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Synthesis and processing of a type I procollagen containing shortened pro-a1(I) chains by fibroblasts from a patient with osteogenesis imperfecta


Synthesis and processing of a type I procollagen containing shortened pro-a1(I) chains by fibroblasts from a patient with osteogenesis imperfecta



The Journal of Biological Chemistry 258: 15-21




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Accession: 018141471

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Related references

Synthesis and processing of a type I procollagen containing shortened pro-alpha 1(I) chains by fibroblasts from a patient with osteogenesis imperfecta. Journal of Biological Chemistry 258(9): 5915-5921, 1983

The mRNAs for the pro-a1(I) and pro-a2(I) chains of type I procollagen are translated at the same rate in normal human fibroblasts and in fibroblasts from two variants of osteogenesis imperfecta with altered steady state ratios of the two mRNAs. The Journal of Biological Chemistry 258: 385-9, 1983

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

The retention of abnormal type I procollagen and correlated expression of HSP 47 in fibroblasts from a patient with lethal osteogenesis imperfecta. Journal of Pathology 184(2): 212-218, 1998

Abnormal procollagen synthesis in fibroblasts from three patients of the same family with a severe form of osteogenesis imperfecta (type III). Biochimica et Biophysica Acta 889(1): 23-34, 1986

The molecular defect in a nonlethal variant of osteogenesis imperfecta. Synthesis of pro-alpha 2(I) chains which are not incorporated into trimers of type I procollagen. Journal of Biological Chemistry 258(24): 15192-15197, 1983

The mRNAs for the pro-alpha 1(I) and pro-alpha 2(I) chains of type I procollagen are translated at the same rate in normal human fibroblasts and in fibroblasts from two variants of osteogenesis imperfecta with altered steady state ratios of the two mRNAs. Journal of Biological Chemistry 258(23): 14385-14389, 1983

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

Type I procollagen in the severe non-lethal form of osteogenesis imperfecta. Defective pro-alpha 1(I) chains in a patient with abnormal proteoglycan metabolism and mineral deposits in the dermis. Human Genetics 79(3): 245-250, 1988

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

Presence of translatable mRNA for pro alpha 2(I) chains in fibroblasts from a patient with osteogenesis imperfecta whose type I collagen does not contain alpha 2(I) chains. Collagen and Related Research 4(5): 389-394, 1984

Synthesis of a shortened pro-a2(I) chain and decreased synthesis of pro-a2(I) chains in a proband with osteogenesis imperfecta. The Journal of Biological Chemistry 258: 21-8, 1983

Type I osteogenesis imperfecta: a nonfunctional allele for pro alpha 1 (I) chains of type I procollagen. Proceedings of the National Academy of Sciences of the United States of America 79(12): 3838-3842, 1982

Subtle structural alterations in the chains of type I procollagen produce osteogenesis imperfecta type II. Nature 316(6026): 363-366, 1985

Defects in the processing of procollagen to collagen are demonstrable in cultured fibroblasts from patients with the Ehlers-Danlos and osteogenesis imperfecta syndromes. Journal of Biological Chemistry 261(21): 10006-10014, 1986