PubMed:8276879 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":73},"obj":"Sentence"},{"id":"T2","span":{"begin":74,"end":162},"obj":"Sentence"},{"id":"T3","span":{"begin":163,"end":364},"obj":"Sentence"},{"id":"T4","span":{"begin":365,"end":483},"obj":"Sentence"},{"id":"T5","span":{"begin":484,"end":679},"obj":"Sentence"},{"id":"T6","span":{"begin":680,"end":944},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":73},"obj":"Sentence"},{"id":"T2","span":{"begin":74,"end":162},"obj":"Sentence"},{"id":"T3","span":{"begin":163,"end":364},"obj":"Sentence"},{"id":"T4","span":{"begin":365,"end":483},"obj":"Sentence"},{"id":"T5","span":{"begin":484,"end":679},"obj":"Sentence"},{"id":"T6","span":{"begin":680,"end":944},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Characterization and crystallization of recombinant human neurotrophin-4.\nNeurotrophin-4 (NT-4) is the most recently discovered member of the neurotrophin family. We have expressed, refolded, and purified recombinant human NT-4 from Escherichia coli and compared it with recombinant human NT-4 secreted into the culture medium of baculovirus-infected insect cells. Both preparations were characterized and determined to be indistinguishable according to several biochemical criteria. Recombinant NT-4 from E. coli was crystallized in a form suitable for x-ray analysis, and characterization of these crystals indicated that NT-4 was present as a dimer within the asymmetric unit. NT-4 was active in promoting the survival of rat TrkB receptor-expressing fibroblasts, but was inactive on embryonic chicken sensory neurons, unlike the other members of the neurotrophin family and in contrast to the reported activities of partially purified NT-4."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":52,"end":57},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":217,"end":222},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":233,"end":249},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":283,"end":288},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":506,"end":513},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":725,"end":728},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"562"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"562"},{"id":"A6","pred":"db_id","subj":"T6","obj":"10114"},{"id":"A7","pred":"db_id","subj":"T6","obj":"10116"}],"text":"Characterization and crystallization of recombinant human neurotrophin-4.\nNeurotrophin-4 (NT-4) is the most recently discovered member of the neurotrophin family. We have expressed, refolded, and purified recombinant human NT-4 from Escherichia coli and compared it with recombinant human NT-4 secreted into the culture medium of baculovirus-infected insect cells. Both preparations were characterized and determined to be indistinguishable according to several biochemical criteria. Recombinant NT-4 from E. coli was crystallized in a form suitable for x-ray analysis, and characterization of these crystals indicated that NT-4 was present as a dimer within the asymmetric unit. NT-4 was active in promoting the survival of rat TrkB receptor-expressing fibroblasts, but was inactive on embryonic chicken sensory neurons, unlike the other members of the neurotrophin family and in contrast to the reported activities of partially purified NT-4."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":754,"end":765},"obj":"Body_part"},{"id":"T2","span":{"begin":805,"end":820},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000101"}],"text":"Characterization and crystallization of recombinant human neurotrophin-4.\nNeurotrophin-4 (NT-4) is the most recently discovered member of the neurotrophin family. We have expressed, refolded, and purified recombinant human NT-4 from Escherichia coli and compared it with recombinant human NT-4 secreted into the culture medium of baculovirus-infected insect cells. Both preparations were characterized and determined to be indistinguishable according to several biochemical criteria. Recombinant NT-4 from E. coli was crystallized in a form suitable for x-ray analysis, and characterization of these crystals indicated that NT-4 was present as a dimer within the asymmetric unit. NT-4 was active in promoting the survival of rat TrkB receptor-expressing fibroblasts, but was inactive on embryonic chicken sensory neurons, unlike the other members of the neurotrophin family and in contrast to the reported activities of partially purified NT-4."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":754,"end":765},"obj":"Cell"},{"id":"T2","span":{"begin":805,"end":820},"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:0000101"}],"text":"Characterization and crystallization of recombinant human neurotrophin-4.\nNeurotrophin-4 (NT-4) is the most recently discovered member of the neurotrophin family. We have expressed, refolded, and purified recombinant human NT-4 from Escherichia coli and compared it with recombinant human NT-4 secreted into the culture medium of baculovirus-infected insect cells. Both preparations were characterized and determined to be indistinguishable according to several biochemical criteria. Recombinant NT-4 from E. coli was crystallized in a form suitable for x-ray analysis, and characterization of these crystals indicated that NT-4 was present as a dimer within the asymmetric unit. NT-4 was active in promoting the survival of rat TrkB receptor-expressing fibroblasts, but was inactive on embryonic chicken sensory neurons, unlike the other members of the neurotrophin family and in contrast to the reported activities of partially purified NT-4."}