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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.
The Journal of Biological Chemistry|August 15, 1988
A 19-base pair deletion in the pro-alpha 2(I) gene of type I procollagen that causes in-frame RNA splicing from exon 10 to exon 12 in a proband with atypical osteogenesis imperfecta and in his asymptomatic motherH Kuivaniemi, C Sabol, G Tromp, et al.
The Journal of Biological Chemistry|February 10, 1985
Synthesis of an altered type III procollagen in a patient with type IV Ehlers-Danlos syndrome. A structural change in the alpha 1(III) chain which makes the protein more susceptible to proteinasesC A Stolle, R E Pyeritz, J C Myers, et al.
Stem Cells (Dayton, Ohio)|May 22, 2001
Rat marrow stromal cells are more sensitive to plating density and expand more rapidly from single-cell-derived colonies than human marrow stromal cellsE H Javazon, D C Colter, E J Schwarz, et al.
The Biochemical Journal|January 1, 1993
Two cysteine substitutions in procollagen I: a glycine replacement near the N-terminus of alpha 1(I) chain causes lethal osteogenesis imperfecta and a glycine replacement in the alpha 2(I) chain markedly destabilizes the triple helixA Fertala, A Westerhausen, G Morris, et al.
The Journal of Biological Chemistry|April 15, 1994
Self-assembly into fibrils of collagen II by enzymic cleavage of recombinant procollagen II. Lag period, critical concentration, and morphology of fibrils differ from collagen IA Fertala, A L Sieron, Y Hojima, et al.
The Journal of Biological Chemistry|July 5, 1989
Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptidesY Hojima, J A McKenzie, M van der Rest, et al.
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