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Article

Recurrent substitutions of arginine 789 by cysteine in pro-alpha 1 (II) collagen chains produce spondyloepiphyseal dysplasia congenita.

The Journal of rheumatology. Supplement - 1 Feb 1995

Chan D, Rogers J F, Bateman J F, Cole W G

Abstract excerpt

A child with typical spondyloepiphyseal dysplasia congenita had a recurrent, heterozygous substitution of arginine 789 by cysteine in the triple helical domain of alpha 1 (II) chains of type II collagen. The amino substitution was due to the transition of cytosine 2913 to thymine in exon 41 of the COL2A1 gene. The amino acid substitution involved the Y position of a Gly-X-Y triplet.

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Source

Identifiers

PMID: 7752132

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Recurrent substitutions of arginine 789 by cysteine in pro-alpha 1 (II) collagen chains produce spondyloepiphyseal dysplasia congenita.PMID 7752132Read ↗

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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.Semantic proximity Read ↗

Spondyloepiphyseal dysplasia congenita caused by double heterozygous mutations in COL2A1.Semantic proximity Read ↗

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A form of autosomal dominant spondyloepiphyseal dysplasia is caused by a glycine to alanine substitution in the COL2A1 gene.Semantic proximity Read ↗

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