PubMed:12746442 / 925-1210 JSONTXT

{"project":"PubTator4TogoVar","denotations":[{"id":"12746442_2","span":{"begin":112,"end":116},"obj":"ProteinMutation"}],"attributes":[{"id":"12746442_2_ProteinMutation","pred":"proteinmutation","subj":"12746442_2","obj":"rs1357942068"}],"text":"The three novel mutations explain the lack of HMG-CoA lyase activity on the basis of the proposed structure: in S75R and S201Y because the new amino acid residues occlude the substrate cavity, and in D204N because the mutation alters the electrochemical environment of the active site."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T6","span":{"begin":0,"end":285},"obj":"Sentence"},{"id":"T6","span":{"begin":0,"end":285},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The three novel mutations explain the lack of HMG-CoA lyase activity on the basis of the proposed structure: in S75R and S201Y because the new amino acid residues occlude the substrate cavity, and in D204N because the mutation alters the electrochemical environment of the active site."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T2","span":{"begin":185,"end":191},"obj":"Body_part"}],"attributes":[{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002553"}],"text":"The three novel mutations explain the lack of HMG-CoA lyase activity on the basis of the proposed structure: in S75R and S201Y because the new amino acid residues occlude the substrate cavity, and in D204N because the mutation alters the electrochemical environment of the active site."}