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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


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




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Related references

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

Substitutions for glycine a1-637 and glycine a2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix. The Journal of Biological Chemistry 266: 608-13, 1991

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, 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

Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix. Journal of Biological Chemistry 266(24): 15608-15613, 1991

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

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 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 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 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 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

Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(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: 747-752, 1991

Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite. Biochemical Journal 311(3): 815-820, 1995

Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite. Biochemical Journal 311: 815-820, 1995

Two cysteine substitutions in procollagen I: a glycine replacement near the N-terminus of alpha 1(I) chain causes lethal osteogenesis imperfecta and a glycine replacement in the alpha 2(I) chain markedly destabilizes the triple helix. Biochemical Journal 289: 195-199, 1993