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A single base mutation that converts glycine 907 of the a2(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 helix


A single base mutation that converts glycine 907 of the a2(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 helix



The Journal of Biological Chemistry 264: 02-6




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Related references

A single base mutation that converts glycine 907 of the α2(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 helix. The Journal of Biological Chemistry 264(5): 3002-3006, 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 helix. Journal of Biological Chemistry 264(5): 3002-3006, 1989

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

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 alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta. Journal of Biological Chemistry 262(30): 14737-14744, 1987

A single base mutation in type i procollagen that converts glycine alpha 1 541 to aspartate in a lethal variant of osteogenesis imperfecta detection of the mutation with carbodiimide reaction. Matrix 10(4): 252, 1990

Substitution of cysteine for glycine alpha 1 691 in the proalpha 1i chain of type i procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site carboxyl terminal to the substitution. Biochemical Journal 279(3): 747-752, 1991

A single base mutation in type I procollagen (COLIAI) that converts glycine a1-541 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. American Journal of Human Genetics 48: 86-91, 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 PCR. American Journal of Human Genetics 48(6): 1186-1191, 1991

A single base mutation in type i procollagen that converts glycine alpha 1 541 to aspartate in lethal osteogenesis imperfecta detection of the mutation with a carbodiimide reaction. FASEB Journal 4(7): A2284, 1990

Substitution of cysteine for glycine-1-691 in the pro1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C -terminal to the substitution. Biochemical Journal 279(3): 747-752, 1991

Substitution of cysteine for glycine-α1-691 in the proα1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution. Biochemical Journal (London 1984) 279: 747-752, 1991

Substitution of serine for a1(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. The Journal of Biological Chemistry 264: 694-9, 1989

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. The Journal of Biological Chemistry 264(33): 19694-19699, 1989

Substitution of serine for alpha 1(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 of amino acid specific. Journal of Biological Chemistry 264(33): 19694-19699, 1989