PubMed:22270369 / 901-1180 JSONTXT

{"project":"sentences","denotations":[{"id":"T6","span":{"begin":0,"end":279},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":68,"end":72},"obj":"http://purl.obolibrary.org/obo/MAT_0000135"},{"id":"T2","span":{"begin":77,"end":83},"obj":"http://purl.obolibrary.org/obo/MAT_0000132"},{"id":"T3","span":{"begin":174,"end":178},"obj":"http://purl.obolibrary.org/obo/MAT_0000135"},{"id":"T4","span":{"begin":183,"end":189},"obj":"http://purl.obolibrary.org/obo/MAT_0000132"}],"text":"Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":68,"end":72},"obj":"Body_part"},{"id":"T2","span":{"begin":77,"end":83},"obj":"Body_part"},{"id":"T3","span":{"begin":174,"end":178},"obj":"Body_part"},{"id":"T4","span":{"begin":183,"end":189},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000135"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000132"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000135"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000132"}],"text":"Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T5","span":{"begin":68,"end":72},"obj":"Body_part"},{"id":"T6","span":{"begin":77,"end":83},"obj":"Body_part"},{"id":"T7","span":{"begin":174,"end":178},"obj":"Body_part"},{"id":"T8","span":{"begin":183,"end":189},"obj":"Body_part"}],"attributes":[{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000473"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000473"}],"text":"Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":68,"end":72},"obj":"Body_part"},{"id":"T2","span":{"begin":77,"end":83},"obj":"Body_part"},{"id":"T3","span":{"begin":174,"end":178},"obj":"Body_part"},{"id":"T4","span":{"begin":183,"end":189},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000135"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000132"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000135"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000132"}],"text":"Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity."}

{"project":"sentences","denotations":[{"id":"T6","span":{"begin":0,"end":279},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T6","span":{"begin":0,"end":279},"obj":"Sentence"}],"text":"Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T5","span":{"begin":68,"end":72},"obj":"Body_part"},{"id":"T6","span":{"begin":77,"end":83},"obj":"Body_part"},{"id":"T7","span":{"begin":174,"end":178},"obj":"Body_part"},{"id":"T8","span":{"begin":183,"end":189},"obj":"Body_part"}],"attributes":[{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000473"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000473"}],"text":"Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity."}