Browsing by Author "Prockop, D. J."
Now showing items 1-17 of 17
-
Article
Expression of type I procollagen genes.
Prockop, D. J.; Kadler, K. E.; Hojima, Y.; Constantinou-Deltas, Constantinos D.; Dombrowski, K. E.; Kuivaniemi, H.; Tromp, G.; Vogel, B. (1988)All of the type I collagen in connective tissue is the product of one structural gene for the pro alpha 1(I) chain and another for the pro alpha 2(I) chain of type I procollagen. An intriguing question therefore is how the ...
-
Article
G to A polymorphism in exon 45 of the COL1A1 gene
Sokolov, B. P.; Constantinou-Deltas, Constantinos D.; Tsuneyoshi, T.; Zhuang, J.; Prockop, D. J. (1991)
-
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
Pvull polymorphism at the COL1A2 locus
Constantinou-Deltas, Constantinos D.; Spotila, L. D.; Zhuang, J.; Sereda, L.; Hanning, C.; Prockop, D. J. (1990)
-
Article
A sequence polymorphism in the 3′-nontranslated region of the proα1 chain of type I procollagen
Westerhausen, A. I.; Constantinou-Deltas, Constantinos D.; Prockop, D. J. (1990)
-
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
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 ...