PMC:7712180 / 37131-37484 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"1264","span":{"begin":86,"end":89},"obj":"Species"},{"id":"1282","span":{"begin":44,"end":48},"obj":"Species"},{"id":"1283","span":{"begin":115,"end":119},"obj":"Species"},{"id":"1284","span":{"begin":223,"end":227},"obj":"Species"},{"id":"1295","span":{"begin":310,"end":315},"obj":"Mutation"},{"id":"1296","span":{"begin":290,"end":294},"obj":"Mutation"},{"id":"1297","span":{"begin":175,"end":180},"obj":"Mutation"}],"attributes":[{"id":"A1264","pred":"tao:has_database_id","subj":"1264","obj":"Tax:10116"},{"id":"A1282","pred":"tao:has_database_id","subj":"1282","obj":"Tax:290028"},{"id":"A1283","pred":"tao:has_database_id","subj":"1283","obj":"Tax:290028"},{"id":"A1284","pred":"tao:has_database_id","subj":"1284","obj":"Tax:290028"},{"id":"A1295","pred":"tao:has_standard_notation","subj":"1295","obj":"p.N251Q"},{"id":"A1296","pred":"tao:has_standard_notation","subj":"1296","obj":"p.N29Q"},{"id":"A1297","pred":"tao:has_standard_notation","subj":"1297","obj":"p.N251Q"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"In comparison with binding of the wild-type HKU1 S1A conjugated with nanoparticles to rat erythrocytes, the mutant HKU1 S1A with removal of a glycosylation site at element 2 (N251Q) showed increased binding, and the mutant HKU1 S1A with removal of the glycosylation sites in both elements (N29Q in element 1 + N251Q in element 2) showed greater binding."}

{"project":"LitCovid-sentences","denotations":[{"id":"T212","span":{"begin":0,"end":353},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In comparison with binding of the wild-type HKU1 S1A conjugated with nanoparticles to rat erythrocytes, the mutant HKU1 S1A with removal of a glycosylation site at element 2 (N251Q) showed increased binding, and the mutant HKU1 S1A with removal of the glycosylation sites in both elements (N29Q in element 1 + N251Q in element 2) showed greater binding."}