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Proceedings of the National Academy of Sciences of the United States of America|December 1, 1976
Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagenH P Hoffmann, B R Olsen, H T Chen, et al.The Journal of Biological Chemistry|November 25, 1988
The structural genes for alpha 1 and alpha 2 chains of human type IV collagen are divergently encoded on opposite DNA strands and have an overlapping promoter regionR Soininen, M Huotari, S L Hostikka, et al.The Journal of Clinical Investigation|March 1, 1980
Prevention of collagen deposition following pulmonary oxygen toxicity in the rat by cis-4-hydroxy-L-prolineD J Riley, R A Berg, N H Edelman, et al.Proceedings of the National Academy of Sciences of the United States of America|September 1, 1990
Single base mutation in the type II procollagen gene (COL2A1) as a cause of primary osteoarthritis associated with a mild chondrodysplasiaL Ala-Kokko, C T Baldwin, R W Moskowitz, et al.European Journal of Biochemistry|March 2, 1987
The A and B fragments of normal type I procollagen have a similar thermal stability to proteinase digestion but are selectively destabilized by structural mutationsC D Constantinou, B E Vogel, J J Jeffrey, 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.Pageof 30