PMC:7443692 / 342-722 JSONTXT

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{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T5","span":{"begin":148,"end":153},"obj":"Species"}],"attributes":[{"id":"A5","pred":"ncbi_taxonomy_id","subj":"T5","obj":"NCBItxid:9606"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"ics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacti"}

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to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacti"}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T5","span":{"begin":20,"end":24},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"ics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacti"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T6","span":{"begin":278,"end":291},"obj":"Body_part"},{"id":"T7","span":{"begin":343,"end":355},"obj":"Body_part"}],"attributes":[{"id":"A6","pred":"fma_id","subj":"T6","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A7","pred":"fma_id","subj":"T7","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"ics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacti"}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T1","span":{"begin":56,"end":69},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"ics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacti"}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T1","span":{"begin":56,"end":69},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"ics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacti"}

{"project":"LitCovid-PMC-OGER-BB","denotations":[{"id":"T12","span":{"begin":109,"end":118},"obj":"CHEBI:60816;CHEBI:60816"},{"id":"T13","span":{"begin":148,"end":153},"obj":"SP_6;NCBITaxon:9606;PG_10"},{"id":"T14","span":{"begin":154,"end":158},"obj":"PG_10;PR:000003622"},{"id":"T15","span":{"begin":278,"end":291},"obj":"CHEBI:17089;BV_11;CHEBI:17089"},{"id":"T16","span":{"begin":343,"end":355},"obj":"CHEBI:17089;BV_11;CHEBI:17089"}],"text":"ics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacti"}