Chan D - Search Results

1

A base substitution at a splice site in the COL3A1 gene causes exon skipping and generates abnormal type III procollagen in a patient with Ehlers-Danlos syndrome type IV.

Cole WG, Chiodo AA, Lamande SR, Janeczko R, Ramirez F, Dahl HH, Chan D, Bateman JF. Cole WG, et al. Among authors: chan d. J Biol Chem. 1990 Oct 5;265(28):17070-7. J Biol Chem. 1990. PMID: 2145268 Free article.

2

Lethal perinatal osteogenesis imperfecta due to a type I collagen alpha 2(I) Gly to Arg substitution detected by chemical cleavage of an mRNA:cDNA sequence mismatch.

Bateman JF, Moeller I, Hannagan M, Chan D, Cole WG. Bateman JF, et al. Among authors: chan d. Hum Mutat. 1992;1(1):55-62. doi: 10.1002/humu.1380010109. Hum Mutat. 1992. PMID: 1284475

3

Low basal transcription of genes for tissue-specific collagens by fibroblasts and lymphoblastoid cells. Application to the characterization of a glycine 997 to serine substitution in alpha 1(II) collagen chains of a patient with spondyloepiphyseal dysplasia.

Chan D, Cole WG. Chan D, et al. J Biol Chem. 1991 Jul 5;266(19):12487-94. J Biol Chem. 1991. PMID: 1905723 Free article.

4

Characterization of a type I collagen alpha 2(I) glycine-586 to valine substitution in osteogenesis imperfecta type IV. Detection of the mutation and prenatal diagnosis by a chemical cleavage method.

Bateman JF, Hannagan M, Chan D, Cole WG. Bateman JF, et al. Among authors: chan d. Biochem J. 1991 Jun 15;276 ( Pt 3)(Pt 3):765-70. doi: 10.1042/bj2760765. Biochem J. 1991. PMID: 2064612 Free PMC article.

5

Regulation of procollagen synthesis and processing during ascorbate-induced extracellular matrix accumulation in vitro.

Chan D, Lamande SR, Cole WG, Bateman JF. Chan D, et al. Biochem J. 1990 Jul 1;269(1):175-81. doi: 10.1042/bj2690175. Biochem J. 1990. PMID: 2375750 Free PMC article.

6

A frameshift mutation results in a truncated nonfunctional carboxyl-terminal pro alpha 1(I) propeptide of type I collagen in osteogenesis imperfecta.

Bateman JF, Lamande SR, Dahl HH, Chan D, Mascara T, Cole WG. Bateman JF, et al. Among authors: chan d. J Biol Chem. 1989 Jul 5;264(19):10960-4. J Biol Chem. 1989. PMID: 2500431 Free article.

Only normal type I collagen was incorporated into the extracellular matrix in vivo resulting in a tissue type I collagen content approximately 20% of that of control (Bateman, J. F., Chan, D., Mascara, T., Rogers, J. G., and Cole, W. G. (1986) Biochem. J. 240, 699-7 …

Only normal type I collagen was incorporated into the extracellular matrix in vivo resulting in a tissue type I collagen content approximate …

7

A base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos syndrome type VII.

Weil D, D'Alessio M, Ramirez F, de Wet W, Cole WG, Chan D, Bateman JF. Weil D, et al. Among authors: chan d, d alessio m. EMBO J. 1989 Jun;8(6):1705-10. doi: 10.1002/j.1460-2075.1989.tb03562.x. EMBO J. 1989. PMID: 2767050 Free PMC article.

8

Deletion of 24 amino acids from the pro-alpha 1(I) chain of type I procollagen in a patient with the Ehlers-Danlos syndrome type VII.

Cole WG, Chan D, Chambers GW, Walker ID, Bateman JF. Cole WG, et al. Among authors: chan d. J Biol Chem. 1986 Apr 25;261(12):5496-503. J Biol Chem. 1986. PMID: 3082886 Free article.

9

Lethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the alpha 1(I) chain of type I collagen.

Bateman JF, Chan D, Walker ID, Rogers JG, Cole WG. Bateman JF, et al. Among authors: chan d. J Biol Chem. 1987 May 25;262(15):7021-7. J Biol Chem. 1987. PMID: 3108247 Free article.

10

Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA.

Bateman JF, Lamande SR, Dahl HH, Chan D, Cole WG. Bateman JF, et al. Among authors: chan d. J Biol Chem. 1988 Aug 25;263(24):11627-30. J Biol Chem. 1988. PMID: 3403550 Free article.

Two-dimensional gel electrophoresis of the CNBr peptides demonstrated that the alpha 1(I)CB7 peptide from the alpha 1(I) chain of type I collagen existed in a normal form and a mutant form with a more basic charge distribution (Bateman, J. F., Mascara, T., Chan, D., …

Two-dimensional gel electrophoresis of the CNBr peptides demonstrated that the alpha 1(I)CB7 peptide from the alpha 1(I) chain of type I col …

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