References
- Wozney, J. M., V. Rosen, A. J. Celeste, J. M. Mitsock, M. J. Whitters, R. W. Kriz, R. M. Hewick, and E. A. Wang (1988) Novel regulators of bone formation: molecular clones and activities. Science 242: 1528-1534. https://doi.org/10.1126/science.3201241
- Kingsley, D. M. (1994) The TGF-beta superfamily: new members, new receptors, and new genetic tests of function in different organisms. Genes Dev. 8: 133-146. https://doi.org/10.1101/gad.8.2.133
- Urist, M. R. (1965) Bone formation by autoinduction. Science 150: 893-899. https://doi.org/10.1126/science.150.3698.893
- Urist, M. R. and B. S. Strates (1971) Bone morphogenetic protein. J. Dent. Res. 50: 1392-1406. https://doi.org/10.1177/00220345710500060601
- Wang, E. A., V. Rosen, and P. Cordes (1988) Purification and characterization of other distinct bone inducing factors. Proc. Natl. Acad. Sci. USA. 85: 9484-9488. https://doi.org/10.1073/pnas.85.24.9484
- Luyten, F. P., N. S. Cunningham, and S. Ma (1989) Purification and partial amino acid sequence of osteogenin a protein in initiating bone differentiation. J. Biol. Chem. 264: 13377-13380.
- Wozney, J. M., V. Rosen, and A. J. Celeste (1988) Novel regulatiors of bone formation: Molecular clones and activities. Science 242: 1528-1534. https://doi.org/10.1126/science.3201241
- Daluiski, A., T. Engstrand, and M. E. Bahamonde (2001) Bone morphogenetic protein-3 is a negative regulator of bone density. Nat. Genet. 27: 84-88.
- Gazit, D., G. Turgeman, and P. Kelley (1999) Engineered pluripotent mesenchymal cells integrate and differentiate in regenerating bone: a novel cellmediated gene therapy. J. Gene. Med. 1: 121-133. https://doi.org/10.1002/(SICI)1521-2254(199903/04)1:2<121::AID-JGM26>3.0.CO;2-J
- Groeneveld, E. H. and E. H. Burger (2000) Bone morphogentic proteins in human bone regenration. Eur. J. Endocrinol. 142: 9-21. https://doi.org/10.1530/eje.0.1420009
- Geesink, R. G. T., N. H. M. Hoefnagels, and S. K. Bulstra (1999) Osteogenic activity of OP-1 bone morphogenetic protein (BMP-7) in a human fibular defect. J. Bone Joint. Surg. 81-B: 710-718. https://doi.org/10.1302/0301-620X.81B4.0810710
- Yamagiwa, H., N. Endo, K. Tokunaga, T. Hayami, H. Hatano, and H. E. Takahashi (2001) In vivo boneforming capacity of human bone marrow-derived stromal cells is stimulated by recombinant human bone morphogentic protein-2. J. Bone Miner Metab. 19: 20-28. https://doi.org/10.1007/s007740170056
- Gentry, L. E., N. R. Webb, G. J. Lim, A. M. Brunner, J. E. Ranchalis, D. R. Twardzik, M. N. Lioubin, H. Marquardt, and A. F. Purchio (1987) Type I transforming growth factor beta: amplified expression and secretion of mature and precursor polypeptides in Chinese hamster ovary cells. Mol. Cell Biol. 7: 3418-3427. https://doi.org/10.1128/MCB.7.10.3418
- Wang, E. A., V. Rosen, J. S. D_Alessandro, M. Bauduy, P. Cordes, T. Harada, D. I. Israel, R. M. Hewick, K. M. Kerns, P. LaPan, D. P. Luxenberg, D. Mcqaid, J. K. Moutsatsos, J. Nove, and J. M. Wozney (1990) Recombinant human bone morphogenetic protein induces bone formation. Proc. Natl. Acad. Sci. USA 87: 2220-2224. https://doi.org/10.1073/pnas.87.6.2220
- Ruppert, R., E. Hoffmann, and W. Sebald (1996) Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity. Eur. J. Biochem. 237: 295-302. https://doi.org/10.1111/j.1432-1033.1996.0295n.x
- Vallejo, L. F., M. Brokelmann, S. Marten, S. Trappe, J. Cabrera-Crespo, A. Hoffmann, G. Gross, H. A. Weich, and U. Rinas (2002) Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli. J. Biotech. 94: 185-194. https://doi.org/10.1016/S0168-1656(01)00425-4
- Baneyx, F. (1999) Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 10: 411-421. https://doi.org/10.1016/S0958-1669(99)00003-8
- Wely, K. H. M., J. Swaving, R. Freudl, and A. J. M. Driessen (2001) Translocation of proteins across the cell envelope of Gram-positive bacteria, FEMS Microbiol. Rev. 25: 437-454. https://doi.org/10.1111/j.1574-6976.2001.tb00586.x
- Schallmey, M., A. Singh, and O. P. Ward (2004) Developments in the use of Bacillus species for industrial production. Can. J. Microbiol. 50: 1-17. https://doi.org/10.1139/w03-076
- Hakamada, Y., K. Koike, T. Yoshimatsu, H. Mori, T. Kobayashi, and S. Ito (1997) Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237. Extremophiles 1: 151-156. https://doi.org/10.1007/s007920050028
- Sumitomo, N., K. Ozaki, S. Kawai, and S. Ito (1992) Nucleotide sequence of the gene for an alkaline endoglucanase from an alkalophilic Bacillus and its expression in Escherichia coli and Bacillus subtilis. Biosci. Biotechnol. Biochem. 56: 872-877. https://doi.org/10.1271/bbb.56.872
- Sumitomo, N., K. Ozaki, J. Hitomi, S. Kawaminami, T. Kobayashi, S. Kawai, and S. Ito (1995) Application of the upstream region of a Bacillus endoglucanase gene to high-level expression of foreign genes in Bacillus subtilis. Biosci. Biotechnol. Biochem. 59: 2172-2175. https://doi.org/10.1271/bbb.59.2172
- Hakamada, Y., Y. Hatada, K. Koike, T. Yoshimatsu, S. Kawai, T. Kobayashi, and S. Ito (2000) Deduced amino acid sequence and possible catalytic residues of a thermostable, alkaline cellulase from an alkaliphilic Bacillus strain. Biosci. Biotechnol. Biochem. 64: 2281-2289. https://doi.org/10.1271/bbb.64.2281
- Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166: 557-580. https://doi.org/10.1016/S0022-2836(83)80284-8
- Chang, S. and S. N. Cohen (1979) High frequency transformation of Bacillus subtilis. Mol. Gen. Genet. 168: 111-115. https://doi.org/10.1007/BF00267940
- Ito, M. and M. Nagane (2001) Improvement of the electro-transformation efficiency of facultatively alkaliphlic Bacillus pseudofirmus OF4 by high osmolarity and glycine treatment. Biosci Biotechnol Biochem. 65: 2773-2775. https://doi.org/10.1271/bbb.65.2773
- Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall (1951) Protein measurement with the foline phenol reagent. J. Biol. Chem. 193: 265-275.
- Bethany, S.-U., J. K. Mills, J. Vennarini, K. Boakye, J. Luo, S. Pomerantz, M. R. Cunningham, F. X. Farrell, M. F. Naso, B. Amegadzie (2008) Expression and characterization of a human BMP-7 variant with improved biochemical properties. Protein Expr. Purif. 57: 312-319. https://doi.org/10.1016/j.pep.2007.09.016