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A tripeptide deletion in the triple-helical domain of the Proα1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase


A tripeptide deletion in the triple-helical domain of the Proα1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase



The Journal of Biological Chemistry 267(35): 25529-25534



ISSN/ISBN: 0021-9258


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Accession: 073839846

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Related references

A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase. Journal of Biological Chemistry 267(35): 25529-25534, 1992

A tripeptide deletion in the triple-helical domain of the proa1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase. The Journal of Biological Chemistry 267: 529-34, 1992

Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase. Journal of Biological Chemistry 269(48): 30352-30357, 1994

Substitution of serine for glycine 883 in the triple helix of the proa1(I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase. The Journal of Biological Chemistry 269: 352-7, 1994

Substitutions for arginine at position 780 in triple helical domain of the α1(I) chain alter folding of the type I procollagen molecule and cause osteogenesis imperfecta. Plos one 13(7): E0200264, 2018

Altered triple helical structure of type I procollagen in lethal perinatal osteogenesis imperfecta. Journal of Biological Chemistry 260(3): 1734-1742, 1985

Structural study of a mutant type I collagen from a patient with lethal osteogenesis imperfecta containing an intramolecular disulfide bond in the triple-helical domain. Febs Letters 198(2): 213-216, 1986

Substitution of arginine for glycine at position 847 in the triple-helical domain of the a1(I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion. The Journal of Biological Chemistry 265: 628-33, 1990

Substitution of arginine for glycine at position 847 in the triple- helical domain of the α1(I) chain of type I collagen produces lethal osteogenesis imperfecta : molecules that contain one or two abnormal chains differ in stability and secretion. The Journal of Biological Chemistry 265(30): 18628-18633, 1990

Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion. Journal of Biological Chemistry 265(30): 18628-18633, 1990

The molecular defect in an autosomal dominant form of osteogenesis imperfecta. Synthesis of type I procollagen containing cysteine in the triple-helical domain of pro-a1(I) chains. The Journal of Biological Chemistry 261: 56-64, 1986

The molecular defect in an autosomal dominant form of osteogenesis imperfecta: synthesis of type I procollagen containing cysteine in the triple-helical domain of pro-α1(I) chains. The Journal of Biological Chemistry 261(19): 9056-9064, 1986

The molecular defect in an autosomal dominant form of osteogenesis imperfecta. Synthesis of type I procollagen containing cysteine in the triple-helical domain of pro-alpha 1(I) chains. Journal of Biological Chemistry 261(19): 9056-9064, 1986

A point mutation in a type I procollagen gene converts glycine 748 of the α1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta. The Journal of Biological Chemistry 262(30): 14737-14744, 1987

A point mutation in a type I procollagen gene converts glycine 748 of the a1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta. The Journal of Biological Chemistry 262: 737-44, 1987