PubMed:27502283 / 748-1173 JSONTXT

{"project":"pqqtest_sentence","denotations":[{"id":"T20238","span":{"begin":400,"end":413},"obj":"xzyao:38936"},{"id":"T95495","span":{"begin":285,"end":289},"obj":"PO:0009010, funRiceGene:180"},{"id":"T50215","span":{"begin":400,"end":404},"obj":"PO:0009010, funRiceGene:180"},{"id":"T97076","span":{"begin":395,"end":404},"obj":"xzyao:29448"},{"id":"M_31","span":{"begin":0,"end":6},"obj":"hunflair:NA:Gene"},{"id":"M_32","span":{"begin":52,"end":58},"obj":"hunflair:NA:Gene"},{"id":"M_39","span":{"begin":419,"end":425},"obj":"hunflair:NA:Gene"},{"id":"M_47","span":{"begin":395,"end":399},"obj":"hunflair:NA:Species"},{"id":"M_55","span":{"begin":395,"end":399},"obj":"pubtator:4530:Species"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"21k_plant_trait_mention","denotations":[{"id":"M_7","span":{"begin":285,"end":289},"obj":"PO:0009010, funRiceGene:180"},{"id":"M_8","span":{"begin":400,"end":404},"obj":"PO:0009010, funRiceGene:180"},{"id":"M_14","span":{"begin":395,"end":399},"obj":"hunflair:NA:Species"},{"id":"M_19","span":{"begin":419,"end":425},"obj":"hunflair:NA:Gene"},{"id":"M_22","span":{"begin":0,"end":6},"obj":"hunflair:NA:Gene"},{"id":"M_23","span":{"begin":52,"end":58},"obj":"hunflair:NA:Gene"},{"id":"M_38","span":{"begin":395,"end":399},"obj":"pubtator:4530:Species"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"OryzaGP_2021","denotations":[{"id":"T7","span":{"begin":0,"end":6},"obj":"http://identifiers.org/oryzabase.gene/21327"},{"id":"T8","span":{"begin":52,"end":58},"obj":"http://identifiers.org/oryzabase.gene/21327"},{"id":"T9","span":{"begin":419,"end":425},"obj":"http://identifiers.org/oryzabase.gene/11812"},{"id":"T58692","span":{"begin":0,"end":6},"obj":"http://identifiers.org/ricegap/LOC_Os07g43390"},{"id":"T40698","span":{"begin":52,"end":58},"obj":"http://identifiers.org/ricegap/LOC_Os07g43390"},{"id":"T52289","span":{"begin":419,"end":425},"obj":"http://identifiers.org/ricegap/LOC_Os03g55090"},{"id":"T75324","span":{"begin":0,"end":6},"obj":"http://identifiers.org/rapdb.locus/Os07g0627000"},{"id":"T30975","span":{"begin":52,"end":58},"obj":"http://identifiers.org/rapdb.locus/Os07g0627000"},{"id":"T85499","span":{"begin":419,"end":425},"obj":"http://identifiers.org/rapdb.locus/Os03g0758100"},{"id":"T12951","span":{"begin":0,"end":6},"obj":"http://identifiers.org/uniprot/Q8LI30"},{"id":"T40771","span":{"begin":52,"end":58},"obj":"http://identifiers.org/uniprot/Q8LI30"},{"id":"T63666","span":{"begin":419,"end":425},"obj":"http://identifiers.org/uniprot/B3IYE3"},{"id":"M_9","span":{"begin":395,"end":399},"obj":"hunflair:NA:Species"},{"id":"M_14","span":{"begin":0,"end":6},"obj":"hunflair:NA:Gene"},{"id":"M_15","span":{"begin":52,"end":58},"obj":"hunflair:NA:Gene"},{"id":"M_22","span":{"begin":419,"end":425},"obj":"hunflair:NA:Gene"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"OryzaGP_2022","denotations":[{"id":"T1","span":{"begin":211,"end":212},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T2","span":{"begin":213,"end":214},"obj":"http://identifiers.org/oryzabase.gene/11216"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"sentences","denotations":[{"id":"T6","span":{"begin":9,"end":146},"obj":"Sentence"},{"id":"T7","span":{"begin":147,"end":414},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"OryzaGP_2021_v2","denotations":[{"id":"T7","span":{"begin":0,"end":6},"obj":"http://identifiers.org/oryzabase.gene/21327"},{"id":"T8","span":{"begin":52,"end":58},"obj":"http://identifiers.org/oryzabase.gene/21327"},{"id":"T9","span":{"begin":419,"end":425},"obj":"http://identifiers.org/oryzabase.gene/11812"},{"id":"T77106","span":{"begin":0,"end":6},"obj":"http://identifiers.org/rapdb.locus/Os07g0627000"},{"id":"T42104","span":{"begin":52,"end":58},"obj":"http://identifiers.org/rapdb.locus/Os07g0627000"},{"id":"T65292","span":{"begin":419,"end":425},"obj":"http://identifiers.org/rapdb.locus/Os03g0758100"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"OryzaGP_2021_FLAIR","denotations":[{"id":"M_9","span":{"begin":395,"end":399},"obj":"hunflair:NA:Species"},{"id":"M_14","span":{"begin":0,"end":6},"obj":"hunflair:NA:Gene"},{"id":"M_15","span":{"begin":52,"end":58},"obj":"hunflair:NA:Gene"},{"id":"M_22","span":{"begin":419,"end":425},"obj":"hunflair:NA:Gene"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"OryzaGP","denotations":[{"id":"T5","span":{"begin":0,"end":6},"obj":"gene"},{"id":"T6","span":{"begin":419,"end":425},"obj":"gene"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"NCBITAXON","denotations":[{"id":"T5","span":{"begin":395,"end":399},"obj":"OrganismTaxon"}],"attributes":[{"id":"A5","pred":"db_id","subj":"T5","obj":"4530"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":196,"end":201},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0003655"}],"text":"OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1"}