PubMed:2511192 / 811-1056 JSONTXT

{"project":"CL-cell","denotations":[{"id":"T8","span":{"begin":36,"end":42},"obj":"Cell"}],"attributes":[{"id":"A8","pred":"cl_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CL:0004120"},{"id":"A9","pred":"cl_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CL:0004138"}],"text":"The thermal stability of the intact type I collagen was normal as assayed by protease digestion under conditions in which a decrease in thermal stability was previously observed with eight other substitutions for glycine in the alpha 1(I) chain."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T5","span":{"begin":0,"end":245},"obj":"Sentence"},{"id":"T5","span":{"begin":0,"end":245},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The thermal stability of the intact type I collagen was normal as assayed by protease digestion under conditions in which a decrease in thermal stability was previously observed with eight other substitutions for glycine in the alpha 1(I) chain."}

{"project":"NCBITAXON","denotations":[{"id":"T4","span":{"begin":213,"end":220},"obj":"OrganismTaxon"}],"attributes":[{"id":"A4","pred":"db_id","subj":"T4","obj":"3846"}],"text":"The thermal stability of the intact type I collagen was normal as assayed by protease digestion under conditions in which a decrease in thermal stability was previously observed with eight other substitutions for glycine in the alpha 1(I) chain."}