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

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

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Veröffentlicht in:The Journal of biological chemistry 1989, Vol.264 (5), p.3002-3006
Hauptverfasser: BALDWIN, C. T, CONSTANTINOU, C. D, DUMARS, K. W, PROCKOP, D. J
Format: Artikel
Sprache:eng
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Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Molecular and cellular biology
Molecular genetics
Mutagenesis. Repair
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container_title The Journal of biological chemistry
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creator BALDWIN, C. T
CONSTANTINOU, C. D
DUMARS, K. W
PROCKOP, D. J
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1083-351X
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source EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Molecular and cellular biology
Molecular genetics
Mutagenesis. Repair
title 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
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