Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-104 |
Sentence |
denotes |
An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II) chain produces hypochondrogenesis. |
T1 |
0-104 |
Sentence |
denotes |
An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II) chain produces hypochondrogenesis. |
TextSentencer_T2 |
105-264 |
Sentence |
denotes |
The spondyloepiphyseal dysplasia subclassification of bone dysplasias includes achondrogenesis, hypochondrogenesis, and spondyloepiphyseal dysplasia congenita. |
T2 |
105-264 |
Sentence |
denotes |
The spondyloepiphyseal dysplasia subclassification of bone dysplasias includes achondrogenesis, hypochondrogenesis, and spondyloepiphyseal dysplasia congenita. |
TextSentencer_T3 |
265-353 |
Sentence |
denotes |
The phenotypic expression of these disorders ranges from mild to perinatal lethal forms. |
T3 |
265-353 |
Sentence |
denotes |
The phenotypic expression of these disorders ranges from mild to perinatal lethal forms. |
TextSentencer_T4 |
354-488 |
Sentence |
denotes |
We report the detection and partial characterization of a defect in type II collagen in a perinatal lethal form of hypochondrogenesis. |
T4 |
354-488 |
Sentence |
denotes |
We report the detection and partial characterization of a defect in type II collagen in a perinatal lethal form of hypochondrogenesis. |
TextSentencer_T5 |
489-839 |
Sentence |
denotes |
Electrophoresis in sodium dodecyl sulfate-polyacrylamide of CB peptides (where CB represents cyanogen bromide) from type II collagen of the diseased cartilage showed a doublet band for peptide alpha 1(II)CB10 and evidence for post-translational overmodification of the major peptides (CB8, CB10, and CB11) seen as a retarded electrophoretic mobility. |
T5 |
489-839 |
Sentence |
denotes |
Electrophoresis in sodium dodecyl sulfate-polyacrylamide of CB peptides (where CB represents cyanogen bromide) from type II collagen of the diseased cartilage showed a doublet band for peptide alpha 1(II)CB10 and evidence for post-translational overmodification of the major peptides (CB8, CB10, and CB11) seen as a retarded electrophoretic mobility. |
TextSentencer_T6 |
840-991 |
Sentence |
denotes |
Peptide CB10 was digested by endoproteinase Asp-N; and on reverse-phase high pressure liquid chromatography, fragments of abnormal mobility were noted. |
T6 |
840-991 |
Sentence |
denotes |
Peptide CB10 was digested by endoproteinase Asp-N; and on reverse-phase high pressure liquid chromatography, fragments of abnormal mobility were noted. |
TextSentencer_T7 |
992-1133 |
Sentence |
denotes |
Sequence analysis of a unique peptide D12 revealed a single amino acid substitution (Gly-->Glu) at position 853 of the triple helical domain. |
T7 |
992-1133 |
Sentence |
denotes |
Sequence analysis of a unique peptide D12 revealed a single amino acid substitution (Gly-->Glu) at position 853 of the triple helical domain. |
TextSentencer_T8 |
1134-1278 |
Sentence |
denotes |
This was confirmed by sequence analysis of amplified COL2A1 cDNA, which revealed a single nucleotide substitution (GGA-->GAA) in 5 of 10 clones. |
T8 |
1134-1278 |
Sentence |
denotes |
This was confirmed by sequence analysis of amplified COL2A1 cDNA, which revealed a single nucleotide substitution (GGA-->GAA) in 5 of 10 clones. |
TextSentencer_T9 |
1279-1498 |
Sentence |
denotes |
Electron micrographs of the diseased cartilage showed a sparse extracellular matrix and chondrocytes containing dilated rough endoplasmic reticulum, which suggested impaired assembly and secretion of the mutant protein. |
T9 |
1279-1498 |
Sentence |
denotes |
Electron micrographs of the diseased cartilage showed a sparse extracellular matrix and chondrocytes containing dilated rough endoplasmic reticulum, which suggested impaired assembly and secretion of the mutant protein. |
TextSentencer_T10 |
1499-1636 |
Sentence |
denotes |
This case further documents the molecular basis of the spondyloepiphyseal dysplasia spectrum of chondrodysplasias as mutations in COL2A1. |
T10 |
1499-1636 |
Sentence |
denotes |
This case further documents the molecular basis of the spondyloepiphyseal dysplasia spectrum of chondrodysplasias as mutations in COL2A1. |