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PubMed:12746442 JSONTXT 28 Projects

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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-88 Sentence denotes Structural (betaalpha)8 TIM barrel model of 3-hydroxy-3-methylglutaryl-coenzyme A lyase.
T1 0-88 Sentence denotes Structural (betaalpha)8 TIM barrel model of 3-hydroxy-3-methylglutaryl-coenzyme A lyase.
TextSentencer_T2 89-335 Sentence denotes This study describes three novel homozygous missense mutations (S75R, S201Y, and D204N) in the 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) lyase gene, which caused 3-hydroxy-3-methylglutaric aciduria in patients from Germany, England, and Argentina.
T2 89-335 Sentence denotes This study describes three novel homozygous missense mutations (S75R, S201Y, and D204N) in the 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) lyase gene, which caused 3-hydroxy-3-methylglutaric aciduria in patients from Germany, England, and Argentina.
TextSentencer_T3 336-531 Sentence denotes Expression studies in Escherichia coli show that S75R and S201Y substitutions completely abolished the HMG-CoA lyase activity, whereas D204N reduced catalytic efficiency to 6.6% of the wild type.
T3 336-531 Sentence denotes Expression studies in Escherichia coli show that S75R and S201Y substitutions completely abolished the HMG-CoA lyase activity, whereas D204N reduced catalytic efficiency to 6.6% of the wild type.
TextSentencer_T4 532-647 Sentence denotes We also propose a three-dimensional model for human HMG-CoA lyase containing a (betaalpha)8 (TIM) barrel structure.
T4 532-647 Sentence denotes We also propose a three-dimensional model for human HMG-CoA lyase containing a (betaalpha)8 (TIM) barrel structure.
TextSentencer_T5 648-924 Sentence denotes The model is supported by the similarity with analogous TIM barrel structures of functionally related proteins, by the localization of catalytic amino acids at the active site, and by the coincidence between the shape of the substrate (HMG-CoA) and the predicted inner cavity.
T5 648-924 Sentence denotes The model is supported by the similarity with analogous TIM barrel structures of functionally related proteins, by the localization of catalytic amino acids at the active site, and by the coincidence between the shape of the substrate (HMG-CoA) and the predicted inner cavity.
TextSentencer_T6 925-1210 Sentence denotes 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.
T6 925-1210 Sentence denotes 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.
TextSentencer_T7 1211-1375 Sentence denotes We also report the localization of all missense mutations reported to date and show that these mutations are located in the beta-sheets around the substrate cavity.
T7 1211-1375 Sentence denotes We also report the localization of all missense mutations reported to date and show that these mutations are located in the beta-sheets around the substrate cavity.