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The Biochemical Journal|November 1, 1991
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 substitutionB Steinmann, A Westerhausen, C D Constantinou, et al.
The Journal of Biological Chemistry|September 29, 1995
The human COL11A2 gene structure indicates that the gene has not evolved with the genes for the major fibrillar collagensM M Vuristo, T Pihlajamaa, P Vandenberg, et al.
The Journal of Biological Chemistry|December 5, 1991
Transgenic mice that express a mini-gene version of the human gene for type I procollagen (COL1A1) develop a phenotype resembling a lethal form of osteogenesis imperfectaJ S Khillan, A S Olsen, S Kontusaari, et al.
Genomics|May 1, 1989
Detection and location of single-base mutations in large DNA fragments by immunomicroscopyA Ganguly, J E Rooney, S Hosomi, et al.
Gene Therapy|January 9, 2004
Stable transfection of MSCs by electroporationA Peister, J A Mellad, M Wang, et al.
American Journal of Medical Genetics|May 8, 2000
Widely distributed mutations in the COL2A1 gene produce achondrogenesis type II/hypochondrogenesisJ Körkkö, D H Cohn, L Ala-Kokko, et al.
The Journal of Clinical Investigation|April 1, 1994
Phenotypic variability and incomplete penetrance of spontaneous fractures in an inbred strain of transgenic mice expressing a mutated collagen gene (COL1A1)R Pereira, K Halford, B P Sokolov, et al.
The Journal of Biological Chemistry|November 25, 1989
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 specificM Pack, C D Constantinou, K Kalia, et al.
The Biochemical Journal|June 1, 1989
Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferencesL Ala-Kokko, S Kontusaari, C T Baldwin, et al.
Hepatology (Baltimore, Md.)|July 1, 1992
Hepatic fibrosis in rats produced by carbon tetrachloride and dimethylnitrosamine: observations suggesting immunoassays of serum for the 7S fragment of type IV collagen are a more sensitive index of liver damage than immunoassays for the NH2-terminal propeptide of type III procollagenL Ala-Kokko, V Günzler, J B Hoek, et al.
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