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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 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




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Related references

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

Osteogenesis imperfecta. The position of substitution for glycine by cysteine in the triple helical domain of the pro alpha 1(I) chains of type I collagen determines the clinical phenotype. Journal of Clinical Investigation 84(4): 1206-1214, 1989

Osteogenesis imperfecta: the position of substitution for glycine by cysteine in the triple helical domain of the proα1(I) chains of type I collagen determines the clinical phenotype. The Journal of Clinical Investigation 84(4): 1206-1214, 1989

Cysteine in the triple-helical domain of one allelic product of the α1(I) gene of type I collagen produces a lethal form of osteogenesis imperfecta. The Journal of Biological Chemistry 259(17): 11129-11138, 1984

Cysteine in the triple-helical domain of one allelic product of the a1(I) gene of type I collagen produces a lethal form of osteogenesis imperfecta. The Journal of Biological Chemistry 259: 129-38, 1984

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The molecular defect in a nonlethal variant of osteogenesis imperfecta: synthesis of pro-a2(I) chains which are not incorporated into trimers of type I procollagen. The Journal of Biological Chemistry 258: 7, 1983

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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

Restriction fragment length polymorphism associated with the pro alpha 2(I) gene of human type I procollagen. Application to a family with an autosomal dominant form of osteogenesis imperfecta. Journal of Clinical Investigation 72(4): 1262-1267, 1983

Restriction fragment length polymorphism associated with the proα2(I) gene of human type I procollagen: application to a family with an autosomal dominant form of osteogenesis imperfecta. The Journal of Clinical Investigation 72(4): 1262-1267, 1983

Cysteine in the triple helical domain of the pro alpha 2(I) chain of type-I collagen in nonlethal forms of osteogenesis imperfecta. Human Genetics 87(2): 167-172, 1991

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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