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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 mother
H 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 proteinases
C 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 cells
E 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 helix
A 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 I
A 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 polypeptides
Y Hojima, J A McKenzie, M van der Rest, et al.
The Journal of Biological Chemistry
|
November 15, 1989
Single base mutation in the type III procollagen gene that converts the codon for glycine 883 to aspartate in a mild variant of Ehlers-Danlos syndrome IV
G Tromp, H Kuivaniemi, C Stolle, et al.
The Journal of Biological Chemistry
|
July 5, 1991
Copolymerization of pNcollagen III and collagen I. pNcollagen III decreases the rate of incorporation of collagen I into fibrils, the amount of collagen I incorporated, and the diameter of the fibrils formed
A M Romanic, E Adachi, K E Kadler, et al.
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 substitution
B 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 collagens
M M Vuristo, T Pihlajamaa, P Vandenberg, et al.
Page
of 27
Search research articles
Search
Showing results (131-140 of 266) with videos related to
Sort By:
Page
of 27
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 mother
H 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 proteinases
C 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 cells
E 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 helix
A 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 I
A 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 polypeptides
Y Hojima, J A McKenzie, M van der Rest, et al.
The Journal of Biological Chemistry
|
November 15, 1989
Single base mutation in the type III procollagen gene that converts the codon for glycine 883 to aspartate in a mild variant of Ehlers-Danlos syndrome IV
G Tromp, H Kuivaniemi, C Stolle, et al.
The Journal of Biological Chemistry
|
July 5, 1991
Copolymerization of pNcollagen III and collagen I. pNcollagen III decreases the rate of incorporation of collagen I into fibrils, the amount of collagen I incorporated, and the diameter of the fibrils formed
A M Romanic, E Adachi, K E Kadler, et al.
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 substitution
B 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 collagens
M M Vuristo, T Pihlajamaa, P Vandenberg, et al.
Page
of 27