PubMed:27502283 / 630-1173 JSONTXT

{"project":"pqqtest_sentence","denotations":[{"id":"T92573","span":{"begin":21,"end":31},"obj":"xzyao:31834"},{"id":"T20238","span":{"begin":518,"end":531},"obj":"xzyao:38936"},{"id":"T95495","span":{"begin":403,"end":407},"obj":"PO:0009010, funRiceGene:180"},{"id":"T50215","span":{"begin":518,"end":522},"obj":"PO:0009010, funRiceGene:180"},{"id":"T72931","span":{"begin":53,"end":65},"obj":"xzyao:24527"},{"id":"T97076","span":{"begin":513,"end":522},"obj":"xzyao:29448"},{"id":"M_26","span":{"begin":66,"end":80},"obj":"hunflair:NA:Gene"},{"id":"M_31","span":{"begin":118,"end":124},"obj":"hunflair:NA:Gene"},{"id":"M_32","span":{"begin":170,"end":176},"obj":"hunflair:NA:Gene"},{"id":"M_38","span":{"begin":0,"end":6},"obj":"hunflair:NA:Gene"},{"id":"M_39","span":{"begin":537,"end":543},"obj":"hunflair:NA:Gene"},{"id":"M_47","span":{"begin":513,"end":517},"obj":"hunflair:NA:Species"},{"id":"M_51","span":{"begin":60,"end":65},"obj":"hunflair:NA:Species"},{"id":"M_55","span":{"begin":513,"end":517},"obj":"pubtator:4530:Species"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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":403,"end":407},"obj":"PO:0009010, funRiceGene:180"},{"id":"M_8","span":{"begin":518,"end":522},"obj":"PO:0009010, funRiceGene:180"},{"id":"M_9","span":{"begin":60,"end":65},"obj":"hunflair:NA:Species"},{"id":"M_14","span":{"begin":513,"end":517},"obj":"hunflair:NA:Species"},{"id":"M_18","span":{"begin":0,"end":6},"obj":"hunflair:NA:Gene"},{"id":"M_19","span":{"begin":537,"end":543},"obj":"hunflair:NA:Gene"},{"id":"M_22","span":{"begin":118,"end":124},"obj":"hunflair:NA:Gene"},{"id":"M_23","span":{"begin":170,"end":176},"obj":"hunflair:NA:Gene"},{"id":"M_26","span":{"begin":66,"end":80},"obj":"hunflair:NA:Gene"},{"id":"M_38","span":{"begin":513,"end":517},"obj":"pubtator:4530:Species"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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":"T6","span":{"begin":0,"end":6},"obj":"http://identifiers.org/oryzabase.gene/11812"},{"id":"T7","span":{"begin":118,"end":124},"obj":"http://identifiers.org/oryzabase.gene/21327"},{"id":"T8","span":{"begin":170,"end":176},"obj":"http://identifiers.org/oryzabase.gene/21327"},{"id":"T9","span":{"begin":537,"end":543},"obj":"http://identifiers.org/oryzabase.gene/11812"},{"id":"T10218","span":{"begin":0,"end":6},"obj":"http://identifiers.org/ricegap/LOC_Os03g55090"},{"id":"T58692","span":{"begin":118,"end":124},"obj":"http://identifiers.org/ricegap/LOC_Os07g43390"},{"id":"T40698","span":{"begin":170,"end":176},"obj":"http://identifiers.org/ricegap/LOC_Os07g43390"},{"id":"T52289","span":{"begin":537,"end":543},"obj":"http://identifiers.org/ricegap/LOC_Os03g55090"},{"id":"T35022","span":{"begin":0,"end":6},"obj":"http://identifiers.org/rapdb.locus/Os03g0758100"},{"id":"T75324","span":{"begin":118,"end":124},"obj":"http://identifiers.org/rapdb.locus/Os07g0627000"},{"id":"T30975","span":{"begin":170,"end":176},"obj":"http://identifiers.org/rapdb.locus/Os07g0627000"},{"id":"T85499","span":{"begin":537,"end":543},"obj":"http://identifiers.org/rapdb.locus/Os03g0758100"},{"id":"T59889","span":{"begin":0,"end":6},"obj":"http://identifiers.org/uniprot/B3IYE3"},{"id":"T12951","span":{"begin":118,"end":124},"obj":"http://identifiers.org/uniprot/Q8LI30"},{"id":"T40771","span":{"begin":170,"end":176},"obj":"http://identifiers.org/uniprot/Q8LI30"},{"id":"T63666","span":{"begin":537,"end":543},"obj":"http://identifiers.org/uniprot/B3IYE3"},{"id":"M_5","span":{"begin":60,"end":65},"obj":"hunflair:NA:Species"},{"id":"M_9","span":{"begin":513,"end":517},"obj":"hunflair:NA:Species"},{"id":"M_14","span":{"begin":118,"end":124},"obj":"hunflair:NA:Gene"},{"id":"M_15","span":{"begin":170,"end":176},"obj":"hunflair:NA:Gene"},{"id":"M_18","span":{"begin":66,"end":80},"obj":"hunflair:NA:Gene"},{"id":"M_21","span":{"begin":0,"end":6},"obj":"hunflair:NA:Gene"},{"id":"M_22","span":{"begin":537,"end":543},"obj":"hunflair:NA:Gene"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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":329,"end":330},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T2","span":{"begin":331,"end":332},"obj":"http://identifiers.org/oryzabase.gene/11216"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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":127,"end":264},"obj":"Sentence"},{"id":"T7","span":{"begin":265,"end":532},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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":"T6","span":{"begin":0,"end":6},"obj":"http://identifiers.org/oryzabase.gene/11812"},{"id":"T7","span":{"begin":118,"end":124},"obj":"http://identifiers.org/oryzabase.gene/21327"},{"id":"T8","span":{"begin":170,"end":176},"obj":"http://identifiers.org/oryzabase.gene/21327"},{"id":"T9","span":{"begin":537,"end":543},"obj":"http://identifiers.org/oryzabase.gene/11812"},{"id":"T69809","span":{"begin":0,"end":6},"obj":"http://identifiers.org/rapdb.locus/Os03g0758100"},{"id":"T77106","span":{"begin":118,"end":124},"obj":"http://identifiers.org/rapdb.locus/Os07g0627000"},{"id":"T42104","span":{"begin":170,"end":176},"obj":"http://identifiers.org/rapdb.locus/Os07g0627000"},{"id":"T65292","span":{"begin":537,"end":543},"obj":"http://identifiers.org/rapdb.locus/Os03g0758100"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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_5","span":{"begin":60,"end":65},"obj":"hunflair:NA:Species"},{"id":"M_9","span":{"begin":513,"end":517},"obj":"hunflair:NA:Species"},{"id":"M_14","span":{"begin":118,"end":124},"obj":"hunflair:NA:Gene"},{"id":"M_15","span":{"begin":170,"end":176},"obj":"hunflair:NA:Gene"},{"id":"M_18","span":{"begin":66,"end":80},"obj":"hunflair:NA:Gene"},{"id":"M_21","span":{"begin":0,"end":6},"obj":"hunflair:NA:Gene"},{"id":"M_22","span":{"begin":537,"end":543},"obj":"hunflair:NA:Gene"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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":"T4","span":{"begin":0,"end":6},"obj":"gene"},{"id":"T5","span":{"begin":118,"end":124},"obj":"gene"},{"id":"T6","span":{"begin":537,"end":543},"obj":"gene"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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":"T4","span":{"begin":53,"end":65},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":513,"end":517},"obj":"OrganismTaxon"}],"attributes":[{"id":"A4","pred":"db_id","subj":"T4","obj":"3193"},{"id":"A5","pred":"db_id","subj":"T5","obj":"4530"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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":314,"end":319},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0003655"}],"text":"OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (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"}