메뉴 건너뛰기




Volumn 8, Issue 10, 2013, Pages 1183-1192

Spider silks from plants - A challenge to create native-sized spidroins

Author keywords

Intein; Multimerization; Spider silk; Transgenic plants; Transglutaminase

Indexed keywords

INTEIN; MULTIMERIZATION; SPIDER SILKS; TRANSGENIC PLANTS; TRANSGLUTAMINASES;

EID: 84884965518     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201300204     Document Type: Review
Times cited : (17)

References (119)
  • 2
    • 2542558121 scopus 로고    scopus 로고
    • Broad patterns of speciation are correlated with the evolution of new silk proteins in spiders but not in the lepidoptera.
    • Craig, C. L., Broad patterns of speciation are correlated with the evolution of new silk proteins in spiders but not in the lepidoptera. Biomacromolecules 2004, 5, 739-743.
    • (2004) Biomacromolecules , vol.5 , pp. 739-743
    • Craig, C.L.1
  • 4
    • 0033377495 scopus 로고    scopus 로고
    • The mechanical design of spider silks: From fibroin sequence to mechanical function.
    • Gosline, J. M., Guerette, P. A., Ortlepp, C. S., Savage, K. N., The mechanical design of spider silks: From fibroin sequence to mechanical function. J. Exp. Biol. 1999, 202, 3295-3303.
    • (1999) J. Exp. Biol. , vol.202 , pp. 3295-3303
    • Gosline, J.M.1    Guerette, P.A.2    Ortlepp, C.S.3    Savage, K.N.4
  • 5
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk.
    • Vollrath, F., Knight, D. P., Liquid crystalline spinning of spider silk. Nature 2001, 410, 541-548.
    • (2001) Nature , vol.410 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 6
    • 0025008260 scopus 로고
    • Structure of a protein superfiber: Spider dragline silk.
    • Xu, M., Lewis, R. V., Structure of a protein superfiber: Spider dragline silk. Proc. Natl. Acad. Sci. USA 1990, 87, 7120-7124.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7120-7124
    • Xu, M.1    Lewis, R.V.2
  • 7
    • 0026657815 scopus 로고
    • Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber.
    • Hinman, M. B., Lewis, R. V., Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber. J. Biol. Chem. 1992, 267, 19320-19324.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19320-19324
    • Hinman, M.B.1    Lewis, R.V.2
  • 8
    • 0001354187 scopus 로고
    • Modulation of the mechanical-properties of spider silk by coating with water.
    • Vollrath, F., Edmonds, D. T., Modulation of the mechanical-properties of spider silk by coating with water. Nature 1989, 340, 305-307.
    • (1989) Nature , vol.340 , pp. 305-307
    • Vollrath, F.1    Edmonds, D.T.2
  • 9
    • 84993586739 scopus 로고
    • Thread biomechanics in the 2 orb-weaving spiders Araneus diadematus (Araneae, Araneidae) and Uloborus walckenaerius (Araneae, Uloboridae).
    • Kohler, T., Vollrath, F., Thread biomechanics in the 2 orb-weaving spiders Araneus diadematus (Araneae, Araneidae) and Uloborus walckenaerius (Araneae, Uloboridae). J. Exp. Zool. 1995, 271, 1-17.
    • (1995) J. Exp. Zool. , vol.271 , pp. 1-17
    • Kohler, T.1    Vollrath, F.2
  • 10
    • 63049104932 scopus 로고    scopus 로고
    • The elaborate structure of spider silk: Structure and function of a natural high performance fiber.
    • Römer, L., Scheibel, T., The elaborate structure of spider silk: Structure and function of a natural high performance fiber. Prion 2008, 2, 154-161.
    • (2008) Prion , vol.2 , pp. 154-161
    • Römer, L.1    Scheibel, T.2
  • 11
    • 0034858667 scopus 로고    scopus 로고
    • Spider flagelliform silk: Lessons in protein design, gene structure, and molecular evolution.
    • Hayashi, C. Y., Lewis, R. V., Spider flagelliform silk: Lessons in protein design, gene structure, and molecular evolution. Bioessays 2001, 23, 750-756.
    • (2001) Bioessays , vol.23 , pp. 750-756
    • Hayashi, C.Y.1    Lewis, R.V.2
  • 13
    • 0032963575 scopus 로고    scopus 로고
    • Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins.
    • Hayashi, C. Y., Shipley, N. H., Lewis, R. V., Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins. Int. J. Biol. Macromol. 1999, 24, 271-275.
    • (1999) Int. J. Biol. Macromol. , vol.24 , pp. 271-275
    • Hayashi, C.Y.1    Shipley, N.H.2    Lewis, R.V.3
  • 14
    • 13644260108 scopus 로고    scopus 로고
    • Spider silks: Recombinant synthesis, assembly, spinning, and engineering of synthetic proteins.
    • Scheibel, T., Spider silks: Recombinant synthesis, assembly, spinning, and engineering of synthetic proteins. Microb. Cell Factories 2004, 3, 14.
    • (2004) Microb. Cell Factories , vol.3 , pp. 14
    • Scheibel, T.1
  • 15
    • 0034711997 scopus 로고    scopus 로고
    • Molecular architecture and evolution of a modular spider silk protein gene.
    • Hayashi, C. Y., Lewis, R. V., Molecular architecture and evolution of a modular spider silk protein gene. Science 2000, 287, 1477-1479.
    • (2000) Science , vol.287 , pp. 1477-1479
    • Hayashi, C.Y.1    Lewis, R.V.2
  • 16
    • 33745633089 scopus 로고    scopus 로고
    • An essential role for the C-terminal domain of a dragline spider silk protein in directing fiber formation.
    • Ittah, S., Cohen, S., Garty, S., Cohn, D., Gat, U., An essential role for the C-terminal domain of a dragline spider silk protein in directing fiber formation. Biomacromolecules 2006, 7, 1790-1795.
    • (2006) Biomacromolecules , vol.7 , pp. 1790-1795
    • Ittah, S.1    Cohen, S.2    Garty, S.3    Cohn, D.4    Gat, U.5
  • 17
    • 78650693161 scopus 로고    scopus 로고
    • pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk - implications for fiber formation.
    • Hagn, F., Thamm, C., Scheibel, T., Kessler, H., pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk - implications for fiber formation. Angew. Chem. 2011, 50, 310-313.
    • (2011) Angew. Chem. , vol.50 , pp. 310-313
    • Hagn, F.1    Thamm, C.2    Scheibel, T.3    Kessler, H.4
  • 18
    • 77952337074 scopus 로고    scopus 로고
    • Self-assembly of spider silk proteins is controlled by a pH-sensitive relay.
    • Askarieh, G., Hedhammar, M., Nordling, K., Saenz, A. et al., Self-assembly of spider silk proteins is controlled by a pH-sensitive relay. Nature 2010, 465, 236-238.
    • (2010) Nature , vol.465 , pp. 236-238
    • Askarieh, G.1    Hedhammar, M.2    Nordling, K.3    Saenz, A.4
  • 20
    • 15444368211 scopus 로고    scopus 로고
    • Characterization of the protein components of Nephila clavipes dragline silk.
    • Sponner, A., Schlott, B., Vollrath, F., Unger, E. et al., Characterization of the protein components of Nephila clavipes dragline silk. Biochemistry 2005, 44, 4727-4736.
    • (2005) Biochemistry , vol.44 , pp. 4727-4736
    • Sponner, A.1    Schlott, B.2    Vollrath, F.3    Unger, E.4
  • 21
    • 36649007963 scopus 로고    scopus 로고
    • Blueprint for a high-performance biomaterial: Full-length spider dragline silk genes.
    • Ayoub, N. A., Garb, J. E., Tinghitella, R. M., Collin, M. A., Hayashi, C. Y., Blueprint for a high-performance biomaterial: Full-length spider dragline silk genes. PLoS ONE 2007, 2, e514.
    • (2007) PLoS ONE , vol.2
    • Ayoub, N.A.1    Garb, J.E.2    Tinghitella, R.M.3    Collin, M.A.4    Hayashi, C.Y.5
  • 22
    • 77956296603 scopus 로고    scopus 로고
    • Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber.
    • Xia, X. X., Qian, Z. G., Ki, C. S., Park, Y. H. et al., Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber. Proc. Natl. Acad. Sci. USA 2010, 107, 14059-14063.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 14059-14063
    • Xia, X.X.1    Qian, Z.G.2    Ki, C.S.3    Park, Y.H.4
  • 23
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants.
    • Hiatt, A., Cafferkey, R., Bowdish, K., Production of antibodies in transgenic plants. Nature 1989, 342, 76-78.
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Cafferkey, R.2    Bowdish, K.3
  • 24
    • 0027048769 scopus 로고
    • Expression of hepatitis B surface antigen in transgenic plants.
    • Mason, H. S., Lam, D. M., Arntzen, C. J., Expression of hepatitis B surface antigen in transgenic plants. Proc. Natl. Acad. Sci. USA 1992, 89, 11745-11749.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11745-11749
    • Mason, H.S.1    Lam, D.M.2    Arntzen, C.J.3
  • 25
    • 84884945053 scopus 로고    scopus 로고
    • Fischer, R., Schillberg, S., Molecular Farming, Wiley VCH Verlag GmbH & Co. KGaA, Weinheim 2004.
    • Fischer, R., Schillberg, S., Molecular Farming, Wiley VCH Verlag GmbH & Co. KGaA, Weinheim 2004.
  • 26
    • 70349759364 scopus 로고    scopus 로고
    • Plants as bioreactors: Recent developments and emerging opportunities.
    • Sharma, A. K., Sharma, M. K., Plants as bioreactors: Recent developments and emerging opportunities. Biotechnol. Adv. 2009, 27, 811-832.
    • (2009) Biotechnol. Adv. , vol.27 , pp. 811-832
    • Sharma, A.K.1    Sharma, M.K.2
  • 27
    • 84881351111 scopus 로고    scopus 로고
    • Phan, H. T., Floss, D. M., Conrad, U., Veterinary vaccines from transgenic plants: Highlights of two decades of research and a promising example. Curr. Pharm. Des. 2013, 19, 5601-5611.
    • Phan, H. T., Floss, D. M., Conrad, U., Veterinary vaccines from transgenic plants: Highlights of two decades of research and a promising example. Curr. Pharm. Des. 2013, 19, 5601-5611.
  • 28
    • 23744514106 scopus 로고    scopus 로고
    • Molecular farming for new drugs and vaccines. Current perspectives on the production of pharmaceuticals in transgenic plants.
    • Ma, J. K., Barros, E., Bock, R., Christou, P. et al., Molecular farming for new drugs and vaccines. Current perspectives on the production of pharmaceuticals in transgenic plants. EMBO Rep. 2005, 6, 593-599.
    • (2005) EMBO Rep. , vol.6 , pp. 593-599
    • Ma, J.K.1    Barros, E.2    Bock, R.3    Christou, P.4
  • 29
    • 14744305129 scopus 로고    scopus 로고
    • Vaccines and sera through plant biotechnology.
    • Koprowski, H., Vaccines and sera through plant biotechnology. Vaccine 2005, 23, 1757-1763.
    • (2005) Vaccine , vol.23 , pp. 1757-1763
    • Koprowski, H.1
  • 30
    • 17044406723 scopus 로고    scopus 로고
    • Sowing the seeds of success: Pharmaceutical proteins from plants.
    • Stoger, E., Ma, J. K., Fischer, R., Christou, P., Sowing the seeds of success: Pharmaceutical proteins from plants. Curr. Opin. Biotechnol. 2005, 16, 167-173.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 167-173
    • Stoger, E.1    Ma, J.K.2    Fischer, R.3    Christou, P.4
  • 31
    • 23444462483 scopus 로고    scopus 로고
    • Plant-based vaccines for animal health.
    • Streatfield, S. J., Plant-based vaccines for animal health. Rev. Sci. Tech. 2005, 24, 189-199.
    • (2005) Rev. Sci. Tech. , vol.24 , pp. 189-199
    • Streatfield, S.J.1
  • 32
    • 70349538837 scopus 로고    scopus 로고
    • The green vaccine: A global strategy to combat infectious and autoimmune diseases.
    • Davoodi-Semiromi, A., Samson, N., Daniell, H., The green vaccine: A global strategy to combat infectious and autoimmune diseases. Hum. Vaccines 2009, 5, 488-493.
    • (2009) Hum. Vaccines , vol.5 , pp. 488-493
    • Davoodi-Semiromi, A.1    Samson, N.2    Daniell, H.3
  • 33
    • 53849112341 scopus 로고    scopus 로고
    • Recent progress in the development of plant derived vaccines.
    • Yusibov, V., Rabindran, S., Recent progress in the development of plant derived vaccines. Expert Rev. Vaccines 2008, 7, 1173-1183.
    • (2008) Expert Rev. Vaccines , vol.7 , pp. 1173-1183
    • Yusibov, V.1    Rabindran, S.2
  • 34
    • 49349095531 scopus 로고    scopus 로고
    • Considerations for extraction of monoclonal antibodies targeted to different subcellular compartments in transgenic tobacco plants.
    • Hassan, S., van Dolleweerd, C. J., Ioakeimidis, F., Keshavarz-Moore, E., Ma, J. K., Considerations for extraction of monoclonal antibodies targeted to different subcellular compartments in transgenic tobacco plants. Plant Biotechnol. J. 2008, 6, 733-748.
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 733-748
    • Hassan, S.1    van Dolleweerd, C.J.2    Ioakeimidis, F.3    Keshavarz-Moore, E.4    Ma, J.K.5
  • 35
    • 0036901079 scopus 로고    scopus 로고
    • Monoclonal antibody manufacturing in transgenic plants - myths and realities.
    • Hood, E. E., Woodard, S. L., Horn, M. E., Monoclonal antibody manufacturing in transgenic plants - myths and realities. Curr. Opin. Biotechnol. 2002, 13, 630-635.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 630-635
    • Hood, E.E.1    Woodard, S.L.2    Horn, M.E.3
  • 36
    • 77949837380 scopus 로고    scopus 로고
    • Purification of plant-derived antibodies through direct immobilization of affinity ligands on cellulose.
    • Hussack, G., Grohs, B. M., Almquist, K. C., McLean, M. D. et al., Purification of plant-derived antibodies through direct immobilization of affinity ligands on cellulose. J. Agric. Food Chem. 2010, 58, 3451-3459.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 3451-3459
    • Hussack, G.1    Grohs, B.M.2    Almquist, K.C.3    McLean, M.D.4
  • 37
    • 71849085389 scopus 로고    scopus 로고
    • Elastin-like polypeptides revolutionize recombinant protein expression and their biomedical application.
    • Floss, D. M., Schallau, K., Rose-John, S., Conrad, U., Scheller, J., Elastin-like polypeptides revolutionize recombinant protein expression and their biomedical application. Trends Biotechnol. 2010, 28, 37-45.
    • (2010) Trends Biotechnol. , vol.28 , pp. 37-45
    • Floss, D.M.1    Schallau, K.2    Rose-John, S.3    Conrad, U.4    Scheller, J.5
  • 38
    • 79954759457 scopus 로고    scopus 로고
    • Protein body-inducing fusions for high-level production and purification of recombinant proteins in plants.
    • Conley, A. J., Joensuu, J. J., Richman, A., Menassa, R., Protein body-inducing fusions for high-level production and purification of recombinant proteins in plants. Plant Biotechnol. J. 2011, 9, 419-433.
    • (2011) Plant Biotechnol. J. , vol.9 , pp. 419-433
    • Conley, A.J.1    Joensuu, J.J.2    Richman, A.3    Menassa, R.4
  • 39
    • 84886200449 scopus 로고    scopus 로고
    • Floss, D. M., Conrad, U., Rose-John, S., Scheller, J., ELP fusion technology for biopharmaceuticals, in: Schmidt, S. R. (Ed.), Fusion Protein Technologies for Biopharmaceuticals: Applications and Challenges, Wiley Blackwell, Hoboken, NJ 2013 211-226.
    • Floss, D. M., Conrad, U., Rose-John, S., Scheller, J., ELP fusion technology for biopharmaceuticals, in: Schmidt, S. R. (Ed.), Fusion Protein Technologies for Biopharmaceuticals: Applications and Challenges, Wiley Blackwell, Hoboken, NJ 2013, pp. 211-226.
  • 40
    • 0020741494 scopus 로고
    • Regeneration of intact tobacco plants containing full length copies of genetically engineered T-DNA, and transmission of T-DNA to R1 progeny.
    • Barton, K. A., Binns, A. N., Matzke, A. J., Chilton, M. D., Regeneration of intact tobacco plants containing full length copies of genetically engineered T-DNA, and transmission of T-DNA to R1 progeny. Cell 1983, 32, 1033-1043.
    • (1983) Cell , vol.32 , pp. 1033-1043
    • Barton, K.A.1    Binns, A.N.2    Matzke, A.J.3    Chilton, M.D.4
  • 41
  • 42
    • 84884940283 scopus 로고    scopus 로고
    • Faye, L., Gomord, V., Recombinant Proteins From Plants, Humana Press, New York 2009.
    • Faye, L., Gomord, V., Recombinant Proteins From Plants, Humana Press, New York 2009.
  • 43
    • 0035007556 scopus 로고    scopus 로고
    • Production of spider silk proteins in tobacco and potato.
    • Scheller, J., Guhrs, K. H., Grosse, F., Conrad, U., Production of spider silk proteins in tobacco and potato. Nat. Biotechnol. 2001, 19, 573-577.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 573-577
    • Scheller, J.1    Guhrs, K.H.2    Grosse, F.3    Conrad, U.4
  • 44
    • 13444310778 scopus 로고    scopus 로고
    • Spider dragline silk proteins in transgenic tobacco leaves: Accumulation and field production.
    • Menassa, R., Zhu, H., Karatzas, C. N., Lazaris, A. et al., Spider dragline silk proteins in transgenic tobacco leaves: Accumulation and field production. Plant Biotechnol. J. 2004, 2, 431-438.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 431-438
    • Menassa, R.1    Zhu, H.2    Karatzas, C.N.3    Lazaris, A.4
  • 45
    • 4043127730 scopus 로고    scopus 로고
    • Production and purification of recombinant DP1B silk-like protein in plants.
    • Barr, L. A., Fahnestock, S. R., Yang, J. J., Production and purification of recombinant DP1B silk-like protein in plants. Mol. Breeding 2004, 13, 345-356.
    • (2004) Mol. Breeding , vol.13 , pp. 345-356
    • Barr, L.A.1    Fahnestock, S.R.2    Yang, J.J.3
  • 46
    • 84884947745 scopus 로고    scopus 로고
    • Rakhimova, M., Martin-Luther-Universität Halle-Wittenberg, Halle/Saale 2007.
    • Rakhimova, M., Martin-Luther-Universität Halle-Wittenberg, Halle/Saale 2007.
  • 48
    • 22144493886 scopus 로고    scopus 로고
    • High yield recombinant silk-like protein production in transgenic plants through protein targeting.
    • Yang, J., Barr, L. A., Fahnestock, S. R., Liu, Z. B., High yield recombinant silk-like protein production in transgenic plants through protein targeting. Transgenic Res. 2005, 14, 313-324.
    • (2005) Transgenic Res. , vol.14 , pp. 313-324
    • Yang, J.1    Barr, L.A.2    Fahnestock, S.R.3    Liu, Z.B.4
  • 49
    • 0028889621 scopus 로고
    • High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds.
    • Fiedler, U., Conrad, U., High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds. Biotechnology 1995, 13, 1090-1093.
    • (1995) Biotechnology , vol.13 , pp. 1090-1093
    • Fiedler, U.1    Conrad, U.2
  • 50
    • 1542646078 scopus 로고    scopus 로고
    • Purification of spider silk-elastin from transgenic plants and application for human chondrocyte proliferation.
    • Scheller, J., Henggeler, D., Viviani, A., Conrad, U., Purification of spider silk-elastin from transgenic plants and application for human chondrocyte proliferation. Transgenic Res. 2004, 13, 51-57.
    • (2004) Transgenic Res. , vol.13 , pp. 51-57
    • Scheller, J.1    Henggeler, D.2    Viviani, A.3    Conrad, U.4
  • 51
    • 33947315594 scopus 로고    scopus 로고
    • Elastin-like polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves.
    • Patel, J., Zhu, H., Menassa, R., Gyenis, L. et al., Elastin-like polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves. Transgenic Res. 2007, 16, 239-249.
    • (2007) Transgenic Res. , vol.16 , pp. 239-249
    • Patel, J.1    Zhu, H.2    Menassa, R.3    Gyenis, L.4
  • 52
    • 84874809999 scopus 로고    scopus 로고
    • Native-sized spider silk proteins synthesized in planta via intein-based multimerization.
    • Hauptmann, V., Weichert, N., Menzel, M., Knoch, D. et al., Native-sized spider silk proteins synthesized in planta via intein-based multimerization. Transgenic Res. 2013, 22, 369-377.
    • (2013) Transgenic Res. , vol.22 , pp. 369-377
    • Hauptmann, V.1    Weichert, N.2    Menzel, M.3    Knoch, D.4
  • 53
    • 0029100089 scopus 로고
    • Construction, cloning, and expression of synthetic genes encoding spider dragline silk.
    • Prince, J. T., McGrath, K. P., DiGirolamo, C. M., Kaplan, D. L., Construction, cloning, and expression of synthetic genes encoding spider dragline silk. Biochemistry 1995, 34, 10879-10885.
    • (1995) Biochemistry , vol.34 , pp. 10879-10885
    • Prince, J.T.1    McGrath, K.P.2    DiGirolamo, C.M.3    Kaplan, D.L.4
  • 54
    • 0030174911 scopus 로고    scopus 로고
    • Expression and purification of a spider silk protein: A new strategy for producing repetitive proteins.
    • Lewis, R. V., Hinman, M., Kothakota, S., Fournier, M. J., Expression and purification of a spider silk protein: A new strategy for producing repetitive proteins. Protein Expr. Purif. 1996, 7, 400-406.
    • (1996) Protein Expr. Purif. , vol.7 , pp. 400-406
    • Lewis, R.V.1    Hinman, M.2    Kothakota, S.3    Fournier, M.J.4
  • 55
    • 0031039711 scopus 로고    scopus 로고
    • Synthetic spider dragline silk proteins and their production in Escherichia coli.
    • Fahnestock, S. R., Irwin, S. L., Synthetic spider dragline silk proteins and their production in Escherichia coli. Appl. Microbiol. Biotechnol. 1997, 47, 23-32.
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 23-32
    • Fahnestock, S.R.1    Irwin, S.L.2
  • 56
    • 0031962660 scopus 로고    scopus 로고
    • Purification and characterization of recombinant spider silk expressed in Escherichia coli.
    • Arcidiacono, S., Mello, C., Kaplan, D., Cheley, S., Bayley, H., Purification and characterization of recombinant spider silk expressed in Escherichia coli. Appl. Microbiol. Biotechnol. 1998, 49, 31-38.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 31-38
    • Arcidiacono, S.1    Mello, C.2    Kaplan, D.3    Cheley, S.4    Bayley, H.5
  • 57
    • 78651367978 scopus 로고    scopus 로고
    • Spider silk proteins: Recent advances in recombinant production, structure-function relationships and biomedical applications.
    • Rising, A., Widhe, M., Johansson, J., Hedhammar, M., Spider silk proteins: Recent advances in recombinant production, structure-function relationships and biomedical applications. Cell. Molecul. Life Sci. 2011, 68, 169-184.
    • (2011) Cell. Molecul. Life Sci. , vol.68 , pp. 169-184
    • Rising, A.1    Widhe, M.2    Johansson, J.3    Hedhammar, M.4
  • 58
    • 84884932300 scopus 로고    scopus 로고
    • Mello, C., Arcidiacono, S., Butler, M., Methods for the purification and aqueous fiber spinning of spider silks and other structural proteins. US Patent 7, 335, 739 B2, 2008.
    • Mello, C., Arcidiacono, S., Butler, M., Methods for the purification and aqueous fiber spinning of spider silks and other structural proteins. US Patent 7, 335, 739 B2, 2008.
  • 59
    • 6344228390 scopus 로고    scopus 로고
    • Primary structure elements of spider dragline silks and their contribution to protein solubility.
    • Huemmerich, D., Helsen, C. W., Quedzuweit, S., Oschmann, J. et al., Primary structure elements of spider dragline silks and their contribution to protein solubility. Biochemistry 2004, 43, 13604-13612.
    • (2004) Biochemistry , vol.43 , pp. 13604-13612
    • Huemmerich, D.1    Helsen, C.W.2    Quedzuweit, S.3    Oschmann, J.4
  • 61
    • 14744279937 scopus 로고    scopus 로고
    • Plant-based material, protein and biodegradable plastic.
    • Scheller, J., Conrad, U., Plant-based material, protein and biodegradable plastic. Curr. Opin. Plant Biol. 2005, 8, 188-196.
    • (2005) Curr. Opin. Plant Biol. , vol.8 , pp. 188-196
    • Scheller, J.1    Conrad, U.2
  • 62
    • 0023953406 scopus 로고
    • Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics.
    • Urry, D. W., Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics. J. Protein Chem. 1988, 7, 1-34.
    • (1988) J. Protein Chem. , vol.7 , pp. 1-34
    • Urry, D.W.1
  • 63
    • 0026468684 scopus 로고
    • Free energy transduction in polypeptides and proteins based on inverse temperature transitions.
    • Urry, D. W., Free energy transduction in polypeptides and proteins based on inverse temperature transitions. Prog. Biophys. Mol. Biol. 1992, 57, 23-57.
    • (1992) Prog. Biophys. Mol. Biol. , vol.57 , pp. 23-57
    • Urry, D.W.1
  • 64
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides.
    • Meyer, D. E., Chilkoti, A., Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat. Biotechnol. 1999, 17, 1112-1115.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1112-1115
    • Meyer, D.E.1    Chilkoti, A.2
  • 65
    • 79957837910 scopus 로고    scopus 로고
    • Membrane-based inverse transition cycling: An improved means for purifying plant-derived recombinant protein-elastin-like polypeptide fusions.
    • Phan, H. T., Conrad, U., Membrane-based inverse transition cycling: An improved means for purifying plant-derived recombinant protein-elastin-like polypeptide fusions. Int. J. Mol. Sci. 2011, 12, 2808-2821.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 2808-2821
    • Phan, H.T.1    Conrad, U.2
  • 66
    • 33749342367 scopus 로고    scopus 로고
    • Purification of an elastin-like fusion protein by microfiltration.
    • Ge, X., Trabbic-Carlson, K., Chilkoti, A., Filipe, C. D., Purification of an elastin-like fusion protein by microfiltration. Biotechnol. Bioeng. 2006, 95, 424-432.
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 424-432
    • Ge, X.1    Trabbic-Carlson, K.2    Chilkoti, A.3    Filipe, C.D.4
  • 67
    • 24044491571 scopus 로고    scopus 로고
    • Simple bioseparations using self-cleaving elastin-like polypeptide tags.
    • Banki, M. R., Feng, L., Wood, D. W., Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nat. Methods 2005, 2, 659-661.
    • (2005) Nat. Methods , vol.2 , pp. 659-661
    • Banki, M.R.1    Feng, L.2    Wood, D.W.3
  • 68
    • 23844438834 scopus 로고    scopus 로고
    • Self-cleavable stimulus responsive tags for protein purification without chromatography.
    • Ge, X., Yang, D. S., Trabbic-Carlson, K., Kim, B. et al., Self-cleavable stimulus responsive tags for protein purification without chromatography. J. Am. Chem. Soc. 2005, 127, 11228-11229.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11228-11229
    • Ge, X.1    Yang, D.S.2    Trabbic-Carlson, K.3    Kim, B.4
  • 69
    • 77952736311 scopus 로고    scopus 로고
    • Purification of Escherichia coli RNA polymerase using a self-cleaving elastin-like polypeptide tag.
    • Fong, B. A., Gillies, A. R., Ghazi, I., LeRoy, G. et al., Purification of Escherichia coli RNA polymerase using a self-cleaving elastin-like polypeptide tag. Protein Sci. 2010, 19, 1243-1252.
    • (2010) Protein Sci. , vol.19 , pp. 1243-1252
    • Fong, B.A.1    Gillies, A.R.2    Ghazi, I.3    LeRoy, G.4
  • 70
    • 0032488823 scopus 로고    scopus 로고
    • Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks.
    • Hayashi, C. Y., Lewis, R. V., Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks. J. Mol. Biol. 1998, 275, 773-784.
    • (1998) J. Mol. Biol. , vol.275 , pp. 773-784
    • Hayashi, C.Y.1    Lewis, R.V.2
  • 71
    • 0029925013 scopus 로고    scopus 로고
    • Silk properties determined by gland-specific expression of a spider fibroin gene family.
    • Guerette, P. A., Ginzinger, D. G., Weber, B. H., Gosline, J. M., Silk properties determined by gland-specific expression of a spider fibroin gene family. Science 1996, 272, 112-115.
    • (1996) Science , vol.272 , pp. 112-115
    • Guerette, P.A.1    Ginzinger, D.G.2    Weber, B.H.3    Gosline, J.M.4
  • 72
    • 0028223512 scopus 로고
    • Sequence conservation in the C-terminal region of spider silk proteins (Spidroin) from Nephila clavipes (Tetragnathidae) and Araneus bicentenarius (Araneidae).
    • Beckwitt, R., Arcidiacono, S., Sequence conservation in the C-terminal region of spider silk proteins (Spidroin) from Nephila clavipes (Tetragnathidae) and Araneus bicentenarius (Araneidae). J. Biol. Chem. 1994, 269, 6661-6663.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6661-6663
    • Beckwitt, R.1    Arcidiacono, S.2
  • 73
    • 33749832915 scopus 로고    scopus 로고
    • Spider silk: Ancient ideas for new biomaterials.
    • Lewis, R. V., Spider silk: Ancient ideas for new biomaterials. Chem. Rev. 2006, 106, 3762-3774.
    • (2006) Chem. Rev. , vol.106 , pp. 3762-3774
    • Lewis, R.V.1
  • 74
    • 0030940619 scopus 로고    scopus 로고
    • Evolution of arthropod silks.
    • Craig, C. L., Evolution of arthropod silks. Ann. Rev. Entomol. 1997, 42, 231-267.
    • (1997) Ann. Rev. Entomol. , vol.42 , pp. 231-267
    • Craig, C.L.1
  • 75
    • 2542619069 scopus 로고    scopus 로고
    • Conserved C-termini of Spidroins are secreted by the major ampullate glands and retained in the silk thread.
    • Sponner, A., Unger, E., Grosse, F., Weisshart, K., Conserved C-termini of Spidroins are secreted by the major ampullate glands and retained in the silk thread. Biomacromolecules 2004, 5, 840-845.
    • (2004) Biomacromolecules , vol.5 , pp. 840-845
    • Sponner, A.1    Unger, E.2    Grosse, F.3    Weisshart, K.4
  • 76
    • 79951949195 scopus 로고    scopus 로고
    • Model based optimization of the fed-batch production of a highly active transglutaminase variant in Escherichia coli.
    • Sommer, C., Volk, N., Pietzsch, M., Model based optimization of the fed-batch production of a highly active transglutaminase variant in Escherichia coli. Protein Expr. Purif. 2011, 77, 9-19.
    • (2011) Protein Expr. Purif. , vol.77 , pp. 9-19
    • Sommer, C.1    Volk, N.2    Pietzsch, M.3
  • 77
    • 84861715727 scopus 로고    scopus 로고
    • Investigations on the activation of recombinant microbial pro-transglutaminase: In contrast to proteinase K, dispase removes the histidine-tag.
    • Sommer, C., Hertel, T. C., Schmelzer, C. E., Pietzsch, M., Investigations on the activation of recombinant microbial pro-transglutaminase: In contrast to proteinase K, dispase removes the histidine-tag. Amino Acids 2012, 42, 997-1006.
    • (2012) Amino Acids , vol.42 , pp. 997-1006
    • Sommer, C.1    Hertel, T.C.2    Schmelzer, C.E.3    Pietzsch, M.4
  • 78
    • 84355161672 scopus 로고    scopus 로고
    • Enzymatic cross-linking of human recombinant elastin (HELP) as biomimetic approach in vascular tissue engineering.
    • Bozzini, S., Giuliano, L., Altomare, L., Petrini, P. et al., Enzymatic cross-linking of human recombinant elastin (HELP) as biomimetic approach in vascular tissue engineering. J. Mater. Sci. Mater. Med. 2011, 22, 2641-2650.
    • (2011) J. Mater. Sci. Mater. Med. , vol.22 , pp. 2641-2650
    • Bozzini, S.1    Giuliano, L.2    Altomare, L.3    Petrini, P.4
  • 79
    • 80051797782 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed preparation of human elastin-like polypeptide-based three-dimensional matrices for cell encapsulation.
    • Bandiera, A., Transglutaminase-catalyzed preparation of human elastin-like polypeptide-based three-dimensional matrices for cell encapsulation. Enzyme Microbial. Technol. 2011, 49, 347-352.
    • (2011) Enzyme Microbial. Technol. , vol.49 , pp. 347-352
    • Bandiera, A.1
  • 80
    • 84884947218 scopus 로고    scopus 로고
    • Schallau, K., Martin-Luther Universität Halle-Wittenberg 2008.
    • Schallau, K., Martin-Luther Universität Halle-Wittenberg 2008.
  • 81
    • 0028214350 scopus 로고
    • Protein splicing elements: Inteins and exteins - a definition of terms and recommended nomenclature.
    • Perler, F. B., Davis, E. O., Dean, G. E., Gimble, F. S. et al., Protein splicing elements: Inteins and exteins - a definition of terms and recommended nomenclature. Nucleic Acids Res. 1994, 22, 1125-1127.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1125-1127
    • Perler, F.B.1    Davis, E.O.2    Dean, G.E.3    Gimble, F.S.4
  • 82
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The intein database.
    • Perler, F. B., InBase: The intein database. Nucleic Acids Res. 2002, 30, 383-384.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 83
    • 17744415288 scopus 로고    scopus 로고
    • Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element.
    • Chong, S., Mersha, F. B., Comb, D. G., Scott, M. E. et al., Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene 1997, 192, 271-281.
    • (1997) Gene , vol.192 , pp. 271-281
    • Chong, S.1    Mersha, F.B.2    Comb, D.G.3    Scott, M.E.4
  • 84
    • 0034881178 scopus 로고    scopus 로고
    • Cloning, expression, and purification of the Staphylococcus simulans lysostaphin using the intein-chitin-binding domain (CBD) system.
    • Szweda, P., Pladzyk, R., Kotlowski, R., Kur, J., Cloning, expression, and purification of the Staphylococcus simulans lysostaphin using the intein-chitin-binding domain (CBD) system. Protein Expr. Purif. 2001, 22, 467-471.
    • (2001) Protein Expr. Purif. , vol.22 , pp. 467-471
    • Szweda, P.1    Pladzyk, R.2    Kotlowski, R.3    Kur, J.4
  • 85
    • 54349103050 scopus 로고    scopus 로고
    • One-step refolding and purification of disulfide-containing proteins with a C-terminal MESNA thioester.
    • Bastings, M. M., van Baal, I., Meijer, E. W., Merkx, M., One-step refolding and purification of disulfide-containing proteins with a C-terminal MESNA thioester. BMC Biotechnology. 2008, 8, 76.
    • (2008) BMC Biotechnology. , vol.8 , pp. 76
    • Bastings, M.M.1    van Baal, I.2    Meijer, E.W.3    Merkx, M.4
  • 86
    • 77953043452 scopus 로고    scopus 로고
    • Inteins, valuable genetic elements in molecular biology and biotechnology.
    • Elleuche, S., Poggeler, S., Inteins, valuable genetic elements in molecular biology and biotechnology. Appl. Microbiol. Biotechnol. 2010, 87, 479-489.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 479-489
    • Elleuche, S.1    Poggeler, S.2
  • 87
    • 77957921588 scopus 로고    scopus 로고
    • Expression and purification of ELP-intein-tagged target proteins in high cell density E.coli fermentation.
    • Fong, B. A., Wood, D. W., Expression and purification of ELP-intein-tagged target proteins in high cell density E.coli fermentation. Microb. Cell Factories 2010, 9, 77.
    • (2010) Microb. Cell Factories , vol.9 , pp. 77
    • Fong, B.A.1    Wood, D.W.2
  • 88
    • 24944448735 scopus 로고    scopus 로고
    • Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies.
    • Zuger, S., Iwai, H., Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies. Nat. Biotechnol. 2005, 23, 736-740.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 736-740
    • Zuger, S.1    Iwai, H.2
  • 89
    • 0344351815 scopus 로고    scopus 로고
    • Semisynthesis of cytotoxic proteins using a modified protein splicing element.
    • Evans, T. C. Jr., Benner, J., Xu, M. Q., Semisynthesis of cytotoxic proteins using a modified protein splicing element. Protein Sci. 1998, 7, 2256-2264.
    • (1998) Protein Sci. , vol.7 , pp. 2256-2264
    • Evans Jr, T.C.1    Benner, J.2    Xu, M.Q.3
  • 90
    • 37349020079 scopus 로고    scopus 로고
    • Expression of a cytotoxic cationic antibacterial peptide in Escherichia coli using two fusion partners.
    • Chen, Y. Q., Zhang, S. Q., Li, B. C., Qiu, W. et al., Expression of a cytotoxic cationic antibacterial peptide in Escherichia coli using two fusion partners. Protein Expr. Purif. 2008, 57, 303-311.
    • (2008) Protein Expr. Purif. , vol.57 , pp. 303-311
    • Chen, Y.Q.1    Zhang, S.Q.2    Li, B.C.3    Qiu, W.4
  • 91
    • 62149136168 scopus 로고    scopus 로고
    • Intein-mediated protein assembly in transgenic wheat: Production of active barnase and acetolactate synthase from split genes.
    • Kempe, K., Rubtsova, M., Gils, M., Intein-mediated protein assembly in transgenic wheat: Production of active barnase and acetolactate synthase from split genes. Plant Biotechnol. J. 2009, 7, 283-297.
    • (2009) Plant Biotechnol. J. , vol.7 , pp. 283-297
    • Kempe, K.1    Rubtsova, M.2    Gils, M.3
  • 92
    • 70349446285 scopus 로고    scopus 로고
    • Protein splicing: A versatile tool for drug discovery.
    • Cheriyan, M., Perler, F. B., Protein splicing: A versatile tool for drug discovery. Adv. Drug Deliv. Rev. 2009, 61, 899-907.
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 899-907
    • Cheriyan, M.1    Perler, F.B.2
  • 93
    • 79958716452 scopus 로고    scopus 로고
    • Expression of a new chimeric protein with a highly repeated sequence in tobacco cells.
    • Saumonneau, A., Rottier, K., Conrad, U., Popineau, Y. et al., Expression of a new chimeric protein with a highly repeated sequence in tobacco cells. Plant Cell Rep. 2011, 30, 1289-1302.
    • (2011) Plant Cell Rep. , vol.30 , pp. 1289-1302
    • Saumonneau, A.1    Rottier, K.2    Conrad, U.3    Popineau, Y.4
  • 94
    • 58149308835 scopus 로고    scopus 로고
    • Molecular design of performance proteins with repetitive sequences: Recombinant flagelliform spider silk as basis for biomaterials.
    • Vendrely, C., Ackerschott, C., Römer, L., Scheibel, T., Molecular design of performance proteins with repetitive sequences: Recombinant flagelliform spider silk as basis for biomaterials. Methods Mol. Biol. 2008, 474, 3-14.
    • (2008) Methods Mol. Biol. , vol.474 , pp. 3-14
    • Vendrely, C.1    Ackerschott, C.2    Römer, L.3    Scheibel, T.4
  • 96
    • 0036342066 scopus 로고    scopus 로고
    • Local tolerance to spider silks and protein polymers in vivo.
    • Vollrath, F., Barth, P., Basedow, A., Engstrom, W., List, H., Local tolerance to spider silks and protein polymers in vivo. In Vivo 2002, 16, 229-234.
    • (2002) In Vivo , vol.16 , pp. 229-234
    • Vollrath, F.1    Barth, P.2    Basedow, A.3    Engstrom, W.4    List, H.5
  • 98
    • 84862602764 scopus 로고    scopus 로고
    • Evidence for antimicrobial activity associated with common house spider silk.
    • Wright, S., Goodacre, S. L., Evidence for antimicrobial activity associated with common house spider silk. BMC Res. Notes 2012, 5, 326.
    • (2012) BMC Res. Notes , vol.5 , pp. 326
    • Wright, S.1    Goodacre, S.L.2
  • 99
  • 100
    • 43749110254 scopus 로고    scopus 로고
    • Spider silk fibres in artificial nerve constructs promote peripheral nerve regeneration.
    • Allmeling, C., Jokuszies, A., Reimers, K., Kall, S. et al., Spider silk fibres in artificial nerve constructs promote peripheral nerve regeneration. Cell Prolif. 2008, 41, 408-420.
    • (2008) Cell Prolif. , vol.41 , pp. 408-420
    • Allmeling, C.1    Jokuszies, A.2    Reimers, K.3    Kall, S.4
  • 101
    • 79952133242 scopus 로고    scopus 로고
    • Spider silk constructs enhance axonal regeneration and remyelination in long nerve defects in sheep.
    • Radtke, C., Allmeling, C., Waldmann, K. H., Reimers, K. et al., Spider silk constructs enhance axonal regeneration and remyelination in long nerve defects in sheep. PLoS ONE 2011, 6, e16990.
    • (2011) PLoS ONE , vol.6
    • Radtke, C.1    Allmeling, C.2    Waldmann, K.H.3    Reimers, K.4
  • 102
    • 33845332079 scopus 로고    scopus 로고
    • Use of spider silk fibres as an innovative material in a biocompatible artificial nerve conduit.
    • Allmeling, C., Jokuszies, A., Reimers, K., Kall, S., Vogt, P. M., Use of spider silk fibres as an innovative material in a biocompatible artificial nerve conduit. J. Cell Mol. Med. 2006, 10, 770-777.
    • (2006) J. Cell Mol. Med. , vol.10 , pp. 770-777
    • Allmeling, C.1    Jokuszies, A.2    Reimers, K.3    Kall, S.4    Vogt, P.M.5
  • 103
    • 33846005182 scopus 로고    scopus 로고
    • RGD-functionalized bioengineered spider dragline silk biomaterial.
    • Bini, E., Foo, C. W., Huang, J., Karageorgiou, V. et al., RGD-functionalized bioengineered spider dragline silk biomaterial. Biomacromolecules 2006, 7, 3139-3145.
    • (2006) Biomacromolecules , vol.7 , pp. 3139-3145
    • Bini, E.1    Foo, C.W.2    Huang, J.3    Karageorgiou, V.4
  • 104
    • 1842484779 scopus 로고    scopus 로고
    • Designing materials for biology and medicine.
    • Langer, R., Tirrell, D. A., Designing materials for biology and medicine. Nature 2004, 428, 487-492.
    • (2004) Nature , vol.428 , pp. 487-492
    • Langer, R.1    Tirrell, D.A.2
  • 105
    • 78649846843 scopus 로고    scopus 로고
    • Cell penetrating elastin-like polypeptides for therapeutic peptide delivery.
    • Bidwell, G. L., Raucher, D., Cell penetrating elastin-like polypeptides for therapeutic peptide delivery. Adv. Drug Deliv. Reviews 2010, 62, 1486-1496.
    • (2010) Adv. Drug Deliv. Reviews , vol.62 , pp. 1486-1496
    • Bidwell, G.L.1    Raucher, D.2
  • 106
    • 26944459231 scopus 로고    scopus 로고
    • Silk implants for the healing of critical size bone defects.
    • Meinel, L., Fajardo, R., Hofmann, S., Langer, R. et al., Silk implants for the healing of critical size bone defects. Bone 2005, 37, 688-698.
    • (2005) Bone , vol.37 , pp. 688-698
    • Meinel, L.1    Fajardo, R.2    Hofmann, S.3    Langer, R.4
  • 107
    • 78049421751 scopus 로고    scopus 로고
    • Ingrowth of human mesenchymal stem cells into porous silk particle reinforced silk composite scaffolds: An in vitro study.
    • Rockwood, D. N., Gil, E. S., Park, S. H., Kluge, J. A. et al., Ingrowth of human mesenchymal stem cells into porous silk particle reinforced silk composite scaffolds: An in vitro study. Acta Biomat. 2011, 7, 144-151.
    • (2011) Acta Biomat. , vol.7 , pp. 144-151
    • Rockwood, D.N.1    Gil, E.S.2    Park, S.H.3    Kluge, J.A.4
  • 109
    • 8544278195 scopus 로고    scopus 로고
    • Bone morphogenetic protein-2 decorated silk fibroin films induce osteogenic differentiation of human bone marrow stromal cells.
    • Karageorgiou, V., Meinel, L., Hofmann, S., Malhotra, A. et al., Bone morphogenetic protein-2 decorated silk fibroin films induce osteogenic differentiation of human bone marrow stromal cells. J. Biomed. Mater. Res. Part A 2004, 71, 528-537.
    • (2004) J. Biomed. Mater. Res. Part A , vol.71 , pp. 528-537
    • Karageorgiou, V.1    Meinel, L.2    Hofmann, S.3    Malhotra, A.4
  • 110
    • 4043074966 scopus 로고    scopus 로고
    • Fibroin hydrogels for biomedical applications: Preparation, characterization and in vitro cell culture studies.
    • Motta, A., Migliaresi, C., Faccioni, F., Torricelli, P. et al., Fibroin hydrogels for biomedical applications: Preparation, characterization and in vitro cell culture studies. J. Biomater. Sci. Polym. Ed. 2004, 15, 851-864.
    • (2004) J. Biomater. Sci. Polym. Ed. , vol.15 , pp. 851-864
    • Motta, A.1    Migliaresi, C.2    Faccioni, F.3    Torricelli, P.4
  • 111
    • 27544465971 scopus 로고    scopus 로고
    • Biological efficacy of silk fibroin nanofiber membranes for guided bone regeneration.
    • Kim, K. H., Jeong, L., Park, H. N., Shin, S. Y. et al., Biological efficacy of silk fibroin nanofiber membranes for guided bone regeneration. J. Biotechnol. 2005, 120, 327-339.
    • (2005) J. Biotechnol. , vol.120 , pp. 327-339
    • Kim, K.H.1    Jeong, L.2    Park, H.N.3    Shin, S.Y.4
  • 112
    • 78651351099 scopus 로고
    • A discourse upon the usefulness of the silk of spiders.
    • Bon, M., A discourse upon the usefulness of the silk of spiders. Philos. Trans. 1710, 27, 2-16.
    • (1710) Philos. Trans. , vol.27 , pp. 2-16
    • Bon, M.1
  • 113
    • 0028933997 scopus 로고
    • Oh what a tangled web: The medicinal uses of spider silk.
    • Newman, J., Newman, C., Oh what a tangled web: The medicinal uses of spider silk. Int. J. Dermatol. 1995, 34, 290-292.
    • (1995) Int. J. Dermatol. , vol.34 , pp. 290-292
    • Newman, J.1    Newman, C.2
  • 114
    • 79960825396 scopus 로고    scopus 로고
    • Artificial skin - culturing of different skin cell lines for generating an artificial skin substitute on cross-weaved spider silk fibres.
    • Wendt, H., Hillmer, A., Reimers, K., Kuhbier, J. W. et al., Artificial skin - culturing of different skin cell lines for generating an artificial skin substitute on cross-weaved spider silk fibres. PLoS ONE 2011, 6, e21833.
    • (2011) PLoS ONE , vol.6
    • Wendt, H.1    Hillmer, A.2    Reimers, K.3    Kuhbier, J.W.4
  • 115
    • 0031687593 scopus 로고    scopus 로고
    • Effect of surface properties on the antithrombogenicity of silk fibroin/S-carboxymethyl kerateine blend films.
    • Lee, K. Y., Kong, S. J., Park, W. H., Ha, W. S., Kwon, I. C., Effect of surface properties on the antithrombogenicity of silk fibroin/S-carboxymethyl kerateine blend films. J. Biomater. Sci. Polym. Ed. 1998, 9, 905-914.
    • (1998) J. Biomater. Sci. Polym. Ed. , vol.9 , pp. 905-914
    • Lee, K.Y.1    Kong, S.J.2    Park, W.H.3    Ha, W.S.4    Kwon, I.C.5
  • 116
    • 0030731752 scopus 로고    scopus 로고
    • Optimization of scFv antibody production in transgenic plants.
    • Fiedler, U., Phillips, J., Artsaenko, O., Conrad, U., Optimization of scFv antibody production in transgenic plants. Immunotechnology 1997, 3, 205-216.
    • (1997) Immunotechnology , vol.3 , pp. 205-216
    • Fiedler, U.1    Phillips, J.2    Artsaenko, O.3    Conrad, U.4
  • 117
    • 0032168897 scopus 로고    scopus 로고
    • Compartment-specific accumulation of recombinant immunoglobulins in plant cells: An essential tool for antibody production and immunomodulation of physiological functions and pathogen activity.
    • Conrad, U., Fiedler, U., Compartment-specific accumulation of recombinant immunoglobulins in plant cells: An essential tool for antibody production and immunomodulation of physiological functions and pathogen activity. Plant Mol. Biol. 1998, 38, 101-109.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 101-109
    • Conrad, U.1    Fiedler, U.2
  • 118
    • 60549083981 scopus 로고    scopus 로고
    • Immunomodulation of plant function by in vitro selected single-chain Fv intrabodies.
    • Gahrtz, M., Conrad, U., Immunomodulation of plant function by in vitro selected single-chain Fv intrabodies. Methods Mol. Biol. 2009, 483, 289-312.
    • (2009) Methods Mol. Biol. , vol.483 , pp. 289-312
    • Gahrtz, M.1    Conrad, U.2
  • 119
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein.
    • Kyte, J., Doolittle, R. F., A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.