메뉴 건너뛰기




Volumn 30, Issue 3, 2009, Pages 409-422

Elastin-mimetic protein polymers capable of physical and chemical crosslinking

Author keywords

In vivo biocompatibility; Mechanical testing; Protein polymer; Recombinant elastin mimetic

Indexed keywords

ABS RESINS; ALDEHYDES; BIOCOMPATIBILITY; CHEMICAL PROPERTIES; GLYCOPROTEINS; MATERIALS PROPERTIES; MECHANICAL TESTING; POLYMERS; SYNTHESIS (CHEMICAL);

EID: 55249122886     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2008.09.040     Document Type: Article
Times cited : (91)

References (72)
  • 1
    • 0032541038 scopus 로고    scopus 로고
    • Reversible hydrogels from self-assembling artificial proteins
    • Petka W.A., Harden J.L., McGrath K.P., Wirtz D., and Tirrell D.A. Reversible hydrogels from self-assembling artificial proteins. Science 281 (1998) 389-392
    • (1998) Science , vol.281 , pp. 389-392
    • Petka, W.A.1    Harden, J.L.2    McGrath, K.P.3    Wirtz, D.4    Tirrell, D.A.5
  • 2
    • 33751531364 scopus 로고    scopus 로고
    • Genetic engineering of protein-based polymers: the example of elastinlike polymers
    • Rodríguez-Cabello J.C., Reguera J., Girotti A., Arias F.J., and Alonso M. Genetic engineering of protein-based polymers: the example of elastinlike polymers. Adv Polym Sci 200 (2006) 119-167
    • (2006) Adv Polym Sci , vol.200 , pp. 119-167
    • Rodríguez-Cabello, J.C.1    Reguera, J.2    Girotti, A.3    Arias, F.J.4    Alonso, M.5
  • 3
    • 0037131001 scopus 로고    scopus 로고
    • Self-assembly of block copolymers derived from elastin-mimetic polypeptide sequences
    • Wright E.R., and Conticello V.P. Self-assembly of block copolymers derived from elastin-mimetic polypeptide sequences. Adv Drug Deliv Rev 54 (2002) 1057-1073
    • (2002) Adv Drug Deliv Rev , vol.54 , pp. 1057-1073
    • Wright, E.R.1    Conticello, V.P.2
  • 5
    • 0036469685 scopus 로고    scopus 로고
    • Thermoplastic elastomer hydrogels via self-assembly of an elastin-mimetic triblock polypeptide
    • Wright E.R., McMillan R.A., Cooper A., Apkarian R.P., and Conticello V.P. Thermoplastic elastomer hydrogels via self-assembly of an elastin-mimetic triblock polypeptide. Adv Funct Mater 12 2 (2002) 1-6
    • (2002) Adv Funct Mater , vol.12 , Issue.2 , pp. 1-6
    • Wright, E.R.1    McMillan, R.A.2    Cooper, A.3    Apkarian, R.P.4    Conticello, V.P.5
  • 6
    • 33748511669 scopus 로고    scopus 로고
    • Micelle density regulated by a reversible switch of protein secondary structure
    • Sallach R.E., Wei M., Biswas N., Conticello V.P., Lecommandoux S., Dluhy R.A., et al. Micelle density regulated by a reversible switch of protein secondary structure. J Am Chem Soc 128 36 (2006) 12014-12019
    • (2006) J Am Chem Soc , vol.128 , Issue.36 , pp. 12014-12019
    • Sallach, R.E.1    Wei, M.2    Biswas, N.3    Conticello, V.P.4    Lecommandoux, S.5    Dluhy, R.A.6
  • 8
    • 28844502777 scopus 로고    scopus 로고
    • Alterations in physical cross-linking modulate mechanical properties of two-phase protein polymer networks
    • Wu X., Sallach R., Haller C.A., Caves J.A., Nagapudi K., Conticello V.P., et al. Alterations in physical cross-linking modulate mechanical properties of two-phase protein polymer networks. Biomacromolecules 6 6 (2005) 3037-3044
    • (2005) Biomacromolecules , vol.6 , Issue.6 , pp. 3037-3044
    • Wu, X.1    Sallach, R.2    Haller, C.A.3    Caves, J.A.4    Nagapudi, K.5    Conticello, V.P.6
  • 9
    • 0346850628 scopus 로고    scopus 로고
    • Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties
    • Bellingham C.M., Lillie M.A., Gosline J.M., Wright G.M., Starcher B.C., Bailey A.J., et al. Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties. Biopolymers 70 4 (2003) 445-455
    • (2003) Biopolymers , vol.70 , Issue.4 , pp. 445-455
    • Bellingham, C.M.1    Lillie, M.A.2    Gosline, J.M.3    Wright, G.M.4    Starcher, B.C.5    Bailey, A.J.6
  • 10
    • 0034158145 scopus 로고    scopus 로고
    • Engineering the extracellular matrix: a novel approach to polymeric biomaterials. I. Control of the physical properties of artificial protein matrices designed to support adhesion of vascular endothelial cells
    • Welsh E.R., and Tirrell D.A. Engineering the extracellular matrix: a novel approach to polymeric biomaterials. I. Control of the physical properties of artificial protein matrices designed to support adhesion of vascular endothelial cells. Biomacromolecules 1 1 (2000) 23-30
    • (2000) Biomacromolecules , vol.1 , Issue.1 , pp. 23-30
    • Welsh, E.R.1    Tirrell, D.A.2
  • 11
    • 0038245213 scopus 로고    scopus 로고
    • Mechanics of elastin: molecular mechanism of biological elasticity and its relationship to contraction
    • Urry D.W., and Parker T.M. Mechanics of elastin: molecular mechanism of biological elasticity and its relationship to contraction. J Muscle Res Cell Motil 23 5-6 (2002) 543-559
    • (2002) J Muscle Res Cell Motil , vol.23 , Issue.5-6 , pp. 543-559
    • Urry, D.W.1    Parker, T.M.2
  • 12
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin
    • Vrhovski B., and Weiss A.S. Biochemistry of tropoelastin. Eur J Biochem 258 1 (1998) 1-18
    • (1998) Eur J Biochem , vol.258 , Issue.1 , pp. 1-18
    • Vrhovski, B.1    Weiss, A.S.2
  • 13
    • 33847286372 scopus 로고    scopus 로고
    • Microstructural and tensile properties of elastin-based polypeptides crosslinked with genipin and pyrroloquinoline quinone
    • Vieth S., Bellingham C.M., Keeley F.W., Hodge S.M., and Rousseau D. Microstructural and tensile properties of elastin-based polypeptides crosslinked with genipin and pyrroloquinoline quinone. Biopolymers 85 3 (2007) 199-206
    • (2007) Biopolymers , vol.85 , Issue.3 , pp. 199-206
    • Vieth, S.1    Bellingham, C.M.2    Keeley, F.W.3    Hodge, S.M.4    Rousseau, D.5
  • 14
    • 3543005321 scopus 로고    scopus 로고
    • Design and bioproduction of a recombinant multi(bio)functional elastin-like protein polymer containing cell adhesion sequences for tissue engineering purposes
    • Girotti A., Reguera J., Rodriguez-Cabello J.C., Arias F.J., Alonso M., and Matestera A. Design and bioproduction of a recombinant multi(bio)functional elastin-like protein polymer containing cell adhesion sequences for tissue engineering purposes. J Mater Sci Mater Med 15 4 (2004) 479-484
    • (2004) J Mater Sci Mater Med , vol.15 , Issue.4 , pp. 479-484
    • Girotti, A.1    Reguera, J.2    Rodriguez-Cabello, J.C.3    Arias, F.J.4    Alonso, M.5    Matestera, A.6
  • 15
    • 0035014513 scopus 로고    scopus 로고
    • Chemical synthesis of cross-linked poly(KGGVG). An elastin-like biopolymer
    • Martino M., and Tamburro A.M. Chemical synthesis of cross-linked poly(KGGVG). An elastin-like biopolymer. Biopolymers 59 1 (2001) 29-37
    • (2001) Biopolymers , vol.59 , Issue.1 , pp. 29-37
    • Martino, M.1    Tamburro, A.M.2
  • 16
    • 0034894236 scopus 로고    scopus 로고
    • Elastomeric polypentapeptides cross-linked into matrixes and fibers
    • Lee J., Macoscko C.W., and Urry D.W. Elastomeric polypentapeptides cross-linked into matrixes and fibers. Biomacromolecules 2 (2001) 170-179
    • (2001) Biomacromolecules , vol.2 , pp. 170-179
    • Lee, J.1    Macoscko, C.W.2    Urry, D.W.3
  • 17
    • 0344393657 scopus 로고    scopus 로고
    • Physical properties of artificial extracellular matrix protein films prepared by isocyanate crosslinking
    • Nowatzki P.J., and Tirrell D.A. Physical properties of artificial extracellular matrix protein films prepared by isocyanate crosslinking. Biomaterials 25 (2004) 1261-1267
    • (2004) Biomaterials , vol.25 , pp. 1261-1267
    • Nowatzki, P.J.1    Tirrell, D.A.2
  • 18
    • 0038517754 scopus 로고    scopus 로고
    • Swelling and mechanical behaviors of chemically cross-linked hydrogels of elastin-like polypeptides
    • Trabbic-Carlson K., Setton L.A., and Chilkoti A. Swelling and mechanical behaviors of chemically cross-linked hydrogels of elastin-like polypeptides. Biomacromolecules 4 (2003) 572-580
    • (2003) Biomacromolecules , vol.4 , pp. 572-580
    • Trabbic-Carlson, K.1    Setton, L.A.2    Chilkoti, A.3
  • 19
    • 0032675950 scopus 로고    scopus 로고
    • Rapid assembly of synthetic genes encoding protein polymers
    • McMillan R.A., Lee T.A.T., and Conticello V.P. Rapid assembly of synthetic genes encoding protein polymers. Macromolecules 32 (1999) 3643-3648
    • (1999) Macromolecules , vol.32 , pp. 3643-3648
    • McMillan, R.A.1    Lee, T.A.T.2    Conticello, V.P.3
  • 20
    • 0034206072 scopus 로고    scopus 로고
    • Synthesis and characterization of elastin-mimetic protein gels derived from a well-defined polypeptide precursor
    • McMillan R.A., and Conticello V.P. Synthesis and characterization of elastin-mimetic protein gels derived from a well-defined polypeptide precursor. Macromolecules 33 (2000) 4809-4821
    • (2000) Macromolecules , vol.33 , pp. 4809-4821
    • McMillan, R.A.1    Conticello, V.P.2
  • 21
    • 0037432360 scopus 로고    scopus 로고
    • Mechanical properties of artificial protein matrices engineered for control of cell and tissue behavior
    • Zio K.D., and Tirrell D.A. Mechanical properties of artificial protein matrices engineered for control of cell and tissue behavior. Macromolecules 36 (2003) 1553-1558
    • (2003) Macromolecules , vol.36 , pp. 1553-1558
    • Zio, K.D.1    Tirrell, D.A.2
  • 22
    • 38849138521 scopus 로고    scopus 로고
    • In situ cross-linking of elastin-like polypeptide block copolymers for tissue repair
    • Lim D.W., Nettles D.L., Setton L.A., and Chilkoti A. In situ cross-linking of elastin-like polypeptide block copolymers for tissue repair. Biomacromolecules 9 1 (2008) 222-230
    • (2008) Biomacromolecules , vol.9 , Issue.1 , pp. 222-230
    • Lim, D.W.1    Nettles, D.L.2    Setton, L.A.3    Chilkoti, A.4
  • 23
    • 34249867928 scopus 로고    scopus 로고
    • Rapid cross-linking of elastin-like polypeptides with (hydroxymethyl) phosphines in aqueous solution
    • Lim D.W., Nettles D.L., Setton L.A., and Chilkoti A. Rapid cross-linking of elastin-like polypeptides with (hydroxymethyl) phosphines in aqueous solution. Biomacromolecules 8 5 (2007) 1463-1470
    • (2007) Biomacromolecules , vol.8 , Issue.5 , pp. 1463-1470
    • Lim, D.W.1    Nettles, D.L.2    Setton, L.A.3    Chilkoti, A.4
  • 24
    • 31044449508 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of enzymatically cross-linked elastin-like polypeptide gels for cartilaginous tissue repair
    • McHale M.K., Setton L.A., and Chilkoti A. Synthesis and in vitro evaluation of enzymatically cross-linked elastin-like polypeptide gels for cartilaginous tissue repair. Tissue Eng 11 11-12 (2005) 1768-1779
    • (2005) Tissue Eng , vol.11 , Issue.11-12 , pp. 1768-1779
    • McHale, M.K.1    Setton, L.A.2    Chilkoti, A.3
  • 26
    • 0018076544 scopus 로고
    • Elastin cross-linking in vitro. Studies on factors influencing the formation of desmosines by lysyl oxidase action on tropoelastin
    • Narayanan A.S., Page R.C., Kuzan F., and Cooper C.G. Elastin cross-linking in vitro. Studies on factors influencing the formation of desmosines by lysyl oxidase action on tropoelastin. Biochem J 173 3 (1978) 857-862
    • (1978) Biochem J , vol.173 , Issue.3 , pp. 857-862
    • Narayanan, A.S.1    Page, R.C.2    Kuzan, F.3    Cooper, C.G.4
  • 28
    • 0038015691 scopus 로고    scopus 로고
    • Endothelial cell adhesion to the fibronectin CS5 domain in artificial extracellular matrix proteins
    • Heilshorn S.C., DiZio K.A., Welsh E.R., and Tirrell D.A. Endothelial cell adhesion to the fibronectin CS5 domain in artificial extracellular matrix proteins. Biomaterials 24 23 (2003) 4245-4252
    • (2003) Biomaterials , vol.24 , Issue.23 , pp. 4245-4252
    • Heilshorn, S.C.1    DiZio, K.A.2    Welsh, E.R.3    Tirrell, D.A.4
  • 29
    • 0036200174 scopus 로고    scopus 로고
    • Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system
    • Meyer D.E., and Chilkoti A. Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system. Biomacromolecules 3 2 (2002) 357-367
    • (2002) Biomacromolecules , vol.3 , Issue.2 , pp. 357-367
    • Meyer, D.E.1    Chilkoti, A.2
  • 30
    • 0036328129 scopus 로고    scopus 로고
    • Swelling behavior of a genetically engineered silk-elastinlike protein polymer hydrogel
    • Dinerman A.A., Cappello J., Ghandehari H., and Hoag S.W. Swelling behavior of a genetically engineered silk-elastinlike protein polymer hydrogel. Biomaterials 23 21 (2002) 4203-4210
    • (2002) Biomaterials , vol.23 , Issue.21 , pp. 4203-4210
    • Dinerman, A.A.1    Cappello, J.2    Ghandehari, H.3    Hoag, S.W.4
  • 31
    • 14044254822 scopus 로고    scopus 로고
    • Inhibition of cellular immune responses to encapsulated porcine islet xenografts by simultaneous blockade of two different costimulatory pathways
    • Safley S.A., Kapp L.M., Tucker-Burden C., Hering B., Kapp J.A., and Weber C.J. Inhibition of cellular immune responses to encapsulated porcine islet xenografts by simultaneous blockade of two different costimulatory pathways. Transplantation 79 4 (2005) 409-418
    • (2005) Transplantation , vol.79 , Issue.4 , pp. 409-418
    • Safley, S.A.1    Kapp, L.M.2    Tucker-Burden, C.3    Hering, B.4    Kapp, J.A.5    Weber, C.J.6
  • 32
    • 0035823759 scopus 로고    scopus 로고
    • Protein-based materials, toward a new level of structural control
    • van Hest J.C., and Tirrell D.A. Protein-based materials, toward a new level of structural control. Chem Commun 19 (2001) 1897-1904
    • (2001) Chem Commun , Issue.19 , pp. 1897-1904
    • van Hest, J.C.1    Tirrell, D.A.2
  • 33
    • 0004320464 scopus 로고
    • Molecular dynamics calculations on relaxed and extended states of the polypentapeptide of elastin
    • Chang D.K., and Urry D.W. Molecular dynamics calculations on relaxed and extended states of the polypentapeptide of elastin. Chem Phys Lett 147 4 (1988) 395-400
    • (1988) Chem Phys Lett , vol.147 , Issue.4 , pp. 395-400
    • Chang, D.K.1    Urry, D.W.2
  • 34
    • 0026926763 scopus 로고
    • Hydrophobicity scale for proteins based on inverse transition temperature
    • Urry D.W., Gowda D.C., Parker T.M., Luan C.H., Reid M.C., Harris C.M., et al. Hydrophobicity scale for proteins based on inverse transition temperature. Biopolymers 32 (1992) 1243-1250
    • (1992) Biopolymers , vol.32 , pp. 1243-1250
    • Urry, D.W.1    Gowda, D.C.2    Parker, T.M.3    Luan, C.H.4    Reid, M.C.5    Harris, C.M.6
  • 35
    • 84984621304 scopus 로고
    • Temperature of polypeptide inverse temperature transition depends on mean residue hydrophobicity
    • Urry D.W., Luan C.H., Parker T.M., Gowda D.C., Prasad K.U., Reid M.C., et al. Temperature of polypeptide inverse temperature transition depends on mean residue hydrophobicity. J Am Chem Soc 113 (1991) 4346-4348
    • (1991) J Am Chem Soc , vol.113 , pp. 4346-4348
    • Urry, D.W.1    Luan, C.H.2    Parker, T.M.3    Gowda, D.C.4    Prasad, K.U.5    Reid, M.C.6
  • 36
    • 0022691591 scopus 로고
    • In vitro calcification and in vivo biocompatibility of the crosslinked polypentapeptide of elastin
    • Wood S.A., Lemons J.E., Prasad K.U., and Urry D.W. In vitro calcification and in vivo biocompatibility of the crosslinked polypentapeptide of elastin. J Biomed Mater Res 20 3 (1986) 315-335
    • (1986) J Biomed Mater Res , vol.20 , Issue.3 , pp. 315-335
    • Wood, S.A.1    Lemons, J.E.2    Prasad, K.U.3    Urry, D.W.4
  • 38
    • 0027422979 scopus 로고
    • Extracellular matrix 4: the elastic fiber
    • Rosenbloom J., Abrams W.R., and Mecham R. Extracellular matrix 4: the elastic fiber. FASEB J 7 (1993) 1208-1218
    • (1993) FASEB J , vol.7 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 39
    • 0015967414 scopus 로고
    • Communication: coacervation of tropoelastin results in fiber formation
    • Cox B.A., Starcher B.C., and Urry D.W. Communication: coacervation of tropoelastin results in fiber formation. J Biol Chem 249 3 (1974) 997-998
    • (1974) J Biol Chem , vol.249 , Issue.3 , pp. 997-998
    • Cox, B.A.1    Starcher, B.C.2    Urry, D.W.3
  • 40
    • 0033618373 scopus 로고    scopus 로고
    • Glycosaminoglycans mediate the coacervation of human tropoelastin through dominant charge interactions involving lysine side chains
    • Wu W.J., Vrhovski B., and Weiss A.S. Glycosaminoglycans mediate the coacervation of human tropoelastin through dominant charge interactions involving lysine side chains. J Biol Chem 274 31 (1999) 21719-21724
    • (1999) J Biol Chem , vol.274 , Issue.31 , pp. 21719-21724
    • Wu, W.J.1    Vrhovski, B.2    Weiss, A.S.3
  • 42
    • 0033537594 scopus 로고    scopus 로고
    • Design and biosynthesis of elastin-like artificial extracellular matrix proteins containing periodically spaced fibronectin CS5 domains
    • Panitch A., Yamaoka T., Fournier M.J., Mason T.L., and Tirrell D.A. Design and biosynthesis of elastin-like artificial extracellular matrix proteins containing periodically spaced fibronectin CS5 domains. Macromolecules 32 (1999) 1701-1703
    • (1999) Macromolecules , vol.32 , pp. 1701-1703
    • Panitch, A.1    Yamaoka, T.2    Fournier, M.J.3    Mason, T.L.4    Tirrell, D.A.5
  • 43
    • 0036010376 scopus 로고    scopus 로고
    • In vivo evaluation of cellular and acellular bovine pericardia fixed with a naturally occurring crosslinking agent (genipin)
    • Chang Y., Tsai C.C., Liang H.C., and Sung H.W. In vivo evaluation of cellular and acellular bovine pericardia fixed with a naturally occurring crosslinking agent (genipin). Biomaterials 23 12 (2002) 2447-2457
    • (2002) Biomaterials , vol.23 , Issue.12 , pp. 2447-2457
    • Chang, Y.1    Tsai, C.C.2    Liang, H.C.3    Sung, H.W.4
  • 44
    • 0030111405 scopus 로고    scopus 로고
    • Glutaraldehyde as a fixative in bioprostheses and drug delivery matrices
    • Jayakrishnan A., and Jameela S.R. Glutaraldehyde as a fixative in bioprostheses and drug delivery matrices. Biomaterials 17 5 (1996) 471-484
    • (1996) Biomaterials , vol.17 , Issue.5 , pp. 471-484
    • Jayakrishnan, A.1    Jameela, S.R.2
  • 45
    • 0018294163 scopus 로고
    • Dynamic mechanical properties of elastin
    • Gosline J.M., and French C.J. Dynamic mechanical properties of elastin. Biopolymers 18 8 (1979) 2091-2103
    • (1979) Biopolymers , vol.18 , Issue.8 , pp. 2091-2103
    • Gosline, J.M.1    French, C.J.2
  • 47
    • 0034434786 scopus 로고    scopus 로고
    • Biaxial mechanical evaluation of planar biological materials
    • Sacks M.S. Biaxial mechanical evaluation of planar biological materials. J Elast 61 (2000) 199-246
    • (2000) J Elast , vol.61 , pp. 199-246
    • Sacks, M.S.1
  • 48
    • 2642565332 scopus 로고    scopus 로고
    • Stress relaxation preconditioning of porcine aortic valves
    • Carew E.O., Garg A., Barber J.E., and Vesely I. Stress relaxation preconditioning of porcine aortic valves. Ann Biomed Eng 32 4 (2004) 563-572
    • (2004) Ann Biomed Eng , vol.32 , Issue.4 , pp. 563-572
    • Carew, E.O.1    Garg, A.2    Barber, J.E.3    Vesely, I.4
  • 49
    • 0034352216 scopus 로고    scopus 로고
    • Role of preconditioning and recovery time in repeated testing of aortic valve tissues: validation through quasilinear viscoelastic theory
    • Carew E.O., Barber J.E., and Vesely I. Role of preconditioning and recovery time in repeated testing of aortic valve tissues: validation through quasilinear viscoelastic theory. Ann Biomed Eng 28 9 (2000) 1093-1100
    • (2000) Ann Biomed Eng , vol.28 , Issue.9 , pp. 1093-1100
    • Carew, E.O.1    Barber, J.E.2    Vesely, I.3
  • 50
    • 0026196257 scopus 로고
    • Biocompatibility of the bioelastic materials, poly(GVGVP) and its gamma-irradiation cross-linked matrix: summary of generic biological test results
    • Urry D.W., and Parker T.M. Biocompatibility of the bioelastic materials, poly(GVGVP) and its gamma-irradiation cross-linked matrix: summary of generic biological test results. J Bioact Compat Polym 6 (1991) 263-282
    • (1991) J Bioact Compat Polym , vol.6 , pp. 263-282
    • Urry, D.W.1    Parker, T.M.2
  • 52
    • 0028330008 scopus 로고
    • Use of polypentapeptides of elastin to prevent postoperative adhesions: efficacy in a contaminated peritoneal model
    • Hoban L.D., Pierce M., Quance J., Hayward I., McKee A., Gowda D.C., et al. Use of polypentapeptides of elastin to prevent postoperative adhesions: efficacy in a contaminated peritoneal model. J Surg Res 56 2 (1994) 179-183
    • (1994) J Surg Res , vol.56 , Issue.2 , pp. 179-183
    • Hoban, L.D.1    Pierce, M.2    Quance, J.3    Hayward, I.4    McKee, A.5    Gowda, D.C.6
  • 54
    • 33751316549 scopus 로고    scopus 로고
    • The effect of a recombinant elastin-mimetic coating of an ePTFE prosthesis on acute thrombogenicity in a baboon arteriovenous shunt
    • Jordan S.W., Haller C.A., Sallach R.E., Apkarian R.P., Hanson S.R., and Chaikof E.L. The effect of a recombinant elastin-mimetic coating of an ePTFE prosthesis on acute thrombogenicity in a baboon arteriovenous shunt. Biomaterials 28 6 (2007) 1191-1197
    • (2007) Biomaterials , vol.28 , Issue.6 , pp. 1191-1197
    • Jordan, S.W.1    Haller, C.A.2    Sallach, R.E.3    Apkarian, R.P.4    Hanson, S.R.5    Chaikof, E.L.6
  • 55
    • 2342424502 scopus 로고    scopus 로고
    • Investigation of recombinant human elastin polypeptides as non-thrombogenic coatings
    • Woodhouse K.A., Klement P., Chen V., Gorbet M.B., Keeley F.W., Stahl R., et al. Investigation of recombinant human elastin polypeptides as non-thrombogenic coatings. Biomaterials 25 19 (2004) 4543-4553
    • (2004) Biomaterials , vol.25 , Issue.19 , pp. 4543-4553
    • Woodhouse, K.A.1    Klement, P.2    Chen, V.3    Gorbet, M.B.4    Keeley, F.W.5    Stahl, R.6
  • 56
    • 0035866357 scopus 로고    scopus 로고
    • Targeting a genetically engineered elastin-like polypeptide to solid tumors by local hypothermia
    • Meyer D.E., Kong G.A., Dewhirst M.W., Zalutsky M.R., and Chilkoti A. Targeting a genetically engineered elastin-like polypeptide to solid tumors by local hypothermia. Cancer Res 61 (2001) 1548-1554
    • (2001) Cancer Res , vol.61 , pp. 1548-1554
    • Meyer, D.E.1    Kong, G.A.2    Dewhirst, M.W.3    Zalutsky, M.R.4    Chilkoti, A.5
  • 57
    • 33747875376 scopus 로고    scopus 로고
    • Tracking the in vivo fate of recombinant polypeptides by isotopic labeling
    • Liu W., Dreher M.R., Chow D.C., Zalutsky M.R., and Chilkoti A. Tracking the in vivo fate of recombinant polypeptides by isotopic labeling. J Controlled Release 114 (2006) 184-192
    • (2006) J Controlled Release , vol.114 , pp. 184-192
    • Liu, W.1    Dreher, M.R.2    Chow, D.C.3    Zalutsky, M.R.4    Chilkoti, A.5
  • 59
    • 1942468636 scopus 로고    scopus 로고
    • Synthetic elastin hydrogels derived from massive elastic assemblies of self-organized human protein monomers
    • Mithieux S.M., Rasko J.E.J., and Weiss A.S. Synthetic elastin hydrogels derived from massive elastic assemblies of self-organized human protein monomers. Biomaterials 25 (2004) 4921-4927
    • (2004) Biomaterials , vol.25 , pp. 4921-4927
    • Mithieux, S.M.1    Rasko, J.E.J.2    Weiss, A.S.3
  • 60
    • 0032580524 scopus 로고    scopus 로고
    • In-situ self-assembling protein polymer gel systems for administration, delivery, and release of drugs
    • Cappello J., Crissman J.W., Crissman M., Ferrari F.A., Textor G., Wallis O., et al. In-situ self-assembling protein polymer gel systems for administration, delivery, and release of drugs. J Control Release 53 1-3 (1998) 105-117
    • (1998) J Control Release , vol.53 , Issue.1-3 , pp. 105-117
    • Cappello, J.1    Crissman, J.W.2    Crissman, M.3    Ferrari, F.A.4    Textor, G.5    Wallis, O.6
  • 61
    • 33947143774 scopus 로고    scopus 로고
    • Adenoviral gene delivery to solid tumors by recombinant silk-elastinlike protein polymers
    • Hatefi A., Cappello J., and Ghandehari H. Adenoviral gene delivery to solid tumors by recombinant silk-elastinlike protein polymers. Pharm Res 24 4 (2007) 773-779
    • (2007) Pharm Res , vol.24 , Issue.4 , pp. 773-779
    • Hatefi, A.1    Cappello, J.2    Ghandehari, H.3
  • 62
    • 1642441833 scopus 로고    scopus 로고
    • In vitro and in vivo evaluation of recombinant silk-elastinlike hydrogels for cancer gene therapy
    • Megeed Z., Haider M., Li D., O'Malley Jr. B.W., Cappello J., and Ghandehari H. In vitro and in vivo evaluation of recombinant silk-elastinlike hydrogels for cancer gene therapy. J Control Release 94 2-3 (2004) 433-445
    • (2004) J Control Release , vol.94 , Issue.2-3 , pp. 433-445
    • Megeed, Z.1    Haider, M.2    Li, D.3    O'Malley Jr., B.W.4    Cappello, J.5    Ghandehari, H.6
  • 63
    • 0028213869 scopus 로고
    • In vivo biocompatibility of implantable delivery systems and biomaterials
    • Anderson J.M. In vivo biocompatibility of implantable delivery systems and biomaterials. Eur J Pharm Biopharm 40 (1994) 1-8
    • (1994) Eur J Pharm Biopharm , vol.40 , pp. 1-8
    • Anderson, J.M.1
  • 64
    • 0027480354 scopus 로고
    • Image analysis in the evaluation of biomaterials
    • Hunt J.A., Vince D.G., and Williams D.F. Image analysis in the evaluation of biomaterials. J Biomed Eng 15 (1993) 39-45
    • (1993) J Biomed Eng , vol.15 , pp. 39-45
    • Hunt, J.A.1    Vince, D.G.2    Williams, D.F.3
  • 65
    • 39049162364 scopus 로고    scopus 로고
    • Effect of molecular mobility of polymeric implants on soft tissue reactions: an in vivo study in rats
    • Andersson M., Suska F., Johansson A., Berglin M., Emanuelsson L., Elwing H., et al. Effect of molecular mobility of polymeric implants on soft tissue reactions: an in vivo study in rats. J Biomed Mater Res A 84 3 (2008) 652-660
    • (2008) J Biomed Mater Res A , vol.84 , Issue.3 , pp. 652-660
    • Andersson, M.1    Suska, F.2    Johansson, A.3    Berglin, M.4    Emanuelsson, L.5    Elwing, H.6
  • 66
    • 0031396304 scopus 로고    scopus 로고
    • A comparison of fibrous tissue formation surrounding intraperitoneal and subcutaneous implantation of ALCAP, HA, and TCP ceramic devices
    • Butler K., Benghuzzui H., Tucci M., and Cason Z. A comparison of fibrous tissue formation surrounding intraperitoneal and subcutaneous implantation of ALCAP, HA, and TCP ceramic devices. Biomed Sci Instrum 34 (1997) 18-23
    • (1997) Biomed Sci Instrum , vol.34 , pp. 18-23
    • Butler, K.1    Benghuzzui, H.2    Tucci, M.3    Cason, Z.4
  • 67
    • 0037620279 scopus 로고    scopus 로고
    • In vivo bone and soft tissue response to injectable, biodegradable oligo(poly(ethylene glycol) fumarate) hydrogels
    • Shin H., Quinten Ruhe P., Mikos A.G., and Jansen J.A. In vivo bone and soft tissue response to injectable, biodegradable oligo(poly(ethylene glycol) fumarate) hydrogels. Biomaterials 24 19 (2003) 3201-3211
    • (2003) Biomaterials , vol.24 , Issue.19 , pp. 3201-3211
    • Shin, H.1    Quinten Ruhe, P.2    Mikos, A.G.3    Jansen, J.A.4
  • 68
    • 10644254868 scopus 로고    scopus 로고
    • Blood vessel formation after soft-tissue implantation of hyaluronan-based hydrogel supplemented with copper ions
    • Giavaresi G., Torricelli P., Fornasari P.M., Giardino R., Barbucci R., and Leone G. Blood vessel formation after soft-tissue implantation of hyaluronan-based hydrogel supplemented with copper ions. Biomaterials 26 16 (2005) 3001-3008
    • (2005) Biomaterials , vol.26 , Issue.16 , pp. 3001-3008
    • Giavaresi, G.1    Torricelli, P.2    Fornasari, P.M.3    Giardino, R.4    Barbucci, R.5    Leone, G.6
  • 69
    • 33745564665 scopus 로고    scopus 로고
    • The influence of functional groups of self-assembled monolayers on fibrous capsule formation and cell recruitment
    • Barbosa J.N., Madureira P., Barbosa M.A., and Aguas A.P. The influence of functional groups of self-assembled monolayers on fibrous capsule formation and cell recruitment. J Biomed Mater Res A 76 4 (2006) 737-743
    • (2006) J Biomed Mater Res A , vol.76 , Issue.4 , pp. 737-743
    • Barbosa, J.N.1    Madureira, P.2    Barbosa, M.A.3    Aguas, A.P.4
  • 70
    • 41849120802 scopus 로고    scopus 로고
    • Species and density of implant surface chemistry affect the extent of foreign body reactions
    • Nair A., Zou L., Bhattacharyya D., Timmons R.B., and Tang L. Species and density of implant surface chemistry affect the extent of foreign body reactions. Langmuir 24 5 (2008) 2015-2024
    • (2008) Langmuir , vol.24 , Issue.5 , pp. 2015-2024
    • Nair, A.1    Zou, L.2    Bhattacharyya, D.3    Timmons, R.B.4    Tang, L.5
  • 71
    • 33645097169 scopus 로고    scopus 로고
    • Macroporous condensed poly(tetrafluoroethylene). I. In vivo inflammatory response and healing characteristics
    • Voskerician G., Gingras P.H., and Anderson J.M. Macroporous condensed poly(tetrafluoroethylene). I. In vivo inflammatory response and healing characteristics. J Biomed Mater Res A 76 2 (2006) 234-242
    • (2006) J Biomed Mater Res A , vol.76 , Issue.2 , pp. 234-242
    • Voskerician, G.1    Gingras, P.H.2    Anderson, J.M.3
  • 72
    • 48449089863 scopus 로고    scopus 로고
    • Deformation responses of a physically cross-linked high molecular weight elastin-like protein polymer
    • Wu X., Sallach R.E., Caves J.M., Conticello V.P., and Chaikof E.L. Deformation responses of a physically cross-linked high molecular weight elastin-like protein polymer. Biomacromolecules 9 (2008) 1787-1794
    • (2008) Biomacromolecules , vol.9 , pp. 1787-1794
    • Wu, X.1    Sallach, R.E.2    Caves, J.M.3    Conticello, V.P.4    Chaikof, E.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.