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Volumn , Issue , 2007, Pages 1-183

Plenty of room for biology at the bottom: An introduction to bionanotechnology

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED APPLICATIONS; BIONANOTECHNOLOGY; NANO-BIOLOGY;

EID: 84967386494     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1142/P465     Document Type: Book
Times cited : (36)

References (136)
  • 1
    • 0030934379 scopus 로고    scopus 로고
    • Responsive gels formed by the spontaneous selfassembly of peptides into polymeric beta-sheet tapes
    • Aggeli, A., Bell, M., Boden, N., Keen, J. N., Knowles, P. F., McLeish, T. C., Pitkeathly, M., and Radford, S. E. (1997) Responsive gels formed by the spontaneous selfassembly of peptides into polymeric beta-sheet tapes. Nature 386, 259-262.
    • (1997) Nature , vol.386 , pp. 259-262
    • Aggeli, A.1    Bell, M.2    Boden, N.3    Keen, J.N.4    Knowles, P.F.5    McLeish, T.C.6    Pitkeathly, M.7    Radford, S.E.8
  • 2
    • 22044457920 scopus 로고    scopus 로고
    • Skeleton of Euplectella sp.: Structural hierarchy from the nanoscale to the macroscale
    • Aizenberg, J., Weaver, J. C., Thanawala, M. S., Sundar, V. C., Morse, D. E., and Fratzl, P. (2005) Skeleton of Euplectella sp.: Structural hierarchy from the nanoscale to the macroscale. Science 309, 275-278.
    • (2005) Science , vol.309 , pp. 275-278
    • Aizenberg, J.1    Weaver, J.C.2    Thanawala, M.S.3    Sundar, V.C.4    Morse, D.E.5    Fratzl, P.6
  • 3
    • 0033937682 scopus 로고    scopus 로고
    • Conformational behavior of ionic self-complementary peptides
    • Altman, M., Lee, P., Rich, A., and Zhang, S. (2000) Conformational behavior of ionic self-complementary peptides. Protein Sci. 9, 1095-1105.
    • (2000) Protein Sci. , vol.9 , pp. 1095-1105
    • Altman, M.1    Lee, P.2    Rich, A.3    Zhang, S.4
  • 4
    • 0345166881 scopus 로고    scopus 로고
    • Cu nanocrystal growth on peptide nanotubes by biomineralization: Size control of Cu nanocrystals by tuning peptide conformation
    • Banerjee, I. A., Yu, L., and Matsui, H. (2003) Cu nanocrystal growth on peptide nanotubes by biomineralization: size control of Cu nanocrystals by tuning peptide conformation. Proc. Natl. Acad. Sci. USA 100, 14678-14682.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14678-14682
    • Banerjee, I.A.1    Yu, L.2    Matsui, H.3
  • 6
    • 0032546024 scopus 로고    scopus 로고
    • DNA-templated assembly and electrode attachment of a conducting silver wire
    • Braun, E., Eichen, Y., Sivan, U., and Ben-Yoseph, G. (1998) DNA-templated assembly and electrode attachment of a conducting silver wire. Nature 391, 775-778.
    • (1998) Nature , vol.391 , pp. 775-778
    • Braun, E.1    Eichen, Y.2    Sivan, U.3    Ben-Yoseph, G.4
  • 8
    • 0345118157 scopus 로고    scopus 로고
    • Mapping domain structures in silks from insects and spiders related to protein assembly
    • Bini, E., Knight, D. P., and Kaplan, D. L. (2004) Mapping domain structures in silks from insects and spiders related to protein assembly. J. Mol. Biol. 335, 27-40.
    • (2004) J. Mol. Biol. , vol.335 , pp. 27-40
    • Bini, E.1    Knight, D.P.2    Kaplan, D.L.3
  • 11
    • 3343010284 scopus 로고    scopus 로고
    • Novel cell patterning using microheater-controlled thermoresponsive plasma films
    • Cheng, X., Wang, Y., Hanein, Y., Bohringer, K. F., and Ratner, B. D. (2004) Novel cell patterning using microheater-controlled thermoresponsive plasma films. J. Biomed. Mater. Res. A. 70, 159-168.
    • (2004) J. Biomed. Mater. Res. A. , vol.70 , pp. 159-168
    • Cheng, X.1    Wang, Y.2    Hanein, Y.3    Bohringer, K.F.4    Ratner, B.D.5
  • 12
    • 0031438892 scopus 로고    scopus 로고
    • Immunoassay of human chorionic gonadotropin, its free subunits, and metabolites
    • Cole, L. A. (1997) Immunoassay of human chorionic gonadotropin, its free subunits, and metabolites. Clin. Chem. 43, 2233-2243.
    • (1997) Clin. Chem. , vol.43 , pp. 2233-2243
    • Cole, L.A.1
  • 13
    • 0035957717 scopus 로고    scopus 로고
    • Engineering carbon nanotubes and nanotube circuits using electrical breakdown
    • Collins, P. G., Arnold, M. S., and Avouris, P. (2001) Engineering carbon nanotubes and nanotube circuits using electrical breakdown. Science 292, 706-709.
    • (2001) Science , vol.292 , pp. 706-709
    • Collins, P.G.1    Arnold, M.S.2    Avouris, P.3
  • 14
    • 0035527414 scopus 로고    scopus 로고
    • Environmental diversity of bacteria and archaea
    • DeLong, E. F., and Pace, N. R. (2001) Environmental diversity of bacteria and archaea. Syst. Biol. 50, 470-478.
    • (2001) Syst. Biol , vol.50 , pp. 470-478
    • DeLong, E.F.1    Pace, N.R.2
  • 16
    • 0037620437 scopus 로고    scopus 로고
    • Au nanocrystal growth on nanotubes controlled by conformations and charges of sequenced peptide templates
    • Djalali, R., Chen, Y.F., and Matsui, H. (2003) Au nanocrystal growth on nanotubes controlled by conformations and charges of sequenced peptide templates. J. Am. Chem. Soc. 125, 5873-5879.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5873-5879
    • Djalali, R.1    Chen, Y.F.2    Matsui, H.3
  • 17
    • 0037458811 scopus 로고    scopus 로고
    • Materials science. A bright bio-inspired future
    • Douglas, T. (2003) Materials science. A bright bio-inspired future. Science 299, 1192- 1193.
    • (2003) Science , vol.299 , pp. 1192-1193
    • Douglas, T.1
  • 18
    • 0019774747 scopus 로고
    • Molecular engineering: An approach to the development of general capabilities for molecular manipulation
    • Drexler, E. K. (1981) Molecular engineering: An approach to the development of general capabilities for molecular manipulation. Proc. Natl. Acad. Sci. USA 78, 5275-5278.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5275-5278
    • Drexler, E.K.1
  • 21
    • 0012064449 scopus 로고
    • Positioning single atoms with a scanning tunneling microscope
    • Eigler, D. M., and Schweizer, E. K. (1990) Positioning single atoms with a scanning tunneling microscope. Nature 344, 524-526.
    • (1990) Nature , vol.344 , pp. 524-526
    • Eigler, D.M.1    Schweizer, E.K.2
  • 22
    • 0038681008 scopus 로고    scopus 로고
    • The chaplins: A family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor
    • Elliot, M. A., Karoonuthaisiri, N., Huang, J., Bibb, M. J., Cohen, S. N., Kao, C. M., and Buttner, M. J. (2003) The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor. Genes Dev. 17, 1727-1740.
    • (2003) Genes Dev , vol.17 , pp. 1727-1740
    • Elliot, M.A.1    Karoonuthaisiri, N.2    Huang, J.3    Bibb, M.J.4    Cohen, S.N.5    Kao, C.M.6    Buttner, M.J.7
  • 23
    • 0031472139 scopus 로고    scopus 로고
    • Quantum-confined stark effect in single CdSe nanocrystallite quantum dots
    • Empedocles, S. A. and Bawendi, M. G. (1997) Quantum-confined stark effect in single CdSe nanocrystallite quantum dots. Science 278, 2114-2117.
    • (1997) Science , vol.278 , pp. 2114-2117
    • Empedocles, S.A.1    Bawendi, M.G.2
  • 24
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for pi-stacking in the self-assembly of amyloid fibrils
    • Gazit, E. (2002) A possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB J. 16, 77-83.
    • (2002) FASEB J. , vol.16 , pp. 77-83
    • Gazit, E.1
  • 25
    • 0036385453 scopus 로고    scopus 로고
    • Mechanistic studies of the process of amyloid fibrils formation by the use of peptide fragments and analogues: Implications for the design of fibrillization inhibitors
    • Gazit, E. (2002) Mechanistic studies of the process of amyloid fibrils formation by the use of peptide fragments and analogues: Implications for the design of fibrillization inhibitors. Curr. Med. Chem. 9, 1725-1735.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 1725-1735
    • Gazit, E.1
  • 26
    • 0027703505 scopus 로고
    • Self-assembling organic nanotubes based on a cyclic peptide architecture
    • Ghadiri, M. R., Granja, J. R., Milligan, R. A., McRee, D.E., and Khazanovich, N. (1993) Self-assembling organic nanotubes based on a cyclic peptide architecture. Nature 366, 324-347.
    • (1993) Nature , vol.366 , pp. 324-347
    • Ghadiri, M.R.1    Granja, J.R.2    Milligan, R.A.3    McRee, D.E.4    Khazanovich, N.5
  • 27
    • 0028174318 scopus 로고
    • Artificial transmembrane ion channels from self-assembling peptide nanotubes
    • Ghadiri, M. R., Granja, J. R., and Buehler, L. K. (1994) Artificial transmembrane ion channels from self-assembling peptide nanotubes. Nature 369, 301-304.
    • (1994) Nature , vol.369 , pp. 301-304
    • Ghadiri, M.R.1    Granja, J.R.2    Buehler, L.K.3
  • 28
    • 12744273899 scopus 로고    scopus 로고
    • Self-organization of short peptide fragments: From amyloid fibrils to nanoscale supramolecular assemblies
    • Gilead, S., and Gazit, E. (2005) Self-organization of short peptide fragments: from amyloid fibrils to nanoscale supramolecular assemblies. Supramol. Chem. 17, 87- 92.
    • (2005) Supramol. Chem. , vol.17 , pp. 87-92
    • Gilead, S.1    Gazit, E.2
  • 29
    • 3042774906 scopus 로고    scopus 로고
    • Size analysis of single fullerene molecules by electron microscopy
    • Goel, A., Howard, J. B., and Sande, J. B. V. (2004) Size analysis of single fullerene molecules by electron microscopy. Carbon 42, 1907-1915.
    • (2004) Carbon , vol.42 , pp. 1907-1915
    • Goel, A.1    Howard, J.B.2    Sande, J.B.V.3
  • 31
    • 0035929124 scopus 로고    scopus 로고
    • Hydrogen sensors and switches from electrodeposited palladium mesowire arrays
    • Favier, F., Walter, E.C., Zach, M.P., Benter, T., and Penner, R.M. (2001) Hydrogen sensors and switches from electrodeposited palladium mesowire arrays. Science 293, 2227-2231.
    • (2001) Science , vol.293 , pp. 2227-2231
    • Favier, F.1    Walter, E.C.2    Zach, M.P.3    Benter, T.4    Penner, R.M.5
  • 32
    • 33646587741 scopus 로고    scopus 로고
    • Rational design of DNA nanoarchitectures
    • Feldkamp, U., and Niemeyer, C. M. (2006) Rational design of DNA nanoarchitectures. Angew. Chem. Int. Ed. 45, 1856-1876.
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 1856-1876
    • Feldkamp, U.1    Niemeyer, C.M.2
  • 34
    • 28844463647 scopus 로고    scopus 로고
    • Microcontact printing of proteins inside microstructures
    • Foley, J., Schmid, H., Stutz, R., and Delamarche, E. (2005) Microcontact printing of proteins inside microstructures. Langmuir 21, 11296-11303.
    • (2005) Langmuir , vol.21 , pp. 11296-11303
    • Foley, J.1    Schmid, H.2    Stutz, R.3    Delamarche, E.4
  • 35
    • 0037066261 scopus 로고    scopus 로고
    • Electrical interfacing of nerve cells and semiconductor chips
    • Fromherz, P. (2002) Electrical interfacing of nerve cells and semiconductor chips. Chemphyschem 3, 276-284.
    • (2002) Chemphyschem , vol.3 , pp. 276-284
    • Fromherz, P.1
  • 36
    • 1642563960 scopus 로고    scopus 로고
    • Engineering amyloidogenicity towards the development of nanofibrillar materials
    • Hamada, D., Yanagihara, I., and Tsumoto, K. (2004) Engineering amyloidogenicity towards the development of nanofibrillar materials. Trends Biotechnol. 22, 93-97.
    • (2004) Trends Biotechnol. , vol.22 , pp. 93-97
    • Hamada, D.1    Yanagihara, I.2    Tsumoto, K.3
  • 37
    • 24644491823 scopus 로고    scopus 로고
    • Lipid carriers for gene therapy
    • Hart, S. L. (2005) Lipid carriers for gene therapy. Curr. Drug Deliv. 2, 423-428.
    • (2005) Curr. Drug Deliv. , vol.2 , pp. 423-428
    • Hart, S.L.1
  • 38
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink, J. D., Beniash, E., and Stupp, S. I. (2001) Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 294, 1684-1688.
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 39
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • Holmes, T. C., de Lacalle, S., Su, X., Liu, G., Rich, A., and Zhang, S. (2000) Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds. Proc. Natl. Acad. Sci. USA 97, 6728-6733.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6728-6733
    • Holmes, T.C.1    de Lacalle, S.2    Su, X.3    Liu, G.4    Rich, A.5    Zhang, S.6
  • 40
    • 14544281493 scopus 로고    scopus 로고
    • Modulating charge transfer through cyclic D, L-alpha-peptide self-assembly
    • Horne, W.S., Ashkenasy, N., and Ghadiri, M. R. (2005) Modulating charge transfer through cyclic D, L-alpha-peptide self-assembly. Chemistry 11, 1137-1144.
    • (2005) Chemistry , vol.11 , pp. 1137-1144
    • Horne, W.S.1    Ashkenasy, N.2    Ghadiri, M.R.3
  • 41
    • 33748228968 scopus 로고
    • Arene-Arene Interactions: Electrostatic or charge transfer
    • Hunter, C. A. (1993) Arene-Arene Interactions: Electrostatic or charge transfer. Angew. Chem. Int. Ed. 32, 1584-1586.
    • (1993) Angew. Chem. Int. Ed. , vol.32 , pp. 1584-1586
    • Hunter, C.A.1
  • 42
    • 0342819025 scopus 로고
    • Helical microtubules of graphitic carbon
    • Iijima, S. (1991) Helical microtubules of graphitic carbon Nature 354, 56-58.
    • (1991) Nature , vol.354 , pp. 56-58
    • Iijima, S.1
  • 43
    • 0028842373 scopus 로고
    • Recent advances in amperometric glucose biosensors for in vivo monitoring
    • Jaffari, S. A., and Turner, A. P. (1995) Recent advances in amperometric glucose biosensors for in vivo monitoring. Physiol Meas. 16, 1-15
    • (1995) Physiol Meas. , vol.16 , pp. 1-15
    • Jaffari, S.A.1    Turner, A.P.2
  • 44
    • 0031932903 scopus 로고    scopus 로고
    • Advances toward the implantable artificial pancreas for treatment of diabetes
    • Jaremko, J., and Rorstad, O. (1998) Advances toward the implantable artificial pancreas for treatment of diabetes. Diabetes Care 21, 444-450
    • (1998) Diabetes Care , vol.21 , pp. 444-450
    • Jaremko, J.1    Rorstad, O.2
  • 45
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T., and Lansbury, P. T. Jr. (1993) Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 46
    • 0042364941 scopus 로고    scopus 로고
    • Mechanism of silk processing in insects and spiders
    • Jin, H.-J., and Kaplan, D.E. (2003) Mechanism of silk processing in insects and spiders. Nature 424, 1057-1061.
    • (2003) Nature , vol.424 , pp. 1057-1061
    • Jin, H.-J.1    Kaplan, D.E.2
  • 47
    • 12844279902 scopus 로고    scopus 로고
    • Molecular structure of glucopyranosylamide lipid and nanotube morphology
    • Kamiya, S., Minamikawa, H., Jung, J. H., Yang, B., Masuda, M., and Shimizu, T. (2005) Molecular structure of glucopyranosylamide lipid and nanotube morphology. Langmuir 21, 743-750.
    • (2005) Langmuir , vol.21 , pp. 743-750
    • Kamiya, S.1    Minamikawa, H.2    Jung, J.H.3    Yang, B.4    Masuda, M.5    Shimizu, T.6
  • 49
    • 4544310436 scopus 로고    scopus 로고
    • Biomolecule-functionalized carbon nanotubes: Applications in nanobioelectronics
    • Katz, E., and Willner, I. (2004) Biomolecule-functionalized carbon nanotubes: applications in nanobioelectronics. Chemphyschem 5, 1084-1104.
    • (2004) Chemphyschem , vol.5 , pp. 1084-1104
    • Katz, E.1    Willner, I.2
  • 50
    • 1442355645 scopus 로고    scopus 로고
    • Neuron-semiconductor chip with chemical synapse between identified neurons
    • Kaul, R. A., Syed, N. I., and Fromherz, P. (2004) Neuron-semiconductor chip with chemical synapse between identified neurons. Phys. Rev. Lett. 92, 038102.
    • (2004) Phys. Rev. Lett. , vol.92
    • Kaul, R.A.1    Syed, N.I.2    Fromherz, P.3
  • 51
    • 0037025199 scopus 로고    scopus 로고
    • Sequence-specific molecular lithography on single DNA molecules
    • Keren, K., Krueger, M., Gilad, R., Ben-Yoseph, G., Sivan, U., and Braun E. (2002) Sequence-specific molecular lithography on single DNA molecules. Science 297, 72-75.
    • (2002) Science , vol.297 , pp. 72-75
    • Keren, K.1    Krueger, M.2    Gilad, R.3    Ben-Yoseph, G.4    Sivan, U.5    Braun, E.6
  • 52
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King, C. Y., Tittmann, P., Gross, H., Gebert, R., Aebi, M., and Wuthrich, K. (1997). Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad. Sci. USA 94, 6618-6622.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6618-6622
    • King, C.Y.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5    Wuthrich, K.6
  • 53
    • 0037162463 scopus 로고    scopus 로고
    • Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair
    • Kisiday, J., Jin, M., Kurz, B, Hung, H., Semino, C., Zhang, S., and Grodzinsky, A. J. (2002) Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: implications for cartilage tissue repair. Proc. Natl. Acad. Sci. USA 99, 9996-10001.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9996-10001
    • Kisiday, J.1    Jin, M.2    Kurz, B.3    Hung, H.4    Semino, C.5    Zhang, S.6    Grodzinsky, A.J.7
  • 54
    • 22744432209 scopus 로고    scopus 로고
    • Selfassembling peptide detergents stabilize isolated photosystem I on a dry surface for an extended time
    • Kiley, P., Zhao, X., Vaughn, M., Baldo, M. A., Bruce, B. D., and Zhang, S. (2005) Selfassembling peptide detergents stabilize isolated photosystem I on a dry surface for an extended time. PLoS Biol. 3, e230.
    • (2005) PLoS Biol. , vol.3
    • Kiley, P.1    Zhao, X.2    Vaughn, M.3    Baldo, M.A.4    Bruce, B.D.5    Zhang, S.6
  • 57
    • 23144442139 scopus 로고    scopus 로고
    • Selfassembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures
    • Kol, N., Abramovich, L., Barlam, D., Shneck, R. Z., Gazit E., and Rousso, I. (2005) Selfassembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures. Nano Lett. 5, 1343-1346.
    • (2005) Nano Lett. , vol.5 , pp. 1343-1346
    • Kol, N.1    Abramovich, L.2    Barlam, D.3    Shneck, R.Z.4    Gazit, E.5    Rousso, I.6
  • 59
    • 0037008162 scopus 로고    scopus 로고
    • High-performance fibers from spider silk
    • Kubik, S. (2002) High-performance fibers from spider silk. Angew. Chem. Int. Ed. 41, 2721-2723.
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 2721-2723
    • Kubik, S.1
  • 60
    • 0033956526 scopus 로고    scopus 로고
    • Biomaterials in drug delivery and tissue engineering: One laboratory's experience
    • Langer, R. (2000) Biomaterials in drug delivery and tissue engineering: One laboratory's experience. Acc. Chem. Res. 33, 94-101.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 94-101
    • Langer, R.1
  • 61
    • 0037012921 scopus 로고    scopus 로고
    • Ordering of quantum dots using genetically engineered viruses
    • Lee, S. W., Mao, C., Flynn, C. E., and Belcher, A. M. (2002a) Ordering of quantum dots using genetically engineered viruses. Science 296, 892-895.
    • (2002) Science , vol.296 , pp. 892-895
    • Lee, S.W.1    Mao, C.2    Flynn, C.E.3    Belcher, A.M.4
  • 62
    • 0036499986 scopus 로고    scopus 로고
    • Protein nanoarrays generated by dip-pen nanolithography
    • Lee, K.-B., Park, S.-J., Mirkin, C. A., Smith, J. C., and Mrksich, M. (2002b) Protein nanoarrays generated by dip-pen nanolithography. Science 295, 1702-1705.
    • (2002) Science , vol.295 , pp. 1702-1705
    • Lee, K.-B.1    Park, S.-J.2    Mirkin, C.A.3    Smith, J.C.4    Mrksich, M.5
  • 63
    • 0038075523 scopus 로고    scopus 로고
    • Protein Nanostructures Formed Via Direct-Write Dip-Pen Nanolithography
    • Lee, K-B., Lim, J-H., and Mirkin, C.A. (2003) Protein Nanostructures Formed Via Direct-Write Dip-Pen Nanolithography. J. Am. Chem. Soc. 125, 5588-5589.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5588-5589
    • Lee, K.-B.1    Lim, J.-H.2    Mirkin, C.A.3
  • 64
    • 0037192455 scopus 로고    scopus 로고
    • Toward self-organization and complex matter
    • Lehn, J. M. (2002) Toward self-organization and complex matter. Science 295, 2400- 2403.
    • (2002) Science , vol.295 , pp. 2400-2403
    • Lehn, J.M.1
  • 65
    • 0036022527 scopus 로고    scopus 로고
    • Neutrophil chemotaxis in linear and complex gradients of interleukin-8 formed in a microfabricated device
    • Li Jeon, N., Baskaran, H., Dertinger, S. K., Whitesides, G. M., Van de Water, L., and Toner, M. (2002) Neutrophil chemotaxis in linear and complex gradients of interleukin-8 formed in a microfabricated device. Nat. Biotechnol. 20, 826-830.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 826-830
    • Li Jeon, N.1    Baskaran, H.2    Dertinger, S.K.3    Whitesides, G.M.4    Van de Water, L.5    Toner, M.6
  • 67
    • 1642474289 scopus 로고    scopus 로고
    • DNA nanotubes selfassembled from triple-crossover tiles as templates for conductive nanowires
    • Liu, D., Park, S. H., Reif, J. H., and LaBean, T. H. (2004) DNA nanotubes selfassembled from triple-crossover tiles as templates for conductive nanowires. Proc. Natl. Acad. Sci. USA 101, 717-722.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 717-722
    • Liu, D.1    Park, S.H.2    Reif, J.H.3    LaBean, T.H.4
  • 69
    • 1842484196 scopus 로고    scopus 로고
    • Self-aggregation of reverse bis peptide conjugate derived from the unstructured region of the prion protein
    • Madhavaiah, C., and Verma, S. (2004) Self-aggregation of reverse bis peptide conjugate derived from the unstructured region of the prion protein. Chem. Commun. 21, 638-639.
    • (2004) Chem. Commun. , vol.21 , pp. 638-639
    • Madhavaiah, C.1    Verma, S.2
  • 70
    • 16244374319 scopus 로고    scopus 로고
    • Copper-metalated peptide palindrome derived from prion octarepeat: Synthesis, aggregation, and oxidative transformations
    • Madhavaiah, C., and Verma, S. (2005) Copper-metalated peptide palindrome derived from prion octarepeat: synthesis, aggregation, and oxidative transformations. Bioorg. Med. Chem. 13, 3241-3248.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 3241-3248
    • Madhavaiah, C.1    Verma, S.2
  • 73
    • 24644451580 scopus 로고    scopus 로고
    • Orientation discrimination of single-stranded DNA inside the alpha-hemolysin membrane channel
    • Mathe, J., Aksimentiev, A., Nelson, D. R., Schulten, K., and Meller, A. (2005) Orientation discrimination of single-stranded DNA inside the alpha-hemolysin membrane channel. Proc. Natl. Acad. Sci. USA 102, 12377-12382.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12377-12382
    • Mathe, J.1    Aksimentiev, A.2    Nelson, D.R.3    Schulten, K.4    Meller, A.5
  • 74
    • 33845378156 scopus 로고
    • Optical microscopic study of helical superstructures of chiral bilayer membranes
    • Nakashima, N., Asakuma, S., and Kunitake, T. (1985) Optical microscopic study of helical superstructures of chiral bilayer membranes. J. Am. Chem. Soc. 107, 509- 510.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 509-510
    • Nakashima, N.1    Asakuma, S.2    Kunitake, T.3
  • 75
    • 0141868926 scopus 로고    scopus 로고
    • Nanoparticle-based bio-bar codes for the ultrasensitive detection of proteins
    • Nam, J-M., Thaxton, C. S., and Mirkin, C. A. (2003) Nanoparticle-based bio-bar codes for the ultrasensitive detection of proteins. Science 301, 1884-1886.
    • (2003) Science , vol.301 , pp. 1884-1886
    • Nam, J.-M.1    Thaxton, C.S.2    Mirkin, C.A.3
  • 77
    • 0033617951 scopus 로고    scopus 로고
    • Biomineralization: Structural questions at all length scales
    • Mann, S., and Weiner, S. (1999) Biomineralization: Structural questions at all length scales. J. Struct. Biol. 126, 179-181.
    • (1999) J. Struct. Biol. , vol.126 , pp. 179-181
    • Mann, S.1    Weiner, S.2
  • 79
    • 0346850626 scopus 로고    scopus 로고
    • Supramolecular assembly of collagen triblock peptides
    • Martin, R., Waldmann, L., and Kaplan, D. L. (2003) Supramolecular assembly of collagen triblock peptides. Biopolymers 70, 435-444.
    • (2003) Biopolymers , vol.70 , pp. 435-444
    • Martin, R.1    Waldmann, L.2    Kaplan, D.L.3
  • 80
    • 26844579689 scopus 로고    scopus 로고
    • The structure of microtubule motor proteins
    • Marx, A., Muller, J., and Mandelkow, E. (2005) The structure of microtubule motor proteins. Adv. Protein Chem. 71, 299-344.
    • (2005) Adv. Protein Chem. , vol.71 , pp. 299-344
    • Marx, A.1    Muller, J.2    Mandelkow, E.3
  • 82
    • 0013844446 scopus 로고
    • Automated synthesis of peptides
    • Merrifield R. B. (1965) Automated synthesis of peptides. Science 150, 178-185.
    • (1965) Science , vol.150 , pp. 178-185
    • Merrifield, R.B.1
  • 83
    • 16844381761 scopus 로고    scopus 로고
    • Folding of beta-structured fibrous proteins and self-assembling peptides
    • Mitraki, A., and van Raaij, M. J. (2005) Folding of beta-structured fibrous proteins and self-assembling peptides. Methods Mol. Biol. 300, 125-140.
    • (2005) Methods Mol. Biol. , vol.300 , pp. 125-140
    • Mitraki, A.1    van Raaij, M.J.2
  • 84
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the HERG potassium channel N terminus: A eukaryotic PAS domain
    • Morais-Cabral, J. H., Lee, A., Cohen, S. L., Chait, B. T., Li, M., and Mackinnon, R. (1998) Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell 95, 649-655.
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais-Cabral, J.H.1    Lee, A.2    Cohen, S.L.3    Chait, B.T.4    Li, M.5    McKinnon, R.6
  • 86
    • 0029132791 scopus 로고
    • DNA analogues with nonphosphodiester backbones
    • Nielsen, P. E. (1995) DNA analogues with nonphosphodiester backbones. Annu Rev Biophys. Biomol. Struct. 24, 167-183.
    • (1995) Annu Rev Biophys. Biomol. Struct. , vol.24 , pp. 167-183
    • Nielsen, P.E.1
  • 87
    • 0037161668 scopus 로고    scopus 로고
    • Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles
    • Nowak, A. P., Breedveld, V., Pakstis, L., Ozbas, B., Pine, D. J., Pochan, D., Deming, T. J. (2002) Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles. Nature 417, 424-428.
    • (2002) Nature , vol.417 , pp. 424-428
    • Nowak, A.P.1    Breedveld, V.2    Pakstis, L.3    Ozbas, B.4    Pine, D.J.5    Pochan, D.6    Deming, T.J.7
  • 88
    • 0346219435 scopus 로고    scopus 로고
    • Unusual salt stability in highly charged diblock co-polypeptide hydrogels
    • Nowak, A. P., Breedveld, V., Pine, D. J., and Deming, T. J. (2003) Unusual salt stability in highly charged diblock co-polypeptide hydrogels. J. Am. Chem. Soc. 125, 15666-15670.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 15666-15670
    • Nowak, A.P.1    Breedveld, V.2    Pine, D.J.3    Deming, T.J.4
  • 89
    • 3042776770 scopus 로고    scopus 로고
    • Biological bottom-up assembly of antibody nanotubes on patterned antigen arrays
    • Nuraje, N., Banerjee, I. A., MacCuspie, R. I., Yu, L., and Matsui, H. (2004) Biological bottom-up assembly of antibody nanotubes on patterned antigen arrays. J. Am. Chem. Soc. 126, 8088-8089.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8088-8089
    • Nuraje, N.1    Banerjee, I.A.2    McCuspie, R.I.3    Yu, L.4    Matsui, H.5
  • 91
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: From structure to function
    • Parker, M. W., and Feil, S. C. (2005) Pore-forming protein toxins: from structure to function. Prog. Biophys. Mol. Biol. 88, 91-142.
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 92
    • 5444224746 scopus 로고    scopus 로고
    • Actin-based metallic nanowires as bio-nanotransporters
    • Patolsky, F., Weizmann, Y., and Willner, I. (2004) Actin-based metallic nanowires as bio-nanotransporters. Nat. Mater. 3, 692-695.
    • (2004) Nat. Mater. , vol.3 , pp. 692-695
    • Patolsky, F.1    Weizmann, Y.2    Willner, I.3
  • 94
    • 0033792955 scopus 로고    scopus 로고
    • Biosilicification: The role of the organic matrix in structure control
    • Perry, C. C., and Keeling-Tucker, T. (2000) Biosilicification: the role of the organic matrix in structure control. J. Biol. Inorg. Chem. 5, 537-550.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 537-550
    • Perry, C.C.1    Keeling-Tucker, T.2
  • 96
    • 0141653970 scopus 로고    scopus 로고
    • The human islet amyloid polypeptide forms transient membrane-active protofilaments
    • Porat, Y., Kolusheva, S., Jelinek, R., and Gazit, E. (2003) The human islet amyloid polypeptide forms transient membrane-active protofilaments. Biochemistry 42, 10971-10977.
    • (2003) Biochemistry , vol.42 , pp. 10971-10977
    • Porat, Y.1    Kolusheva, S.2    Jelinek, R.3    Gazit, E.4
  • 97
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • Reches, M, and Gazit, E. (2003) Casting metal nanowires within discrete self-assembled peptide nanotubes. Science 300, 625-627.
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 98
    • 2342595738 scopus 로고    scopus 로고
    • Formation of closed-cage nanostructures by selfassembly of aromatic dipeptides
    • Reches, M., and Gazit, E. (2004) Formation of closed-cage nanostructures by selfassembly of aromatic dipeptides. Nano Lett. 4, 581-585.
    • (2004) Nano Lett. , vol.4 , pp. 581-585
    • Reches, M.1    Gazit, E.2
  • 99
    • 23344437452 scopus 로고    scopus 로고
    • Self-assembly of peptide nanotubes and amyloid-like structures by charged-termini capped diphenylalanine peptide analogues
    • Reches, M., and Gazit, E. (2005) Self-assembly of peptide nanotubes and amyloid-like structures by charged-termini capped diphenylalanine peptide analogues. Israel J. Chem. 45, 363-371.
    • (2005) Israel J. Chem. , vol.45 , pp. 363-371
    • Reches, M.1    Gazit, E.2
  • 100
    • 33745165393 scopus 로고    scopus 로고
    • Molecular self-assembly of peptide nanostructures: Mechanism of association and potential uses
    • Reches, M., and Gazit, E. (2006) Molecular self-assembly of peptide nanostructures: mechanism of association and potential uses. Curr. Nanoscience 2, 105-111.
    • (2006) Curr. Nanoscience , vol.2 , pp. 105-111
    • Reches, M.1    Gazit, E.2
  • 101
    • 0027255192 scopus 로고
    • Synthesis and virucidal activity of a water-soluble, configurationally stable, derivatized C60 fullerene
    • Schinazi, R. F., Sijbesma, R., Srdanov, G., Hill, C. L., and Wudl, F. (1993) Synthesis and virucidal activity of a water-soluble, configurationally stable, derivatized C60 fullerene. Antimicrob. Agents Chemother. 37, 1707-1710.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1707-1710
    • Schinazi, R.F.1    Sijbesma, R.2    Srdanov, G.3    Hill, C.L.4    Wudl, F.5
  • 102
    • 0035846805 scopus 로고    scopus 로고
    • Alkyl Phosphonate/Phosphate Coating on Magnetite Nanoparticles: A Comparison with Fatty Acids
    • Sahoo, Y., Pizem, H., Fried, T., Goldnitsky, D., Burstein, L., Sukenik, C.M., and Markovich, G. (2001) Alkyl Phosphonate/Phosphate Coating on Magnetite Nanoparticles: A Comparison with Fatty Acids. Langmuir 17, 7907-7911.
    • (2001) Langmuir , vol.17 , pp. 7907-7911
    • Sahoo, Y.1    Pizem, H.2    Fried, T.3    Goldnitsky, D.4    Burstein, L.5    Sukenik, C.M.6    Markovich, G.7
  • 104
  • 105
  • 106
    • 16844364574 scopus 로고    scopus 로고
    • Nanotechnology with Slayer proteins. Nanotechnology with S-layer proteins
    • Schuster, B., Gyorvary, E., Pum, D., and Sleytr, U. B. (2005) Nanotechnology with Slayer proteins. Nanotechnology with S-layer proteins. Methods Mol. Biol. 300, 101-123.
    • (2005) Methods Mol. Biol. , vol.300 , pp. 101-123
    • Schuster, B.1    Gyorvary, E.2    Pum, D.3    Sleytr, U.B.4
  • 107
    • 0025635653 scopus 로고
    • De novo design of sequences for nucleic acid structural engineering
    • Seeman, N. C. (1990) De novo design of sequences for nucleic acid structural engineering. J. Biomol. Struct. Dyn. 8, 573-581.
    • (1990) J. Biomol. Struct. Dyn. , vol.8 , pp. 573-581
    • Seeman, N.C.1
  • 108
    • 22844450839 scopus 로고    scopus 로고
    • Structural DNA nanotechnology: An overview
    • Seeman, N. C. (2005) Structural DNA nanotechnology: an overview. Methods Mol. Biol. 303, 143-166.
    • (2005) Methods Mol. Biol. , vol.303 , pp. 143-166
    • Seeman, N.C.1
  • 109
    • 33744819149 scopus 로고    scopus 로고
    • Design of minimally strained nucleic Acid nanotubes
    • Sherman, W. B., and Seeman, N. C. (2006) Design of minimally strained nucleic Acid nanotubes. Biophys. J. 90, 4546-4557.
    • (2006) Biophys. J. , vol.90 , pp. 4546-4557
    • Sherman, W.B.1    Seeman, N.C.2
  • 111
  • 112
    • 2442454992 scopus 로고    scopus 로고
    • Electron holography of non-stained bacterial surface layer proteins
    • Simon, P., Lichte, H., Wahl, R., Mertig, M., and Pompe W. (2004) Electron holography of non-stained bacterial surface layer proteins. Biochim. Biophys. Acta. 1663, 178- 187.
    • (2004) Biochim. Biophys. Acta. , vol.1663 , pp. 178-187
    • Simon, P.1    Lichte, H.2    Wahl, R.3    Mertig, M.4    Pompe, W.5
  • 113
    • 0000714715 scopus 로고    scopus 로고
    • Aromatic van der Waals Clusters: Strcture and nonrigidity
    • Sun, S., and Bernstein, E. R. (1996) Aromatic van der Waals Clusters: Strcture and nonrigidity. J. Phys. Chem. 100, 13348-13366.
    • (1996) J. Phys. Chem. , vol.100 , pp. 13348-13366
    • Sun, S.1    Bernstein, E.R.2
  • 117
    • 0037011052 scopus 로고    scopus 로고
    • Inorganic nanotubes and fullerene-like materials
    • Tenne, R. (2002) Inorganic nanotubes and fullerene-like materials. Chemistry 8, 5296- 5304.
    • (2002) Chemistry , vol.8 , pp. 5296-5304
    • Tenne, R.1
  • 119
    • 4544235083 scopus 로고    scopus 로고
    • Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits
    • True, H. L., Berlin, I., and Lindquist, S. L. (2004) Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 431, 184-187.
    • (2004) Nature , vol.431 , pp. 184-187
    • True, H.L.1    Berlin, I.2    Lindquist, S.L.3
  • 121
    • 0037117535 scopus 로고    scopus 로고
    • Molecular selfassembly of surfactant-like peptides to form nanotubes and nanovesicles
    • Vauthey, S, Santoso, S., Gong, H., Watson, N., and Zhang, S. (2002) Molecular selfassembly of surfactant-like peptides to form nanotubes and nanovesicles. Proc. Natl. Acad. Sci. USA 99, 5355-5360.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5355-5360
    • Vauthey, S.1    Santoso, S.2    Gong, H.3    Watson, N.4    Zhang, S.5
  • 122
    • 14744276690 scopus 로고    scopus 로고
    • Label-free detection of small-molecule-protein interactions by using nanowire nanosensors
    • Wang, W. U., Chen, C., Lin, K. H., Fang, Y., and Lieber, C. M. (2005) Label-free detection of small-molecule-protein interactions by using nanowire nanosensors. Proc. Natl. Acad. Sci. USA 102, 3208-3212.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3208-3212
    • Wang, W.U.1    Chen, C.2    Lin, K.H.3    Fang, Y.4    Lieber, C.M.5
  • 123
    • 2442673146 scopus 로고    scopus 로고
    • Micropatterning of proteins and mammalian cells on biomaterials
    • Wang, Y. C., and Ho, C. C. (2004) Micropatterning of proteins and mammalian cells on biomaterials. FASEB J. 18, 525-527.
    • (2004) FASEB J. , vol.18 , pp. 525-527
    • Wang, Y.C.1    Ho, C.C.2
  • 124
    • 23644458286 scopus 로고    scopus 로고
    • Structural biology. Choosing the crystallization path less traveled
    • Weiner, S., Sagi, I., and Addadi, L. (2005) Structural biology. Choosing the crystallization path less traveled. Science 309, 1027-1028.
    • (2005) Science , vol.309 , pp. 1027-1028
    • Weiner, S.1    Sagi, I.2    Addadi, L.3
  • 125
    • 0025281379 scopus 로고
    • Introduction to avidin-biotin technology
    • Wilchek, M, and Bayer, E. A. (1990) Introduction to avidin-biotin technology. Methods Enzymol. 184, 5-13.
    • (1990) Methods Enzymol. , vol.184 , pp. 5-13
    • Wilchek, M.1    Bayer, E.A.2
  • 126
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
    • Whitesides, G.M., Mathias, J.P., and Seto, C.T. (1991) Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures. Science 254, 1312-1319.
    • (1991) Science , vol.254 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.T.3
  • 128
    • 4444367423 scopus 로고    scopus 로고
    • Chemical cytometry on a picoliter-scale integrated microfluidic chip
    • Wu, H., Wheeler, A., Zare, R. N. (2004) Chemical cytometry on a picoliter-scale integrated microfluidic chip. Proc. Natl. Acad. Sci. USA 101, 12809-12813.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12809-12813
    • Wu, H.1    Wheeler, A.2    Zare, R.N.3
  • 129
    • 0037459369 scopus 로고    scopus 로고
    • "Plugging into Enzymes": Nanowiring of redox enzymes by a gold nanoparticle
    • Xiao, Y., Patolsky, F., Katz, E., Hainfeld, J. F., and Willner, I. (2003) "Plugging into Enzymes": Nanowiring of redox enzymes by a gold nanoparticle. Science 299, 1877-1881.
    • (2003) Science , vol.299 , pp. 1877-1881
    • Xiao, Y.1    Patolsky, F.2    Katz, E.3    Hainfeld, J.F.4    Willner, I.5
  • 130
    • 0020747256 scopus 로고
    • Formation of tubules by a polymerizable surfactant
    • Yager, P., and Schoen, P. E. (1984) Formation of tubules by a polymerizable surfactant. Mol. Cryst. Liq. Cryst. 106, 371-381.
    • (1984) Mol. Cryst. Liq. Cryst. , vol.106 , pp. 371-381
    • Yager, P.1    Schoen, P.E.2
  • 131
    • 0000433841 scopus 로고
    • Formation of helical super structure from single-walled bilayers by amphiphiles with oligo-Lglutamic acid-head group
    • Yamada, K., Ihara, H., Ide, T., Fukumoto, T., and Hirayama, C. (1984) Formation of helical super structure from single-walled bilayers by amphiphiles with oligo-Lglutamic acid-head group. Chem. Lett. 1984, 1713-1716.
    • (1984) Chem. Lett. , vol.1984 , pp. 1713-1716
    • Yamada, K.1    Ihara, H.2    Ide, T.3    Fukumoto, T.4    Hirayama, C.5
  • 132
    • 0037816375 scopus 로고    scopus 로고
    • Directed nucleation assembly of DNA tile complexes for barcode-patterned lattices
    • Yan, H., LaBean, T. H., Feng, L., and Reif, J. H. (2003) Directed nucleation assembly of DNA tile complexes for barcode-patterned lattices. Proc. Natl. Acad. Sci. USA 100, 8103-8108.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8103-8108
    • Yan, H.1    LaBean, T.H.2    Feng, L.3    Reif, J.H.4
  • 133
    • 12844264701 scopus 로고    scopus 로고
    • Novel electrochemical biosensing platform using self-assembled peptide nanotubes
    • Yemini, M., Reches, M., Rishpon, J., and Gazit, E. (2005a) Novel electrochemical biosensing platform using self-assembled peptide nanotubes. Nano Lett. 5, 183- 186.
    • (2005) Nano Lett , vol.5 , pp. 183-186
    • Yemini, M.1    Reches, M.2    Rishpon, J.3    Gazit, E.4
  • 134
    • 23744509819 scopus 로고    scopus 로고
    • Peptide nanotubes modified electrodes for enzyme-biosensors applications
    • Yemini, M., Reches, M., Gazit, E., and Rishpon, J. (2005b) Peptide nanotubes modified electrodes for enzyme-biosensors applications. Anal. Chem. 77, 5155-5159.
    • (2005) Anal. Chem , vol.77 , pp. 5155-5159
    • Yemini, M.1    Reches, M.2    Gazit, E.3    Rishpon, J.4
  • 135
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang, S. (2003) Fabrication of novel biomaterials through molecular self-assembly. Nat Biotechnol. 21, 1171-1178.
    • (2003) Nat Biotechnol , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 136
    • 27144513329 scopus 로고    scopus 로고
    • Multiplexed electrical detection of cancer markers with nanowire sensor arrays
    • Zheng, G., Patolsky, F., Cui, Y., Wang, W. U., and Lieber, C. M. (2005) Multiplexed electrical detection of cancer markers with nanowire sensor arrays. Nat. Biotechnol. 23, 1294-1301.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1294-1301
    • Zheng, G.1    Patolsky, F.2    Cui, Y.3    Wang, W.U.4    Lieber, C.M.5


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