Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-112 |
Sentence |
denotes |
A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a moderate case of osteogenesis imperfecta. |
TextSentencer_T2 |
113-183 |
Sentence |
denotes |
Substitution of cysteine for glycine 178 in the triple helical domain. |
TextSentencer_T3 |
184-550 |
Sentence |
denotes |
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. |
TextSentencer_T4 |
551-614 |
Sentence |
denotes |
The proband's parents were clinically and biochemically normal. |
TextSentencer_T5 |
615-851 |
Sentence |
denotes |
The cysteine was localized within peptide alpha 1(I)CB8 between residues 170 and 200 of the triple helical domain using a chemical procedure with 2-nitro-5-thiocyanobenzoic acid (Tenni, R., Rossi, A., Valli, M., Mottes, M., Pignatti, P. |
TextSentencer_T6 |
852-895 |
Sentence |
denotes |
F., and Cetta, G. (1990) Matrix 10, 20-26). |
TextSentencer_T7 |
896-1145 |
Sentence |
denotes |
Type I procollagen heterotrimers containing either one or two mutant chains showed (i) a slight abnormality in secretion from cells; (ii) a low degree of post-translational overmodifications; (iii) the same, but lower than normal, thermal stability. |
TextSentencer_T8 |
1146-1277 |
Sentence |
denotes |
Total RNA was isolated from the proband's dermal fibroblast cultures, and cDNAs for pro-alpha 1(I) were prepared d using total RNA. |
TextSentencer_T9 |
1278-1429 |
Sentence |
denotes |
A portion of cDNA, coding for the region encompassing residues 119-193 of alpha 1(I) triple helical domain, was amplified by polymerase chain reaction. |
TextSentencer_T10 |
1430-1614 |
Sentence |
denotes |
A single base pair mismatch was identified by chemical cleavage of DNA.DNA heteroduplexes, indicating a possible substitution of a guanine in the triplet coding for glycine 178 or 181. |
TextSentencer_T11 |
1615-1797 |
Sentence |
denotes |
The same unique mismatch was detected by chemical cleavage in about one-half of the molecules in heteroduplexes formed between patient's pro-alpha 1(I) mRNAs and a normal cDNA probe. |
TextSentencer_T12 |
1798-2150 |
Sentence |
denotes |
The amplified products were cloned and sequenced, confirming the heterozygous nature of the patient and demonstrating the presence and the location of a missense mutation; a single T for G substitution was found in the first base of the triplet coding for residue 178 of alpha 1(I) triple helical domain, leading to a cysteine for glycine substitution. |
TextSentencer_T13 |
2151-2273 |
Sentence |
denotes |
Allele-specific oligonucleotide hybridization to amplified DNA confirmed a de novo point mutation in the proband's genome. |
TextSentencer_T14 |
2274-2465 |
Sentence |
denotes |
The findings in this patient are in accord with the phenotypic gradient model, which correlates the localization of the structural defect with the clinical outcome of osteogenesis imperfecta. |
TextSentencer_T15 |
2466-2671 |
Sentence |
denotes |
The mutant protein has some properties that differ from the caused by the cysteine for glycine 175 substitution, suggesting a direct influence of the neighboring amino acids on the effects of the mutation. |
T1 |
0-112 |
Sentence |
denotes |
A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a moderate case of osteogenesis imperfecta. |
T2 |
113-183 |
Sentence |
denotes |
Substitution of cysteine for glycine 178 in the triple helical domain. |
T3 |
184-550 |
Sentence |
denotes |
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. |
T4 |
551-614 |
Sentence |
denotes |
The proband's parents were clinically and biochemically normal. |
T5 |
615-851 |
Sentence |
denotes |
The cysteine was localized within peptide alpha 1(I)CB8 between residues 170 and 200 of the triple helical domain using a chemical procedure with 2-nitro-5-thiocyanobenzoic acid (Tenni, R., Rossi, A., Valli, M., Mottes, M., Pignatti, P. |
T6 |
852-895 |
Sentence |
denotes |
F., and Cetta, G. (1990) Matrix 10, 20-26). |
T7 |
896-1145 |
Sentence |
denotes |
Type I procollagen heterotrimers containing either one or two mutant chains showed (i) a slight abnormality in secretion from cells; (ii) a low degree of post-translational overmodifications; (iii) the same, but lower than normal, thermal stability. |
T8 |
1146-1277 |
Sentence |
denotes |
Total RNA was isolated from the proband's dermal fibroblast cultures, and cDNAs for pro-alpha 1(I) were prepared d using total RNA. |
T9 |
1278-1429 |
Sentence |
denotes |
A portion of cDNA, coding for the region encompassing residues 119-193 of alpha 1(I) triple helical domain, was amplified by polymerase chain reaction. |
T10 |
1430-1614 |
Sentence |
denotes |
A single base pair mismatch was identified by chemical cleavage of DNA.DNA heteroduplexes, indicating a possible substitution of a guanine in the triplet coding for glycine 178 or 181. |
T11 |
1615-1797 |
Sentence |
denotes |
The same unique mismatch was detected by chemical cleavage in about one-half of the molecules in heteroduplexes formed between patient's pro-alpha 1(I) mRNAs and a normal cDNA probe. |
T12 |
1798-2150 |
Sentence |
denotes |
The amplified products were cloned and sequenced, confirming the heterozygous nature of the patient and demonstrating the presence and the location of a missense mutation; a single T for G substitution was found in the first base of the triplet coding for residue 178 of alpha 1(I) triple helical domain, leading to a cysteine for glycine substitution. |
T13 |
2151-2273 |
Sentence |
denotes |
Allele-specific oligonucleotide hybridization to amplified DNA confirmed a de novo point mutation in the proband's genome. |
T14 |
2274-2465 |
Sentence |
denotes |
The findings in this patient are in accord with the phenotypic gradient model, which correlates the localization of the structural defect with the clinical outcome of osteogenesis imperfecta. |
T15 |
2466-2671 |
Sentence |
denotes |
The mutant protein has some properties that differ from the caused by the cysteine for glycine 175 substitution, suggesting a direct influence of the neighboring amino acids on the effects of the mutation. |