메뉴 건너뛰기




Volumn 64, Issue 12, 2012, Pages 1078-1089

Biomimetic hydrogels for controlled biomolecule delivery to augment bone regeneration

Author keywords

Biomimetic hydrogels; Bone; Controlled delivery; ECM mimicking; Growth factors

Indexed keywords

ADVERSE SIDE EFFECTS; AFFINITY BINDING; BIOMIMETIC HYDROGELS; BONE DEFECT; BONE MORPHOGENETIC PROTEINS; BONE REGENERATION; CLINICAL PROBLEMS; CONTROLLED DELIVERY; COVALENT GRAFTING; DYNAMIC INTERACTION; ECM-MIMICKING; EXTRACELLULAR MATRICES; FUTURE TECHNOLOGIES; GOLD STANDARDS; GROWTH FACTOR; ORDERS OF MAGNITUDE; PHYSIOLOGICAL DOSE; PROTEIN THERAPEUTICS; SOLID-PHASE; TREATMENT COSTS;

EID: 84865282959     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2012.03.010     Document Type: Review
Times cited : (162)

References (170)
  • 1
    • 36349024668 scopus 로고    scopus 로고
    • Current and future clinical applications of bone morphogenetic proteins in orthopaedic trauma surgery
    • Bishop G.B., Einhorn T.A. Current and future clinical applications of bone morphogenetic proteins in orthopaedic trauma surgery. Int. Orthop. 2007, 31:721-727.
    • (2007) Int. Orthop. , vol.31 , pp. 721-727
    • Bishop, G.B.1    Einhorn, T.A.2
  • 2
    • 20144388313 scopus 로고    scopus 로고
    • Impact of smoking on fracture healing and risk of complications in limb-threatening open tibia fractures
    • Castillo R.C., Bosse M.J., MacKenzie E.J., Patterson B.M. Impact of smoking on fracture healing and risk of complications in limb-threatening open tibia fractures. J. Orthop. Trauma 2005, 19:151-157.
    • (2005) J. Orthop. Trauma , vol.19 , pp. 151-157
    • Castillo, R.C.1    Bosse, M.J.2    MacKenzie, E.J.3    Patterson, B.M.4
  • 7
    • 46749135647 scopus 로고    scopus 로고
    • The management of ankle fractures in patients with diabetes
    • Wukich D.K., Kline A.J. The management of ankle fractures in patients with diabetes. J. Bone Joint Surg. Am. 2008, 90:1570-1578.
    • (2008) J. Bone Joint Surg. Am. , vol.90 , pp. 1570-1578
    • Wukich, D.K.1    Kline, A.J.2
  • 9
    • 0031834195 scopus 로고    scopus 로고
    • Postoperative drains at the donor sites of iliac-crest bone grafts. A prospective, randomized study of morbidity at the donor site in patients who had a traumatic injury of the spine
    • Sasso R.C., Williams J.I., Dimasi N., Meyer P.R. Postoperative drains at the donor sites of iliac-crest bone grafts. A prospective, randomized study of morbidity at the donor site in patients who had a traumatic injury of the spine. J. Bone Joint Surg. Am. 1998, 80:631-635.
    • (1998) J. Bone Joint Surg. Am. , vol.80 , pp. 631-635
    • Sasso, R.C.1    Williams, J.I.2    Dimasi, N.3    Meyer, P.R.4
  • 10
    • 0242659880 scopus 로고    scopus 로고
    • Collagen sponges for bone regeneration with rhBMP-2
    • Geiger M., Li R.H., Friess W. Collagen sponges for bone regeneration with rhBMP-2. Adv. Drug Deliv. Rev. 2003, 55:1613-1629.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1613-1629
    • Geiger, M.1    Li, R.H.2    Friess, W.3
  • 12
    • 72749117438 scopus 로고    scopus 로고
    • Spatiotemporal delivery strategies for promoting musculoskeletal tissue regeneration
    • Guldberg R.E. Spatiotemporal delivery strategies for promoting musculoskeletal tissue regeneration. J. Bone Miner. Res. 2009, 24:1507-1511.
    • (2009) J. Bone Miner. Res. , vol.24 , pp. 1507-1511
    • Guldberg, R.E.1
  • 13
    • 0035400037 scopus 로고    scopus 로고
    • Delivering on the promise of bone morphogenetic proteins
    • Li R.H., Wozney J.M. Delivering on the promise of bone morphogenetic proteins. Trends Biotechnol. 2001, 19:255-265.
    • (2001) Trends Biotechnol. , vol.19 , pp. 255-265
    • Li, R.H.1    Wozney, J.M.2
  • 16
    • 34447343823 scopus 로고    scopus 로고
    • Bone morphogenetic proteins in clinical applications
    • Gautschi O.P., Frey S.P., Zellweger R. Bone morphogenetic proteins in clinical applications. ANZ J. Surg. 2007, 77:626-631.
    • (2007) ANZ J. Surg. , vol.77 , pp. 626-631
    • Gautschi, O.P.1    Frey, S.P.2    Zellweger, R.3
  • 17
    • 77649127531 scopus 로고    scopus 로고
    • BMPs: options, indications, and effectiveness
    • Giannoudis P.V., Dinopoulos H.T. BMPs: options, indications, and effectiveness. J. Orthop. Trauma 2010, 24(Suppl. 1):S9-S16.
    • (2010) J. Orthop. Trauma , vol.24 , Issue.SUPPL. 1
    • Giannoudis, P.V.1    Dinopoulos, H.T.2
  • 18
    • 0042626183 scopus 로고    scopus 로고
    • Clinical applications of recombinant human BMPs: early experience and future development
    • Einhorn T.A. Clinical applications of recombinant human BMPs: early experience and future development. J. Bone Joint Surg. Am. 2003, 85-A(Suppl. 3):82-88.
    • (2003) J. Bone Joint Surg. Am. , Issue.SUPPL. 3 , pp. 82-88
    • Einhorn, T.A.1
  • 19
    • 79959950769 scopus 로고    scopus 로고
    • A critical review of recombinant human bone morphogenetic protein-2 trials in spinal surgery: emerging safety concerns and lessons learned
    • Carragee E.J., Hurwitz E.L., Weiner B.K. A critical review of recombinant human bone morphogenetic protein-2 trials in spinal surgery: emerging safety concerns and lessons learned. Spine J. 2011, 11:471-491.
    • (2011) Spine J. , vol.11 , pp. 471-491
    • Carragee, E.J.1    Hurwitz, E.L.2    Weiner, B.K.3
  • 21
    • 0242606216 scopus 로고    scopus 로고
    • Therapeutic angiogenesis in cardiovascular disease
    • Simons M., Ware J.A. Therapeutic angiogenesis in cardiovascular disease. Nat. Rev. Drug Discov. 2003, 2:863-871.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 863-871
    • Simons, M.1    Ware, J.A.2
  • 22
    • 0042626603 scopus 로고    scopus 로고
    • Polymeric growth factor delivery strategies for tissue engineering
    • Chen R.R., Mooney D.J. Polymeric growth factor delivery strategies for tissue engineering. Pharm. Res. 2003, 20:1103-1112.
    • (2003) Pharm. Res. , vol.20 , pp. 1103-1112
    • Chen, R.R.1    Mooney, D.J.2
  • 25
    • 66249146049 scopus 로고    scopus 로고
    • Complexity in biomaterials for tissue engineering
    • Place E.S., Evans N.D., Stevens M.M. Complexity in biomaterials for tissue engineering. Nat. Mater. 2009, 8:457-470.
    • (2009) Nat. Mater. , vol.8 , pp. 457-470
    • Place, E.S.1    Evans, N.D.2    Stevens, M.M.3
  • 26
    • 40549131272 scopus 로고    scopus 로고
    • Extracellular matrix dynamics in development and regenerative medicine
    • Daley W.P., Peters S.B., Larsen M. Extracellular matrix dynamics in development and regenerative medicine. J. Cell Sci. 2008, 121:255-264.
    • (2008) J. Cell Sci. , vol.121 , pp. 255-264
    • Daley, W.P.1    Peters, S.B.2    Larsen, M.3
  • 27
    • 0023080985 scopus 로고
    • Dynamic reciprocity: how do extracellular matrix and hormones direct gene expression?
    • Bissell M.J., Aggeler J. Dynamic reciprocity: how do extracellular matrix and hormones direct gene expression?. Prog. Clin. Biol. Res. 1987, 249:251-262.
    • (1987) Prog. Clin. Biol. Res. , vol.249 , pp. 251-262
    • Bissell, M.J.1    Aggeler, J.2
  • 28
    • 0020456385 scopus 로고
    • How does the extracellular matrix direct gene expression?
    • Bissell M.J., Hall H.G., Parry G. How does the extracellular matrix direct gene expression?. J. Theor. Biol. 1982, 99:31-68.
    • (1982) J. Theor. Biol. , vol.99 , pp. 31-68
    • Bissell, M.J.1    Hall, H.G.2    Parry, G.3
  • 32
    • 54249128761 scopus 로고    scopus 로고
    • Regulation of angiogenesis: apoptotic cues from the ECM
    • Cheresh D.A., Stupack D.G. Regulation of angiogenesis: apoptotic cues from the ECM. Oncogene 2008, 27:6285-6298.
    • (2008) Oncogene , vol.27 , pp. 6285-6298
    • Cheresh, D.A.1    Stupack, D.G.2
  • 33
    • 51449105239 scopus 로고    scopus 로고
    • Biological basis of bone formation, remodeling, and repair-part II: extracellular matrix
    • Allori A.C., Sailon A.M., Warren S.M. Biological basis of bone formation, remodeling, and repair-part II: extracellular matrix. Tissue Eng. Part B Rev. 2008, 14:275-283.
    • (2008) Tissue Eng. Part B Rev. , vol.14 , pp. 275-283
    • Allori, A.C.1    Sailon, A.M.2    Warren, S.M.3
  • 34
    • 34247610845 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans fine-tune mammalian physiology
    • Bishop J.R., Schuksz M., Esko J.D. Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature 2007, 446:1030-1037.
    • (2007) Nature , vol.446 , pp. 1030-1037
    • Bishop, J.R.1    Schuksz, M.2    Esko, J.D.3
  • 35
    • 21744450786 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans: the sweet side of development
    • Hacker U., Nybakken K., Perrimon N. Heparan sulphate proteoglycans: the sweet side of development. Nat. Rev. Mol. Cell Biol. 2005, 6:530-541.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 530-541
    • Hacker, U.1    Nybakken, K.2    Perrimon, N.3
  • 36
    • 36048958903 scopus 로고    scopus 로고
    • Growth factor binding to the pericellular matrix and its importance in tissue engineering
    • Macri L., Silverstein D., Clark R.A. Growth factor binding to the pericellular matrix and its importance in tissue engineering. Adv. Drug Deliv. Rev. 2007, 59:1366-1381.
    • (2007) Adv. Drug Deliv. Rev. , vol.59 , pp. 1366-1381
    • Macri, L.1    Silverstein, D.2    Clark, R.A.3
  • 37
    • 70249092883 scopus 로고    scopus 로고
    • Free energy calculations of glycosaminoglycan-protein interactions
    • Gandhi N.S., Mancera R.L. Free energy calculations of glycosaminoglycan-protein interactions. Glycobiology 2009, 19:1103-1115.
    • (2009) Glycobiology , vol.19 , pp. 1103-1115
    • Gandhi, N.S.1    Mancera, R.L.2
  • 38
    • 0021265097 scopus 로고
    • Heparin binds endothelial cell growth factor, the principal endothelial cell mitogen in bovine brain
    • Maciag T., Mehlman T., Friesel R., Schreiber A.B. Heparin binds endothelial cell growth factor, the principal endothelial cell mitogen in bovine brain. Science 1984, 225:932-935.
    • (1984) Science , vol.225 , pp. 932-935
    • Maciag, T.1    Mehlman, T.2    Friesel, R.3    Schreiber, A.B.4
  • 39
    • 0026776936 scopus 로고
    • Transforming growth factor-beta 1 is a heparin-binding protein: identification of putative heparin-binding regions and isolation of heparins with varying affinity for TGF-beta 1
    • McCaffrey T.A., Falcone D.J., Du B. Transforming growth factor-beta 1 is a heparin-binding protein: identification of putative heparin-binding regions and isolation of heparins with varying affinity for TGF-beta 1. J. Cell. Physiol. 1992, 152:430-440.
    • (1992) J. Cell. Physiol. , vol.152 , pp. 430-440
    • McCaffrey, T.A.1    Falcone, D.J.2    Du, B.3
  • 40
    • 0026648812 scopus 로고
    • Kinetics of basic fibroblast growth factor binding to its receptor and heparan sulfate proteoglycan: a mechanism for cooperactivity
    • Nugent M.A., Edelman E.R. Kinetics of basic fibroblast growth factor binding to its receptor and heparan sulfate proteoglycan: a mechanism for cooperactivity. Biochemistry 1992, 31:8876-8883.
    • (1992) Biochemistry , vol.31 , pp. 8876-8883
    • Nugent, M.A.1    Edelman, E.R.2
  • 42
    • 0037108152 scopus 로고    scopus 로고
    • Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis
    • Ruhrberg C., Gerhardt H., Golding M., Watson R., Ioannidou S., Fujisawa H., Betsholtz C., Shima D.T. Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis. Genes Dev. 2002, 16:2684-2698.
    • (2002) Genes Dev. , vol.16 , pp. 2684-2698
    • Ruhrberg, C.1    Gerhardt, H.2    Golding, M.3    Watson, R.4    Ioannidou, S.5    Fujisawa, H.6    Betsholtz, C.7    Shima, D.T.8
  • 44
    • 0033830523 scopus 로고    scopus 로고
    • Isoforms of vascular endothelial growth factor act in a coordinate fashion to recruit and expand tumor vasculature
    • Grunstein J., Masbad J.J., Hickey R., Giordano F., Johnson R.S. Isoforms of vascular endothelial growth factor act in a coordinate fashion to recruit and expand tumor vasculature. Mol. Cell. Biol. 2000, 20:7282-7291.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7282-7291
    • Grunstein, J.1    Masbad, J.J.2    Hickey, R.3    Giordano, F.4    Johnson, R.S.5
  • 45
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: not just pretty fibrils
    • Hynes R.O. The extracellular matrix: not just pretty fibrils. Science 2009, 326:1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 46
    • 0024413453 scopus 로고
    • EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation?
    • Engel J. EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation?. FEBS Lett. 1989, 251:1-7.
    • (1989) FEBS Lett. , vol.251 , pp. 1-7
    • Engel, J.1
  • 49
    • 0037437146 scopus 로고    scopus 로고
    • Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution
    • Schenk S., Hintermann E., Bilban M., Koshikawa N., Hojilla C., Khokha R., Quaranta V. Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution. J. Cell Biol. 2003, 161:197-209.
    • (2003) J. Cell Biol. , vol.161 , pp. 197-209
    • Schenk, S.1    Hintermann, E.2    Bilban, M.3    Koshikawa, N.4    Hojilla, C.5    Khokha, R.6    Quaranta, V.7
  • 50
    • 25844440918 scopus 로고    scopus 로고
    • A protein canyon in the FGF-FGF receptor dimer selects from an a la carte menu of heparan sulfate motifs
    • Mohammadi M., Olsen S.K., Goetz R. A protein canyon in the FGF-FGF receptor dimer selects from an a la carte menu of heparan sulfate motifs. Curr. Opin. Struct. Biol. 2005, 15:506-516.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 506-516
    • Mohammadi, M.1    Olsen, S.K.2    Goetz, R.3
  • 52
    • 67649354634 scopus 로고    scopus 로고
    • Extracellular microfibrils in vertebrate development and disease processes
    • Ramirez F., Dietz H.C. Extracellular microfibrils in vertebrate development and disease processes. J. Biol. Chem. 2009, 284:14677-14681.
    • (2009) J. Biol. Chem. , vol.284 , pp. 14677-14681
    • Ramirez, F.1    Dietz, H.C.2
  • 53
    • 0141756154 scopus 로고    scopus 로고
    • Interactions between growth factor receptors and adhesion molecules: breaking the rules
    • Comoglio P.M., Boccaccio C., Trusolino L. Interactions between growth factor receptors and adhesion molecules: breaking the rules. Curr. Opin. Cell Biol. 2003, 15:565-571.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 565-571
    • Comoglio, P.M.1    Boccaccio, C.2    Trusolino, L.3
  • 54
    • 62149091091 scopus 로고    scopus 로고
    • Signal co-operation between integrins and other receptor systems
    • Streuli C.H., Akhtar N. Signal co-operation between integrins and other receptor systems. Biochem. J. 2009, 418:491-506.
    • (2009) Biochem. J. , vol.418 , pp. 491-506
    • Streuli, C.H.1    Akhtar, N.2
  • 55
    • 0030814976 scopus 로고    scopus 로고
    • Alphavbeta3 integrin associates with activated insulin and PDGFbeta receptors and potentiates the biological activity of PDGF
    • Schneller M., Vuori K., Ruoslahti E. Alphavbeta3 integrin associates with activated insulin and PDGFbeta receptors and potentiates the biological activity of PDGF. EMBO J. 1997, 16:5600-5607.
    • (1997) EMBO J. , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 56
    • 4444249880 scopus 로고    scopus 로고
    • Alpha(v)beta(3) Integrin interacts with the transforming growth factor beta (TGFbeta) type II receptor to potentiate the proliferative effects of TGFbeta1 in living human lung fibroblasts
    • Scaffidi A.K., Petrovic N., Moodley Y.P., Fogel-Petrovic M., Kroeger K.M., Seeber R.M., Eidne K.A., Thompson P.J., Knight D.A. alpha(v)beta(3) Integrin interacts with the transforming growth factor beta (TGFbeta) type II receptor to potentiate the proliferative effects of TGFbeta1 in living human lung fibroblasts. J. Biol. Chem. 2004, 279:37726-37733.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37726-37733
    • Scaffidi, A.K.1    Petrovic, N.2    Moodley, Y.P.3    Fogel-Petrovic, M.4    Kroeger, K.M.5    Seeber, R.M.6    Eidne, K.A.7    Thompson, P.J.8    Knight, D.A.9
  • 57
    • 0033558087 scopus 로고    scopus 로고
    • Role of alphavbeta3 integrin in the activation of vascular endothelial growth factor receptor-2
    • Soldi R., Mitola S., Strasly M., Defilippi P., Tarone G., Bussolino F. Role of alphavbeta3 integrin in the activation of vascular endothelial growth factor receptor-2. EMBO J. 1999, 18:882-892.
    • (1999) EMBO J. , vol.18 , pp. 882-892
    • Soldi, R.1    Mitola, S.2    Strasly, M.3    Defilippi, P.4    Tarone, G.5    Bussolino, F.6
  • 58
    • 0032538798 scopus 로고    scopus 로고
    • Integrins induce activation of EGF receptor: role in MAP kinase induction and adhesion-dependent cell survival
    • Moro L., Venturino M., Bozzo C., Silengo L., Altruda F., Beguinot L., Tarone G., Defilippi P. Integrins induce activation of EGF receptor: role in MAP kinase induction and adhesion-dependent cell survival. EMBO J. 1998, 17:6622-6632.
    • (1998) EMBO J. , vol.17 , pp. 6622-6632
    • Moro, L.1    Venturino, M.2    Bozzo, C.3    Silengo, L.4    Altruda, F.5    Beguinot, L.6    Tarone, G.7    Defilippi, P.8
  • 60
    • 0035977147 scopus 로고    scopus 로고
    • A signaling adapter function for alpha6beta4 integrin in the control of HGF-dependent invasive growth
    • Trusolino L., Bertotti A., Comoglio P.M. A signaling adapter function for alpha6beta4 integrin in the control of HGF-dependent invasive growth. Cell 2001, 107:643-654.
    • (2001) Cell , vol.107 , pp. 643-654
    • Trusolino, L.1    Bertotti, A.2    Comoglio, P.M.3
  • 61
    • 0345687500 scopus 로고    scopus 로고
    • Positional control of cell fate through joint integrin/receptor protein kinase signaling
    • Giancotti F.G., Tarone G. Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annu. Rev. Cell Dev. Biol. 2003, 19:173-206.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 173-206
    • Giancotti, F.G.1    Tarone, G.2
  • 62
    • 79955528442 scopus 로고    scopus 로고
    • Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor
    • Kim S.H., Turnbull J., Guimond S. Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor. J. Endocrinol. 2011, 209:139-151.
    • (2011) J. Endocrinol. , vol.209 , pp. 139-151
    • Kim, S.H.1    Turnbull, J.2    Guimond, S.3
  • 64
    • 0037376627 scopus 로고    scopus 로고
    • Fracture healing as a post-natal developmental process: molecular, spatial, and temporal aspects of its regulation
    • Gerstenfeld L.C., Cullinane D.M., Barnes G.L., Graves D.T., Einhorn T.A. Fracture healing as a post-natal developmental process: molecular, spatial, and temporal aspects of its regulation. J. Cell. Biochem. 2003, 88:873-884.
    • (2003) J. Cell. Biochem. , vol.88 , pp. 873-884
    • Gerstenfeld, L.C.1    Cullinane, D.M.2    Barnes, G.L.3    Graves, D.T.4    Einhorn, T.A.5
  • 65
    • 0026544215 scopus 로고
    • Degradation of collagen in the bone-resorbing compartment underlying the osteoclast involves both cysteine-proteinases and matrix metalloproteinases
    • Everts V., Delaisse J.M., Korper W., Niehof A., Vaes G., Beertsen W. Degradation of collagen in the bone-resorbing compartment underlying the osteoclast involves both cysteine-proteinases and matrix metalloproteinases. J. Cell. Physiol. 1992, 150:221-231.
    • (1992) J. Cell. Physiol. , vol.150 , pp. 221-231
    • Everts, V.1    Delaisse, J.M.2    Korper, W.3    Niehof, A.4    Vaes, G.5    Beertsen, W.6
  • 67
    • 0023111721 scopus 로고
    • In vitro evidence that bone formation may be coupled to resorption by release of mitogen(s) from resorbing bone
    • Farley J.R., Tarbaux N., Murphy L.A., Masuda T., Baylink D.J. In vitro evidence that bone formation may be coupled to resorption by release of mitogen(s) from resorbing bone. Metabolism 1987, 36:314-321.
    • (1987) Metabolism , vol.36 , pp. 314-321
    • Farley, J.R.1    Tarbaux, N.2    Murphy, L.A.3    Masuda, T.4    Baylink, D.J.5
  • 70
    • 77649187986 scopus 로고    scopus 로고
    • Immunolocalization of BMPs, BMP antagonists, receptors, and effectors during fracture repair
    • Yu Y.Y., Lieu S., Lu C., Miclau T., Marcucio R.S., Colnot C. Immunolocalization of BMPs, BMP antagonists, receptors, and effectors during fracture repair. Bone 2010, 46:841-851.
    • (2010) Bone , vol.46 , pp. 841-851
    • Yu, Y.Y.1    Lieu, S.2    Lu, C.3    Miclau, T.4    Marcucio, R.S.5    Colnot, C.6
  • 71
    • 0031734171 scopus 로고    scopus 로고
    • The cell and molecular biology of fracture healing
    • Einhorn T.A. The cell and molecular biology of fracture healing. Clin. Orthop. Relat. Res. 1998, S7-S21.
    • (1998) Clin. Orthop. Relat. Res.
    • Einhorn, T.A.1
  • 73
    • 0026769957 scopus 로고
    • Regulation of fracture repair by growth factors
    • Bolander M.E. Regulation of fracture repair by growth factors. Proc. Soc. Exp. Biol. Med. 1992, 200:165-170.
    • (1992) Proc. Soc. Exp. Biol. Med. , vol.200 , pp. 165-170
    • Bolander, M.E.1
  • 74
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases
    • Whitelock J.M., Murdoch A.D., Iozzo R.V., Underwood P.A. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J. Biol. Chem. 1996, 271:10079-10086.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3    Underwood, P.A.4
  • 75
    • 34250019537 scopus 로고
    • Bone: formation by autoinduction
    • Urist M.R. Bone: formation by autoinduction. Science 1965, 150:893-899.
    • (1965) Science , vol.150 , pp. 893-899
    • Urist, M.R.1
  • 77
    • 0026721147 scopus 로고
    • The bone morphogenetic protein family and osteogenesis
    • Wozney J.M. The bone morphogenetic protein family and osteogenesis. Mol. Reprod. Dev. 1992, 32:160-167.
    • (1992) Mol. Reprod. Dev. , vol.32 , pp. 160-167
    • Wozney, J.M.1
  • 78
    • 33947109490 scopus 로고    scopus 로고
    • Therapeutic angiogenesis in the heart: protect and serve
    • Molin D., Post M.J. Therapeutic angiogenesis in the heart: protect and serve. Curr. Opin. Pharmacol. 2007, 7:158-163.
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 158-163
    • Molin, D.1    Post, M.J.2
  • 81
    • 78650842405 scopus 로고    scopus 로고
    • Growth factor delivery-based tissue engineering: general approaches and a review of recent developments
    • Lee K., Silva E.A., Mooney D.J. Growth factor delivery-based tissue engineering: general approaches and a review of recent developments. J. R. Soc. Interface 2011, 8:153-170.
    • (2011) J. R. Soc. Interface , vol.8 , pp. 153-170
    • Lee, K.1    Silva, E.A.2    Mooney, D.J.3
  • 82
    • 78049427358 scopus 로고    scopus 로고
    • Covalently immobilized platelet-derived growth factor-BB promotes angiogenesis in biomimetic poly(ethylene glycol) hydrogels
    • Saik J.E., Gould D.J., Watkins E.M., Dickinson M.E., West J.L. Covalently immobilized platelet-derived growth factor-BB promotes angiogenesis in biomimetic poly(ethylene glycol) hydrogels. Acta Biomater. 2011, 7:133-143.
    • (2011) Acta Biomater. , vol.7 , pp. 133-143
    • Saik, J.E.1    Gould, D.J.2    Watkins, E.M.3    Dickinson, M.E.4    West, J.L.5
  • 83
    • 0034076189 scopus 로고    scopus 로고
    • Mechanisms of angiogenesis and arteriogenesis
    • Carmeliet P. Mechanisms of angiogenesis and arteriogenesis. Nat. Med. 2000, 6:389-395.
    • (2000) Nat. Med. , vol.6 , pp. 389-395
    • Carmeliet, P.1
  • 87
    • 0142122292 scopus 로고    scopus 로고
    • Materials as morphogenetic guides in tissue engineering
    • Hubbell J.A. Materials as morphogenetic guides in tissue engineering. Curr. Opin. Biotechnol. 2003, 14:551-558.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 551-558
    • Hubbell, J.A.1
  • 88
    • 0032521332 scopus 로고    scopus 로고
    • Improved local delivery of TGF-beta2 by binding to injectable fibrillar collagen via difunctional polyethylene glycol
    • Bentz H., Schroeder J.A., Estridge T.D. Improved local delivery of TGF-beta2 by binding to injectable fibrillar collagen via difunctional polyethylene glycol. J. Biomed. Mater. Res. 1998, 39:539-548.
    • (1998) J. Biomed. Mater. Res. , vol.39 , pp. 539-548
    • Bentz, H.1    Schroeder, J.A.2    Estridge, T.D.3
  • 90
    • 0035284541 scopus 로고    scopus 로고
    • Tethered-TGF-beta increases extracellular matrix production of vascular smooth muscle cells
    • Mann B.K., Schmedlen R.H., West J.L. Tethered-TGF-beta increases extracellular matrix production of vascular smooth muscle cells. Biomaterials 2001, 22:439-444.
    • (2001) Biomaterials , vol.22 , pp. 439-444
    • Mann, B.K.1    Schmedlen, R.H.2    West, J.L.3
  • 91
    • 10644257537 scopus 로고    scopus 로고
    • Covalently immobilized gradients of bFGF on hydrogel scaffolds for directed cell migration
    • DeLong S.A., Moon J.J., West J.L. Covalently immobilized gradients of bFGF on hydrogel scaffolds for directed cell migration. Biomaterials 2005, 26:3227-3234.
    • (2005) Biomaterials , vol.26 , pp. 3227-3234
    • DeLong, S.A.1    Moon, J.J.2    West, J.L.3
  • 92
    • 0347413684 scopus 로고    scopus 로고
    • Effects of epidermal growth factor on fibroblast migration through biomimetic hydrogels
    • Gobin A.S., West J.L. Effects of epidermal growth factor on fibroblast migration through biomimetic hydrogels. Biotechnol. Prog. 2003, 19:1781-1785.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1781-1785
    • Gobin, A.S.1    West, J.L.2
  • 93
  • 94
    • 56449125956 scopus 로고    scopus 로고
    • Effect of grafting RGD and BMP-2 protein-derived peptides to a hydrogel substrate on osteogenic differentiation of marrow stromal cells
    • He X., Ma J., Jabbari E. Effect of grafting RGD and BMP-2 protein-derived peptides to a hydrogel substrate on osteogenic differentiation of marrow stromal cells. Langmuir 2008, 24:12508-12516.
    • (2008) Langmuir , vol.24 , pp. 12508-12516
    • He, X.1    Ma, J.2    Jabbari, E.3
  • 96
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: a review of problems and solutions
    • Veronese F.M. Peptide and protein PEGylation: a review of problems and solutions. Biomaterials 2001, 22:405-417.
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 98
    • 0032764946 scopus 로고    scopus 로고
    • Incorporation of heparin-binding peptides into fibrin gels enhances neurite extension: an example of designer matrices in tissue engineering
    • Sakiyama S.E., Schense J.C., Hubbell J.A. Incorporation of heparin-binding peptides into fibrin gels enhances neurite extension: an example of designer matrices in tissue engineering. FASEB J. 1999, 13:2214-2224.
    • (1999) FASEB J. , vol.13 , pp. 2214-2224
    • Sakiyama, S.E.1    Schense, J.C.2    Hubbell, J.A.3
  • 99
    • 0035344210 scopus 로고    scopus 로고
    • Development of growth factor fusion proteins for cell-triggered drug delivery
    • Sakiyama-Elbert S.E., Panitch A., Hubbell J.A. Development of growth factor fusion proteins for cell-triggered drug delivery. FASEB J. 2001, 15:1300-1302.
    • (2001) FASEB J. , vol.15 , pp. 1300-1302
    • Sakiyama-Elbert, S.E.1    Panitch, A.2    Hubbell, J.A.3
  • 100
    • 0032940534 scopus 로고    scopus 로고
    • Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa
    • Schense J.C., Hubbell J.A. Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa. Bioconjug. Chem. 1999, 10:75-81.
    • (1999) Bioconjug. Chem. , vol.10 , pp. 75-81
    • Schense, J.C.1    Hubbell, J.A.2
  • 103
    • 10044253411 scopus 로고    scopus 로고
    • Endothelial cell proliferation and progenitor maturation by fibrin-bound VEGF variants with differential susceptibilities to local cellular activity
    • Ehrbar M., Metters A., Zammaretti P., Hubbell J.A., Zisch A.H. Endothelial cell proliferation and progenitor maturation by fibrin-bound VEGF variants with differential susceptibilities to local cellular activity. J. Control. Release 2005, 101:93-109.
    • (2005) J. Control. Release , vol.101 , pp. 93-109
    • Ehrbar, M.1    Metters, A.2    Zammaretti, P.3    Hubbell, J.A.4    Zisch, A.H.5
  • 104
    • 38749138430 scopus 로고    scopus 로고
    • The role of actively released fibrin-conjugated VEGF for VEGF receptor 2 gene activation and the enhancement of angiogenesis
    • Ehrbar M., Zeisberger S.M., Raeber G.P., Hubbell J.A., Schnell C., Zisch A.H. The role of actively released fibrin-conjugated VEGF for VEGF receptor 2 gene activation and the enhancement of angiogenesis. Biomaterials 2008, 29:1720-1729.
    • (2008) Biomaterials , vol.29 , pp. 1720-1729
    • Ehrbar, M.1    Zeisberger, S.M.2    Raeber, G.P.3    Hubbell, J.A.4    Schnell, C.5    Zisch, A.H.6
  • 106
    • 1242317764 scopus 로고    scopus 로고
    • Engineered fibrin matrices for functional display of cell membrane-bound growth factor-like activities: study of angiogenic signaling by ephrin-B2
    • Zisch A.H., Zeisberger S.M., Ehrbar M., Djonov V., Weber C.C., Ziemiecki A., Pasquale E.B., Hubbell J.A. Engineered fibrin matrices for functional display of cell membrane-bound growth factor-like activities: study of angiogenic signaling by ephrin-B2. Biomaterials 2004, 25:3245-3257.
    • (2004) Biomaterials , vol.25 , pp. 3245-3257
    • Zisch, A.H.1    Zeisberger, S.M.2    Ehrbar, M.3    Djonov, V.4    Weber, C.C.5    Ziemiecki, A.6    Pasquale, E.B.7    Hubbell, J.A.8
  • 107
    • 12444280044 scopus 로고    scopus 로고
    • Heterophilic interactions between cell adhesion molecule L1 and alphavbeta3-integrin induce HUVEC process extension in vitro and angiogenesis in vivo
    • Hall H., Djonov V., Ehrbar M., Hoechli M., Hubbell J.A. Heterophilic interactions between cell adhesion molecule L1 and alphavbeta3-integrin induce HUVEC process extension in vitro and angiogenesis in vivo. Angiogenesis 2004, 7:213-223.
    • (2004) Angiogenesis , vol.7 , pp. 213-223
    • Hall, H.1    Djonov, V.2    Ehrbar, M.3    Hoechli, M.4    Hubbell, J.A.5
  • 108
    • 14244262503 scopus 로고    scopus 로고
    • Matrix-bound sixth Ig-like domain of cell adhesion molecule L1 acts as an angiogenic factor by ligating alphavbeta3-integrin and activating VEGF-R2
    • Hall H., Hubbell J.A. Matrix-bound sixth Ig-like domain of cell adhesion molecule L1 acts as an angiogenic factor by ligating alphavbeta3-integrin and activating VEGF-R2. Microvasc. Res. 2004, 68:169-178.
    • (2004) Microvasc. Res. , vol.68 , pp. 169-178
    • Hall, H.1    Hubbell, J.A.2
  • 109
    • 67651163419 scopus 로고    scopus 로고
    • The induction of cell alignment by covalently immobilized gradients of the 6th Ig-like domain of cell adhesion molecule L1 in 3D-fibrin matrices
    • Luhmann T., Hanseler P., Grant B., Hall H. The induction of cell alignment by covalently immobilized gradients of the 6th Ig-like domain of cell adhesion molecule L1 in 3D-fibrin matrices. Biomaterials 2009, 30:4503-4512.
    • (2009) Biomaterials , vol.30 , pp. 4503-4512
    • Luhmann, T.1    Hanseler, P.2    Grant, B.3    Hall, H.4
  • 110
    • 14844293090 scopus 로고    scopus 로고
    • Neurite extension and in vitro myelination within three-dimensional modified fibrin matrices
    • Pittier R., Sauthier F., Hubbell J.A., Hall H. Neurite extension and in vitro myelination within three-dimensional modified fibrin matrices. J. Neurobiol. 2005, 63:1-14.
    • (2005) J. Neurobiol. , vol.63 , pp. 1-14
    • Pittier, R.1    Sauthier, F.2    Hubbell, J.A.3    Hall, H.4
  • 112
    • 80055104248 scopus 로고    scopus 로고
    • Engineered insulin-like growth factor-1 for improved smooth muscle regeneration
    • Lorentz K.M., Yang L., Frey P., Hubbell J.A. Engineered insulin-like growth factor-1 for improved smooth muscle regeneration. Biomaterials 2012, 33:494-503.
    • (2012) Biomaterials , vol.33 , pp. 494-503
    • Lorentz, K.M.1    Yang, L.2    Frey, P.3    Hubbell, J.A.4
  • 114
    • 28244497338 scopus 로고    scopus 로고
    • Biomimetic delivery of keratinocyte growth factor upon cellular demand for accelerated wound healing in vitro and in vivo
    • Geer D.J., Swartz D.D., Andreadis S.T. Biomimetic delivery of keratinocyte growth factor upon cellular demand for accelerated wound healing in vitro and in vivo. Am. J. Pathol. 2005, 167:1575-1586.
    • (2005) Am. J. Pathol. , vol.167 , pp. 1575-1586
    • Geer, D.J.1    Swartz, D.D.2    Andreadis, S.T.3
  • 117
    • 67651232458 scopus 로고    scopus 로고
    • Controlling affinity binding with peptide-functionalized poly(ethylene glycol) hydrogels
    • Lin C.C., Anseth K.S. Controlling affinity binding with peptide-functionalized poly(ethylene glycol) hydrogels. Adv. Funct. Mater. 2009, 19:2325.
    • (2009) Adv. Funct. Mater. , vol.19 , pp. 2325
    • Lin, C.C.1    Anseth, K.S.2
  • 118
    • 69949145647 scopus 로고    scopus 로고
    • Biopolymer-based growth factor delivery for tissue repair: from natural concepts to engineered systems
    • Uebersax L., Merkle H.P., Meinel L. Biopolymer-based growth factor delivery for tissue repair: from natural concepts to engineered systems. Tissue Eng. Part B Rev. 2009, 15:263-289.
    • (2009) Tissue Eng. Part B Rev. , vol.15 , pp. 263-289
    • Uebersax, L.1    Merkle, H.P.2    Meinel, L.3
  • 119
    • 0034601101 scopus 로고    scopus 로고
    • Endothelial cell seeding of (heparinized) collagen matrices: effects of bFGF pre-loading on proliferation (after low density seeding) and pro-coagulant factors
    • Wissink M.J., Beernink R., Scharenborg N.M., Poot A.A., Engbers G.H., Beugeling T., van Aken W.G., Feijen J. Endothelial cell seeding of (heparinized) collagen matrices: effects of bFGF pre-loading on proliferation (after low density seeding) and pro-coagulant factors. J. Control. Release 2000, 67:141-155.
    • (2000) J. Control. Release , vol.67 , pp. 141-155
    • Wissink, M.J.1    Beernink, R.2    Scharenborg, N.M.3    Poot, A.A.4    Engbers, G.H.5    Beugeling, T.6    van Aken, W.G.7    Feijen, J.8
  • 120
    • 76749161775 scopus 로고    scopus 로고
    • Tissue substitutes with improved angiogenic capabilities: an in vitro investigation with endothelial cells and endothelial progenitor cells
    • Grieb G., Groger A., Piatkowski A., Markowicz M., Steffens G.C., Pallua N. Tissue substitutes with improved angiogenic capabilities: an in vitro investigation with endothelial cells and endothelial progenitor cells. Cells Tissues Organs 2010, 191:96-104.
    • (2010) Cells Tissues Organs , vol.191 , pp. 96-104
    • Grieb, G.1    Groger, A.2    Piatkowski, A.3    Markowicz, M.4    Steffens, G.C.5    Pallua, N.6
  • 121
    • 28944435673 scopus 로고    scopus 로고
    • Effects of modified collagen matrices on human umbilical vein endothelial cells
    • Markowicz M., Heitland A., Steffens G.C., Pallua N. Effects of modified collagen matrices on human umbilical vein endothelial cells. Int. J. Artif. Organs 2005, 28:1251-1258.
    • (2005) Int. J. Artif. Organs , vol.28 , pp. 1251-1258
    • Markowicz, M.1    Heitland, A.2    Steffens, G.C.3    Pallua, N.4
  • 122
    • 9344223942 scopus 로고    scopus 로고
    • Modulation of angiogenic potential of collagen matrices by covalent incorporation of heparin and loading with vascular endothelial growth factor
    • Steffens G.C., Yao C., Prevel P., Markowicz M., Schenck P., Noah E.M., Pallua N. Modulation of angiogenic potential of collagen matrices by covalent incorporation of heparin and loading with vascular endothelial growth factor. Tissue Eng. 2004, 10:1502-1509.
    • (2004) Tissue Eng. , vol.10 , pp. 1502-1509
    • Steffens, G.C.1    Yao, C.2    Prevel, P.3    Markowicz, M.4    Schenck, P.5    Noah, E.M.6    Pallua, N.7
  • 127
    • 34548637042 scopus 로고    scopus 로고
    • Production of heparin-functionalized hydrogels for the development of responsive and controlled growth factor delivery systems
    • Nie T., Baldwin A., Yamaguchi N., Kiick K.L. Production of heparin-functionalized hydrogels for the development of responsive and controlled growth factor delivery systems. J. Control. Release 2007, 122:287-296.
    • (2007) J. Control. Release , vol.122 , pp. 287-296
    • Nie, T.1    Baldwin, A.2    Yamaguchi, N.3    Kiick, K.L.4
  • 129
    • 0033997601 scopus 로고    scopus 로고
    • Development of fibrin derivatives for controlled release of heparin-binding growth factors
    • Sakiyama-Elbert S.E., Hubbell J.A. Development of fibrin derivatives for controlled release of heparin-binding growth factors. J. Control. Release 2000, 65:389-402.
    • (2000) J. Control. Release , vol.65 , pp. 389-402
    • Sakiyama-Elbert, S.E.1    Hubbell, J.A.2
  • 130
    • 0034601868 scopus 로고    scopus 로고
    • Controlled release of nerve growth factor from a heparin-containing fibrin-based cell ingrowth matrix
    • Sakiyama-Elbert S.E., Hubbell J.A. Controlled release of nerve growth factor from a heparin-containing fibrin-based cell ingrowth matrix. J. Control. Release 2000, 69:149-158.
    • (2000) J. Control. Release , vol.69 , pp. 149-158
    • Sakiyama-Elbert, S.E.1    Hubbell, J.A.2
  • 131
    • 73549086992 scopus 로고    scopus 로고
    • Fibrin-based tissue engineering scaffolds enhance neural fiber sprouting and delay the accumulation of reactive astrocytes at the lesion in a subacute model of spinal cord injury
    • Johnson P.J., Parker S.R., Sakiyama-Elbert S.E. Fibrin-based tissue engineering scaffolds enhance neural fiber sprouting and delay the accumulation of reactive astrocytes at the lesion in a subacute model of spinal cord injury. J. Biomed. Mater. Res. A 2010, 92:152-163.
    • (2010) J. Biomed. Mater. Res. A , vol.92 , pp. 152-163
    • Johnson, P.J.1    Parker, S.R.2    Sakiyama-Elbert, S.E.3
  • 132
    • 70350495751 scopus 로고    scopus 로고
    • Controlled release of neurotrophin-3 from fibrin-based tissue engineering scaffolds enhances neural fiber sprouting following subacute spinal cord injury
    • Johnson P.J., Parker S.R., Sakiyama-Elbert S.E. Controlled release of neurotrophin-3 from fibrin-based tissue engineering scaffolds enhances neural fiber sprouting following subacute spinal cord injury. Biotechnol. Bioeng. 2009, 104:1207-1214.
    • (2009) Biotechnol. Bioeng. , vol.104 , pp. 1207-1214
    • Johnson, P.J.1    Parker, S.R.2    Sakiyama-Elbert, S.E.3
  • 133
    • 77950557850 scopus 로고    scopus 로고
    • Controlled release of neurotrophin-3 and platelet-derived growth factor from fibrin scaffolds containing neural progenitor cells enhances survival and differentiation into neurons in a subacute model of SCI
    • Johnson P.J., Tatara A., Shiu A., Sakiyama-Elbert S.E. Controlled release of neurotrophin-3 and platelet-derived growth factor from fibrin scaffolds containing neural progenitor cells enhances survival and differentiation into neurons in a subacute model of SCI. Cell Transplant. 2010, 19:89-101.
    • (2010) Cell Transplant. , vol.19 , pp. 89-101
    • Johnson, P.J.1    Tatara, A.2    Shiu, A.3    Sakiyama-Elbert, S.E.4
  • 134
    • 3242728530 scopus 로고    scopus 로고
    • Controlled release of neurotrophin-3 from fibrin gels for spinal cord injury
    • Taylor S.J., McDonald J.W., Sakiyama-Elbert S.E. Controlled release of neurotrophin-3 from fibrin gels for spinal cord injury. J. Control. Release 2004, 98:281-294.
    • (2004) J. Control. Release , vol.98 , pp. 281-294
    • Taylor, S.J.1    McDonald, J.W.2    Sakiyama-Elbert, S.E.3
  • 135
    • 33745504598 scopus 로고    scopus 로고
    • Delivery of neurotrophin-3 from fibrin enhances neuronal fiber sprouting after spinal cord injury
    • Taylor S.J., Rosenzweig E.S., McDonald J.W., Sakiyama-Elbert S.E. Delivery of neurotrophin-3 from fibrin enhances neuronal fiber sprouting after spinal cord injury. J. Control. Release 2006, 113:226-235.
    • (2006) J. Control. Release , vol.113 , pp. 226-235
    • Taylor, S.J.1    Rosenzweig, E.S.2    McDonald, J.W.3    Sakiyama-Elbert, S.E.4
  • 136
    • 33845193518 scopus 로고    scopus 로고
    • Effect of controlled delivery of neurotrophin-3 from fibrin on spinal cord injury in a long term model
    • Taylor S.J., Sakiyama-Elbert S.E. Effect of controlled delivery of neurotrophin-3 from fibrin on spinal cord injury in a long term model. J. Control. Release 2006, 116:204-210.
    • (2006) J. Control. Release , vol.116 , pp. 204-210
    • Taylor, S.J.1    Sakiyama-Elbert, S.E.2
  • 137
    • 54949089299 scopus 로고    scopus 로고
    • Controlled-release kinetics and biologic activity of platelet-derived growth factor-BB for use in flexor tendon repair
    • Sakiyama-Elbert S.E., Das R., Gelberman R.H., Harwood F., Amiel D., Thomopoulos S. Controlled-release kinetics and biologic activity of platelet-derived growth factor-BB for use in flexor tendon repair. J. Hand Surg. Am. 2008, 33:1548-1557.
    • (2008) J. Hand Surg. Am. , vol.33 , pp. 1548-1557
    • Sakiyama-Elbert, S.E.1    Das, R.2    Gelberman, R.H.3    Harwood, F.4    Amiel, D.5    Thomopoulos, S.6
  • 139
    • 33746036846 scopus 로고    scopus 로고
    • Heparin-regulated release of growth factors in vitro and angiogenic response in vivo to implanted hyaluronan hydrogels containing VEGF and bFGF
    • Pike D.B., Cai S., Pomraning K.R., Firpo M.A., Fisher R.J., Shu X.Z., Prestwich G.D., Peattie R.A. Heparin-regulated release of growth factors in vitro and angiogenic response in vivo to implanted hyaluronan hydrogels containing VEGF and bFGF. Biomaterials 2006, 27:5242-5251.
    • (2006) Biomaterials , vol.27 , pp. 5242-5251
    • Pike, D.B.1    Cai, S.2    Pomraning, K.R.3    Firpo, M.A.4    Fisher, R.J.5    Shu, X.Z.6    Prestwich, G.D.7    Peattie, R.A.8
  • 140
    • 33748469357 scopus 로고    scopus 로고
    • Stimulation of in vivo angiogenesis using dual growth factor-loaded crosslinked glycosaminoglycan hydrogels
    • Riley C.M., Fuegy P.W., Firpo M.A., Shu X.Z., Prestwich G.D., Peattie R.A. Stimulation of in vivo angiogenesis using dual growth factor-loaded crosslinked glycosaminoglycan hydrogels. Biomaterials 2006, 27:5935-5943.
    • (2006) Biomaterials , vol.27 , pp. 5935-5943
    • Riley, C.M.1    Fuegy, P.W.2    Firpo, M.A.3    Shu, X.Z.4    Prestwich, G.D.5    Peattie, R.A.6
  • 141
    • 33847714354 scopus 로고    scopus 로고
    • Release of basic fibroblast growth factor from a crosslinked glycosaminoglycan hydrogel promotes wound healing
    • Liu Y., Cai S., Shu X.Z., Shelby J., Prestwich G.D. Release of basic fibroblast growth factor from a crosslinked glycosaminoglycan hydrogel promotes wound healing. Wound Repair Regen 2007, 15:245-251.
    • (2007) Wound Repair Regen , vol.15 , pp. 245-251
    • Liu, Y.1    Cai, S.2    Shu, X.Z.3    Shelby, J.4    Prestwich, G.D.5
  • 142
    • 20444412662 scopus 로고    scopus 로고
    • Injectable glycosaminoglycan hydrogels for controlled release of human basic fibroblast growth factor
    • Cai S., Liu Y., Zheng Shu X., Prestwich G.D. Injectable glycosaminoglycan hydrogels for controlled release of human basic fibroblast growth factor. Biomaterials 2005, 26:6054-6067.
    • (2005) Biomaterials , vol.26 , pp. 6054-6067
    • Cai, S.1    Liu, Y.2    Zheng Shu, X.3    Prestwich, G.D.4
  • 143
    • 56049127384 scopus 로고    scopus 로고
    • Recruitment of endogenous stem cells for tissue repair
    • Zhao J., Zhang N., Prestwich G.D., Wen X. Recruitment of endogenous stem cells for tissue repair. Macromol. Biosci. 2008, 8:836-842.
    • (2008) Macromol. Biosci. , vol.8 , pp. 836-842
    • Zhao, J.1    Zhang, N.2    Prestwich, G.D.3    Wen, X.4
  • 144
    • 40649121229 scopus 로고    scopus 로고
    • Microvascular maturity elicited in tissue treated with cytokine-loaded hyaluronan-based hydrogels
    • Hosack L.W., Firpo M.A., Scott J.A., Prestwich G.D., Peattie R.A. Microvascular maturity elicited in tissue treated with cytokine-loaded hyaluronan-based hydrogels. Biomaterials 2008, 29:2336-2347.
    • (2008) Biomaterials , vol.29 , pp. 2336-2347
    • Hosack, L.W.1    Firpo, M.A.2    Scott, J.A.3    Prestwich, G.D.4    Peattie, R.A.5
  • 145
    • 78649727712 scopus 로고    scopus 로고
    • The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain
    • Martino M.M., Hubbell J.A. The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J. 2010, 24:4711-4721.
    • (2010) FASEB J. , vol.24 , pp. 4711-4721
    • Martino, M.M.1    Hubbell, J.A.2
  • 147
    • 12344327314 scopus 로고    scopus 로고
    • Photo- and electropatterning of hydrogel-encapsulated living cell arrays
    • Albrecht D.R., Tsang V.L., Sah R.L., Bhatia S.N. Photo- and electropatterning of hydrogel-encapsulated living cell arrays. Lab Chip 2005, 5:111-118.
    • (2005) Lab Chip , vol.5 , pp. 111-118
    • Albrecht, D.R.1    Tsang, V.L.2    Sah, R.L.3    Bhatia, S.N.4
  • 148
    • 80155205233 scopus 로고    scopus 로고
    • Artificial niche microarrays for probing single stem cell fate in high throughput
    • Gobaa S., Hoehnel S., Roccio M., Negro A., Kobel S., Lutolf M.P. Artificial niche microarrays for probing single stem cell fate in high throughput. Nat. Methods 2011, 8:949-955.
    • (2011) Nat. Methods , vol.8 , pp. 949-955
    • Gobaa, S.1    Hoehnel, S.2    Roccio, M.3    Negro, A.4    Kobel, S.5    Lutolf, M.P.6
  • 149
    • 80053386321 scopus 로고    scopus 로고
    • Biomaterials meet microfluidics: building the next generation of artificial niches
    • Kobel S., Lutolf M.P. Biomaterials meet microfluidics: building the next generation of artificial niches. Curr. Opin. Biotechnol. 2011, 22:690-697.
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 690-697
    • Kobel, S.1    Lutolf, M.P.2
  • 150
    • 80155133565 scopus 로고    scopus 로고
    • Engineering 3D cell instructive microenvironments by rational assembly of artificial extracellular matrices and cell patterning
    • Sala A., Hanseler P., Ranga A., Lutolf M.P., Voros J., Ehrbar M., Weber F.E. Engineering 3D cell instructive microenvironments by rational assembly of artificial extracellular matrices and cell patterning. Integr. Biol. (Camb) 2011, 3:1102-1111.
    • (2011) Integr. Biol. (Camb) , vol.3 , pp. 1102-1111
    • Sala, A.1    Hanseler, P.2    Ranga, A.3    Lutolf, M.P.4    Voros, J.5    Ehrbar, M.6    Weber, F.E.7
  • 151
    • 69949145696 scopus 로고    scopus 로고
    • Artificial stem cell niches
    • Lutolf M.P., Blau H.M. Artificial stem cell niches. Adv. Mater. 2009, 21:3255-3268.
    • (2009) Adv. Mater. , vol.21 , pp. 3255-3268
    • Lutolf, M.P.1    Blau, H.M.2
  • 152
    • 64249113913 scopus 로고    scopus 로고
    • Photodegradable hydrogels for dynamic tuning of physical and chemical properties
    • Kloxin A.M., Kasko A.M., Salinas C.N., Anseth K.S. Photodegradable hydrogels for dynamic tuning of physical and chemical properties. Science 2009, 324:59-63.
    • (2009) Science , vol.324 , pp. 59-63
    • Kloxin, A.M.1    Kasko, A.M.2    Salinas, C.N.3    Anseth, K.S.4
  • 153
    • 4444314207 scopus 로고    scopus 로고
    • Three-dimensional tissue fabrication
    • Tsang V.L., Bhatia S.N. Three-dimensional tissue fabrication. Adv. Drug Deliv. Rev. 2004, 56:1635-1647.
    • (2004) Adv. Drug Deliv. Rev. , vol.56 , pp. 1635-1647
    • Tsang, V.L.1    Bhatia, S.N.2
  • 155
    • 41549140437 scopus 로고    scopus 로고
    • Vascular endothelial growth factor immobilized in collagen scaffold promotes penetration and proliferation of endothelial cells
    • Shen Y.H., Shoichet M.S., Radisic M. Vascular endothelial growth factor immobilized in collagen scaffold promotes penetration and proliferation of endothelial cells. Acta Biomater. 2008, 4:477-489.
    • (2008) Acta Biomater. , vol.4 , pp. 477-489
    • Shen, Y.H.1    Shoichet, M.S.2    Radisic, M.3
  • 156
    • 34548063167 scopus 로고    scopus 로고
    • Controlled release of stromal cell-derived factor-1 alpha in situ increases c-kit+ cell homing to the infarcted heart
    • Zhang G., Nakamura Y., Wang X., Hu Q., Suggs L.J., Zhang J. Controlled release of stromal cell-derived factor-1 alpha in situ increases c-kit+ cell homing to the infarcted heart. Tissue Eng. 2007, 13:2063-2071.
    • (2007) Tissue Eng. , vol.13 , pp. 2063-2071
    • Zhang, G.1    Nakamura, Y.2    Wang, X.3    Hu, Q.4    Suggs, L.J.5    Zhang, J.6
  • 157
    • 77950193801 scopus 로고    scopus 로고
    • Functional immobilization of interferon-gamma induces neuronal differentiation of neural stem cells
    • Leipzig N.D., Xu C., Zahir T., Shoichet M.S. Functional immobilization of interferon-gamma induces neuronal differentiation of neural stem cells. J. Biomed. Mater. Res. A 2010, 93:625-633.
    • (2010) J. Biomed. Mater. Res. A , vol.93 , pp. 625-633
    • Leipzig, N.D.1    Xu, C.2    Zahir, T.3    Shoichet, M.S.4
  • 159
    • 78449258828 scopus 로고    scopus 로고
    • Engineered aprotinin for improved stability of fibrin biomaterials
    • Lorentz K.M., Kontos S., Frey P., Hubbell J.A. Engineered aprotinin for improved stability of fibrin biomaterials. Biomaterials 2011, 32:430-438.
    • (2011) Biomaterials , vol.32 , pp. 430-438
    • Lorentz, K.M.1    Kontos, S.2    Frey, P.3    Hubbell, J.A.4
  • 160
    • 33746038183 scopus 로고    scopus 로고
    • PEG-cross-linked heparin is an affinity hydrogel for sustained release of vascular endothelial growth factor
    • Tae G., Scatena M., Stayton P.S., Hoffman A.S. PEG-cross-linked heparin is an affinity hydrogel for sustained release of vascular endothelial growth factor. J. Biomater. Sci. Polym. Ed. 2006, 17:187-197.
    • (2006) J. Biomater. Sci. Polym. Ed. , vol.17 , pp. 187-197
    • Tae, G.1    Scatena, M.2    Stayton, P.S.3    Hoffman, A.S.4
  • 161
    • 33747892712 scopus 로고    scopus 로고
    • Manipulation of hydrogel assembly and growth factor delivery via the use of peptide-polysaccharide interactions
    • Zhang L., Furst E.M., Kiick K.L. Manipulation of hydrogel assembly and growth factor delivery via the use of peptide-polysaccharide interactions. J. Control. Release 2006, 114:130-142.
    • (2006) J. Control. Release , vol.114 , pp. 130-142
    • Zhang, L.1    Furst, E.M.2    Kiick, K.L.3
  • 162
    • 22944449025 scopus 로고    scopus 로고
    • Polysaccharide-poly(ethylene glycol) star copolymer as a scaffold for the production of bioactive hydrogels
    • Yamaguchi N., Kiick K.L. Polysaccharide-poly(ethylene glycol) star copolymer as a scaffold for the production of bioactive hydrogels. Biomacromolecules 2005, 6:1921-1930.
    • (2005) Biomacromolecules , vol.6 , pp. 1921-1930
    • Yamaguchi, N.1    Kiick, K.L.2
  • 163
    • 33644809242 scopus 로고    scopus 로고
    • Heparin functionalized PEG gels that modulate protein adsorption for hMSC adhesion and differentiation
    • Benoit D.S., Anseth K.S. Heparin functionalized PEG gels that modulate protein adsorption for hMSC adhesion and differentiation. Acta Biomater. 2005, 1:461-470.
    • (2005) Acta Biomater. , vol.1 , pp. 461-470
    • Benoit, D.S.1    Anseth, K.S.2
  • 165
    • 77954383096 scopus 로고    scopus 로고
    • Hyaluronic acid hydrogels with controlled degradation properties for oriented bone regeneration
    • Patterson J., Siew R., Herring S.W., Lin A.S., Guldberg R., Stayton P.S. Hyaluronic acid hydrogels with controlled degradation properties for oriented bone regeneration. Biomaterials 2010, 31:6772-6781.
    • (2010) Biomaterials , vol.31 , pp. 6772-6781
    • Patterson, J.1    Siew, R.2    Herring, S.W.3    Lin, A.S.4    Guldberg, R.5    Stayton, P.S.6
  • 166
    • 66249112529 scopus 로고    scopus 로고
    • Human basic fibroblast growth factor fused with Kringle4 peptide binds to a fibrin scaffold and enhances angiogenesis
    • Zhao W., Han Q., Lin H., Sun W., Gao Y., Zhao Y., Wang B., Wang X., Chen B., Xiao Z., Dai J. Human basic fibroblast growth factor fused with Kringle4 peptide binds to a fibrin scaffold and enhances angiogenesis. Tissue Eng. Part A 2009, 15:991-998.
    • (2009) Tissue Eng. Part A , vol.15 , pp. 991-998
    • Zhao, W.1    Han, Q.2    Lin, H.3    Sun, W.4    Gao, Y.5    Zhao, Y.6    Wang, B.7    Wang, X.8    Chen, B.9    Xiao, Z.10    Dai, J.11
  • 167
    • 52549122771 scopus 로고    scopus 로고
    • Improved neovascularization and wound repair by targeting human basic fibroblast growth factor (bFGF) to fibrin
    • Zhao W., Han Q., Lin H., Gao Y., Sun W., Zhao Y., Wang B., Chen B., Xiao Z., Dai J. Improved neovascularization and wound repair by targeting human basic fibroblast growth factor (bFGF) to fibrin. J. Mol. Med. (Berl.) 2008, 86:1127-1138.
    • (2008) J. Mol. Med. (Berl.) , vol.86 , pp. 1127-1138
    • Zhao, W.1    Han, Q.2    Lin, H.3    Gao, Y.4    Sun, W.5    Zhao, Y.6    Wang, B.7    Chen, B.8    Xiao, Z.9    Dai, J.10
  • 168
    • 72649101231 scopus 로고    scopus 로고
    • Collagen-binding human epidermal growth factor promotes cellularization of collagen scaffolds
    • Yang Y., Zhao Y., Chen B., Han Q., Sun W., Xiao Z., Dai J. Collagen-binding human epidermal growth factor promotes cellularization of collagen scaffolds. Tissue Eng. Part A 2009, 15:3589-3596.
    • (2009) Tissue Eng. Part A , vol.15 , pp. 3589-3596
    • Yang, Y.1    Zhao, Y.2    Chen, B.3    Han, Q.4    Sun, W.5    Xiao, Z.6    Dai, J.7
  • 169
    • 38849118281 scopus 로고    scopus 로고
    • Collagen membranes loaded with collagen-binding human PDGF-BB accelerate wound healing in a rabbit dermal ischemic ulcer model
    • Sun W., Lin H., Xie H., Chen B., Zhao W., Han Q., Zhao Y., Xiao Z., Dai J. Collagen membranes loaded with collagen-binding human PDGF-BB accelerate wound healing in a rabbit dermal ischemic ulcer model. Growth Factors 2007, 25:309-318.
    • (2007) Growth Factors , vol.25 , pp. 309-318
    • Sun, W.1    Lin, H.2    Xie, H.3    Chen, B.4    Zhao, W.5    Han, Q.6    Zhao, Y.7    Xiao, Z.8    Dai, J.9
  • 170
    • 73349103199 scopus 로고    scopus 로고
    • Linear ordered collagen scaffolds loaded with collagen-binding brain-derived neurotrophic factor improve the recovery of spinal cord injury in rats
    • Han Q., Sun W., Lin H., Zhao W., Gao Y., Zhao Y., Chen B., Xiao Z., Hu W., Li Y., Yang B., Dai J. Linear ordered collagen scaffolds loaded with collagen-binding brain-derived neurotrophic factor improve the recovery of spinal cord injury in rats. Tissue Eng. Part A 2009, 15:2927-2935.
    • (2009) Tissue Eng. Part A , vol.15 , pp. 2927-2935
    • Han, Q.1    Sun, W.2    Lin, H.3    Zhao, W.4    Gao, Y.5    Zhao, Y.6    Chen, B.7    Xiao, Z.8    Hu, W.9    Li, Y.10    Yang, B.11    Dai, J.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.