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Biochemistry|January 12, 1993
Use of an antisense oligonucleotide to inhibit expression of a mutated human procollagen gene (COL1A1) in transfected mouse 3T3 cellsA Colige, B P Sokolov, P Nugent, et al.Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research|December 1, 1995
Bone fragility in transgenic mice expressing a mutated gene for type I procollagen (COL1A1) parallels the age-dependent phenotype of human osteogenesis imperfectaR F Pereira, E L Hume, K W Halford, et al.The Journal of Biological Chemistry|November 5, 1992
Polymerization of pNcollagen I and copolymerization of pNcollagen I with collagen I. A kinetic, thermodynamic, and morphologic studyA M Romanic, E Adachi, Y Hojima, et al.European Journal of Biochemistry|May 1, 1980
Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerizationH P Bächinger, P Bruckner, R Timpl, et al.Proceedings of the National Academy of Sciences of the United States of America|March 21, 1998
Conformation sensitive gel electrophoresis for simple and accurate detection of mutations: comparison with denaturing gradient gel electrophoresis and nucleotide sequencingJ Körkkö, S Annunen, T Pihlajamaa, et al.Biochemistry|September 7, 1993
Tissue- and development-specific expression in transgenic mice of a type I procollagen (COL1A1) minigene construct with 2.3 kb of the promoter region and 2 kb of the 3'-flanking region. Specificity is independent of the putative regulatory sequences in the first intronB P Sokolov, P K Mays, J S Khillan, et al.Matrix (Stuttgart, Germany)|February 1, 1992
A 15 base-pair AT-rich variable number tandem repeat in the type III procollagen gene (COL3A1) as an informative marker for 2q31-2q32.3P K Mays, G Tromp, H Kuivaniemi, et al.Proceedings of the National Academy of Sciences of the United States of America|October 15, 1992
Growing tips of type I collagen fibrils formed in vitro are near-paraboloidal in shape, implying a reciprocal relationship between accretion and diameterD F Holmes, J A Chapman, D J Prockop, et al.The Journal of Biological Chemistry|February 15, 1989
A single base mutation that converts glycine 907 of the alpha 2(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 helixC T Baldwin, C D Constantinou, K W Dumars, et al.American Journal of Human Genetics|July 1, 1990
Inheritance of an RNA splicing mutation (G+ 1 IVS20) in the type III procollagen gene (COL3A1) in a family having aortic aneurysms and easy bruisability: phenotypic overlap between familial arterial aneurysms and Ehlers-Danlos syndrome type IVS Kontusaari, G Tromp, H Kuivaniemi, et al.Pageof 30