PubMed:9727000 / 533-819 JSONTXT

{"project":"sentences","denotations":[{"id":"T5","span":{"begin":0,"end":286},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"FK506.FKBP12 drug-immunophilin complexes inhibited the interaction of NFAT with activated calcineurin much more effectively than they inhibited the interaction with inactive calcineurin, suggesting that part of the interaction with activated calcineurin involved the enzyme active site."}

{"project":"jnlpba-st-training","denotations":[{"id":"T13","span":{"begin":70,"end":74},"obj":"protein"},{"id":"T14","span":{"begin":90,"end":101},"obj":"protein"},{"id":"T15","span":{"begin":174,"end":185},"obj":"protein"},{"id":"T16","span":{"begin":242,"end":253},"obj":"protein"},{"id":"T17","span":{"begin":267,"end":285},"obj":"DNA"}],"text":"FK506.FKBP12 drug-immunophilin complexes inhibited the interaction of NFAT with activated calcineurin much more effectively than they inhibited the interaction with inactive calcineurin, suggesting that part of the interaction with activated calcineurin involved the enzyme active site."}

{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S5","span":{"begin":0,"end":286},"obj":"Sentence"}],"text":"FK506.FKBP12 drug-immunophilin complexes inhibited the interaction of NFAT with activated calcineurin much more effectively than they inhibited the interaction with inactive calcineurin, suggesting that part of the interaction with activated calcineurin involved the enzyme active site."}

{"project":"genia-medco-coref","denotations":[{"id":"C6","span":{"begin":0,"end":40},"obj":"NP"},{"id":"C7","span":{"begin":70,"end":74},"obj":"NP"},{"id":"C8","span":{"begin":80,"end":101},"obj":"NP"},{"id":"C9","span":{"begin":129,"end":133},"obj":"NP"},{"id":"C10","span":{"begin":232,"end":253},"obj":"NP"}],"relations":[{"id":"R5","pred":"coref-pron","subj":"C9","obj":"C6"},{"id":"R6","pred":"coref-ident","subj":"C10","obj":"C8"}],"text":"FK506.FKBP12 drug-immunophilin complexes inhibited the interaction of NFAT with activated calcineurin much more effectively than they inhibited the interaction with inactive calcineurin, suggesting that part of the interaction with activated calcineurin involved the enzyme active site."}

{"project":"GENIAcorpus","denotations":[{"id":"T16","span":{"begin":0,"end":40},"obj":"other_organic_compound"},{"id":"T17","span":{"begin":70,"end":74},"obj":"protein_family_or_group"},{"id":"T18","span":{"begin":90,"end":101},"obj":"protein_molecule"},{"id":"T19","span":{"begin":174,"end":185},"obj":"protein_molecule"},{"id":"T20","span":{"begin":242,"end":253},"obj":"protein_molecule"},{"id":"T21","span":{"begin":267,"end":285},"obj":"DNA_domain_or_region"}],"text":"FK506.FKBP12 drug-immunophilin complexes inhibited the interaction of NFAT with activated calcineurin much more effectively than they inhibited the interaction with inactive calcineurin, suggesting that part of the interaction with activated calcineurin involved the enzyme active site."}