PubMed:32985653 / 508-767 JSONTXT

{"project":"sentences","denotations":[{"id":"T5","span":{"begin":0,"end":259},"obj":"Sentence"},{"id":"T5","span":{"begin":0,"end":259},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In other glycosylated viral proteins, glycosylation is required for interaction with calnexin and chaperone-mediated folding in the endoplasmic reticulum, and prevention of this interaction leads to unfolded viral proteins and thus inhibits viral replication."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":144,"end":153},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"}],"text":"In other glycosylated viral proteins, glycosylation is required for interaction with calnexin and chaperone-mediated folding in the endoplasmic reticulum, and prevention of this interaction leads to unfolded viral proteins and thus inhibits viral replication."}