Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-170 |
Sentence |
denotes |
Procollagen with skipping of alpha 1(I) exon 41 has lower binding affinity for alpha 1(I) C-telopeptide, impaired in vitro fibrillogenesis, and altered fibril morphology. |
TextSentencer_T2 |
171-432 |
Sentence |
denotes |
Previous in vitro data on type I collagen self-assembly into fibrils suggested that the amino acid 776-796 region of the alpha1(I) chain is crucial for fibril formation because it serves as the recognition site for the telopeptide of a docking collagen monomer. |
TextSentencer_T3 |
433-579 |
Sentence |
denotes |
We used a natural collagen mutation with a deletion of amino acids 766-801 to confirm the importance of this region for collagen fibril formation. |
TextSentencer_T4 |
580-694 |
Sentence |
denotes |
The proband has type III osteogenesis imperfecta and is heterozygous for a COL1A1 IVS 41 A(+4) --> C substitution. |
TextSentencer_T5 |
695-826 |
Sentence |
denotes |
The intronic mutation causes splicing of exon 41, confirmed by sequencing of normal and shorter reverse transcriptase-PCR products. |
TextSentencer_T6 |
827-978 |
Sentence |
denotes |
Reverse transcriptase-PCR using RNA from proband dermal fibroblasts and clonal cell lines showed the mutant cDNA was about 15% of total alpha1(I) cDNA. |
TextSentencer_T7 |
979-1126 |
Sentence |
denotes |
The mutant transcript is translated; structurally abnormal alpha chains are demonstrated in the cell layer of proband fibroblasts by SDS-urea-PAGE. |
TextSentencer_T8 |
1127-1332 |
Sentence |
denotes |
The proportion of mutant chains in the secreted procollagen was determined to be 10% by resistance to digestion with MMP-1, since chains lacking exon 41 are missing the vertebral collagenase cleavage site. |
TextSentencer_T9 |
1333-1458 |
Sentence |
denotes |
Secreted proband collagen was used for analysis of kinetics of binding of alpha1(I) C-telopeptide using an optical biosensor. |
TextSentencer_T10 |
1459-1557 |
Sentence |
denotes |
Telopeptide had slower association and faster dissociation from proband than from normal collagen. |
TextSentencer_T11 |
1558-1622 |
Sentence |
denotes |
Purified proband pC-collagen was used to study fibril formation. |
TextSentencer_T12 |
1623-1699 |
Sentence |
denotes |
The presence of the mutant molecules decreases the rate of fibril formation. |
TextSentencer_T13 |
1700-1883 |
Sentence |
denotes |
The fibrils formed in the presence of 10-15% mutant molecules have strikingly increased length compared with normal collagen, but are well organized, as demonstrated by D-periodicity. |
TextSentencer_T14 |
1884-2120 |
Sentence |
denotes |
These results suggest that some collagen molecules containing the mutant chain are incorporated into fibrils and that the absence of the telopeptide binding region from even a small portion of the monomers interferes with fibril growth. |
TextSentencer_T15 |
2121-2206 |
Sentence |
denotes |
Both abnormal fibrils and slower remodeling may contribute to the severe phenotype.in |
T1 |
0-170 |
Sentence |
denotes |
Procollagen with skipping of alpha 1(I) exon 41 has lower binding affinity for alpha 1(I) C-telopeptide, impaired in vitro fibrillogenesis, and altered fibril morphology. |
T2 |
171-432 |
Sentence |
denotes |
Previous in vitro data on type I collagen self-assembly into fibrils suggested that the amino acid 776-796 region of the alpha1(I) chain is crucial for fibril formation because it serves as the recognition site for the telopeptide of a docking collagen monomer. |
T3 |
433-579 |
Sentence |
denotes |
We used a natural collagen mutation with a deletion of amino acids 766-801 to confirm the importance of this region for collagen fibril formation. |
T4 |
580-694 |
Sentence |
denotes |
The proband has type III osteogenesis imperfecta and is heterozygous for a COL1A1 IVS 41 A(+4) --> C substitution. |
T5 |
695-826 |
Sentence |
denotes |
The intronic mutation causes splicing of exon 41, confirmed by sequencing of normal and shorter reverse transcriptase-PCR products. |
T6 |
827-978 |
Sentence |
denotes |
Reverse transcriptase-PCR using RNA from proband dermal fibroblasts and clonal cell lines showed the mutant cDNA was about 15% of total alpha1(I) cDNA. |
T7 |
979-1126 |
Sentence |
denotes |
The mutant transcript is translated; structurally abnormal alpha chains are demonstrated in the cell layer of proband fibroblasts by SDS-urea-PAGE. |
T8 |
1127-1332 |
Sentence |
denotes |
The proportion of mutant chains in the secreted procollagen was determined to be 10% by resistance to digestion with MMP-1, since chains lacking exon 41 are missing the vertebral collagenase cleavage site. |
T9 |
1333-1458 |
Sentence |
denotes |
Secreted proband collagen was used for analysis of kinetics of binding of alpha1(I) C-telopeptide using an optical biosensor. |
T10 |
1459-1557 |
Sentence |
denotes |
Telopeptide had slower association and faster dissociation from proband than from normal collagen. |
T11 |
1558-1622 |
Sentence |
denotes |
Purified proband pC-collagen was used to study fibril formation. |
T12 |
1623-1699 |
Sentence |
denotes |
The presence of the mutant molecules decreases the rate of fibril formation. |
T13 |
1700-1883 |
Sentence |
denotes |
The fibrils formed in the presence of 10-15% mutant molecules have strikingly increased length compared with normal collagen, but are well organized, as demonstrated by D-periodicity. |
T14 |
1884-2120 |
Sentence |
denotes |
These results suggest that some collagen molecules containing the mutant chain are incorporated into fibrils and that the absence of the telopeptide binding region from even a small portion of the monomers interferes with fibril growth. |
T15 |
2121-2206 |
Sentence |
denotes |
Both abnormal fibrils and slower remodeling may contribute to the severe phenotype.in |