Lethal osteogenesis imperfecta resulting from a single nucleotide change in one human pro alpha 1(I) collagen allele.
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Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulationFamilial Scheuermann disease: a genetic and linkage studyOsteogenesis imperfecta: translation of mutation to phenotypeDetection of point mutations in type I collagen by RNase digestion of RNA/RNA hybridsTandem duplication within a type II collagen gene (COL2A1) exon in an individual with spondyloepiphyseal dysplasia.The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagenThe clinical features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by arginine in the pro alpha 1(I) chain of type I procollagen.Substitution of cysteine for glycine at residue 415 of one allele of the alpha 1(I) chain of type I procollagen in type III/IV osteogenesis imperfecta.The clinical features of osteogenesis imperfecta resulting from a non-functional carboxy terminal pro alpha 1(I) propeptide of type I procollagen and a severe deficiency of normal type I collagen in tissuesSingle base mutation in the pro alpha 2(I) collagen gene that causes efficient splicing of RNA from exon 27 to exon 29 and synthesis of a shortened but in-frame pro alpha 2(I) chain.Osteogenesis imperfecta type IV. Biochemical confirmation of genetic linkage to the pro alpha 2(I) gene of type I collagen.A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstabIntroduction of the human pro alpha 1(I) collagen gene into pro alpha 1(I)-deficient Mov-13 mouse cells leads to formation of functional mouse-human hybrid type I collagenTesting for osteogenesis imperfecta in cases of suspected non-accidental injuryPhenotype and genotype analysis of Chinese patients with osteogenesis imperfecta type V.Type II collagen defects in the chondrodysplasias. I. Spondyloepiphyseal dysplasias.Distinct biochemical phenotypes predict clinical severity in nonlethal variants of osteogenesis imperfecta.Recurrence of lethal osteogenesis imperfecta due to parental mosaicism for a dominant mutation in a human type I collagen gene (COL1A1).Perinatal lethal osteogenesis imperfecta (OI type II): a biochemically heterogeneous disorder usually due to new mutations in the genes for type I collagen.Osteogenesis imperfecta. The position of substitution for glycine by cysteine in the triple helical domain of the pro alpha 1(I) chains of type I collagen determines the clinical phenotypeHuman-mouse interspecies collagen I heterotrimer is functional during embryonic development of Mov13 mutant mouse embryos.Rescue of type I collagen-deficient phenotype by retroviral-vector-mediated transfer of human pro alpha 1(I) collagen gene into Mov-13 cellsConnective tissue diseases in the skin--from molecules to symptoms.A brilliant breakthrough in OI type V.IFITM5 mutations and osteogenesis imperfecta.Osteogenesis imperfecta: the molecular basis of clinical heterogeneity.General strategies for isolating the genes encoding type I collagen and for characterizing mutations which produce osteogenesis imperfecta.Clinical and genetical heterogeneity of osteogenesis imperfecta.Molecular and clinical aspects of connective tissue.Genetic disorders of collagenSubstitution 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.Increased expression of the gene for the pro alpha 1(IV) chain of basement-membrane procollagen in cultured skin fibroblasts from two variants of osteogenesis imperfecta.Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of alpha 1 (I)-chain glycine-to-arginine substitutions.A cysteine for glycine substitution at position 175 in an alpha 1 (I) chain of type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta.The triple helix of collagens - an ancient protein structure that enabled animal multicellularity and tissue evolution.Recurrence of perinatal lethal osteogenesis imperfecta in sibships: Parsing the risk between parental mosaicism for dominant mutations and autosomal recessive inheritance
P2860
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P2860
Lethal osteogenesis imperfecta resulting from a single nucleotide change in one human pro alpha 1(I) collagen allele.
description
article científic
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article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 1986
@en
vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Lethal osteogenesis imperfecta ...... hange in one human pro alpha 1
@nl
Lethal osteogenesis imperfecta ...... ro alpha 1(I) collagen allele.
@en
type
label
Lethal osteogenesis imperfecta ...... hange in one human pro alpha 1
@nl
Lethal osteogenesis imperfecta ...... ro alpha 1(I) collagen allele.
@en
prefLabel
Lethal osteogenesis imperfecta ...... hange in one human pro alpha 1
@nl
Lethal osteogenesis imperfecta ...... ro alpha 1(I) collagen allele.
@en
P2093
P2860
P356
P1476
Lethal osteogenesis imperfecta ...... ro alpha 1(I) collagen allele.
@en
P2093
B Steinmann
R E Gelinas
P2860
P304
P356
10.1073/PNAS.83.16.6045
P407
P577
1986-08-01T00:00:00Z