Browsing by Subject "glycine"

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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

Model investigations for vanadium-protein interactions: Vanadium(III) compounds with dipeptides and their oxovanadium(IV) analogues

Tasiopoulos, Anastasios J.; Tolis, Evangelos I.; Tsangaris, John Michael; Evangelou, Angelos M.; Woollins, J. D.; Slawin, A. M. Z.; Pessoa, J. C.; Correia, I.; Kabanos, Themistoklis A. (2002)

The reaction of VCl3 with 1,10-phenanthroline and a series of dipeptides (H2dip), having aliphatic as well as aromatic side chains, in methyl alcohol and in the presence of triethylamine affords vanadium(III) compounds of ...
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

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 ...

Browsing by Subject "glycine"

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 ﻿

Model investigations for vanadium-protein interactions: Vanadium(III) compounds with dipeptides and their oxovanadium(IV) analogues ﻿

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 ﻿

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 ﻿

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

Model investigations for vanadium-protein interactions: Vanadium(III) compounds with dipeptides and their oxovanadium(IV) analogues

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

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