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Y Hojima

Showing results (21-30 of 31) with videos related to

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Blood|June 1, 1984
In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate EY Hojima, C G Cochrane, R C Wiggins, et al.
The Journal of Biological Chemistry|April 15, 1994
Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotypeA M Romanic, L D Spotila, E Adachi, et al.
The Journal of Biological Chemistry|December 15, 1988
A substitution of cysteine for glycine 748 of the alpha 1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm awayB E Vogel, R Doelz, K E Kadler, et al.
The Journal of Biological Chemistry|February 5, 1992
Temperature-induced post-translational over-modification of type I procollagen. Effects of over-modification of the protein on the rate of cleavage by procollagen N-proteinase and on self-assembly of collagen into fibrilsA Torre-Blanco, E Adachi, Y Hojima, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 14, 1996
The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1S W Li, A L Sieron, A Fertala, et al.
Biochemistry|May 21, 1991
A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structuresK E Kadler, A Torre-Blanco, E Adachi, et al.
The New England Journal of Medicine|July 13, 1978
Hypotension associated with prekallikrein activator (Hageman-factor fragments) in plasma protein fractionB M Alving, Y Hojima, J J Pisano, et al.
Ciba Foundation Symposium|January 1, 1988
Expression of type I procollagen genesD J Prockop, K E Kadler, Y Hojima, et al.
American Journal of Medical Genetics|September 1, 1989
Type I procollagen: the gene-protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissueD J Prockop, C D Constantinou, K E Dombrowski, et al.
Journal of Molecular Biology|November 20, 1989
Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptideD J Hulmes, K E Kadler, A P Mould, et al.
Pageof 4

Showing results (21-30 of 31) with videos related to

Sort By:
Pageof 4
Blood|June 1, 1984
In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate EY Hojima, C G Cochrane, R C Wiggins, et al.
The Journal of Biological Chemistry|April 15, 1994
Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotypeA M Romanic, L D Spotila, E Adachi, et al.
The Journal of Biological Chemistry|December 15, 1988
A substitution of cysteine for glycine 748 of the alpha 1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm awayB E Vogel, R Doelz, K E Kadler, et al.
The Journal of Biological Chemistry|February 5, 1992
Temperature-induced post-translational over-modification of type I procollagen. Effects of over-modification of the protein on the rate of cleavage by procollagen N-proteinase and on self-assembly of collagen into fibrilsA Torre-Blanco, E Adachi, Y Hojima, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 14, 1996
The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1S W Li, A L Sieron, A Fertala, et al.
Biochemistry|May 21, 1991
A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structuresK E Kadler, A Torre-Blanco, E Adachi, et al.
The New England Journal of Medicine|July 13, 1978
Hypotension associated with prekallikrein activator (Hageman-factor fragments) in plasma protein fractionB M Alving, Y Hojima, J J Pisano, et al.
Ciba Foundation Symposium|January 1, 1988
Expression of type I procollagen genesD J Prockop, K E Kadler, Y Hojima, et al.
American Journal of Medical Genetics|September 1, 1989
Type I procollagen: the gene-protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissueD J Prockop, C D Constantinou, K E Dombrowski, et al.
Journal of Molecular Biology|November 20, 1989
Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptideD J Hulmes, K E Kadler, A P Mould, et al.
Pageof 4