Yoshio Hojima

Thomas Jefferson University — United States

Medicine · Health Sciences

26h-index2.7kcitations73works0.02yr avg
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Research Topics

Coagulation, Bradykinin, Polyphosphates, and Angioedema(33), Collagen: Extraction and Characterization(15), Connective tissue disorders research(13), Protease and Inhibitor Mechanisms(9), Phytochemical compounds biological activities(8)

Publications73 total

Expression of Type I Procollagen Genes
Novartis Foundation symposium·2007· 9 cited
The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1
Matrix Biology·1996
The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1.
Proceedings of the National Academy of Sciences·1996· 218 citedOpen Access
Cleavage of Type I Procollagen by C- and N-Proteinases Is More Rapid If the Substrate Is Aggregated with Dextran Sulfate or Polyethylene Glycol
Analytical Biochemistry·1994· 39 citedOpen Access
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 phenotype
Journal of Biological Chemistry·1994· 9 citedOpen Access
Characterization of type I procollagen N-proteinase from fetal bovine tendon and skin. Purification of the 500-kilodalton form of the enzyme from bovine tendon
Journal of Biological Chemistry·1994· 30 citedOpen Access
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
Journal of Biological Chemistry·1994· 43 citedOpen Access
Cadmium ions inhibit proollagen C-proteinase and cupric ions inhibit procollagen N-proteinase
Matrix Biology·1994· 28 cited
Polymerization of pNcollagen I and copolymerization of pNcollagen I with collagen I. A kinetic, thermodynamic, and morphologic study.
Journal of Biological Chemistry·1992· 33 citedOpen Access
Self-Assembly into Fibrils of a Homotrimer of Type I Collagen
Matrix·1992· 45 cited
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 fibrils.
Journal of Biological Chemistry·1992· 80 citedOpen Access
A new 500-kDa form of type I procollagen N-proteinase from chick embryo tendons.
PubMed·1992· 5 cited
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
Journal of Biological Chemistry·1991· 131 citedOpen Access
A type I collagen with a substitution of a cysteine for glycine-748 in the .alpha.1(I) chain copolymerizes with normal type I collagen and can generate fractallike structures
Biochemistry·1991· 56 cited
The effects of co polymerization of type iii pn collagen with type i collagen in vitro incorporation of type iii pn collagen regulates the growth of type i collagen fibrils
Matrix·1990
Collagen fibrils <i>in vitro</i> grow from pointed tips in the <i>C</i>- to <i>N</i>-terminal direction
Biochemical Journal·1990· 129 citedOpen Access
Assembly of Type I Collagen Fibrils <i>de Novo</i> by the Specific Enzymic Cleavage of pC Collagen
Annals of the New York Academy of Sciences·1990· 47 cited
Assembly of type I collagen fibrils de novo by the specific enzymic cleavage of pC collagen. The fibrils formed at about 37 degrees C are similar in diameter, roundness, and apparent flexibility to the collagen fibrils seen in connective tissue.
HAL (Le Centre pour la Communication Scientifique Directe)·1990
Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide
Journal of Molecular Biology·1989· 85 cited
Type I procollagen: The gene‐protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissue
American Journal of Medical Genetics·1989· 95 cited
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Frequent Co-authors

Darwin J. Prockop(21), CHIAKI MORIWAKI(15), Hiroshi Moriya(15), Karl E. Kadler(12), John J. Pisano(8), Anne M. Romanic(6), Jack V. Pierce(5), Eijiro Adachi(5), Bruce E. Vogel(5), J. Engel(5), Michel van der Rest(3), David Hulmes(3), Aleksander L. Sieroń(2), Andrzej Fertala(2), R. Doelz(2), Constantinos D. Constantinou(2), Kenneth E. Dombrowski(2), Helena Kuivaniemi(2), Gerard Tromp(2), Christine Cummings(2)