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Volumn 2, Issue 9, 2003, Pages 577-585

Molecular biomimetics: Nanotechnology through biology

Author keywords

[No Author keywords available]

Indexed keywords

DNA; MACROMOLECULES; MOLECULAR BIOLOGY; NANOSTRUCTURED MATERIALS; NANOTECHNOLOGY; POLYPEPTIDES; PROTEINS; SELF ASSEMBLY;

EID: 0141780801     PISSN: 14761122     EISSN: None     Source Type: Journal    
DOI: 10.1038/nmat964     Document Type: Review
Times cited : (1482)

References (97)
  • 3
    • 0004132895 scopus 로고
    • Wainwright, S. A., Biggs, W. D., Currey, J. D. & Gosline, J. M. (eds); (Princeton Univ. Press, Princeton)
    • Wainwright, S. A., Biggs, W. D., Currey, J. D. & Gosline, J. M. (eds) Mechanical Design in Organisms (Princeton Univ. Press, Princeton, 1976).
    • (1976) Mechanical Design in Organisms
  • 5
    • 0024106082 scopus 로고
    • Synthesis and biological composites formed by in-situ precipitation
    • Mann, S. & Calvert, P. Synthesis and biological composites formed by in-situ precipitation. J. Mater. Sci. 23, 3801-3815 (1988).
    • (1988) J. Mater. Sci. , vol.23 , pp. 3801-3815
    • Mann, S.1    Calvert, P.2
  • 6
    • 0004042261 scopus 로고
    • Sarikaya, M. & Aksay, I. A. (eds.); (American Institute of Physics, New York)
    • Sarikaya, M. & Aksay, I. A. Biomimetics: Design & Processing of Materials (American Institute of Physics, New York, 1995).
    • (1995) Biomimetics: Design & Processing of Materials
  • 8
    • 0035915124 scopus 로고    scopus 로고
    • Nanoparticles, proteins, and nucleic acids: Biotechnology meets materials science
    • Niemeyer, C.M. Nanoparticles, proteins, and nucleic acids: Biotechnology meets materials science. Angew. Chem. Int. Edn Engl. 40, 4128-4158 (2001).
    • (2001) Angew. Chem. Int. Edn Engl. , vol.40 , pp. 4128-4158
    • Niemeyer, C.M.1
  • 9
    • 0004134837 scopus 로고
    • (Wiley Interscience, New York)
    • Drexler, K. E. Nanosystems (Wiley Interscience, New York, 1992).
    • (1992) Nanosystems
    • Drexler, K.E.1
  • 10
    • 0033963244 scopus 로고    scopus 로고
    • Recent progress in biomolecular engineering
    • Ryu, D. D. Y. & Nam, D. H., Recent progress in biomolecular engineering. Biotechnol. Prog. 16, 2-16 (2000).
    • (2000) Biotechnol. Prog. , vol.16 , pp. 2-16
    • Ryu, D.D.Y.1    Nam, D.H.2
  • 11
    • 0033428813 scopus 로고    scopus 로고
    • Biomimetics: Materials fabrication through biology
    • Sarikaya, M. Biomimetics: Materials fabrication through biology. Proc. Natl Acad. Sci. USA 96, 14183-14185 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14183-14185
    • Sarikaya, M.1
  • 12
    • 0037197883 scopus 로고    scopus 로고
    • Emulating biology: Building nanostructures from the bottom up
    • Seeman, N. C. & Belcher, A. M. Emulating biology: building nanostructures from the bottom up. Proc. Natl Acad. Sci. USA 99, 6452-6455 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 6452-6455
    • Seeman, N.C.1    Belcher, A.M.2
  • 13
    • 0035905775 scopus 로고    scopus 로고
    • Life's lessons in design
    • Ball, P. Life's lessons in design. Nature 409, 413-416 (2001).
    • (2001) Nature , vol.409 , pp. 413-416
    • Ball, P.1
  • 16
    • 0035834444 scopus 로고    scopus 로고
    • Logic circuits with carbon nanotubes transistors
    • Bachtold, A., Hadley, P., Nakanishi, T. & Dekker, C. Logic circuits with carbon nanotubes transistors. Science 294, 1317-1320 (2001).
    • (2001) Science , vol.294 , pp. 1317-1320
    • Bachtold, A.1    Hadley, P.2    Nakanishi, T.3    Dekker, C.4
  • 17
    • 0034597775 scopus 로고    scopus 로고
    • A nanometre-scale electronic switch consisting of a metal cluster and redox-addressable groups
    • Gittins, D. I., Bethell, D., Schiffrin, D. J. & Michols, R. J. A nanometre-scale electronic switch consisting of a metal cluster and redox-addressable groups. Nature 408, 67-69 (2000).
    • (2000) Nature , vol.408 , pp. 67-69
    • Gittins, D.I.1    Bethell, D.2    Schiffrin, D.J.3    Michols, R.J.4
  • 18
    • 0035021785 scopus 로고    scopus 로고
    • Natural formation of nanostructures: From fundamentals in metal heteroepitaxy to applications in optics and biomaterials science
    • Muller, B. Natural formation of nanostructures: from fundamentals in metal heteroepitaxy to applications in optics and biomaterials science. Surf. Rev. Lett. 8, 169-228 (2001).
    • (2001) Surf. Rev. Lett. , vol.8 , pp. 169-228
    • Muller, B.1
  • 21
    • 0036963494 scopus 로고    scopus 로고
    • Rigid biological composite materials: Structural examples for biomimetic design
    • Mayer, G. & Sarikaya, M. Rigid biological composite materials: Structural examples for biomimetic design. Exp. Mech. 42, 395-403 (2002).
    • (2002) Exp. Mech. , vol.42 , pp. 395-403
    • Mayer, G.1    Sarikaya, M.2
  • 22
    • 0040141572 scopus 로고    scopus 로고
    • Nanomechanical properties profiles across DEJ in human incisor teeth
    • Fong, H., Sarikaya, M., White, S. & Snead, M. L. Nanomechanical properties profiles across DEJ in human incisor teeth. J. Mater. Sci. Eng C7, 119-128 (2000).
    • (2000) J. Mater. Sci. Eng C , vol.7 , pp. 119-128
    • Fong, H.1    Sarikaya, M.2    White, S.3    Snead, M.L.4
  • 23
    • 0035352097 scopus 로고    scopus 로고
    • Biomimetic model of a sponge-spicular optical fiber - Mechanical properties and structure
    • Sarikaya, M et al. Biomimetic model of a sponge-spicular optical fiber - mechanical properties and structure. J. Mater. Res. 16, 1420-1428 (2001).
    • (2001) J. Mater. Res. , vol.16 , pp. 1420-1428
    • Sarikaya, M.1
  • 25
    • 0020252686 scopus 로고
    • Optimization of Fe/Cr/C base structural steels for improved strength and toughness
    • Sarikaya, M., Steinberg, B. & Thomas, G. Optimization of Fe/Cr/C base structural steels for improved strength and toughness. Metall. Trans. A 13, 2227-2237 (1982).
    • (1982) Metall. Trans. A , vol.13 , pp. 2227-2237
    • Sarikaya, M.1    Steinberg, B.2    Thomas, G.3
  • 27
    • 0030987036 scopus 로고    scopus 로고
    • Molecular dynamics study of unbinding of avidin-biotin complex
    • Izrailev, S., Stepaniants, S., Basera, M., Oono, Y. & Schulten, K. Molecular dynamics study of unbinding of avidin-biotin complex. Biphys. J. 72, 1568-1581 (1997).
    • (1997) Biphys. J. , vol.72 , pp. 1568-1581
    • Izrailev, S.1    Stepaniants, S.2    Basera, M.3    Oono, Y.4    Schulten, K.5
  • 29
    • 0030969778 scopus 로고    scopus 로고
    • Metal recognition by repeating polypeptides
    • Brown, S. Metal recognition by repeating polypeptides. Nature Biotechnol. 15, 269-272 (1997).
    • (1997) Nature Biotechnol. , vol.15 , pp. 269-272
    • Brown, S.1
  • 30
    • 0031735526 scopus 로고    scopus 로고
    • Artificial neural networks for computer-based molecular design
    • Schneider, G. & Wrede, P. Artificial neural networks for computer-based molecular design. Biophys. Mol. Biol. 70, 175-222 (1988).
    • (1998) Biophys. Mol. Biol. , vol.70 , pp. 175-222
    • Schneider, G.1    Wrede, P.2
  • 31
    • 0042316895 scopus 로고
    • Purification and characterization of calcium-binding conchiolin shell peptides from the mollusk, Haliotis-rufescens, as a function of development
    • Cariolou, M. A. & Morse, D. E. Purification and characterization of calcium-binding conchiolin shell peptides from the mollusk, Haliotis-rufescens, as a function of development. J. Comp. Physiol. B 157, 717-729 (1988).
    • (1988) J. Comp. Physiol. B , vol.157 , pp. 717-729
    • Cariolou, M.A.1    Morse, D.E.2
  • 32
    • 84907041160 scopus 로고
    • Collagen cross-linking and biomineralization
    • Glimcher, M. & Nimni, M. Collagen cross-linking and biomineralization. Connect Tissue Res. 27, 73-83 (1992).
    • (1992) Connect Tissue Res. , vol.27 , pp. 73-83
    • Glimcher, M.1    Nimni, M.2
  • 33
    • 0031034185 scopus 로고    scopus 로고
    • Protein interactions during assembly of the enamel organic extracellular matrix
    • Paine, M. L. & Snead, M. L. Protein interactions during assembly of the enamel organic extracellular matrix. J. Bone Mineral. Res. 12, 221-226 (1996).
    • (1996) J. Bone Mineral. Res. , pp. 221-226
    • Paine, M.L.1    Snead, M.L.2
  • 34
    • 0037814710 scopus 로고    scopus 로고
    • Polycatyonic peptides from diatom biosilica that direct silica nanosphere formation
    • Kroger, N., Deutzman, R. & Sumper, M. Polycatyonic peptides from diatom biosilica that direct silica nanosphere formation. Science 286, 1129-1132 (1996).
    • (1999) Science , vol.286 , pp. 1129-1132
    • Kroger, N.1    Deutzman, R.2    Sumper, M.3
  • 35
    • 0034691568 scopus 로고    scopus 로고
    • Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein
    • Liou, Y. C., Tociji, A., Davies, P. L., Jia, Z. C. Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein. Nature 406, 322-324 (2000).
    • (2000) Nature , vol.406 , pp. 322-324
    • Liou, Y.C.1    Tociji, A.2    Davies, P.L.3    Jia, Z.C.4
  • 36
    • 0001255053 scopus 로고
    • Interactions of sea-urchin skeleton macromolecules with growing calcite crystals: A study of intracrystalline proteins
    • Berman, A., Addadi, L. & Weiner, S. Interactions of sea-urchin skeleton macromolecules with growing calcite crystals: A study of intracrystalline proteins. Nature 331, 546-548 (1988).
    • (1988) Nature , vol.331 , pp. 546-548
    • Berman, A.1    Addadi, L.2    Weiner, S.3
  • 37
    • 0027957459 scopus 로고
    • Atomic force microscopy and molecular modeling of proteins and peptide binding to calcite
    • Weizbicki, A., Sikes, C. S., Madura, J. D. & Drake, B. Atomic force microscopy and molecular modeling of proteins and peptide binding to calcite. Calif. Tissue. Int. 54, 133-141 (1994).
    • (1994) Calif. Tissue. Int. , vol.54 , pp. 133-141
    • Weizbicki, A.1    Sikes, C.S.2    Madura, J.D.3    Drake, B.4
  • 38
    • 0033582234 scopus 로고    scopus 로고
    • Silicatein filaments and subunits from a marine sponge direct the polymerization of silica and silicones in vitro
    • Cha, J. N. et al. Silicatein filaments and subunits from a marine sponge direct the polymerization of silica and silicones in vitro. Proc. Natl Acad. Sci. USA 96, 361-365 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 361-365
    • Cha, J.N.1
  • 39
    • 0029669273 scopus 로고    scopus 로고
    • Control of crystal phase switching and orientation by soluble mollusk-shell proteins
    • Belcher, A. M. et al. Control of crystal phase switching and orientation by soluble mollusk-shell proteins. Nature 381, 56-58 (1996).
    • (1996) Nature , vol.381 , pp. 56-58
    • Belcher, A.M.1
  • 40
    • 0029667586 scopus 로고    scopus 로고
    • Control of aragonite and calcite polymorphism by mollusk shell macromolecules
    • Fallini, G., Albeck, S., Weiner, S. & Addadi, L. Control of aragonite and calcite polymorphism by mollusk shell macromolecules. Science 271, 67-69 (1996).
    • (1996) Science , vol.271 , pp. 67-69
    • Fallini, G.1    Albeck, S.2    Weiner, S.3    Addadi, L.4
  • 41
    • 0032085975 scopus 로고    scopus 로고
    • Combinatorial protein design by in vitro recombination
    • Giver, L. & Arnold, F. H. Combinatorial protein design by in vitro recombination. Curr. Opin. Chem. Biol. 2, 335-338 (1998).
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 335-338
    • Giver, L.1    Arnold, F.H.2
  • 42
    • 0032960161 scopus 로고    scopus 로고
    • Bioaccumulation of heavy metals by fimbrial designer adhesion
    • Schembri, M. A., Kjergaard, K. & Klemm, P. Bioaccumulation of heavy metals by fimbrial designer adhesion. FEMS Microbiol. Lett. 170, 363-371 (1999).
    • (1999) FEMS Microbiol. Lett. , vol.170 , pp. 363-371
    • Schembri, M.A.1    Kjergaard, K.2    Klemm, P.3
  • 43
    • 0034625319 scopus 로고    scopus 로고
    • Genetic analysis of crystal growth
    • Brown, S., Sarikaya, M. & Johnson, E. Genetic analysis of crystal growth. J. Mol. Biol. 299, 725-732 (2000).
    • (2000) J. Mol. Biol. , vol.299 , pp. 725-732
    • Brown, S.1    Sarikaya, M.2    Johnson, E.3
  • 44
    • 0034621827 scopus 로고    scopus 로고
    • Selection of peptides with semiconducting binding specificity for directed nanocrystal assembly
    • Whaley, S. R, English, D. S., Hu, E. L., Barbara, P. F. & Belcher, M. A. Selection of peptides with semiconducting binding specificity for directed nanocrystal assembly. Nature 405, 665-668 (2000).
    • (2000) Nature , vol.405 , pp. 665-668
    • Whaley, S.R.1    English, D.S.2    Hu, E.L.3    Barbara, P.F.4    Belcher, M.A.5
  • 45
    • 0002239134 scopus 로고    scopus 로고
    • Silica precipitating peptides isolated from a combinatorial phage display libraries
    • Naik, R. R., Brott, L., Carlson, S. J. & Stone, M. O. Silica precipitating peptides isolated from a combinatorial phage display libraries. J. Nanosci. Nanotechnol. 2, 1-6 (2002).
    • (2002) J. Nanosci. Nanotechnol. , vol.2 , pp. 1-6
    • Naik, R.R.1    Brott, L.2    Carlson, S.J.3    Stone, M.O.4
  • 46
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith, G. P. Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface. Science 228, 1315-1317 (1985).
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 47
    • 0035471140 scopus 로고    scopus 로고
    • Protein design and phage display
    • Hoess, R. H. Protein design and phage display. Chem. Rev. 101, 3205-3218 (2001).
    • (2001) Chem. Rev. , vol.101 , pp. 3205-3218
    • Hoess, R.H.1
  • 48
    • 0035424822 scopus 로고    scopus 로고
    • Protein engineering by cell surface display
    • Wittrup, K. D. Protein engineering by cell surface display. Curr. Opin. Biotechnol. 12, 395-399 (2001).
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 395-399
    • Wittrup, K.D.1
  • 49
    • 0036281495 scopus 로고    scopus 로고
    • Phage display as a novel screening method to identify extracellular proteins
    • Rosander, A., Bjerketorp, J., Frykberg, L. & Jabobsson, K. Phage display as a novel screening method to identify extracellular proteins. J. Microbiol. Meth. 51, 43-55 (2002).
    • (2002) J. Microbiol. Meth. , vol.51 , pp. 43-55
    • Rosander, A.1    Bjerketorp, J.2    Frykberg, L.3    Jabobsson, K.4
  • 50
    • 0033908030 scopus 로고    scopus 로고
    • Designed evolution of enzymatic properties
    • Petrouna, I. P. & Arnold, F. H. Designed evolution of enzymatic properties. Curr. Opin. Biotechnol. 11, 325-329 (2000).
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 325-329
    • Petrouna, I.P.1    Arnold, F.H.2
  • 52
    • 0035249432 scopus 로고    scopus 로고
    • Biotechnology applications of phage and cell surface display
    • Benhar, I. Biotechnology applications of phage and cell surface display. Biotechnol. Adv. 19, 1-33 (2001).
    • (2001) Biotechnol. Adv. , vol.19 , pp. 1-33
    • Benhar, I.1
  • 53
  • 55
    • 0037012921 scopus 로고    scopus 로고
    • Ordering quantum dots using genetically engineered viruses
    • Lee, W. S., Mao, C., Flynn, C. E. & Belcher, A. M. Ordering quantum dots using genetically engineered viruses. Science 296, 892-895 (2002).
    • (2002) Science , vol.296 , pp. 892-895
    • Lee, W.S.1    Mao, C.2    Flynn, C.E.3    Belcher, A.M.4
  • 57
    • 0037126797 scopus 로고    scopus 로고
    • Surface-specific zeolite-binding proteins
    • Nygaard, S., Wandelbo, R. & Brown, S. Surface-specific zeolite-binding proteins. Adv. Mater. 14, 1853-1856 (2002).
    • (2002) Adv. Mater. , vol.14 , pp. 1853-1856
    • Nygaard, S.1    Wandelbo, R.2    Brown, S.3
  • 58
    • 0033831214 scopus 로고    scopus 로고
    • Identification of inorganic crystal-specific sequences using phage display combinatorial library of short peptides: A feasibility study
    • Gaskin, D. J. H., Starck, K. & Vulfson, E. N. Identification of inorganic crystal-specific sequences using phage display combinatorial library of short peptides: A feasibility study. Biotech. Lett. 22, 1211-1216 (2000).
    • (2000) Biotech. Lett. , vol.22 , pp. 1211-1216
    • Gaskin, D.J.H.1    Starck, K.2    Vulfson, E.N.3
  • 59
    • 0032960161 scopus 로고    scopus 로고
    • Bioaccumulation of heavy metals by fimbrial designer adhesions
    • Scembri, M. A., Kjaergaard, K. & Klemm, P. Bioaccumulation of heavy metals by fimbrial designer adhesions. FEMS Microbial. Lett. 170, 363-371 (1999).
    • (1999) FEMS Microbial. Lett. , vol.170 , pp. 363-371
    • Scembri, M.A.1    Kjaergaard, K.2    Klemm, P.3
  • 60
    • 0026669435 scopus 로고
    • Engineering iron oxide-adhesion mutants of Escherichia coli phage λ receptor
    • Brown, S. Engineering iron oxide-adhesion mutants of Escherichia coli phage λ receptor. Proc. Natl Acad. Sci. USA 89, 8651-8655 (1992)
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8651-8655
    • Brown, S.1
  • 61
    • 0023835389 scopus 로고
    • Molecular recognition in biomineralization
    • Mann, S. Molecular recognition in biomineralization. Nature 332, 119-123 (1988).
    • (1988) Nature , vol.332 , pp. 119-123
    • Mann, S.1
  • 62
  • 64
    • 17544401918 scopus 로고    scopus 로고
    • Monoclonal antibody recognition of histidine-rich peptide capsulated nanoclusters
    • Slocik, J. M., Moore, J. T. & Wright, D. W. Monoclonal antibody recognition of histidine-rich peptide capsulated nanoclusters. Nano Lett. 2, 169-173 (2002).
    • (2002) Nano Lett. , vol.2 , pp. 169-173
    • Slocik, J.M.1    Moore, J.T.2    Wright, D.W.3
  • 65
    • 0036392715 scopus 로고    scopus 로고
    • Genetically engineered gold-binding polypeptides: Structure prediction and molecular dynamics
    • Braun, R., Sarikaya, M. & Schulten, K. S. Genetically engineered gold-binding polypeptides: Structure prediction and molecular dynamics. J. Biomater. Sci. 13, 747-758 (2002).
    • (2002) J. Biomater. Sci. , vol.13 , pp. 747-758
    • Braun, R.1    Sarikaya, M.2    Schulten, K.S.3
  • 66
    • 0004159145 scopus 로고
    • Frankel. R. B. & Blakemore, R. P. (eds); (Plenum, New York)
    • Frankel. R. B. & Blakemore, R. P. (eds) Iron Biominerals (Plenum, New York, 1991).
    • (1991) Iron Biominerals
  • 68
    • 0036901907 scopus 로고    scopus 로고
    • Extracellular synthesis of gold nanoparticles by the fungus Fusarium oxysporum
    • Maukharjee, P. et al. Extracellular synthesis of gold nanoparticles by the fungus Fusarium oxysporum. Chem. Biol. Chem. 5, 461-463 (2002).
    • (2002) Chem. Biol. Chem. , vol.5 , pp. 461-463
    • Maukharjee, P.1
  • 69
    • 33746096072 scopus 로고
    • A study of the nucleation and growth of processes in the synthesis of colloidal gold
    • Turkevich, J., Stevenson, P. C. & Hillier, J. A study of the nucleation and growth of processes in the synthesis of colloidal gold. Trans. Faraday Soc. 11, 55-75 (1951).
    • (1951) Trans. Faraday Soc. , vol.11 , pp. 55-75
    • Turkevich, J.1    Stevenson, P.C.2    Hillier, J.3
  • 70
    • 0013048484 scopus 로고    scopus 로고
    • Photonic crystals based on periodic arrays of aligned carbon nanotubes
    • Kempa, K. et al. Photonic crystals based on periodic arrays of aligned carbon nanotubes. Nano Lett. 3, 13-18 (2003).
    • (2003) Nano Lett. , vol.3 , pp. 13-18
    • Kempa, K.1
  • 71
    • 0037197822 scopus 로고    scopus 로고
    • Quantum dot artificial solids: Understanding the static and dynamic role of size and packing disorder
    • Beverly, K. C. Quantum dot artificial solids: Understanding the static and dynamic role of size and packing disorder. Proc. Natl Acad. Sci. USA 99, 6456-6459 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 6456-6459
    • Beverly, K.C.1
  • 72
    • 0037146030 scopus 로고    scopus 로고
    • Au nanowires from sequenced histidine-rich peptide
    • Djulali, R., Chen, Y. & Matsui, H. Au nanowires from sequenced histidine-rich peptide. J. Am. Chem. Soc. 124, 13660-13661 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13660-13661
    • Djulali, R.1    Chen, Y.2    Matsui, H.3
  • 73
    • 0037073941 scopus 로고    scopus 로고
    • Shape-controlled synthesis of gold and silver nanoparticles
    • Xia, Y. & Sun, Y. Shape-controlled synthesis of gold and silver nanoparticles. Science 298, 2176-2179 (2002).
    • (2002) Science , vol.298 , pp. 2176-2179
    • Xia, Y.1    Sun, Y.2
  • 74
    • 0034314223 scopus 로고    scopus 로고
    • Structure and growth of self-assembled monolayers
    • Schreiber, R. Structure and growth of self-assembled monolayers. Prog. Surf. Sci. 65, 151-256 (2000).
    • (2000) Prog. Surf. Sci. , vol.65 , pp. 151-256
    • Schreiber, R.1
  • 75
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry - A chemical strategy for the synthesis of nanostructures
    • Whitesides, G. M., Mathias, J. P. & Seto, C. T. Molecular Self-assembly and nanochemistry - A chemical strategy for the synthesis of nanostructures. Science 254, 1312-1319 (1991).
    • (1991) Science , vol.254 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.T.3
  • 76
    • 0000967152 scopus 로고    scopus 로고
    • Protein-mediated particle assembly
    • Brown, S. Protein-mediated particle assembly. Nano Lett. 1, 391-394 (2001).
    • (2001) Nano Lett. , vol.1 , pp. 391-394
    • Brown, S.1
  • 78
    • 0003867545 scopus 로고    scopus 로고
    • Ratner, B., Schoen, F., Hoffman, A. & Lemons, J. (eds); (Academic, San Diego, USA)
    • Ratner, B., Schoen, F., Hoffman, A. & Lemons, J. (eds) Biomaterials Science: Introduction to Materials in Medicine (Academic, San Diego, USA, 1996).
    • (1996) Biomaterials Science: Introduction to Materials in Medicine
  • 79
    • 0036898944 scopus 로고    scopus 로고
    • What can surface chemistry do for cell biology
    • Mrksich, M. What can surface chemistry do for cell biology. Curr. Opin. Chem. Biol. 6, 794-797 (2002).
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 794-797
    • Mrksich, M.1
  • 80
    • 0037015367 scopus 로고    scopus 로고
    • Redox properties of cytochrome c adsorbed on self-assembled monolayers: A probe for protein conformation and orientation
    • Chen, X. X., Ferrigno, R., Yang, J. & Whitesides, G. A. Redox properties of cytochrome c adsorbed on self-assembled monolayers: A probe for protein conformation and orientation. Langmuir 18, 7009-7015 (2002).
    • (2002) Langmuir , vol.18 , pp. 7009-7015
    • Chen, X.X.1    Ferrigno, R.2    Yang, J.3    Whitesides, G.A.4
  • 81
    • 0032162964 scopus 로고    scopus 로고
    • Quantitative interpretation of the resonance of surface plasmon resonance sensors to adsorbed films
    • Jung, L. S., Campbell, C. T., Chinowsky, T. M., Mar, M. N. & Yee, S. S. Quantitative interpretation of the resonance of surface plasmon resonance sensors to adsorbed films. Langmuir 14, 5636-5648 (1998).
    • (1998) Langmuir , vol.14 , pp. 5636-5648
    • Jung, L.S.1    Campbell, C.T.2    Chinowsky, T.M.3    Mar, M.N.4    Yee, S.S.5
  • 82
    • 0035951086 scopus 로고    scopus 로고
    • Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR
    • Long, J. R., Shaw, W. J., Stayton, P. S. & Drobny, G. P. Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR. Biochemistry-US 40, 15451-15455 (2001).
    • (2001) Biochemistry-US , vol.40 , pp. 15451-15455
    • Long, J.R.1    Shaw, W.J.2    Stayton, P.S.3    Drobny, G.P.4
  • 83
    • 0037179930 scopus 로고    scopus 로고
    • Fluorescence based nucleic acid detection and microarrays
    • Epstein, J. R., Biran, I. & Walt, D. R. Fluorescence based nucleic acid detection and microarrays. Anal. Chim Acta. 469, 3-36 (2002).
    • (2002) Anal. Chim Acta. , vol.469 , pp. 3-36
    • Epstein, J.R.1    Biran, I.2    Walt, D.R.3
  • 84
    • 0036739330 scopus 로고    scopus 로고
    • Microarrays in pharmagenomics - Advances and future promise
    • Chicurel, M. E. & Dalma-Weiszhausz, D. D. Microarrays in pharmagenomics - advances and future promise. Pharmacogenomics 3, 589-601 (2002).
    • (2002) Pharmacogenomics , vol.3 , pp. 589-601
    • Chicurel, M.E.1    Dalma-Weiszhausz, D.D.2
  • 86
    • 0037073007 scopus 로고    scopus 로고
    • Direct binding procedures of proteins to fine magnetic particles
    • Koneracka, M. et al. Direct binding procedures of proteins to fine magnetic particles. J. Mol. Catal. B 18, 13-18 (2002).
    • (2002) J. Mol. Catal. B , vol.18 , pp. 13-18
    • Koneracka, M.1
  • 87
    • 0036930888 scopus 로고    scopus 로고
    • Recent developments in the synthesis and chemistry of periodic mesoporous organosilicas
    • Asefa, T., Ozin, G. A., Grondey, H., Kruk, H. & Jaroniek, M. Recent developments in the synthesis and chemistry of periodic mesoporous organosilicas. Stud. Surf. Sci Catal. 141, 1-26 (2002).
    • (2002) Stud. Surf. Sci Catal. , vol.141 , pp. 1-26
    • Asefa, T.1    Ozin, G.A.2    Grondey, H.3    Kruk, H.4    Jaroniek, M.5
  • 88
    • 0029791320 scopus 로고    scopus 로고
    • Biomembrane templates for nanoscale conduits and networks
    • Evans, E., Bowman, H., Leung, A., Needham, D. & Tirrell, D. Biomembrane templates for nanoscale conduits and networks. Science 273, 933-935 (1996).
    • (1996) Science , vol.273 , pp. 933-935
    • Evans, E.1    Bowman, H.2    Leung, A.3    Needham, D.4    Tirrell, D.5
  • 89
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink, J. D., Beniash, E. & Stupp, S. I., Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 294, 1684-1688 (2001).
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 90
    • 0037025199 scopus 로고    scopus 로고
    • Sequence specific molecular lithography on single DNA molecules
    • Keren, K. et al. Sequence specific molecular lithography on single DNA molecules. Science 97, 72-75 (2002).
    • (2002) Science , vol.97 , pp. 72-75
    • Keren, K.1
  • 91
    • 0037069325 scopus 로고    scopus 로고
    • S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays
    • Moll, D. et al. S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays. Proc. Natl Acad. Sci. USA 99, 14646-14651 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14646-14651
    • Moll, D.1
  • 92
    • 0036977748 scopus 로고    scopus 로고
    • Ordered nanoparticle arrays formed on engineered chaperonin protein templates
    • McMillan, A. R. et al. Ordered nanoparticle arrays formed on engineered chaperonin protein templates. Nature Mater. 1, 247-252 (2002).
    • (2002) Nature Mater. , vol.1 , pp. 247-252
    • Mcmillan, A.R.1
  • 93
    • 0037885320 scopus 로고    scopus 로고
    • Rotary motion in single-molecule machines
    • Kelly, T. R. & Sestelo, J. P. Rotary motion in single-molecule machines. Struct. Bond. 99, 19-53 (2001).
    • (2001) Struct. Bond. , vol.99 , pp. 19-53
    • Kelly, T.R.1    Sestelo, J.P.2
  • 94
    • 0037497251 scopus 로고    scopus 로고
    • Chaperorin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles
    • Ishli, D. et al. Chaperorin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles. Nature 423, 628-231 (2003).
    • (2003) Nature , vol.423 , pp. 628-231
    • Ishli, D.1
  • 96
    • 0037019549 scopus 로고    scopus 로고
    • A nanoscale optical biosensor: Sensitivity and selectivity of an approach based on the localized surface plasmon resonance spectroscopy of triangular silver nanoparticles
    • Haes, A. J. & Van Duyne, R. P. A nanoscale optical biosensor: Sensitivity and selectivity of an approach based on the localized surface plasmon resonance spectroscopy of triangular silver nanoparticles. J. Am. Chem. Soc. 124, 10596-10604 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10596-10604
    • Haes, A.J.1    Van Duyne, R.P.2
  • 97
    • 0037253089 scopus 로고    scopus 로고
    • Protein arrays: The current state-of-the-art
    • Cutler, P. Protein Arrays: The current state-of-the-art. Proteomics 3, 3-18 (2003).
    • (2003) Proteomics , vol.3 , pp. 3-18
    • Cutler, P.1


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