Browsing by Subject "osteogenesis imperfecta"

Now showing items 1-17 of 17

Article

The A and B fragments of normal type I procollagen have a similar thermal stability to proteinase digestion but are selectively destabilized by structural mutations

Constantinou-Deltas, Constantinos D.; VOGEL, B. E.; JEFFREY, J. J.; PROCKOP, D. J. (1987)

Previous studies demonstrated that the thermal stability of the procollagen triple helix can be assayed by digesting the protein for short periods with high concentrations of trypsin and chymotrypsin. Here we cleaved human ...
Article

A base substitution at IVS-19 3′-end splice junction causes exon 20 skipping in proα2(I) collagen mRNA and produces mild osteogenesis imperfecta

Mottes, M.; Sangalli, A.; Valli, M.; Forlino, A.; Gomez-Lira, M.; Antoniazzi, F.; Constantinou-Deltas, Constantinos D.; Cetta, G.; Pignatti, P. F. (1994)

Molecular investigations on a young patient and her family were undertaken to identify the molecular defect responsible for a mild form of osteogenesis imperfecta (OI) with blue sclerae, dentinogenesis imperfecta and joint ...
Article

DNA variant databases improve test accuracy and phenotype prediction in Alport syndrome

Savige, J.; Ars, E.; Cotton, R. G. H.; Crockett, D.; Dagher, H.; Constantinou-Deltas, Constantinos D.; Ding, J.; Flinter, F.; Pont-Kingdon, G.; Smaoui, N.; Torra, R.; Storey, H. (2014)

X-linked Alport syndrome is a form of progressive renal failure caused by pathogenic variants in the COL4A5 gene. More than 700 variants have been described and a further 400 are estimated to be known to individual ...
Article

A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the α1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen

Constantinou-Deltas, Constantinos D.; Nielsen, K. B.; Prockop, D. J. (1989)

A fraction of the proα1(I) and proα2(I) chains in type I procollagen synthesized by the fibroblasts from a proband with a lethal variant of osteogenesis imperfecta were overmodified by posttranslational reactions. After ...
Article

Mutation analysis of coding sequences for type I procollagen in individuals with low bone density

Spotila, L. D.; Colige, A.; Sereda, L.; Constantinou-Deltas, Constantinos D.; Whyte, M. P.; Riggs, L. B.; Shaker, J. L.; Spector, T. D.; Hume, E.; Olsen, N.; Attie, M.; Tenenhouse, A.; Shane, E.; Briney, W.; Prockop, D. J. (1994)

Mutations in one of the two genes encoding type I procollagen (COL1A1 and COL1A2) are frequently the cause of osteogenesis imperfecta (OI), a disorder characterized by brittle bones. Here we tested whether patients with ...
Article

Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: Evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta

Spotila, L. D.; Constantinou-Deltas, Constantinos D.; Sereda, L.; Ganguly, A.; Riggs, B. L.; Prockop, D. J. (1991)

Mutations in the two genes for type I collagen (COL1A1 or COL1A2) cause osteogenesis imperfecta (OI), a heritable disease characterized by moderate to extreme brittleness of bone early in life. Here we show that a 52-year-old ...
Article

Mutations in type I procollagen genes that cause osteogenesis imperfecta

Prockop, D. J.; Baldwin, C. T.; Constantinou-Deltas, Constantinos D. (1990)
Article

Phenotypic heterogeneity in osteogenesis imperfecta: The mildly affected mother of a proband with a lethal variant has the same mutation substituting cysteine for α1-glycine 904 in a type I procollagen gene (COL1A1)

Constantinou-Deltas, Constantinos D.; Pack, M. A.; Young, S. B.; Prockop, D. J. (1990)

A proband with a lethal variant of osteogenesis imperfecta (OI) has been shown to have, in one allele in a gene for type I procollagen (COL1A1), a single base mutation that converted the codon for α1-glycine 904 to a codon ...
Article

A single base mutation in type I procollagen (COL1A1) that converts glycine α1-541 to aspartate in a lethal variant of osteogenesis imperfecta: Detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR

Zhuang, J.; Constantinou-Deltas, Constantinos D.; Ganguly, A.; Prockop, D. J. (1991)

Skin fibroblasts from a proband with a lethal variant of osteogenesis imperfecta synthesized both apparently normal type I procollagen and a type I procollagen that had slow electrophoretic mobility because of posttranslational ...
Article

A single base mutation that converts glycine 907 of the α2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix

Baldwin, C. T.; Constantinou-Deltas, Constantinos D.; Dumars, K. W.; Prockop, D. J. (1989)

Type I procollagen was examined in cultured skin fibroblasts from a patient with a lethal variant of osteogenesis imperfecta. About half of the pro-α chains were post-translationally overmodified and had a decreased thermal ...
Article

Somatic cell mosaicism: Another source of phenotypic heterogeneity in nuclear families with osteogenesis imperfecta

Constantinou-Deltas, Constantinos D.; Ladda, R. L.; Prockop, D. J. (1993)

Mutations in the genes coding for the proα1 and proα2 chains of type I procollagen have been found in many patients with osteogenesis imperfecta (OI), a heritable disorder of connective tissue. The severity of the disease ...
Article

The substitution of arginine for glycine 85 of the α1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen

Deak, S. B.; Scholz, P. M.; Amenta, P. S.; Constantinou-Deltas, Constantinos D.; Levi-Minzi, S. A.; Gonzalez-Lavin, L.; Mackenzie, J. W. (1991)

We report a case of mild osteogenesis imperfecta in a 56-year-old male undergoing aortic valve replacement surgery. The primary defect in this patient was the substitution of arginine for glycine 85 in one of the two chains ...
Article

A Substitution of Cysteine for Glycine 904 in COL1A1 in a Proband with Lethal Osteogenesis Imperfecta and in Her Asymptomatic Mother

Constantinou-Deltas, Constantinos D.; Pack, M. A.; Young, S. B.; Prockop, D. J. (1990)
Article

Substitution of cysteine for glycine-α1-691 in the proα1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution

Steinmann, B.; Westerhausen, A.; Constantinou-Deltas, Constantinos D.; Superti-Furga, A.; Prockop, D. J. (1991)

Skin fibroblast from a proband with lethal osteogenesis imperfecta synthesized a type I procollagen containing a cysteine residue in the α1(I) helical domain. Assay of thermal stability of the triple helix by proteinase ...
Article

Substitution of serine for α1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position or amino acid specific

Pack, M. A.; Constantinou-Deltas, Constantinos D.; Kalia, K.; Nielsen, K. B.; Prockop, D. J. (1989)

Recent reports have demonstrated that a series of probands with severe osteogenesis imperfecta had single base mutations in one of the two structural genes for type I procollagen that substituted amino acids with bulkier ...
Article

Substitutions for glycine α1-637 and glycine α2-694 of type I procollagen in lethal osteogenesis imperfecta: The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix

Tsuneyoshi, T.; Westerhausen, A.; Constantinou-Deltas, Constantinos D.; Prockop, D. J. (1991)

Two substitutions for glycine in the triple-helical domain were found in type I procollagen synthesized by skin fibroblasts from two probands with lethal osteogenesis imperfecta. One was a substitution of valine for glycine ...
Article

Type I procollagen: The gene-protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissue

Prockop, D. J.; Constantinou-Deltas, Constantinos D.; Dombrowski, K. E.; Hojima, Y.; Kadler, K. E.; Kuivaniemi, H.; Tromp, G.; Vogel, B. E. (1989)

Recent data from several laboratories have established that most variants of osteogenesis imperfecta (OI) are caused by mutations in the 2 structural genes for type I procollagen. There are 2 general reasons for the large ...

Browsing by Subject "osteogenesis imperfecta"

The A and B fragments of normal type I procollagen have a similar thermal stability to proteinase digestion but are selectively destabilized by structural mutations ﻿

A base substitution at IVS-19 3′-end splice junction causes exon 20 skipping in proα2(I) collagen mRNA and produces mild osteogenesis imperfecta ﻿

DNA variant databases improve test accuracy and phenotype prediction in Alport syndrome ﻿

A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the α1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen ﻿

Mutation analysis of coding sequences for type I procollagen in individuals with low bone density ﻿

Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: Evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta ﻿

Mutations in type I procollagen genes that cause osteogenesis imperfecta ﻿

Phenotypic heterogeneity in osteogenesis imperfecta: The mildly affected mother of a proband with a lethal variant has the same mutation substituting cysteine for α1-glycine 904 in a type I procollagen gene (COL1A1) ﻿

A single base mutation in type I procollagen (COL1A1) that converts glycine α1-541 to aspartate in a lethal variant of osteogenesis imperfecta: Detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR ﻿

A single base mutation that converts glycine 907 of the α2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix ﻿

Somatic cell mosaicism: Another source of phenotypic heterogeneity in nuclear families with osteogenesis imperfecta ﻿

The substitution of arginine for glycine 85 of the α1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen ﻿

A Substitution of Cysteine for Glycine 904 in COL1A1 in a Proband with Lethal Osteogenesis Imperfecta and in Her Asymptomatic Mother ﻿

Substitution of cysteine for glycine-α1-691 in the proα1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution ﻿

Substitution of serine for α1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position or amino acid specific ﻿

Substitutions for glycine α1-637 and glycine α2-694 of type I procollagen in lethal osteogenesis imperfecta: The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix ﻿

Type I procollagen: The gene-protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissue ﻿

The A and B fragments of normal type I procollagen have a similar thermal stability to proteinase digestion but are selectively destabilized by structural mutations

A base substitution at IVS-19 3′-end splice junction causes exon 20 skipping in proα2(I) collagen mRNA and produces mild osteogenesis imperfecta

DNA variant databases improve test accuracy and phenotype prediction in Alport syndrome

A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the α1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen

Mutation analysis of coding sequences for type I procollagen in individuals with low bone density

Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: Evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta

Mutations in type I procollagen genes that cause osteogenesis imperfecta

Phenotypic heterogeneity in osteogenesis imperfecta: The mildly affected mother of a proband with a lethal variant has the same mutation substituting cysteine for α1-glycine 904 in a type I procollagen gene (COL1A1)

A single base mutation in type I procollagen (COL1A1) that converts glycine α1-541 to aspartate in a lethal variant of osteogenesis imperfecta: Detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR

A single base mutation that converts glycine 907 of the α2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix

Somatic cell mosaicism: Another source of phenotypic heterogeneity in nuclear families with osteogenesis imperfecta

The substitution of arginine for glycine 85 of the α1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen

A Substitution of Cysteine for Glycine 904 in COL1A1 in a Proband with Lethal Osteogenesis Imperfecta and in Her Asymptomatic Mother

Substitution of cysteine for glycine-α1-691 in the proα1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution

Substitution of serine for α1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position or amino acid specific

Substitutions for glycine α1-637 and glycine α2-694 of type I procollagen in lethal osteogenesis imperfecta: The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix

Type I procollagen: The gene-protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissue