REFERENCES
- Hubbell, J.A. (1995). Biomaterials in tissue engineering. Bio/Technology 13: 565–76, [INFOTRIEVE], [CSA]
- Cai, K.Y., Yao, K.D., Hou, X., Wan, Y.Q., Hou, Y.J., Yang, Z.M., Li, X.Q., Xie, H.Q. (2002). Improvement of the functions of osteoblasts seeded on modified poly(D, L-lactic acid) with poly(aspartic acid). J. Biomed. Mater. Res. 62: 283–291, [INFOTRIEVE], [CROSSREF], [CSA]
- Ruoslahti, E., Pierschbacher, M.D. (1987). New perspectives in cell adhesion: RGD and integrins. Science 238: 491–497, [INFOTRIEVE], [CSA]
- Rezania, A., Healy, K.E. (2000). The effect of peptide surface density on mineralization of a matrix deposited by osteogenic cells. J. Biomed. Mater. Res. 15: 52(4): 595–600, [CROSSREF], [CSA]
- Sakata, N., Sasatomi, Y., Meng, J., Ando, S., Uesugi, N., Takebayashi, S., Nagai, R., Horiuchi, S. (2000). Possible involvement of altered RGD sequence in reduced adhesive and spreading activities of advanced glycation end product-modified fibronectin to vascular smooth muscle cells. Connect Tissue Res. 41(3): 213–28, [INFOTRIEVE], [CSA]
- Yannas, I.V., Burke, J.F. (1980). Design of artificial skin. Basic design principles. J. Biomed. Mater. Res. 14: 65–81, [INFOTRIEVE], [CROSSREF], [CSA]
- Yannas, I.V., Burke, J.F., Gordeon, P.L., Huang, C., Rubenstein, R.H. (1980). Design of artificial skin. Control of chemical composition. J. Biomed. Mater. Res. 14: 107–131, [INFOTRIEVE], [CROSSREF], [CSA]
- Glass, J.R., Dickerson, K.T., Stecker, K., Polarek, J.W. (1996). Characterization of a hyaluronic acid Arg-Gly-Asp peptide cell attachment matrix. Biomaterials 17: 1101–1108, [INFOTRIEVE], [CROSSREF], [CSA]
- Matsumoto, T., Numata, M., Anada, T., Mizu, M., Koumoto, K., Sakurai, K., Nagasaki, T., Shinkai, S. (2004). Chemically modified polysaccharide schizophyllan for antisense oligonucleotides delivery to enhance the cellular uptake efficiency. Biochim. Biophys. Acta 1670(2): 91–104, [INFOTRIEVE], [CSA]
- Grzesiak, J.J., Pierschbacher, M.D., Amodeo, M.F., Malaney, T.I., Glass, J.R. (1997). Enhancement of cell interactions with collagen/glycosaminoglycan matrices by RGD derivatization. Biomaterials 18: 1625–1632, [INFOTRIEVE], [CROSSREF], [CSA]
- Wheeler, T.L., Shackelford, S.D., Koohmaraie, M. (2000). Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. J. Anim. Sci. 78: 958–965, [INFOTRIEVE], [CSA]
- Mao, J.S., Zhao, L.G., Yin, Y.J., Yao, K.D. (2003). Structure and properties of bilayer chitosan-gelatin scaffolds. Biomaterials 24(6): 1067–1074, [INFOTRIEVE], [CROSSREF], [CSA]
- Zhang, L.H., Ma, D.R., Wang, F.J., Zhang, Q.Q. (2002). The modification of scaffold material in building artificial dermis. Artif. Cells Blood Substit. Immobil. Biotechnol. 30(4): 319–32, [INFOTRIEVE], [CROSSREF], [CSA]
- Natsume, T., Ike, O., Okada, T., Takimoto, N., Shimizu, Y., Ikada, Y. (1993). Porous collagen sponge for esophageal replacement. J. Biomed. Mater. Res. 27(7): 867–875, [INFOTRIEVE], [CROSSREF], [CSA]
- Dagalakis, N., Flink, J., Stasikelis, P., Burke, J.F., Yannas, I.V. (1980). Design of artificial skin. Part III. Control of pore structure. J. Biomed. Mater. Res. 14: 511–528, [INFOTRIEVE], [CROSSREF], [CSA]
- Zhang, Q.Q., Ren, L., Liu, L.R. (1997). Structure investigation of poly(vinyl alcohol)-collagen composite. J. Mater. Sci. Technol. 13: 179–183, [CSA]
- Curtis, A.S.G., Forrester, J.V., Clark, P. (1986). Substratum hydroxylation and cell adhesion. J. Cell Sci. 86: 9–24, [CSA]
- Altankov, G., Groth, T. (1997). Fibronectin matrix formation by human fibroblasts on surfaces varying in wettability. J. Biomater. Sci. Polym. Edn. 8: 299–310, [CSA]
- Rickard, D.J., Sullivan, T.A., Shenker, B.J., Leboy, P.S., Kazhdan, I. (1994). Induction of rapid osteoblast differentiation in rat bone marrow stromal cell cultures by dexamethasone and BMP-2. Dev. Biol. 161(1): 218–228, [INFOTRIEVE], [CROSSREF], [CSA]
- Natsume, T., Ike, O., Okada, T., Takimoto, N., Shimizu, Y., Ikada, Y. (1993). Porous collagen sponge for esophageal replacement. J. Biomed. Mater. Res. 27(7): 867–875, [INFOTRIEVE], [CROSSREF], [CSA]
- Dagalakis, N., Flink, J., Stasikelis, P., Burke, J.F., Yannas, I.V. (1980). Design of artificial skin. Part III. Control of pore structure. J. Biomed. Mater. Res. 14: 511–528, [INFOTRIEVE], [CROSSREF], [CSA]
- Mizuno, K., Hayashi, T., Bachinger, H.P. (2003). Hydroxylation-induced stabilization of the collagen triple helix. Further characterization of peptides with 4(R)-hydroxyproline in the Xaa position. J. Biol. Chem. 278(34): 32373–32379, [INFOTRIEVE], [CROSSREF], [CSA]
- Lauer-Fields, J.L., Tuzinski, K.A., Shimokawa, K., Nagase, H., Fields, G.B. (2000). Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases. J. Biol. Chem. 275(18): 13282–13290, [INFOTRIEVE], [CROSSREF], [CSA]
- Curtis, A.S.G., Forrester, J.V., Clark, P. (1986). Substratum hydroxylation and cell adhesion. J. Cell Sci. 86: 9–24, [CSA]
- Altankov, G., Groth, T. (1997). Fibronectin matrix formation by human fibroblasts on surfaces varying in wettability. J. Biomater. Sci. Polym. Edn. 8: 299–310, [CSA]
- Pieper, J.S., Hafmans, T., Veerkamp, J.H., van Kuppevelt, T.H. (1999). Development of tailor-made collagen-glycosaminoglycan matrices: EDC/NHS crosslinking, and ultrastructural aspects. Biomaterials 20: 847–858, [INFOTRIEVE], [CROSSREF], [CSA]