},{"id":"T177","span":{"begin":1250,"end":1259},"obj":"Sentence"},{"id":"T178","span":{"begin":1260,"end":1269},"obj":"Sentence"},{"id":"T179","span":{"begin":1270,"end":1279},"obj":"Sentence"},{"id":"T180","span":{"begin":1280,"end":1289},"obj":"Sentence"},{"id":"T181","span":{"begin":1290,"end":1299},"obj":"Sentence"},{"id":"T182","span":{"begin":1300,"end":1363},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T58","span":{"begin":1174,"end":1184},"obj":"Disease"}],"attributes":[{"id":"A58","pred":"mondo_id","subj":"T58","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T2031","span":{"begin":61,"end":65},"obj":"Protein"},{"id":"T2032","span":{"begin":165,"end":169},"obj":"Protein"},{"id":"T2033","span":{"begin":684,"end":688},"obj":"Protein"}],"attributes":[{"id":"A2031","pred":"uniprot_id","subj":"T2031","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A2032","pred":"uniprot_id","subj":"T2032","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A2033","pred":"uniprot_id","subj":"T2033","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T88","span":{"begin":845,"end":850},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T89","span":{"begin":1197,"end":1201},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T90","span":{"begin":1312,"end":1316},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T97","span":{"begin":637,"end":650},"obj":"Body_part"}],"attributes":[{"id":"A97","pred":"fma_id","subj":"T97","obj":"http://purl.org/sig/ont/fma/fma82784"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T71","span":{"begin":107,"end":120},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T72","span":{"begin":863,"end":876},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T67","span":{"begin":107,"end":120},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T68","span":{"begin":863,"end":876},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}

{"project":"LitCovid-sample-Glycan","denotations":[{"id":"T94","span":{"begin":837,"end":840},"obj":"https://glytoucan.org/Structures/Glycans/G05518TD"}],"text":"Figure 5 Glycomics-Informed Glycoproteomics of Soluble Human ACE2 Reveals High Occupancy, Complex N-linked Glycosylation\n(A) Glycans released from soluble, purified ACE2 were permethylated and analyzed by MSn. Structures were assigned, grouped by type and structural features, and prevalence was determined based on ion current. The pie chart shows basic division by broad N-glycan type. The bar graph provides additional detail about the glycans detected. The most abundant structure with a unique categorization by glycomics for each N-glycan type in the pie chart, or above each feature category in the bar graph, is indicated.\n(B–G) Glycopeptides were prepared from soluble human ACE2 by using multiple combinations of proteases, analyzed by LC-MSn, and the resulting data were searched by using several different software packages. All six sites of N-linked glycosylation are presented here. Displayed in the bar graphs are the individual compositions observed graphed in terms of assigned spectral counts. Representative glycans (as determined by glycomics analysis) for several abundant compositions are shown in SNFG format. The pie chart (analogous to Figure 3 for SARS-CoV-2 S) for each site is displayed in the upper corner of each panel.\n(B) N053.\n(C) N090.\n(D) N103.\n(E) N322.\n(F) N432.\n(G) N546, a site that does not exist in three in 10,000 people."}