PubMed:1988452 / 184-550 JSONTXT

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":9,"end":20},"obj":"Cell"},{"id":"T2","span":{"begin":129,"end":135},"obj":"Cell"},{"id":"T4","span":{"begin":337,"end":343},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000057"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0004120"},{"id":"A3","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0004138"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0004120"},{"id":"A5","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0004138"}],"text":"Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer."}

{"project":"DisGeNET","denotations":[{"id":"T2","span":{"begin":294,"end":301},"obj":"gene:146"},{"id":"T3","span":{"begin":69,"end":92},"obj":"disease:C0029434"},{"id":"T4","span":{"begin":174,"end":181},"obj":"gene:146"},{"id":"T5","span":{"begin":69,"end":92},"obj":"disease:C0029434"}],"relations":[{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"},{"id":"R3","pred":"associated_with","subj":"T4","obj":"T5"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer."}

{"project":"PubCasesORDO","denotations":[{"id":"AB1","span":{"begin":69,"end":92},"obj":"ORDO:666"}],"namespaces":[{"prefix":"ORDO","uri":"http://www.orpha.net/ORDO/Orphanet_"}],"text":"Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T3","span":{"begin":0,"end":366},"obj":"Sentence"},{"id":"T3","span":{"begin":0,"end":366},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer."}

{"project":"mondo_disease","denotations":[{"id":"T2","span":{"begin":69,"end":92},"obj":"Disease"}],"attributes":[{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0019019"}],"text":"Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer."}

{"project":"NCBITAXON","denotations":[{"id":"T2","span":{"begin":28,"end":35},"obj":"OrganismTaxon"}],"attributes":[{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":9,"end":20},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"}],"text":"Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer."}