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Volumn 424, Issue 6952, 2003, Pages 1057-1061

Mechanism of silk processing in insects and spiders

Author keywords

[No Author keywords available]

Indexed keywords

BIREFRINGENCE; PROTEINS; SOLUTIONS; TOUGHNESS;

EID: 0042364941     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01809     Document Type: Article
Times cited : (1244)

References (31)
  • 1
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk
    • Vollrath, F. & Knight, D. P. Liquid crystalline spinning of spider silk. Nature 410, 541-548 (2001).
    • (2001) Nature , vol.410 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 2
    • 0034660201 scopus 로고    scopus 로고
    • Fine organization of Bombyx mori fibroin heavy chain gene
    • Zhou, C. Z. et al. Fine organization of Bombyx mori fibroin heavy chain gene. Nucleic Acids Res. 28, 2413-2419 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2413-2419
    • Zhou, C.Z.1
  • 3
    • 0035988683 scopus 로고    scopus 로고
    • Silk matrix for tissue engineered anterior cruciate ligaments
    • Altman, G. H. et al. Silk matrix for tissue engineered anterior cruciate ligaments. Biomaterials 23, 4131-4141 (2002).
    • (2002) Biomaterials , vol.23 , pp. 4131-4141
    • Altman, G.H.1
  • 4
    • 0028340069 scopus 로고
    • Highly repetitive structure and its organization of the silk fibroin gene
    • Mita, K., Ichimura, S. & James, T. C. Highly repetitive structure and its organization of the silk fibroin gene. J. Mol. Evol. 38, 583-592 (1994).
    • (1994) J. Mol. Evol. , vol.38 , pp. 583-592
    • Mita, K.1    Ichimura, S.2    James, T.C.3
  • 5
    • 0035880720 scopus 로고    scopus 로고
    • Preparation of undegraded native molecular fibroin solution from silkworm cocoons
    • Yamada, H., Nakao, H., Takasu, Y. & Tsubouchi, K. Preparation of undegraded native molecular fibroin solution from silkworm cocoons. Mater. Sci. Eng. C 14, 41-46 (2001).
    • (2001) Mater. Sci. Eng. C , vol.14 , pp. 41-46
    • Yamada, H.1    Nakao, H.2    Takasu, Y.3    Tsubouchi, K.4
  • 8
    • 0024278357 scopus 로고
    • Hydrophilicity of polar amino-acid side-chain is markedly reduced by flanking peptide-bonds
    • Roseman, M. A. Hydrophilicity of polar amino-acid side-chain is markedly reduced by flanking peptide-bonds. J. Mol. Biol. 200, 513-522 (1988).
    • (1988) J. Mol. Biol. , vol.200 , pp. 513-522
    • Roseman, M.A.1
  • 9
    • 0036859560 scopus 로고    scopus 로고
    • Rheology and dynamic light scattering of silk fibroin solution extracted from the middle division of Bombyx mori silkworm
    • Ochi, A., Hossain, K. S., Magoshi, J. & Nemoto, N. Rheology and dynamic light scattering of silk fibroin solution extracted from the middle division of Bombyx mori silkworm. Biomacromolecules 3, 1187-1196 (2002).
    • (2002) Biomacromolecules , vol.3 , pp. 1187-1196
    • Ochi, A.1    Hossain, K.S.2    Magoshi, J.3    Nemoto, N.4
  • 10
    • 0037047627 scopus 로고    scopus 로고
    • Polymer vesicles
    • Discher, D. E. & Eisenberg, A. Polymer vesicles. Science 297, 967-973 (2002).
    • (2002) Science , vol.297 , pp. 967-973
    • Discher, D.E.1    Eisenberg, A.2
  • 11
    • 0026923132 scopus 로고
    • Self-assembly in aqueous block copolymer solutions
    • Malstom, M. & Lindman, B. Self-assembly in aqueous block copolymer solutions. Macromolecules 25, 5440-5445 (1992).
    • (1992) Macromolecules , vol.25 , pp. 5440-5445
    • Malstom, M.1    Lindman, B.2
  • 12
    • 0037018334 scopus 로고    scopus 로고
    • Gelation behavior of PEO-PLGA-PEO triblock copolymers in water
    • Kwon, K. W., Park, M. J., Bae, Y. H., Kim, H. D. & Char, K. Gelation behavior of PEO-PLGA-PEO triblock copolymers in water. Polymer 43, 3353-3358 (2002).
    • (2002) Polymer , vol.43 , pp. 3353-3358
    • Kwon, K.W.1    Park, M.J.2    Bae, Y.H.3    Kim, H.D.4    Char, K.5
  • 13
    • 0018442937 scopus 로고
    • Physical properties and structure of silk. VI. Conformational changes in silk fibroin induced by immersion in water at 2 to 130°C
    • Polymer Physics Edition
    • Magoshi, J., Mizuide, M. & Magoshi, Y. Physical properties and structure of silk. VI. Conformational changes in silk fibroin induced by immersion in water at 2 to 130°C. J. Polym. Sci. 17 (Polymer Physics Edition), 515-520 (1979).
    • (1979) J. Polym. Sci. , vol.17 , pp. 515-520
    • Magoshi, J.1    Mizuide, M.2    Magoshi, Y.3
  • 15
    • 0034620451 scopus 로고    scopus 로고
    • Regenarated spider silk: Processing, properties, and structure
    • Seidel, A. et al. Regenarated spider silk: Processing, properties, and structure. Macromolecules 33, 775-780 (2000).
    • (2000) Macromolecules , vol.33 , pp. 775-780
    • Seidel, A.1
  • 16
    • 0000307064 scopus 로고    scopus 로고
    • Methionine redox controlled crystallization of biosynthetic silk spidroin
    • Valluzzi, R., Szela, S., Avtges, P., Kirschner, D. & Kaplan, D. L. Methionine redox controlled crystallization of biosynthetic silk spidroin. J. Phys. Chem. B 103, 11382-11392 (1999).
    • (1999) J. Phys. Chem. B , vol.103 , pp. 11382-11392
    • Valluzzi, R.1    Szela, S.2    Avtges, P.3    Kirschner, D.4    Kaplan, D.L.5
  • 17
    • 0034023387 scopus 로고    scopus 로고
    • Conformational transitions in model silk peptides
    • Wilson, D., Valluzzi, R. & Kaplan, D. Conformational transitions in model silk peptides. Biophys. J. 78, 2690-2701 (2001).
    • (2001) Biophys. J. , vol.78 , pp. 2690-2701
    • Wilson, D.1    Valluzzi, R.2    Kaplan, D.3
  • 18
    • 0032289250 scopus 로고    scopus 로고
    • Microstructural characterization of Bombyx mori silk fibers
    • Shen, Y., Johnson, M. A. & Martin, D. C. Microstructural characterization of Bombyx mori silk fibers. Macromolecules 31, 8857-8864 (1998).
    • (1998) Macromolecules , vol.31 , pp. 8857-8864
    • Shen, Y.1    Johnson, M.A.2    Martin, D.C.3
  • 19
    • 0000951118 scopus 로고
    • 13C cross polarization-magic angle spinning NMR, X-ray diffraction, and infra spectroscopy
    • 13C cross polarization-magic angle spinning NMR, X-ray diffraction, and infra spectroscopy. Macromolecules 18, 1841-1845 (1985).
    • (1985) Macromolecules , vol.18 , pp. 1841-1845
    • Asakura, T.1    Kuzuhara, A.2    Tabeta, R.3    Saito, H.4
  • 21
    • 0036678028 scopus 로고    scopus 로고
    • The molecular structure of spider dragline silk: Folding and orientation of the protein backbone
    • van Beek, J. D., Hess, S., Vollrath, F. & Meier, B. H. The molecular structure of spider dragline silk: Folding and orientation of the protein backbone. Proc. Natl Acad. Sci. USA 99, 10266-10271 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 10266-10271
    • Van Beek, J.D.1    Hess, S.2    Vollrath, F.3    Meier, B.H.4
  • 24
    • 0001192838 scopus 로고
    • Influence of solvent headgroup interactions on the formation of lyotropic liquid crystal phases of surfactants in water and nonaqueous protic and aprotic solvents
    • Auvray, X. et al. Influence of solvent headgroup interactions on the formation of lyotropic liquid crystal phases of surfactants in water and nonaqueous protic and aprotic solvents. Langmuir 8, 2671-2679 (1992).
    • (1992) Langmuir , vol.8 , pp. 2671-2679
    • Auvray, X.1
  • 25
    • 0035899837 scopus 로고    scopus 로고
    • Deformation induced hydrophobicity: Implications in spider silk formation
    • Lele, A. K. et al. Deformation induced hydrophobicity: Implications in spider silk formation. Chem. Eng. Sci. 56, 5793-5800 (2001).
    • (2001) Chem. Eng. Sci. , vol.56 , pp. 5793-5800
    • Lele, A.K.1
  • 26
    • 0032002505 scopus 로고    scopus 로고
    • Phase separation structure in poly(vinyl alcohol) silk fibroin blend films
    • Tanaka, T. et al. Phase separation structure in poly(vinyl alcohol) silk fibroin blend films. Polym. Int. 45, 175-184 (1998).
    • (1998) Polym. Int. , vol.45 , pp. 175-184
    • Tanaka, T.1
  • 28
    • 0033531474 scopus 로고    scopus 로고
    • Liquid crystals and flow elongation in a spider's silk production line
    • Knight, D. P. & Vollrath, F. Liquid crystals and flow elongation in a spider's silk production line. Proc. R. Soc. Lond. B 266, 519-523 (1999).
    • (1999) Proc. R. Soc. Lond. B , vol.266 , pp. 519-523
    • Knight, D.P.1    Vollrath, F.2
  • 29
    • 0031082016 scopus 로고    scopus 로고
    • Natural silks: Archetypal supramolecular assembly of polymer fibres
    • Viney, C. Natural silks: Archetypal supramolecular assembly of polymer fibres. Supramol. Sci. 4, 75-81 (1997).
    • (1997) Supramol. Sci. , vol.4 , pp. 75-81
    • Viney, C.1
  • 30
    • 0025142798 scopus 로고
    • Physico-chemical properties of silk fibroin membrane as a biomaterial
    • Minoura, N., Tsukada, M. & Nagura, M. Physico-chemical properties of silk fibroin membrane as a biomaterial. Biomaterials 11, 430-434 (1990).
    • (1990) Biomaterials , vol.11 , pp. 430-434
    • Minoura, N.1    Tsukada, M.2    Nagura, M.3
  • 31
    • 0037290140 scopus 로고    scopus 로고
    • Silk-based biomaterials
    • Altman, G. H. et al. Silk-based biomaterials. Biomaterials 24, 401-416 (2003).
    • (2003) Biomaterials , vol.24 , pp. 401-416
    • Altman, G.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.