Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-172 |
Sentence |
denotes |
Clinical variability of osteogenesis imperfecta reflecting molecular heterogeneity: cysteine substitutions in the alpha 1(I) collagen chain producing lethal and mild forms. |
TextSentencer_T2 |
173-360 |
Sentence |
denotes |
We have examined the collagenous proteins extracted from skin and produced by skin fibroblast cultures from the members of a family with mild dominant osteogenesis imperfecta (OI type I). |
TextSentencer_T3 |
361-558 |
Sentence |
denotes |
The two affected patients, mother and son, produce two populations of alpha 1(I) chains of type I collagen, one chain being normal, the other containing a cysteine within the triple-helical domain. |
TextSentencer_T4 |
559-645 |
Sentence |
denotes |
Both forms can be incorporated into triple-helical molecules with an alpha 2(I) chain. |
TextSentencer_T5 |
646-757 |
Sentence |
denotes |
When two mutant alpha (I) chains are incorporated into the same molecule, a disulfide bonded dimer is produced. |
TextSentencer_T6 |
758-929 |
Sentence |
denotes |
We have characterized these chains by sodium dodecyl sulfate-gel electrophoresis and CNBr-peptide mapping and by measuring a number of biosynthetic and physical variables. |
TextSentencer_T7 |
930-1000 |
Sentence |
denotes |
The cysteine was localized to the COOH-terminal peptide alpha (I) CB6. |
TextSentencer_T8 |
1001-1221 |
Sentence |
denotes |
Molecules containing the mutant chains are stable, have a normal denaturation temperature, are secreted normally, and have normal levels of post-translational modification of lysyl residues and intracellular degradation. |
TextSentencer_T9 |
1222-1422 |
Sentence |
denotes |
We have compared and contrasted these observations with those made in a patient with lethal osteogenesis imperfecta in which there was a cysteine substitution in alpha 1(I) CB6 (Steinmann, B., Rao, V. |
TextSentencer_T10 |
1423-1481 |
Sentence |
denotes |
H., Vogel, A., Bruckner, P., Gitzelmann, R., and Byers, P. |
TextSentencer_T11 |
1482-1494 |
Sentence |
denotes |
H. (1984) J. |
TextSentencer_T12 |
1495-1500 |
Sentence |
denotes |
Biol. |
TextSentencer_T13 |
1501-1725 |
Sentence |
denotes |
Chem 259, 11129-11138) and have concluded that the mutation in the present family occurs in the X or Y position of a Gly-X-Y repeating unit of collagen and not in the glycine position shown for the previous patient (Cohn, D. |
TextSentencer_T14 |
1726-1739 |
Sentence |
denotes |
H., Byers, P. |
TextSentencer_T15 |
1740-1773 |
Sentence |
denotes |
H., Steinmann, B, and Gelinas, R. |
TextSentencer_T16 |
1774-1789 |
Sentence |
denotes |
E. (1986) Proc. |
TextSentencer_T17 |
1790-1795 |
Sentence |
denotes |
Natl. |
TextSentencer_T18 |
1796-1801 |
Sentence |
denotes |
Acad. |
TextSentencer_T19 |
1802-1806 |
Sentence |
denotes |
Sci. |
TextSentencer_T20 |
1807-1809 |
Sentence |
denotes |
U. |
TextSentencer_T21 |
1810-1812 |
Sentence |
denotes |
S. |
TextSentencer_T22 |
1813-1826 |
Sentence |
denotes |
A., in press. |
T1 |
0-172 |
Sentence |
denotes |
Clinical variability of osteogenesis imperfecta reflecting molecular heterogeneity: cysteine substitutions in the alpha 1(I) collagen chain producing lethal and mild forms. |
T2 |
173-360 |
Sentence |
denotes |
We have examined the collagenous proteins extracted from skin and produced by skin fibroblast cultures from the members of a family with mild dominant osteogenesis imperfecta (OI type I). |
T3 |
361-558 |
Sentence |
denotes |
The two affected patients, mother and son, produce two populations of alpha 1(I) chains of type I collagen, one chain being normal, the other containing a cysteine within the triple-helical domain. |
T4 |
559-645 |
Sentence |
denotes |
Both forms can be incorporated into triple-helical molecules with an alpha 2(I) chain. |
T5 |
646-757 |
Sentence |
denotes |
When two mutant alpha (I) chains are incorporated into the same molecule, a disulfide bonded dimer is produced. |
T6 |
758-929 |
Sentence |
denotes |
We have characterized these chains by sodium dodecyl sulfate-gel electrophoresis and CNBr-peptide mapping and by measuring a number of biosynthetic and physical variables. |
T7 |
930-1000 |
Sentence |
denotes |
The cysteine was localized to the COOH-terminal peptide alpha (I) CB6. |
T8 |
1001-1221 |
Sentence |
denotes |
Molecules containing the mutant chains are stable, have a normal denaturation temperature, are secreted normally, and have normal levels of post-translational modification of lysyl residues and intracellular degradation. |
T9 |
1222-1422 |
Sentence |
denotes |
We have compared and contrasted these observations with those made in a patient with lethal osteogenesis imperfecta in which there was a cysteine substitution in alpha 1(I) CB6 (Steinmann, B., Rao, V. |
T10 |
1423-1481 |
Sentence |
denotes |
H., Vogel, A., Bruckner, P., Gitzelmann, R., and Byers, P. |
T11 |
1482-1494 |
Sentence |
denotes |
H. (1984) J. |
T12 |
1495-1500 |
Sentence |
denotes |
Biol. |
T13 |
1501-1725 |
Sentence |
denotes |
Chem 259, 11129-11138) and have concluded that the mutation in the present family occurs in the X or Y position of a Gly-X-Y repeating unit of collagen and not in the glycine position shown for the previous patient (Cohn, D. |
T14 |
1726-1739 |
Sentence |
denotes |
H., Byers, P. |
T15 |
1740-1773 |
Sentence |
denotes |
H., Steinmann, B, and Gelinas, R. |
T16 |
1774-1789 |
Sentence |
denotes |
E. (1986) Proc. |
T17 |
1790-1795 |
Sentence |
denotes |
Natl. |
T18 |
1796-1801 |
Sentence |
denotes |
Acad. |
T19 |
1802-1806 |
Sentence |
denotes |
Sci. |
T20 |
1807-1809 |
Sentence |
denotes |
U. |
T21 |
1810-1812 |
Sentence |
denotes |
S. |
T22 |
1813-1826 |
Sentence |
denotes |
A., in press. |