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C D Constantinou

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Matrix (Stuttgart, Germany)|February 1, 1991
Structure of cDNAs encoding the triple-helical domain of murine alpha 2 (VI) collagen chain and comparison to human and chick homologues. Use of polymerase chain reaction and partially degenerate oligonucleotide for generation of novel cDNA clonesC D Constantinou, S A Jimenez
Nucleic Acids Research|August 25, 1990
A sequence polymorphism in the 3'-nontranslated region of the pro alpha 1 chain of type I procollagenA I Westerhausen, C D Constantinou, D J Prockop
The Journal of Clinical Investigation|February 1, 1989
A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagenC D Constantinou, K B Nielsen, D J Prockop
Advances in Human Genetics|January 1, 1990
Mutations in type I procollagen genes that cause osteogenesis imperfectaD J Prockop, C T Baldwin, C D Constantinou
American Journal of Medical Genetics|January 15, 1993
Somatic cell mosaicism: another source of phenotypic heterogeneity in nuclear families with osteogenesis imperfectaC D Constantinou-Deltas, R L Ladda, D J Prockop
The Journal of Biological Chemistry|August 25, 1991
Substitutions for glycine alpha 1-637 and glycine alpha 2-694 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 helixT Tsuneyoshi, A Westerhausen, C D Constantinou, et al.
American Journal of Human Genetics|June 1, 1991
A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 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 PCRJ P Zhuang, C D Constantinou, A Ganguly, et al.
American Journal of Human Genetics|October 1, 1990
Phenotypic heterogeneity in osteogenesis imperfecta: the mildly affected mother of a proband with a lethal variant has the same mutation substituting cysteine for alpha 1-glycine 904 in a type I procollagen gene (COL1A1)C D Constantinou, M Pack, S B Young, et al.
Human Mutation|January 1, 1992
delta F508 cystic fibrosis mutation appears very infrequently in the Greek-Cypriot community of CyprusC D Constantinou-Deltas, C Georgiou, P Ioannou, et al.
The Journal of Biological Chemistry|February 15, 1989
A single base mutation that converts glycine 907 of the alpha 2(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 helixC T Baldwin, C D Constantinou, K W Dumars, et al.
Pageof 3

Showing results (1-10 of 30) with videos related to

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Pageof 3
Matrix (Stuttgart, Germany)|February 1, 1991
Structure of cDNAs encoding the triple-helical domain of murine alpha 2 (VI) collagen chain and comparison to human and chick homologues. Use of polymerase chain reaction and partially degenerate oligonucleotide for generation of novel cDNA clonesC D Constantinou, S A Jimenez
Nucleic Acids Research|August 25, 1990
A sequence polymorphism in the 3'-nontranslated region of the pro alpha 1 chain of type I procollagenA I Westerhausen, C D Constantinou, D J Prockop
The Journal of Clinical Investigation|February 1, 1989
A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagenC D Constantinou, K B Nielsen, D J Prockop
Advances in Human Genetics|January 1, 1990
Mutations in type I procollagen genes that cause osteogenesis imperfectaD J Prockop, C T Baldwin, C D Constantinou
American Journal of Medical Genetics|January 15, 1993
Somatic cell mosaicism: another source of phenotypic heterogeneity in nuclear families with osteogenesis imperfectaC D Constantinou-Deltas, R L Ladda, D J Prockop
The Journal of Biological Chemistry|August 25, 1991
Substitutions for glycine alpha 1-637 and glycine alpha 2-694 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 helixT Tsuneyoshi, A Westerhausen, C D Constantinou, et al.
American Journal of Human Genetics|June 1, 1991
A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 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 PCRJ P Zhuang, C D Constantinou, A Ganguly, et al.
American Journal of Human Genetics|October 1, 1990
Phenotypic heterogeneity in osteogenesis imperfecta: the mildly affected mother of a proband with a lethal variant has the same mutation substituting cysteine for alpha 1-glycine 904 in a type I procollagen gene (COL1A1)C D Constantinou, M Pack, S B Young, et al.
Human Mutation|January 1, 1992
delta F508 cystic fibrosis mutation appears very infrequently in the Greek-Cypriot community of CyprusC D Constantinou-Deltas, C Georgiou, P Ioannou, et al.
The Journal of Biological Chemistry|February 15, 1989
A single base mutation that converts glycine 907 of the alpha 2(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 helixC T Baldwin, C D Constantinou, K W Dumars, et al.
Pageof 3