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Volumn 289, Issue 14, 2014, Pages 9754-9765

Fibroblast growth factor-based signaling through synthetic heparan sulfate blocks copolymers studied using high cell density three-dimensional cell printing

Author keywords

[No Author keywords available]

Indexed keywords

BLOCK COPOLYMERS; CELL CULTURE; CELL PROLIFERATION; CELLS; CHAINS; GROWTH KINETICS; PROTEINS; THREE DIMENSIONAL;

EID: 84898069475     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.546937     Document Type: Article
Times cited : (23)

References (61)
  • 1
    • 77956031216 scopus 로고    scopus 로고
    • Proteoglycomics. Recent progress and future challenges
    • Ly, M., Laremore, T. N., and Linhardt, R. J. (2010) Proteoglycomics. Recent progress and future challenges. OMICS 14, 389-399
    • (2010) OMICS , vol.14 , pp. 389-399
    • Ly, M.1    Laremore, T.N.2    Linhardt, R.J.3
  • 2
    • 0034253761 scopus 로고    scopus 로고
    • Mechanisms involved in cartilage proteoglycan catabolism
    • Caterson, B., Flannery, C. R., Hughes, C. E., and Little, C. B. (2000) Mechanisms involved in cartilage proteoglycan catabolism. Matrix Biol. 19, 333-344
    • (2000) Matrix Biol. , vol.19 , pp. 333-344
    • Caterson, B.1    Flannery, C.R.2    Hughes, C.E.3    Little, C.B.4
  • 3
    • 0035168796 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular matrix and growth control
    • Kresse, H., and Schönherr, E. (2001) Proteoglycans of the extracellular matrix and growth control. J. Cell. Physiol. 189, 266-274
    • (2001) J. Cell. Physiol. , vol.189 , pp. 266-274
    • Kresse, H.1    Schönherr, E.2
  • 4
    • 0033635310 scopus 로고    scopus 로고
    • Heparin and heparan sul-fate. Biosynthesis, structure, and function
    • Sasisekharan, R., and Venkataraman, G. (2000) Heparin and heparan sul-fate. Biosynthesis, structure, and function. Curr. Opin. Chem. Biol. 4, 626-631
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 626-631
    • Sasisekharan, R.1    Venkataraman, G.2
  • 7
    • 0033485553 scopus 로고    scopus 로고
    • Host cyclophilin A mediates HIV-1 attachment to target cells via heparans
    • Saphire, A. C., Bobardt, M. D., and Gallay, P. A. (1999) Host cyclophilin A mediates HIV-1 attachment to target cells via heparans. EMBO J. 18, 6771-6785
    • (1999) EMBO J. , vol.18 , pp. 6771-6785
    • Saphire, A.C.1    Bobardt, M.D.2    Gallay, P.A.3
  • 13
    • 0028855668 scopus 로고
    • Preparation and Structural Characterization of Large Heparin-Derived Oligosaccharides
    • Pervin, A., Gallo, C., Jandik, K. A., Han, X.-J., and Linhardt, R. J. (1995) Preparation and Structural Characterization of Large Heparin-Derived Oligosaccharides. Glycobiology 5, 83-95
    • (1995) Glycobiology , vol.5 , pp. 83-95
    • Pervin, A.1    Gallo, C.2    Jandik, K.A.3    Han, X.-J.4    Linhardt, R.J.5
  • 14
    • 0030929763 scopus 로고    scopus 로고
    • Preparation and structure of heparin lyase-derived heparan sulfate oligosaccha-rides
    • Hileman, R. E., Smith, A. E., Toida, T., and Linhardt, R. J. (1997) Preparation and structure of heparin lyase-derived heparan sulfate oligosaccha-rides. Glycobiology 7, 231-239
    • (1997) Glycobiology , vol.7 , pp. 231-239
    • Hileman, R.E.1    Smith, A.E.2    Toida, T.3    Linhardt, R.J.4
  • 16
    • 80055084998 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis ofstructurally homogeneous ultra-low molecular weight heparins
    • Xu, Y., Masuko, S., Takieddin, M., Xu, H., Liu, R., Jing, J., Mousa, S. A., Linhardt, R. J., and Liu, J. (2011) Chemoenzymatic synthesis ofstructurally homogeneous ultra-low molecular weight heparins. Science 334, 498-501
    • (2011) Science , vol.334 , pp. 498-501
    • Xu, Y.1    Masuko, S.2    Takieddin, M.3    Xu, H.4    Liu, R.5    Jing, J.6    Mousa, S.A.7    Linhardt, R.J.8    Liu, J.9
  • 17
    • 84880467535 scopus 로고    scopus 로고
    • Methods for the Pasteurella glycosaminoglycan synthases. Enzymes that polymerize hyaluronan, chondroitin, or heparo-san chains
    • DeAngelis, P. L. (2013) Methods for the Pasteurella glycosaminoglycan synthases. Enzymes that polymerize hyaluronan, chondroitin, or heparo-san chains. Methods Mol. Biol. 1022, 215-227
    • (2013) Methods Mol. Biol. , vol.1022 , pp. 215-227
    • Deangelis, P.L.1
  • 18
    • 0030736088 scopus 로고    scopus 로고
    • Biosynthesis of heparin/heparan sulfate cDNA cloning and expression of D-glucuronyl C5-epimerase from bovine lung
    • Li, J., Hagner-McWhirter, A., Kjellén, L., Palgi, J., Jalkanen, M., and Lin-dahl, U. (1997) Biosynthesis of heparin/heparan sulfate. cDNA cloning and expression of D-glucuronyl C5-epimerase from bovine lung. J. Biol. Chem. 272, 28158-28163
    • (1997) J. Biol. Chem. , vol.272 , pp. 28158-28163
    • Li, J.1    Hagner-Mcwhirter, A.2    Kjellén, L.3    Palgi, J.4    Jalkanen, M.5    Lin-Dahl, U.6
  • 19
    • 0032502660 scopus 로고    scopus 로고
    • Molecular characterization and expression of heparan-sulfate 6-sulfotransferase. Complete cDNA cloning in human and partial cloning in Chinese hamster ovary cells
    • Habuchi, H., Kobayashi, M., and Kimata, K. (1998) Molecular characterization and expression of heparan-sulfate 6-sulfotransferase. Complete cDNA cloning in human and partial cloning in Chinese hamster ovary cells. J. Biol. Chem. 273, 9208-9213
    • (1998) J. Biol. Chem. , vol.273 , pp. 9208-9213
    • Habuchi, H.1    Kobayashi, M.2    Kimata, K.3
  • 20
    • 0030783519 scopus 로고    scopus 로고
    • Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfo-transferase
    • Shworak, N. W., Liu, J., Fritze, L. M., Schwartz, J. J., Zhang, L., Logeart, D., and Rosenberg, R. D. (1997) Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfo-transferase. J. Biol. Chem. 272, 28008-28019
    • (1997) J. Biol. Chem. , vol.272 , pp. 28008-28019
    • Shworak, N.W.1    Liu, J.2    Fritze, L.M.3    Schwartz, J.J.4    Zhang, L.5    Logeart, D.6    Rosenberg, R.D.7
  • 22
    • 0035818480 scopus 로고    scopus 로고
    • Enzyme interactions in heparan sulfate biosynthesis. Uronosyl 5-epimerase and 2-O-sulfotransferase interact in vivo
    • Pinhal, M. A., Smith, B., Olson, S., Aikawa, J., Kimata, K., and Esko, J. D. (2001) Enzyme interactions in heparan sulfate biosynthesis. Uronosyl 5-epimerase and 2-O-sulfotransferase interact in vivo. Proc. Natl. Acad. Sci. U.S.A. 98, 12984-12989
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12984-12989
    • Pinhal, M.A.1    Smith, B.2    Olson, S.3    Aikawa, J.4    Kimata, K.5    Esko, J.D.6
  • 23
    • 84880038115 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycosaminoglycans Re-creating, re-modeling, and re-designing nature's longest or most complex carbohydrate chains
    • DeAngelis, P. L., Liu, J., and Linhardt, R. J. (2013) Chemoenzymatic synthesis of glycosaminoglycans. Re-creating, re-modeling, and re-designing nature's longest or most complex carbohydrate chains. Glycobiology 23, 764-777
    • (2013) Glycobiology , vol.23 , pp. 764-777
    • Deangelis, P.L.1    Liu, J.2    Linhardt, R.J.3
  • 24
    • 84863011654 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of UDP-GlcNAc and UDP-GalNAc analogs for the preparation of unnatural glycosaminoglycans
    • Masuko, S., Bera, S., Green, D. E., Weïwer, M., Liu, J., DeAngelis, P. L., and Linhardt R. J. (2012) Chemoenzymatic synthesis of UDP-GlcNAc and UDP-GalNAc analogs for the preparation of unnatural glycosaminoglycans. J. Org. Chem. 77, 1449-1456
    • (2012) J. Org. Chem. , vol.77 , pp. 1449-1456
    • Masuko, S.1    Bera, S.2    Green, D.E.3    Weïwer, M.4    Liu, J.5    Deangelis, P.L.6    Linhardt, R.J.7
  • 26
    • 33646849921 scopus 로고    scopus 로고
    • Critical elements of oligosaccharide acceptor substrates for the Pasteu-rella multocida hyaluronan synthase
    • Williams, K. J., Halkes, K. M., Kamerling, J. P., and DeAngelis, P. L (2006) Critical elements of oligosaccharide acceptor substrates for the Pasteu-rella multocida hyaluronan synthase. J. Biol. Chem. 281, 5391-5397
    • (2006) J. Biol. Chem. , vol.281 , pp. 5391-5397
    • Williams, K.J.1    Halkes, K.M.2    Kamerling, J.P.3    Deangelis, P.L.4
  • 27
    • 4744369265 scopus 로고    scopus 로고
    • Synchronized chemoenzymatic synthesis of monodisperse hyaluronan polymers
    • Jing, W., and DeAngelis, P. L. (2004) Synchronized chemoenzymatic synthesis of monodisperse hyaluronan polymers. J. Biol. Chem. 279, 42345-42349
    • (2004) J. Biol. Chem. , vol.279 , pp. 42345-42349
    • Jing, W.1    Deangelis, P.L.2
  • 29
    • 65349085618 scopus 로고    scopus 로고
    • Design of biologically active heparan sulfate and heparin using an enzyme-based approach
    • Peterson, S., Frick, A., and Liu, J. (2009) Design of biologically active heparan sulfate and heparin using an enzyme-based approach. Nat Prod. Rep. 26, 610-627
    • (2009) Nat Prod. Rep. , vol.26 , pp. 610-627
    • Peterson, S.1    Frick, A.2    Liu, J.3
  • 30
    • 84867748658 scopus 로고    scopus 로고
    • Understanding substrate specificity of the heparan sulfate sulfotransferases by an integrated biosynthesis and crystallographic approach
    • Liu, J., Moon, A. F., Sheng, J., and Pedersen, L. C. (2012) Understanding substrate specificity of the heparan sulfate sulfotransferases by an integrated biosynthesis and crystallographic approach. Curr. Opin. Struct. Biol. 22, 550-557
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 550-557
    • Liu, J.1    Moon, A.F.2    Sheng, J.3    Pedersen, L.C.4
  • 31
    • 84862275889 scopus 로고    scopus 로고
    • Uncovering biphasic catalytic mode of C5-epimerase in heparan sulfate biosynthesis
    • Sheng, J., Xu, Y., Dulaney, S. B., Huang, X., and Liu, J. (2012) Uncovering biphasic catalytic mode of C5-epimerase in heparan sulfate biosynthesis. J. Biol. Chem. 287, 20996-21002
    • (2012) J. Biol. Chem. , vol.287 , pp. 20996-21002
    • Sheng, J.1    Xu, Y.2    Dulaney, S.B.3    Huang, X.4    Liu, J.5
  • 33
    • 2442426180 scopus 로고    scopus 로고
    • Epidermal growth factor induces fibroblast contractility and motility via a protein kinase cS-dependent pathway
    • Iwabu, A., Smith, K., Allen, F. D., Lauffenburger, D. A., and Wells, A. (2004) Epidermal growth factor induces fibroblast contractility and motility via a protein kinase cS-dependent pathway. J. Biol. Chem. 279, 14551-14560
    • (2004) J. Biol. Chem. , vol.279 , pp. 14551-14560
    • Iwabu, A.1    Smith, K.2    Allen, F.D.3    Lauffenburger, D.A.4    Wells, A.5
  • 34
    • 0141666454 scopus 로고    scopus 로고
    • Fibroblast growth factor signaling controlling osteoblast differentiation
    • Marie, P. J. (2003) Fibroblast growth factor signaling controlling osteoblast differentiation. Gene 316, 23-32
    • (2003) Gene , vol.316 , pp. 23-32
    • Marie, P.J.1
  • 35
    • 0029793371 scopus 로고    scopus 로고
    • During angiogenesis, vascular endothelial growth factor and basic fibroblast growth factor regulate natural killer cell adhesion to tumor endothelium
    • Melder, R. J., Koenig, G. C, Witwer, B. P., Safabakhsh, N., Munn, L. L., and Jain, R. K. (1996) During angiogenesis, vascular endothelial growth factor and basic fibroblast growth factor regulate natural killer cell adhesion to tumor endothelium. Nat. Med. 2, 992-997
    • (1996) Nat. Med. , vol.2 , pp. 992-997
    • Melder, R.J.1    Koenig, G.C.2    Witwer, B.P.3    Safabakhsh, N.4    Munn, L.L.5    Jain, R.K.6
  • 36
    • 33845950805 scopus 로고    scopus 로고
    • The fibroblast growth factor receptor acid box is essential of interactions with N-cadherin and all of the major isoforms of neural cell adhesion molecule
    • Sanchez-Heras, E., Howell, F. V., Williams, G., and Doherty, P. (2006) The fibroblast growth factor receptor acid box is essential of interactions with N-cadherin and all of the major isoforms of neural cell adhesion molecule. J. Biol. Chem. 281, 35208-35216
    • (2006) J. Biol. Chem. , vol.281 , pp. 35208-35216
    • Sanchez-Heras, E.1    Howell, F.V.2    Williams, G.3    Doherty, P.4
  • 39
    • 18144423534 scopus 로고    scopus 로고
    • Structural basis for fibroblast growth factor receptor activation
    • Mohammadi, M., Olsen, S. K., and Ibrahimi, O. A. (2005) Structural basis for fibroblast growth factor receptor activation. Cytokine Growth Factor Rev. 16, 107-137
    • (2005) Cytokine Growth Factor Rev. , vol.16 , pp. 107-137
    • Mohammadi, M.1    Olsen, S.K.2    Ibrahimi, O.A.3
  • 40
    • 1942470528 scopus 로고    scopus 로고
    • Kinetic model for FGF, FGFR, and proteoglycan signal transduction complex assembly
    • Ibrahimi, O. A., Zhang, F., Hrstka, S. C, Mohammadi, M., and Linhardt, R. J. (2004) Kinetic model for FGF, FGFR, and proteoglycan signal transduction complex assembly. Biochemistry 43, 4724-4730
    • (2004) Biochemistry , vol.43 , pp. 4724-4730
    • Ibrahimi, O.A.1    Zhang, F.2    Hrstka, S.C.3    Mohammadi, M.4    Linhardt, R.J.5
  • 41
    • 84876372433 scopus 로고    scopus 로고
    • Cooperative heparin-mediated oligomerization of fibroblast growth fac-tor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes
    • Brown, A., Robinson, C. J., Gallagher, J. T., and Blundell, T. L. (2013) Cooperative heparin-mediated oligomerization of fibroblast growth fac-tor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes. Bio-phys. J. 104, 1720-1730
    • (2013) Bio-phys. J. , vol.104 , pp. 1720-1730
    • Brown, A.1    Robinson, C.J.2    Gallagher, J.T.3    Blundell, T.L.4
  • 42
    • 0026649742 scopus 로고
    • Fibroblast growth factor receptor tyrosine kinases. Molecular analysis and signal transduction
    • Jaye, M., Schlessinger, J., andDionne, C.A. (1992) Fibroblast growth factor receptor tyrosine kinases. Molecular analysis and signal transduction. Biochim. Biophys. Acta 1135, 185-199
    • (1992) Biochim. Biophys. Acta , vol.1135 , pp. 185-199
    • Jaye, M.1    Schlessinger, J.2    Dionne, C.A.3
  • 43
    • 0035443891 scopus 로고    scopus 로고
    • Order out of complexity. Protein structures that interact with heparin
    • Mulloy, B., and Linhardt, R. J. (2001) Order out of complexity. Protein structures that interact with heparin. Curr. Opin. Struct. Biol. 11, 623-628
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 623-628
    • Mulloy, B.1    Linhardt, R.J.2
  • 44
    • 0037047348 scopus 로고    scopus 로고
    • Fibroblast growth factors 1 and 2 interact differently with heparin/heparan sulfate. Implications for dynamic assembly of a ternary signaling complex
    • Powell, A. K., Fernig, D. G., and Turnbull, J. E. (2002) Fibroblast growth factors 1 and 2 interact differently with heparin/heparan sulfate. Implications for dynamic assembly of a ternary signaling complex. J. Biol. Chem. 277, 28554-28563
    • (2002) J. Biol. Chem. , vol.277 , pp. 28554-28563
    • Powell, A.K.1    Fernig, D.G.2    Turnbull, J.E.3
  • 45
    • 0028068096 scopus 로고
    • Distinct role of 2-O-N-, and 6-O-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble FGF receptor-1
    • Rusnati, M., Coltrini, D., Caccia, P., Dell'Era, P., Zoppetti, G., Oreste, P., Valsasina, B., and Presta, M. (1994) Distinct role of 2-O-, N-, and 6-O-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble FGF receptor-1. Biochem. Biophys. Res. Commun. 203, 450-458
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 450-458
    • Rusnati, M.1    Coltrini, D.2    Caccia, P.3    Dell'Era, P.4    Zoppetti, G.5    Oreste, P.6    Valsasina, B.7    Presta, M.8
  • 49
    • 0026665252 scopus 로고
    • Ligand specificity and heparin dependence of fibroblast growth factor receptors 1 and 3
    • Ornitz, D. M., and Leder, P. (1992) Ligand specificity and heparin dependence of fibroblast growth factor receptors 1 and 3. J. Biol. Chem. 267, 16305-16311
    • (1992) J. Biol. Chem. , vol.267 , pp. 16305-16311
    • Ornitz, D.M.1    Leder, P.2
  • 51
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini, L., Burke, D. F., von Delft, F., Mulloy, B., and Blundell, T. L. (2000) Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 407, 1029-1034
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 52
    • 79957607304 scopus 로고    scopus 로고
    • Highly sulfated nonreducing end-derived heparan sulfate domains bind fibroblast growth factor-2 with high affinity and are enriched in biologically active fractions
    • Naimy, H, Buczek-Thomas, J. A., Nugent, M. A., Leymarie, N., and Zaia, J. (2011) Highly sulfated nonreducing end-derived heparan sulfate domains bind fibroblast growth factor-2 with high affinity and are enriched in biologically active fractions. J. Biol. Chem. 286, 19311-19319
    • (2011) J. Biol. Chem. , vol.286 , pp. 19311-19319
    • Naimy, H.1    Buczek-Thomas, J.A.2    Nugent, M.A.3    Leymarie, N.4    Zaia, J.5
  • 53
    • 84865235998 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of heparin oligosaccharides with both anti-factor Xa and anti-factor IIa activities
    • Xu, Y., Pempe, E. H, and Liu, J. (2012) Chemoenzymatic synthesis of heparin oligosaccharides with both anti-factor Xa and anti-factor IIa activities. J. Biol. Chem. 287, 29054-29061
    • (2012) J. Biol. Chem. , vol.287 , pp. 29054-29061
    • Xu, Y.1    Pempe, E.H.2    Liu, J.3
  • 54
    • 84857710124 scopus 로고    scopus 로고
    • Structure/function analysis of Pasteurella multocida heparosan synthases: Toward defining enzyme specificity and engineering novel catalysts
    • Otto, N. J., Green, D. E., Masuko, S., Mayer, A., Tanner, M. E., Linhardt, R. J., and DeAngelis, P. L. (2012) Structure/function analysis of Pasteurella multocida heparosan synthases: toward defining enzyme specificity and engineering novel catalysts. J. Biol. Chem. 287, 7203-7212
    • (2012) J. Biol. Chem. , vol.287 , pp. 7203-7212
    • Otto, N.J.1    Green, D.E.2    Masuko, S.3    Mayer, A.4    Tanner, M.E.5    Linhardt, R.J.6    Deangelis, P.L.7
  • 55
    • 0031799877 scopus 로고    scopus 로고
    • Conformational changes and anticoagulant activity of chondroitin sulfate following its O-sulfonation
    • Maruyama, T., Toida, T., Imanari, T., Yu, G., and Linhardt, R. J. (1998) Conformational changes and anticoagulant activity of chondroitin sulfate following its O-sulfonation. Carbohydr. Res. 306, 35-43
    • (1998) Carbohydr. Res. , vol.306 , pp. 35-43
    • Maruyama, T.1    Toida, T.2    Imanari, T.3    Yu, G.4    Linhardt, R.J.5
  • 56
    • 84881189446 scopus 로고    scopus 로고
    • N-sulfotestosteronan, a novel substrate for heparan sulfate 6-O-sulfotransferases and its analysis by oxidative degradation
    • Li, G., Masuko, S., Green, D. E., Xu, Y., Li, L., Zhang, F., Xue, C, Liu, J., DeAngelis, P. L., and Linhardt, R. J. (2013) N-sulfotestosteronan, a novel substrate for heparan sulfate 6-O-sulfotransferases and its analysis by oxidative degradation. Biopolymers 99, 675-685
    • (2013) Biopolymers , vol.99 , pp. 675-685
    • Li, G.1    Masuko, S.2    Green, D.E.3    Xu, Y.4    Li, L.5    Zhang, F.6    Xue, C.7    Liu, J.8    Deangelis, P.L.9    Linhardt, R.J.10
  • 57
    • 84856229594 scopus 로고    scopus 로고
    • Disaccharide analysis of glycosaminoglycan mixtures by ultra-high-performance liquid-chromatography-mass spectrometry
    • Yang, B., Chang, Y., Weyers, A. M., Sterner, E., and Linhardt, R. J. (2012) Disaccharide analysis of glycosaminoglycan mixtures by ultra-high-performance liquid-chromatography-mass spectrometry. J. Chromatogr. A. 1225, 91-98
    • (2012) J. Chromatogr. A. , vol.1225 , pp. 91-98
    • Yang, B.1    Chang, Y.2    Weyers, A.M.3    Sterner, E.4    Linhardt, R.J.5
  • 58
    • 84890449786 scopus 로고    scopus 로고
    • FGF-FGFR signaling mediated through glycosaminoglycans in micro-titer plate and cell-based microarray platforms
    • Sterner, E., Meli, L., Kwon, S. J., Dordick, J. S., and Linhardt, R. J. (2013) FGF-FGFR signaling mediated through glycosaminoglycans in micro-titer plate and cell-based microarray platforms. Biochemistry 52, 9009-9019
    • (2013) Biochemistry , vol.52 , pp. 9009-9019
    • Sterner, E.1    Meli, L.2    Kwon, S.J.3    Dordick, J.S.4    Linhardt, R.J.5
  • 60
    • 84867142135 scopus 로고    scopus 로고
    • Influence of a 3D microarray environment on human cell culture in drug screening systems
    • Meli L., Jordan E. T., Clark D. S., Linhardt R. J., and Dordick, J. S. (2012) Influence of a 3D microarray environment on human cell culture in drug screening systems. Biomaterials 33, 9087-9096
    • (2012) Biomaterials , vol.33 , pp. 9087-9096
    • Meli, L.1    Jordan, E.T.2    Clark, D.S.3    Linhardt, R.J.4    Dordick, J.S.5
  • 61
    • 84862778031 scopus 로고    scopus 로고
    • Synthetic heparin.Curr
    • Linhardt, R. J., and Liu, J. (2012) Synthetic heparin.Curr. Opin. Pharmacol. 12, 217-219
    • (2012) Opin. Pharmacol. , vol.12 , pp. 217-219
    • Linhardt, R.J.1    Liu, J.2


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