PMC:7443692 / 6427-8029 JSONTXT

{"project":"LitCovid-sample-MedDRA","denotations":[{"id":"T8","span":{"begin":66,"end":71},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"}],"attributes":[{"id":"A8","pred":"meddra_id","subj":"T8","obj":"http://purl.bioontology.org/ontology/MEDDRA/10038555"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T27","span":{"begin":72,"end":83},"obj":"Chemical"},{"id":"T28","span":{"begin":722,"end":732},"obj":"Chemical"},{"id":"T29","span":{"begin":915,"end":922},"obj":"Chemical"},{"id":"T30","span":{"begin":1007,"end":1020},"obj":"Chemical"},{"id":"T31","span":{"begin":1277,"end":1289},"obj":"Chemical"}],"attributes":[{"id":"A29","pred":"chebi_id","subj":"T29","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A28","pred":"chebi_id","subj":"T28","obj":"http://purl.obolibrary.org/obo/CHEBI_36976"},{"id":"A27","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A31","pred":"chebi_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A30","pred":"chebi_id","subj":"T30","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T30","span":{"begin":121,"end":129},"obj":"Species"},{"id":"T31","span":{"begin":136,"end":146},"obj":"Species"},{"id":"T32","span":{"begin":209,"end":216},"obj":"Species"},{"id":"T33","span":{"begin":799,"end":804},"obj":"Species"},{"id":"T34","span":{"begin":1260,"end":1270},"obj":"Species"},{"id":"T35","span":{"begin":1408,"end":1418},"obj":"Species"}],"attributes":[{"id":"A31","pred":"ncbi_taxonomy_id","subj":"T31","obj":"NCBItxid:2697049"},{"id":"A32","pred":"ncbi_taxonomy_id","subj":"T32","obj":"NCBItxid:10239"},{"id":"A33","pred":"ncbi_taxonomy_id","subj":"T33","obj":"NCBItxid:9606"},{"id":"A34","pred":"ncbi_taxonomy_id","subj":"T34","obj":"NCBItxid:2697049"},{"id":"A30","pred":"ncbi_taxonomy_id","subj":"T30","obj":"NCBItxid:694009"},{"id":"A35","pred":"ncbi_taxonomy_id","subj":"T35","obj":"NCBItxid:2697049"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T34","span":{"begin":0,"end":115},"obj":"Sentence"},{"id":"T35","span":{"begin":116,"end":290},"obj":"Sentence"},{"id":"T36","span":{"begin":291,"end":552},"obj":"Sentence"},{"id":"T37","span":{"begin":553,"end":692},"obj":"Sentence"},{"id":"T38","span":{"begin":693,"end":941},"obj":"Sentence"},{"id":"T39","span":{"begin":942,"end":1312},"obj":"Sentence"},{"id":"T40","span":{"begin":1313,"end":1602},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-PD-UBERON","denotations":[{"id":"T1","span":{"begin":66,"end":90},"obj":"Body_part"},{"id":"T2","span":{"begin":523,"end":528},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0018229"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T23","span":{"begin":121,"end":129},"obj":"Disease"},{"id":"T24","span":{"begin":136,"end":146},"obj":"Disease"},{"id":"T25","span":{"begin":1260,"end":1270},"obj":"Disease"},{"id":"T26","span":{"begin":1408,"end":1418},"obj":"Disease"},{"id":"T27","span":{"begin":1419,"end":1428},"obj":"Disease"}],"attributes":[{"id":"A27","pred":"mondo_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A24","pred":"mondo_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A23","pred":"mondo_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A25","pred":"mondo_id","subj":"T25","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A26","pred":"mondo_id","subj":"T26","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

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is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T33","span":{"begin":169,"end":177},"obj":"http://purl.obolibrary.org/obo/BFO_0000034"},{"id":"T34","span":{"begin":209,"end":216},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T35","span":{"begin":238,"end":242},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T36","span":{"begin":243,"end":248},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T37","span":{"begin":334,"end":338},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T38","span":{"begin":686,"end":691},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T39","span":{"begin":1419,"end":1428},"obj":"http://purl.obolibrary.org/obo/IDO_0000586"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T32","span":{"begin":243,"end":248},"obj":"Body_part"},{"id":"T33","span":{"begin":334,"end":346},"obj":"Body_part"},{"id":"T34","span":{"begin":334,"end":338},"obj":"Body_part"},{"id":"T35","span":{"begin":523,"end":528},"obj":"Body_part"},{"id":"T36","span":{"begin":722,"end":732},"obj":"Body_part"},{"id":"T37","span":{"begin":766,"end":770},"obj":"Body_part"},{"id":"T38","span":{"begin":915,"end":922},"obj":"Body_part"},{"id":"T39","span":{"begin":1007,"end":1020},"obj":"Body_part"},{"id":"T40","span":{"begin":1277,"end":1289},"obj":"Body_part"}],"attributes":[{"id":"A32","pred":"fma_id","subj":"T32","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A37","pred":"fma_id","subj":"T37","obj":"http://purl.org/sig/ont/fma/fma74402"},{"id":"A36","pred":"fma_id","subj":"T36","obj":"http://purl.org/sig/ont/fma/fma82740"},{"id":"A34","pred":"fma_id","subj":"T34","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A33","pred":"fma_id","subj":"T33","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A39","pred":"fma_id","subj":"T39","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A35","pred":"fma_id","subj":"T35","obj":"http://purl.org/sig/ont/fma/fma63083"},{"id":"A40","pred":"fma_id","subj":"T40","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A38","pred":"fma_id","subj":"T38","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-PD-MAT","denotations":[{"id":"T1","span":{"begin":445,"end":451},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T22","span":{"begin":452,"end":462},"obj":"http://purl.obolibrary.org/obo/GO_0046903"},{"id":"T23","span":{"begin":641,"end":654},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T24","span":{"begin":849,"end":862},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T25","span":{"begin":953,"end":966},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T26","span":{"begin":1121,"end":1139},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T27","span":{"begin":1121,"end":1130},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T28","span":{"begin":1207,"end":1220},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T29","span":{"begin":1480,"end":1493},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T20","span":{"begin":452,"end":462},"obj":"http://purl.obolibrary.org/obo/GO_0046903"},{"id":"T21","span":{"begin":641,"end":654},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T22","span":{"begin":849,"end":862},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T23","span":{"begin":953,"end":966},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T24","span":{"begin":1121,"end":1139},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T25","span":{"begin":1121,"end":1130},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T26","span":{"begin":1207,"end":1220},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T27","span":{"begin":1480,"end":1493},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}

{"project":"2_test","denotations":[{"id":"32841605-21099686-19659492","span":{"begin":109,"end":113},"obj":"21099686"},{"id":"32841605-32142651-19659493","span":{"begin":267,"end":271},"obj":"32142651"},{"id":"32841605-14647384-19659494","span":{"begin":284,"end":288},"obj":"14647384"},{"id":"32841605-15983030-19659495","span":{"begin":364,"end":368},"obj":"15983030"},{"id":"32841605-19700132-19659496","span":{"begin":546,"end":550},"obj":"19700132"},{"id":"32841605-15791205-19659497","span":{"begin":935,"end":939},"obj":"15791205"},{"id":"32841605-18846099-19659498","span":{"begin":1159,"end":1163},"obj":"18846099"},{"id":"32841605-27558841-19659499","span":{"begin":1172,"end":1176},"obj":"27558841"},{"id":"32841605-32332765-19659500","span":{"begin":1574,"end":1578},"obj":"32332765"},{"id":"32841605-32333836-19659501","span":{"begin":1596,"end":1600},"obj":"32333836"}],"text":"ACE2 is an integral membrane metalloproteinase that regulates the renin-angiotensin system (Tikellis et al., 2011). Both SARS-CoV-1 and SARS-CoV-2 have co-opted ACE2 to function as the receptor by which these viruses attach and fuse with host cells (Hoffmann et al., 2020; Li et al., 2003). ACE2 is cleavable by ADAM proteases at the cell surface (Lambert et al., 2005), resulting in the shedding of a soluble ectodomain that can be detected in apical secretions of various epithelial layers (gastric, airway, etc.) and in serum (Epelman et al., 2009). The N-terminal extracellular domain of ACE2 contains six canonical sequons for N-linked glycosylation and several potential O-linked sites. Several nonsynonymous single-nucleotide polymorphisms (SNPs) in the ACE2 gene have been identified in the human population and could potentially alter ACE2 glycosylation and/or affinity of the receptor for the viral Spike protein (Li et al., 2005). Given that glycosylation can affect the half-life of circulating glycoproteins in addition to modulating the affinity of their interactions with receptors and immune/inflammatory signaling pathways (Marth and Grewal, 2008; Varki, 2017), understanding the impact of glycosylation of ACE2 with respect to its binding of SARS-CoV-2 Spike glycoprotein is of high importance. The proposed use of soluble extracellular domains of ACE2 as decoy, competitive inhibitors for SARS-CoV-2 infection emphasizes the critical need for understanding the glycosylation profile of ACE2 so that optimally active biologics can be produced (Lei et al., 2020; Monteil et al., 2020)."}