메뉴 건너뛰기




Volumn 1760, Issue 4, 2006, Pages 636-651

Glyconanoparticles: Types, synthesis and applications in glycoscience, biomedicine and material science

Author keywords

Carbohydrate interaction; Glycobiology; Glyconanoparticle; Magnetic nanoparticle; Multivalence; Quantum dot

Indexed keywords

CARBOHYDRATE; NANOPARTICLE;

EID: 33646100301     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2005.12.001     Document Type: Review
Times cited : (272)

References (134)
  • 1
    • 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. Ed. 40 (2001) 4128-4158
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 4128-4158
    • Niemeyer, C.M.1
  • 2
    • 10044258525 scopus 로고    scopus 로고
    • Integrated nanoparticle-biomolecule hybrid systems: synthesis, properties, and applications
    • Katz E., and Willner I. Integrated nanoparticle-biomolecule hybrid systems: synthesis, properties, and applications. Angew. Chem. Int. Ed. 33 (2004) 6042-6108
    • (2004) Angew. Chem. Int. Ed. , vol.33 , pp. 6042-6108
    • Katz, E.1    Willner, I.2
  • 3
    • 0037799670 scopus 로고    scopus 로고
    • Gold glyconanoparticles: synthetic polyvalent ligands mimicking glycocalyx-like surfaces as tools for glycobiological studies
    • Barrientos A.G., de la Fuente J.M., Rojas T.C., Fernández A., and Penadés S. Gold glyconanoparticles: synthetic polyvalent ligands mimicking glycocalyx-like surfaces as tools for glycobiological studies. Chem.-Eur. J. 9 (2003) 1909-1921
    • (2003) Chem.-Eur. J. , vol.9 , pp. 1909-1921
    • Barrientos, A.G.1    de la Fuente, J.M.2    Rojas, T.C.3    Fernández, A.4    Penadés, S.5
  • 4
    • 4544388747 scopus 로고    scopus 로고
    • Use of magnetic nanoparticles as nanosensors to probe for molecular interactions
    • Perez J.M., Josephson L., and Weissleder R. Use of magnetic nanoparticles as nanosensors to probe for molecular interactions. ChemBioChem 5 (2004) 261-264
    • (2004) ChemBioChem , vol.5 , pp. 261-264
    • Perez, J.M.1    Josephson, L.2    Weissleder, R.3
  • 6
    • 0033693570 scopus 로고    scopus 로고
    • Synthesis and characterization of monodisperse nanocrystals and close-packed nanocrystals assemblies
    • Murray C.B., Kagan C.R., and Bawendi M.G. Synthesis and characterization of monodisperse nanocrystals and close-packed nanocrystals assemblies. Annu. Rev. Mater. Sci. 30 (2000) 545-610
    • (2000) Annu. Rev. Mater. Sci. , vol.30 , pp. 545-610
    • Murray, C.B.1    Kagan, C.R.2    Bawendi, M.G.3
  • 7
    • 0742321804 scopus 로고    scopus 로고
    • Gold nanoparticles: assembly, supramolecular chemistry, quantum-sized-related properties, and applications towards biology, catalysis and nanotechnology
    • Daniel M.-C., and Astruc D. Gold nanoparticles: assembly, supramolecular chemistry, quantum-sized-related properties, and applications towards biology, catalysis and nanotechnology. Chem. Rev. 104 (2004) 293-346
    • (2004) Chem. Rev. , vol.104 , pp. 293-346
    • Daniel, M.-C.1    Astruc, D.2
  • 8
    • 9244249136 scopus 로고    scopus 로고
    • Nanoparticles: scaffolds for molecular recognition
    • Drechesler U., Erdogan B., and Rotello V.M. Nanoparticles: scaffolds for molecular recognition. Chem.-Eur. J. 10 (2004) 5570-5579
    • (2004) Chem.-Eur. J. , vol.10 , pp. 5570-5579
    • Drechesler, U.1    Erdogan, B.2    Rotello, V.M.3
  • 9
    • 13244258395 scopus 로고    scopus 로고
    • Surface recognition of biomacromolecules using nanoparticle receptors
    • Verma A., and Rotello V.M. Surface recognition of biomacromolecules using nanoparticle receptors. Chem. Comm. 3 (2005) 303-312
    • (2005) Chem. Comm. , vol.3 , pp. 303-312
    • Verma, A.1    Rotello, V.M.2
  • 10
    • 31544471079 scopus 로고    scopus 로고
    • Nanomaterial-based amplified transduction of biomolecular interactions
    • Wang J. Nanomaterial-based amplified transduction of biomolecular interactions. Small 1 (2005) 1036-1043
    • (2005) Small , vol.1 , pp. 1036-1043
    • Wang, J.1
  • 11
    • 27444446307 scopus 로고    scopus 로고
    • Synthesis, properties, and applications of iron nanoparticles
    • Huber D.L. Synthesis, properties, and applications of iron nanoparticles. Small 1 (2005) 482-501
    • (2005) Small , vol.1 , pp. 482-501
    • Huber, D.L.1
  • 12
    • 6044243647 scopus 로고    scopus 로고
    • Understanding carbohydrate-carbohydrate interactions by means of glyconanotechnology
    • de la Fuente J.M., and Penadés S. Understanding carbohydrate-carbohydrate interactions by means of glyconanotechnology. Glycoconj. J. 21 (2004) 149-163
    • (2004) Glycoconj. J. , vol.21 , pp. 149-163
    • de la Fuente, J.M.1    Penadés, S.2
  • 13
    • 0029787628 scopus 로고    scopus 로고
    • Role of glycocalyx in regulating access of microparticles to apical plasma membranes of intestine epithelial cells: implications for microbial attachment and oral vaccine targeting
    • Frey A., Giannasca K.T., Weltzin R., Giannasca P.J., Reggio H., Lencer W.I., and Neutra M.R. Role of glycocalyx in regulating access of microparticles to apical plasma membranes of intestine epithelial cells: implications for microbial attachment and oral vaccine targeting. J. Exp. Med. 184 (1996) 1045-1059
    • (1996) J. Exp. Med. , vol.184 , pp. 1045-1059
    • Frey, A.1    Giannasca, K.T.2    Weltzin, R.3    Giannasca, P.J.4    Reggio, H.5    Lencer, W.I.6    Neutra, M.R.7
  • 14
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: all of the theories are correct
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3 (1993) 97-130
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 15
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: toward understanding the function of sugars
    • Dwek R.A. Glycobiology: toward understanding the function of sugars. Chem. Rev. 96 (1996) 683-720
    • (1996) Chem. Rev. , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 17
    • 4544343035 scopus 로고    scopus 로고
    • Surface-functionalized nanoparticle library yields probes for apoptotic cells
    • Schellenberger E.A., Reynolds F., Weissleder R., and Josephson L. Surface-functionalized nanoparticle library yields probes for apoptotic cells. ChemBioChem 5 (2004) 275-279
    • (2004) ChemBioChem , vol.5 , pp. 275-279
    • Schellenberger, E.A.1    Reynolds, F.2    Weissleder, R.3    Josephson, L.4
  • 18
    • 2342533902 scopus 로고    scopus 로고
    • Cell response to dextran-derivatised iron oxide nanoparticles post internalisation
    • Berry C.C., Wells S., Charles S., Aitchison G., and Curtis A.S.G. Cell response to dextran-derivatised iron oxide nanoparticles post internalisation. Biomaterials 25 (2004) 5405-5413
    • (2004) Biomaterials , vol.25 , pp. 5405-5413
    • Berry, C.C.1    Wells, S.2    Charles, S.3    Aitchison, G.4    Curtis, A.S.G.5
  • 19
    • 13944281688 scopus 로고    scopus 로고
    • Cytotoxic activities of chitosan nanoparticles an copper-loaded nanoparticles
    • Qi L., Xu Z., Jiang X., Li Y., and Wang M. Cytotoxic activities of chitosan nanoparticles an copper-loaded nanoparticles. Bioorg. Med. Chem. Lett. 15 (2005) 1397-1399
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 1397-1399
    • Qi, L.1    Xu, Z.2    Jiang, X.3    Li, Y.4    Wang, M.5
  • 20
    • 1542268858 scopus 로고    scopus 로고
    • Galactosylated chitosan/DNA nanoparticles prepared using water-soluble chitosan as a gene carrier
    • Kim T.H., Park I.K., Nah J.W., Choi Y.J., and Cho C.S. Galactosylated chitosan/DNA nanoparticles prepared using water-soluble chitosan as a gene carrier. Biomaterials 25 (2004) 3783-3792
    • (2004) Biomaterials , vol.25 , pp. 3783-3792
    • Kim, T.H.1    Park, I.K.2    Nah, J.W.3    Choi, Y.J.4    Cho, C.S.5
  • 22
    • 4043156991 scopus 로고    scopus 로고
    • Magnetic nanoparticles design for medical diagnosis and therapy
    • Mornet S., Vasseur S., Grasset F., and Duguet E. Magnetic nanoparticles design for medical diagnosis and therapy. J. Mater. Chem. 14 (2004) 2161-2175
    • (2004) J. Mater. Chem. , vol.14 , pp. 2161-2175
    • Mornet, S.1    Vasseur, S.2    Grasset, F.3    Duguet, E.4
  • 24
    • 0031587262 scopus 로고    scopus 로고
    • Reversible tuning of silver quantum dots monolayers through the metal-insulator transition
    • Collier C.P., Saykally R.J., Shiang J.J., Henrichs S.E., and Heath J.R. Reversible tuning of silver quantum dots monolayers through the metal-insulator transition. Science 277 (1997) 1978-1981
    • (1997) Science , vol.277 , pp. 1978-1981
    • Collier, C.P.1    Saykally, R.J.2    Shiang, J.J.3    Henrichs, S.E.4    Heath, J.R.5
  • 25
    • 0034508121 scopus 로고    scopus 로고
    • Mercaptoammonium-monolayer-protected, water-soluble gold, silver, and palladium clusters
    • Cliffel D.E., Zamborini F.P., Gross S.M., and Murray R.W. Mercaptoammonium-monolayer-protected, water-soluble gold, silver, and palladium clusters. Langmuir 16 (2000) 9699-9702
    • (2000) Langmuir , vol.16 , pp. 9699-9702
    • Cliffel, D.E.1    Zamborini, F.P.2    Gross, S.M.3    Murray, R.W.4
  • 27
    • 0033524307 scopus 로고    scopus 로고
    • Water-soluble, isolable gold clusters protected by tiopronin and coenzyme A monolayers
    • Templeton A.C., Chen S., Gross S.M., and Murray R.W. Water-soluble, isolable gold clusters protected by tiopronin and coenzyme A monolayers. Langmuir 15 (1999) 66-76
    • (1999) Langmuir , vol.15 , pp. 66-76
    • Templeton, A.C.1    Chen, S.2    Gross, S.M.3    Murray, R.W.4
  • 31
    • 0344741668 scopus 로고    scopus 로고
    • Quantitative analysis of multivalent interactions of carbohydrate-encapsulated gold nanoparticles with concanavalin A
    • Lin C.-C., Yeh Y.-C., Yang C.-Y., Chen G.-F., Chen Y.-C., Wu Y.-C., and Chen C.-C. Quantitative analysis of multivalent interactions of carbohydrate-encapsulated gold nanoparticles with concanavalin A. Chem. Commun. (2003) 2920-2921
    • (2003) Chem. Commun. , pp. 2920-2921
    • Lin, C.-C.1    Yeh, Y.-C.2    Yang, C.-Y.3    Chen, G.-F.4    Chen, Y.-C.5    Wu, Y.-C.6    Chen, C.-C.7
  • 32
    • 0042570783 scopus 로고    scopus 로고
    • Synthesis of gold glyconanoparticles and biological evaluation of recombinant Gp120 interactions
    • Nolting B., Yu J.-J., Liu G.-Y., Cho S.-J., Kauzlarich S., and Gervay-Hague J. Synthesis of gold glyconanoparticles and biological evaluation of recombinant Gp120 interactions. Langmuir 19 (2003) 6465-6473
    • (2003) Langmuir , vol.19 , pp. 6465-6473
    • Nolting, B.1    Yu, J.-J.2    Liu, G.-Y.3    Cho, S.-J.4    Kauzlarich, S.5    Gervay-Hague, J.6
  • 33
    • 12944325785 scopus 로고    scopus 로고
    • Synthesis of gold nanoparticles bearing the Thomsen-Friedenreich disaccharide: a new multivalent presentation of an important tumor antigen
    • Svarovsky S.A., Szekely Z., and Barchi J.J. Synthesis of gold nanoparticles bearing the Thomsen-Friedenreich disaccharide: a new multivalent presentation of an important tumor antigen. Tetrahedron: Asymmetry 16 (2005) 587-598
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 587-598
    • Svarovsky, S.A.1    Szekely, Z.2    Barchi, J.J.3
  • 34
    • 8144226251 scopus 로고    scopus 로고
    • Synthesis of gold glyconanoparticles: possible probes for the exploration of carbohydrate-mediated self-recognition of marine sponge cells
    • de Souza A.C., Halkes K.M., Meeldijk J.D., Verkleij A.J., Vliegenthart J.F.G., and Kamerling J.P. Synthesis of gold glyconanoparticles: possible probes for the exploration of carbohydrate-mediated self-recognition of marine sponge cells. Eur. J. Org. Chem. (2004) 4323-4339
    • (2004) Eur. J. Org. Chem. , pp. 4323-4339
    • de Souza, A.C.1    Halkes, K.M.2    Meeldijk, J.D.3    Verkleij, A.J.4    Vliegenthart, J.F.G.5    Kamerling, J.P.6
  • 35
    • 25144473038 scopus 로고    scopus 로고
    • A facile method for the preparation of gold glyconanoparticle from free oligosaccharides and their applicability in carbohydrate-protein interaction studies
    • Halkes K.M., de Souza A.C., Maljaars C.E.P., Gerwig G.J., and Kamerling J.P. A facile method for the preparation of gold glyconanoparticle from free oligosaccharides and their applicability in carbohydrate-protein interaction studies. Eur. J. Org. Chem. (2005) 3650-3659
    • (2005) Eur. J. Org. Chem. , pp. 3650-3659
    • Halkes, K.M.1    de Souza, A.C.2    Maljaars, C.E.P.3    Gerwig, G.J.4    Kamerling, J.P.5
  • 36
    • 0034809059 scopus 로고    scopus 로고
    • Quantitative and reversible lectin-induced association of gold nanoparticles modified with α-Lactosyl-ω-mercapto-poly(ethylene glycol)
    • Otsuka H., Akiyama Y., Nagasaki Y., and Kataoka K. Quantitative and reversible lectin-induced association of gold nanoparticles modified with α-Lactosyl-ω-mercapto-poly(ethylene glycol). J. Am. Chem. Soc. 123 (2001) 8226-8230
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8226-8230
    • Otsuka, H.1    Akiyama, Y.2    Nagasaki, Y.3    Kataoka, K.4
  • 38
    • 8444228842 scopus 로고    scopus 로고
    • Complexation of polysaccharide and monosaccharide with thiolate boronic acid capped on silver nanoparticle
    • Zhang J., Geddes C.D., and Lakowicz J.R. Complexation of polysaccharide and monosaccharide with thiolate boronic acid capped on silver nanoparticle. Anal. Biochem. 332 (2004) 253-260
    • (2004) Anal. Biochem. , vol.332 , pp. 253-260
    • Zhang, J.1    Geddes, C.D.2    Lakowicz, J.R.3
  • 39
    • 8144225338 scopus 로고    scopus 로고
    • Preparation and characterization of metal-chitosan nanocomposites
    • Huang H., Yuan Q., and Yang X. Preparation and characterization of metal-chitosan nanocomposites. Colloids Surf., B 39 (2004) 31-37
    • (2004) Colloids Surf., B , vol.39 , pp. 31-37
    • Huang, H.1    Yuan, Q.2    Yang, X.3
  • 40
    • 0043188114 scopus 로고
    • Nanostructured materials
    • Gleiter H. Nanostructured materials. Adv. Mater. 4 (1992) 474-481
    • (1992) Adv. Mater. , vol.4 , pp. 474-481
    • Gleiter, H.1
  • 41
    • 0012392952 scopus 로고    scopus 로고
    • Semiconductor nanocrystals as fluorescent biological labels
    • Bruchez M., Moronne M., Gin P., Weiss S., and Alivisatos A.P. Semiconductor nanocrystals as fluorescent biological labels. Science 281 (1998) 2013-2016
    • (1998) Science , vol.281 , pp. 2013-2016
    • Bruchez, M.1    Moronne, M.2    Gin, P.3    Weiss, S.4    Alivisatos, A.P.5
  • 42
    • 0032566763 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for ultrasensitive nonisotopic detection
    • Chan W.C.W., and Nie S. Quantum dot bioconjugates for ultrasensitive nonisotopic detection. Science 281 (1998) 2016-2018
    • (1998) Science , vol.281 , pp. 2016-2018
    • Chan, W.C.W.1    Nie, S.2
  • 44
    • 0034583436 scopus 로고    scopus 로고
    • Colloidal quantum dots. From scaling laws to biological applications
    • Alivisatos A.P. Colloidal quantum dots. From scaling laws to biological applications. Pure Appl. Chem. 72 (2000) 3-9
    • (2000) Pure Appl. Chem. , vol.72 , pp. 3-9
    • Alivisatos, A.P.1
  • 46
    • 0036705946 scopus 로고    scopus 로고
    • Quantum dots as luminescent probes in biological systems
    • Sutherland A.J. Quantum dots as luminescent probes in biological systems. Curr. Opin. Solid State Mater. Sci. 6 (2002) 365-370
    • (2002) Curr. Opin. Solid State Mater. Sci. , vol.6 , pp. 365-370
    • Sutherland, A.J.1
  • 47
    • 0035900533 scopus 로고    scopus 로고
    • Recognition molecule directed interfacing between semiconductor quantum dots and nerve cells
    • Winter J.O., Liu T.Y., Korgel B.A., and Schmidt C.E. Recognition molecule directed interfacing between semiconductor quantum dots and nerve cells. Adv. Mater. 13 (2001) 1673-1677
    • (2001) Adv. Mater. , vol.13 , pp. 1673-1677
    • Winter, J.O.1    Liu, T.Y.2    Korgel, B.A.3    Schmidt, C.E.4
  • 50
    • 0034615057 scopus 로고    scopus 로고
    • Peptide-encapsulated CdS nanoclusters from a combinatorial ligand library
    • Spreitzer G., Whitling J.M., Madura J.D., and Wright D.W. Peptide-encapsulated CdS nanoclusters from a combinatorial ligand library. Chem. Commun. (2000) 209-210
    • (2000) Chem. Commun. , pp. 209-210
    • Spreitzer, G.1    Whitling, J.M.2    Madura, J.D.3    Wright, D.W.4
  • 51
    • 0035824053 scopus 로고    scopus 로고
    • Blue emission from cysteines ester passivated cadmium sulfide nanoclusters
    • Sapra S., Nanda J., Sarma D.D., Abed El-Al F., and Hodes G. Blue emission from cysteines ester passivated cadmium sulfide nanoclusters. Chem. Commun. (2001) 2188-2189
    • (2001) Chem. Commun. , pp. 2188-2189
    • Sapra, S.1    Nanda, J.2    Sarma, D.D.3    Abed El-Al, F.4    Hodes, G.5
  • 54
    • 0348087040 scopus 로고    scopus 로고
    • Long-term multiple color imaging of live cells using quantum dots
    • Jaiswal J.K., Mattousi H., Mauro J.M., and Simon S.M. Long-term multiple color imaging of live cells using quantum dots. Nat. Biotechnol. 21 (2003) 47-51
    • (2003) Nat. Biotechnol. , vol.21 , pp. 47-51
    • Jaiswal, J.K.1    Mattousi, H.2    Mauro, J.M.3    Simon, S.M.4
  • 56
    • 0000858151 scopus 로고
    • Protein-sized quantum dot luminescence can distinguish between "straight", "bent", and "kinked" oligonucleotides
    • Mahtab R., Rogers J.P., and Murphy C.J. Protein-sized quantum dot luminescence can distinguish between "straight", "bent", and "kinked" oligonucleotides. J. Am. Chem. Soc. 117 (1995) 9099-9100
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9099-9100
    • Mahtab, R.1    Rogers, J.P.2    Murphy, C.J.3
  • 58
    • 0037077627 scopus 로고    scopus 로고
    • Self-assembled nanoparticle probes for recognition and detection of biomolecules
    • Maxwell D.J., Taylor J.R., and Nie S.J. Self-assembled nanoparticle probes for recognition and detection of biomolecules. J. Am. Chem. Soc. 124 (2002) 9609-9612
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9609-9612
    • Maxwell, D.J.1    Taylor, J.R.2    Nie, S.J.3
  • 62
    • 0141856506 scopus 로고    scopus 로고
    • Synthesis of glyconanospheres containing luminescent CdSe-ZnS quantum dots
    • Chen Y., Ji T., and Rosenzweig Z. Synthesis of glyconanospheres containing luminescent CdSe-ZnS quantum dots. Nano Lett. 3 (2003) 581-584
    • (2003) Nano Lett. , vol.3 , pp. 581-584
    • Chen, Y.1    Ji, T.2    Rosenzweig, Z.3
  • 63
    • 8844228226 scopus 로고    scopus 로고
    • Site-specific multivalent carbohydrate labeling of quantum dots and magnetic beads
    • Sun X.-L., Cui W., Haller C., and Chaikof E.L. Site-specific multivalent carbohydrate labeling of quantum dots and magnetic beads. ChemBioChem 5 (2004) 1593-1596
    • (2004) ChemBioChem , vol.5 , pp. 1593-1596
    • Sun, X.-L.1    Cui, W.2    Haller, C.3    Chaikof, E.L.4
  • 64
    • 13144269629 scopus 로고    scopus 로고
    • Glyco-quantum dots: a new luminescent system with multivalent carbohydrate display
    • de la Fuente J.M., and Penadés S. Glyco-quantum dots: a new luminescent system with multivalent carbohydrate display. Tetrahedron: Asymmetry 16 (2005) 387-391
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 387-391
    • de la Fuente, J.M.1    Penadés, S.2
  • 66
    • 0037767617 scopus 로고    scopus 로고
    • Functionalisation of magnetic nanoparticles for applications in biomedicine
    • Berry C.C., and Curtis A.S.G. Functionalisation of magnetic nanoparticles for applications in biomedicine. J. Phys., D, Appl. Phys. 36 (2003) R198-R206
    • (2003) J. Phys., D, Appl. Phys. , vol.36
    • Berry, C.C.1    Curtis, A.S.G.2
  • 68
    • 33646105240 scopus 로고    scopus 로고
    • S. Penades, M. Martin-Lomas, J.M. de la Fuente, T.W. Rademacher, Magnetic Nanoparticles, WO 2004/108165 A2
  • 69
    • 33646116158 scopus 로고    scopus 로고
    • J.M. de la Fuente, D. Alcántara, S. Penadés, unpublished results.
  • 71
    • 0000147431 scopus 로고
    • Carbohydrate-carbohydrate interactions as an initial step in cell recognition
    • Hakomori S.-I. Carbohydrate-carbohydrate interactions as an initial step in cell recognition. Pure Appl. Chem. 63 (1991) 473-482
    • (1991) Pure Appl. Chem. , vol.63 , pp. 473-482
    • Hakomori, S.-I.1
  • 72
    • 0024378959 scopus 로고
    • Specific interaction between gangliotriaosylceramide (Gg3) and sialosyllactosylceramide (GM3) as a basis for specific cellular recognition between lymphoma and melanoma cells
    • Kojima N., and Hakomori S.-I. Specific interaction between gangliotriaosylceramide (Gg3) and sialosyllactosylceramide (GM3) as a basis for specific cellular recognition between lymphoma and melanoma cells. J. Biol. Chem. 264 (1989) 20159-20162
    • (1989) J. Biol. Chem. , vol.264 , pp. 20159-20162
    • Kojima, N.1    Hakomori, S.-I.2
  • 73
    • 0032579279 scopus 로고    scopus 로고
    • Globoside-dependent adhesion of human embryonal carcinoma cells, based on carbohydrate-carbohydrate interaction, initiates signal transduction and induces enhanced activity of transcription factors AP1 and CREB
    • Song Y., Withers D.A., and Hakomori S.-I. Globoside-dependent adhesion of human embryonal carcinoma cells, based on carbohydrate-carbohydrate interaction, initiates signal transduction and induces enhanced activity of transcription factors AP1 and CREB. J. Biol. Chem. 273 (1998) 2517-2525
    • (1998) J. Biol. Chem. , vol.273 , pp. 2517-2525
    • Song, Y.1    Withers, D.A.2    Hakomori, S.-I.3
  • 74
    • 0028796509 scopus 로고
    • Inhibition of B16 melanoma metastasis by administration of GM3- or Gg3-liposomes-blocking adhesion of melanoma-cells to endothelial-cells (antiadhesion therapy) via inhibition of GM3-Gg3Cer or GM3-LacCer interaction
    • Otsuji E., Park Y.S., Tashiro K., Kojima N., Toyokuni T., and Hakomori S.-I. Inhibition of B16 melanoma metastasis by administration of GM3- or Gg3-liposomes-blocking adhesion of melanoma-cells to endothelial-cells (antiadhesion therapy) via inhibition of GM3-Gg3Cer or GM3-LacCer interaction. Int. J. Oncol. 6 (1995) 319-327
    • (1995) Int. J. Oncol. , vol.6 , pp. 319-327
    • Otsuji, E.1    Park, Y.S.2    Tashiro, K.3    Kojima, N.4    Toyokuni, T.5    Hakomori, S.-I.6
  • 75
    • 0037022620 scopus 로고    scopus 로고
    • Binding of rainbow trout sperm to eggs is mediated by strong carbohydrate-to-carbohydrate interaction between (KDN)GM3 (deaminated neuraminyl ganglioside) and Gg3-like epitope
    • Yu S., Kojima N., Hakomori S.-I., Kudo S., Inoue S., and Inoue Y. Binding of rainbow trout sperm to eggs is mediated by strong carbohydrate-to-carbohydrate interaction between (KDN)GM3 (deaminated neuraminyl ganglioside) and Gg3-like epitope. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 2854-2859
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2854-2859
    • Yu, S.1    Kojima, N.2    Hakomori, S.-I.3    Kudo, S.4    Inoue, S.5    Inoue, Y.6
  • 77
    • 0027462168 scopus 로고
    • Carbohydrate-carbohydrate interactions of a novel acidic glycan can mediate sponge cell adhesion
    • Misevic G.N., and Burger M.M. Carbohydrate-carbohydrate interactions of a novel acidic glycan can mediate sponge cell adhesion. J. Biol. Chem. 268 (1993) 4922-4929
    • (1993) J. Biol. Chem. , vol.268 , pp. 4922-4929
    • Misevic, G.N.1    Burger, M.M.2
  • 78
    • 0022999307 scopus 로고
    • Reconstitution of high cell binding affinity of a marine sponge aggregation factor by cross-linking of small low affinity fragments into a large polyvalent polymer
    • Burkat W., and Burger M.M. Reconstitution of high cell binding affinity of a marine sponge aggregation factor by cross-linking of small low affinity fragments into a large polyvalent polymer. J. Biol. Chem. 261 (1986) 2853-2859
    • (1986) J. Biol. Chem. , vol.261 , pp. 2853-2859
    • Burkat, W.1    Burger, M.M.2
  • 79
    • 0027378268 scopus 로고
    • Characterization of a novel pyruvylated carbohydrate unit implicated in the cell aggregation of the marine sponge Microciona prolifera
    • Spillmann D., Hard K., Thomas-Oates J.E., Vliegenthart J.F.G., Misevic G.N., Burger M.M., and Finne J. Characterization of a novel pyruvylated carbohydrate unit implicated in the cell aggregation of the marine sponge Microciona prolifera. J. Biol. Chem. 268 (1993) 13378-13387
    • (1993) J. Biol. Chem. , vol.268 , pp. 13378-13387
    • Spillmann, D.1    Hard, K.2    Thomas-Oates, J.E.3    Vliegenthart, J.F.G.4    Misevic, G.N.5    Burger, M.M.6    Finne, J.7
  • 80
    • 0028910997 scopus 로고
    • Characterization of a novel sulfated carbohydrate unit implicated in the carbohydrate-carbohydrate aggregation of the marine sponge Microciona prolifera
    • Spillmann D., Thomas-Oates J.E., Van Kuik J.A., Vliegenthart J.F.G., Misevic G., Burger M.M., and Finne J. Characterization of a novel sulfated carbohydrate unit implicated in the carbohydrate-carbohydrate aggregation of the marine sponge Microciona prolifera. J. Biol. Chem. 270 (1995) 5089-5097
    • (1995) J. Biol. Chem. , vol.270 , pp. 5089-5097
    • Spillmann, D.1    Thomas-Oates, J.E.2    Van Kuik, J.A.3    Vliegenthart, J.F.G.4    Misevic, G.5    Burger, M.M.6    Finne, J.7
  • 83
    • 0027938601 scopus 로고
    • Further-studies on cell-adhesion based on Le(X)-Le(X) interaction, with new approaches-embryoglycan aggregation of F9 teratrocarcinoma cells, and adhesion of various tumor-cells based on Le(X) expression
    • Kojima N., Fenderson B.A., Stroud M.R., Goldberg I.R., Habermann R., Toyokuni T., and Hakomori S.-I. Further-studies on cell-adhesion based on Le(X)-Le(X) interaction, with new approaches-embryoglycan aggregation of F9 teratrocarcinoma cells, and adhesion of various tumor-cells based on Le(X) expression. Glycoconj. J. 11 (1994) 238-248
    • (1994) Glycoconj. J. , vol.11 , pp. 238-248
    • Kojima, N.1    Fenderson, B.A.2    Stroud, M.R.3    Goldberg, I.R.4    Habermann, R.5    Toyokuni, T.6    Hakomori, S.-I.7
  • 84
    • 0002665307 scopus 로고    scopus 로고
    • Model systems for studying polyvalent carbohydrate binding interactions
    • Houseman B.T., and Mrksich M. Model systems for studying polyvalent carbohydrate binding interactions. Top. Curr. Chem. 218 (2002) 1-44
    • (2002) Top. Curr. Chem. , vol.218 , pp. 1-44
    • Houseman, B.T.1    Mrksich, M.2
  • 85
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors
    • Mammen M., Choi S.K., and Whitesides G.M. Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. 37 (1998) 2754-2794
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 2754-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3
  • 86
    • 18244369240 scopus 로고    scopus 로고
    • 2+-mediated self-aggregation of Lewis X gold glyconanoparticles. A model for cell adhesion via carbohydrate-carbohydrate interaction
    • 2+-mediated self-aggregation of Lewis X gold glyconanoparticles. A model for cell adhesion via carbohydrate-carbohydrate interaction. J. Am. Chem. Soc. 127 (2005) 6192-6197
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6192-6197
    • de la Fuente, J.M.1    Eaton, P.2    Barrientos, A.G.3    Menedez, M.4    Penades, S.5
  • 88
    • 0037012739 scopus 로고    scopus 로고
    • A model system mimicking glycosphingolipid clusters to quantify carbohydrate self-interactions by surface plasmon resonance
    • Hernáiz M.J., de la Fuente J.M., Barrientos A.G., and Penadés S. A model system mimicking glycosphingolipid clusters to quantify carbohydrate self-interactions by surface plasmon resonance. Angew. Chem. Int. Ed. 41 (2002) 1554-1557
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 1554-1557
    • Hernáiz, M.J.1    de la Fuente, J.M.2    Barrientos, A.G.3    Penadés, S.4
  • 90
    • 0036462602 scopus 로고    scopus 로고
    • The cluster glycoside effect
    • Lundquist J.J., and Toone E.J. The cluster glycoside effect. Chem. Rev. 102 (2002) 555-578
    • (2002) Chem. Rev. , vol.102 , pp. 555-578
    • Lundquist, J.J.1    Toone, E.J.2
  • 91
    • 0036182796 scopus 로고    scopus 로고
    • Glycodendrimers: novel glycotope isosteres unmasking sugar coding, case with T-antigen markers from breast cancer MUC1 glycoprotein
    • Roy R., and Baek M.G. Glycodendrimers: novel glycotope isosteres unmasking sugar coding, case with T-antigen markers from breast cancer MUC1 glycoprotein. J. Biotechnol. 90 (2002) 291-309
    • (2002) J. Biotechnol. , vol.90 , pp. 291-309
    • Roy, R.1    Baek, M.G.2
  • 93
    • 0036899037 scopus 로고    scopus 로고
    • Biological applications of dendrimers
    • Cloninger M.J. Biological applications of dendrimers. Curr. Opin. Chem. Biol. 6 (2002) 742-748
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 742-748
    • Cloninger, M.J.1
  • 94
    • 0031002854 scopus 로고    scopus 로고
    • Generation and in situ evaluation of libraries of poly(acrylic acid) presenting sialosides as side chains as polyvalents inhibitors of influenza-mediated hemagglutination
    • Choi S.K., Mammen M., and Whitesides G.M. Generation and in situ evaluation of libraries of poly(acrylic acid) presenting sialosides as side chains as polyvalents inhibitors of influenza-mediated hemagglutination. J. Am. Chem. Soc. 119 (1997) 4103-4111
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4103-4111
    • Choi, S.K.1    Mammen, M.2    Whitesides, G.M.3
  • 95
    • 0029870744 scopus 로고    scopus 로고
    • Recognition specificity of neoglycopolymers prepared by ring-opening metathesis
    • Mortell K.H., Weatherman R.V., and Kiessling L.L. Recognition specificity of neoglycopolymers prepared by ring-opening metathesis. J. Am. Chem. Soc. 118 (1996) 2297-2298
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2297-2298
    • Mortell, K.H.1    Weatherman, R.V.2    Kiessling, L.L.3
  • 96
    • 0037032301 scopus 로고    scopus 로고
    • High-avidity, low-affinity multivalent interactions and the block to polyspermy in Xenopus laevis
    • Arranz-Plaza E., Tracy A.S., Siriwardena A., Pierce J.M., and Boons G.-J. High-avidity, low-affinity multivalent interactions and the block to polyspermy in Xenopus laevis. J. Am. Chem. Soc. 124 (2002) 13035-13046
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13035-13046
    • Arranz-Plaza, E.1    Tracy, A.S.2    Siriwardena, A.3    Pierce, J.M.4    Boons, G.-J.5
  • 97
    • 0037774630 scopus 로고    scopus 로고
    • Multivalency and the mode of action of bacterial sialidases
    • Thobhani S., Ember B., Siriwardena A., and Boons G.-J. Multivalency and the mode of action of bacterial sialidases. J. Am. Chem. Soc. 125 (2003) 7154-7155
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7154-7155
    • Thobhani, S.1    Ember, B.2    Siriwardena, A.3    Boons, G.-J.4
  • 98
    • 0000358206 scopus 로고
    • Carbohydrate-protein interactions: basis of glycobiology
    • Lee Y.C., and Lee R.T. Carbohydrate-protein interactions: basis of glycobiology. Acc. Chem. Res. 28 (1995) 321-327
    • (1995) Acc. Chem. Res. , vol.28 , pp. 321-327
    • Lee, Y.C.1    Lee, R.T.2
  • 99
    • 0026782802 scopus 로고
    • The agglutination of erythrocytes by influenza virus is strongly inhibited by liposomes incorporating an analog of sialyl gangliosides
    • Kingery-Wood J.E., Williams K.W., Sigal G.B., and Whitesides G.W. The agglutination of erythrocytes by influenza virus is strongly inhibited by liposomes incorporating an analog of sialyl gangliosides. J. Am. Chem. Soc. 114 (1992) 7303-7305
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7303-7305
    • Kingery-Wood, J.E.1    Williams, K.W.2    Sigal, G.B.3    Whitesides, G.W.4
  • 100
    • 0037009079 scopus 로고    scopus 로고
    • Novel glycodendrimers self-assemble to nanoparticles which function as polyvalent ligands in vitro and in vivo
    • Thoma G., Katopodis A.G., Voelcker N., Duthaler R.O., and Streiff M.B. Novel glycodendrimers self-assemble to nanoparticles which function as polyvalent ligands in vitro and in vivo. Angew. Chem. Int. Ed. 41 (2002) 3195-3198
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 3195-3198
    • Thoma, G.1    Katopodis, A.G.2    Voelcker, N.3    Duthaler, R.O.4    Streiff, M.B.5
  • 101
    • 12244306890 scopus 로고    scopus 로고
    • Lactose-installed poly(ethylene glycol)-poly(d,l-lactide) block copolymer micelles exhibit fast-rate binding and high affinity toward a protein bed simulating a cell surface. A surface plasmon resonance study
    • Jule E., Nagasaki Y., and Kataoka K. Lactose-installed poly(ethylene glycol)-poly(d,l-lactide) block copolymer micelles exhibit fast-rate binding and high affinity toward a protein bed simulating a cell surface. A surface plasmon resonance study. Bioconj. Chem. 14 (2003) 177-186
    • (2003) Bioconj. Chem. , vol.14 , pp. 177-186
    • Jule, E.1    Nagasaki, Y.2    Kataoka, K.3
  • 103
    • 0035814138 scopus 로고    scopus 로고
    • Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to glycoproteins, lactose maxiclusters, and cell surface glycoconjugates
    • André S., Pieters R.J., Vrasidas I., Kaltner H., Kuwabara I., Liu F.-T., Liskamp R.M.J., and Gabius H.-J. Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to glycoproteins, lactose maxiclusters, and cell surface glycoconjugates. ChemBioChem 2 (2001) 822-830
    • (2001) ChemBioChem , vol.2 , pp. 822-830
    • André, S.1    Pieters, R.J.2    Vrasidas, I.3    Kaltner, H.4    Kuwabara, I.5    Liu, F.-T.6    Liskamp, R.M.J.7    Gabius, H.-J.8
  • 104
    • 0012061680 scopus 로고    scopus 로고
    • Lactose-containing starburst dendrimers: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties
    • André S., Ortega P.J., Pérez M.A., Roy R., and Gabius H.-J. Lactose-containing starburst dendrimers: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties. Glycobiology 9 (1999) 1253-1261
    • (1999) Glycobiology , vol.9 , pp. 1253-1261
    • André, S.1    Ortega, P.J.2    Pérez, M.A.3    Roy, R.4    Gabius, H.-J.5
  • 106
    • 0034701264 scopus 로고    scopus 로고
    • High-affinity pentavalent ligands of Escherichia coli heat-labile enterotoxin by modular structure-based design
    • Fan E.K., Zhang Z.S., Minke W.E., Hou Z., Verlinde C.L.M.J., and Hol W.G.J. High-affinity pentavalent ligands of Escherichia coli heat-labile enterotoxin by modular structure-based design. J. Am. Chem. Soc. 122 (2000) 2663-2664
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2663-2664
    • Fan, E.K.1    Zhang, Z.S.2    Minke, W.E.3    Hou, Z.4    Verlinde, C.L.M.J.5    Hol, W.G.J.6
  • 109
    • 0037181083 scopus 로고    scopus 로고
    • Control of multivalent interactions by binding epitope density
    • Cairo C.W., Gestwicki J.E., Kanai M., and Kiessling L.L. Control of multivalent interactions by binding epitope density. J. Am. Chem. Soc. 124 (2002) 1615-1619
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1615-1619
    • Cairo, C.W.1    Gestwicki, J.E.2    Kanai, M.3    Kiessling, L.L.4
  • 111
    • 0037960821 scopus 로고    scopus 로고
    • Altering the strength of lectin binding interactions and controlling the amount of lectin clustering using mannose/hydroxyl-functionalized dendrimers
    • Woller E.K., Walter E.D., Morgan J.R., Singel D.J., and Cloninger M.J. Altering the strength of lectin binding interactions and controlling the amount of lectin clustering using mannose/hydroxyl-functionalized dendrimers. J. Am. Chem Soc. 125 (2003) 8820-8826
    • (2003) J. Am. Chem Soc. , vol.125 , pp. 8820-8826
    • Woller, E.K.1    Walter, E.D.2    Morgan, J.R.3    Singel, D.J.4    Cloninger, M.J.5
  • 112
    • 25144473424 scopus 로고    scopus 로고
    • Gold nanoparticle-based competitive colorimetric assay for detection of protein-protein interactions
    • Tsai C.-S., Yu T.-B., and Chen C.-T. Gold nanoparticle-based competitive colorimetric assay for detection of protein-protein interactions. Chem. Commun. (2005) 4273-4275
    • (2005) Chem. Commun. , pp. 4273-4275
    • Tsai, C.-S.1    Yu, T.-B.2    Chen, C.-T.3
  • 113
    • 25444484386 scopus 로고    scopus 로고
    • Tat peptide as an efficient molecule to translocate gold nanoparticles into the cell nucleus
    • de la Fuente J.M., and Berry C.C. Tat peptide as an efficient molecule to translocate gold nanoparticles into the cell nucleus. Bioconj. Chem. 16 (2005) 1176-1180
    • (2005) Bioconj. Chem. , vol.16 , pp. 1176-1180
    • de la Fuente, J.M.1    Berry, C.C.2
  • 114
    • 0034031149 scopus 로고    scopus 로고
    • Applications of nanotechnology to biotechnology: commentary
    • West J., and Halas N. Applications of nanotechnology to biotechnology: commentary. Curr. Opin. Biotechnol. 11 (2000) 215-217
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 215-217
    • West, J.1    Halas, N.2
  • 115
    • 0036007604 scopus 로고    scopus 로고
    • High throughput magnetic resonance imaging for eveluating targeted nanoparticles probes
    • Hogemann D., Ntziachristos V., Josephnon L., and Weissleder R. High throughput magnetic resonance imaging for eveluating targeted nanoparticles probes. Bioconj. Chem. 13 (2002) 116-121
    • (2002) Bioconj. Chem. , vol.13 , pp. 116-121
    • Hogemann, D.1    Ntziachristos, V.2    Josephnon, L.3    Weissleder, R.4
  • 116
    • 0034893552 scopus 로고    scopus 로고
    • Nanostructured materials designed for cell binding and transduction
    • Liu J., Zhang Q., Remsen E., and Wooley K. Nanostructured materials designed for cell binding and transduction. Biomacromolecules 2 (2001) 362-368
    • (2001) Biomacromolecules , vol.2 , pp. 362-368
    • Liu, J.1    Zhang, Q.2    Remsen, E.3    Wooley, K.4
  • 117
    • 0035922541 scopus 로고    scopus 로고
    • Encapsulation, permeability, and cellular uptake characteristics of hollow nanometer-sized conductive polymer capsules
    • Marikanos S.M., Anderson M.F., Ryan J., Martin L.D., and Feldheim P.L. Encapsulation, permeability, and cellular uptake characteristics of hollow nanometer-sized conductive polymer capsules. J. Phys. Chem., B 105 (2001) 8872-8876
    • (2001) J. Phys. Chem., B , vol.105 , pp. 8872-8876
    • Marikanos, S.M.1    Anderson, M.F.2    Ryan, J.3    Martin, L.D.4    Feldheim, P.L.5
  • 118
    • 0026447434 scopus 로고
    • Signal-mediated nuclear transport in simian virus 40-transformed cells is regulated by large tumor antigen
    • Feldherr C., Lanford R., and Akin D. Signal-mediated nuclear transport in simian virus 40-transformed cells is regulated by large tumor antigen. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 11002-11005
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11002-11005
    • Feldherr, C.1    Lanford, R.2    Akin, D.3
  • 120
    • 0037051601 scopus 로고    scopus 로고
    • Selective binding of mannose-encapsulated gold nanoparticles to type 1 pili in Escherichia coli
    • Lin C.-C., Yeh Y.-C., Yang C.-Y., Chen C.-L., Chen G.-F., Chen C.-C., and Wu Y.-C. Selective binding of mannose-encapsulated gold nanoparticles to type 1 pili in Escherichia coli. J. Am. Chem. Soc. 124 (2002) 3508-3509
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3508-3509
    • Lin, C.-C.1    Yeh, Y.-C.2    Yang, C.-Y.3    Chen, C.-L.4    Chen, G.-F.5    Chen, C.-C.6    Wu, Y.-C.7
  • 121
    • 2942549400 scopus 로고    scopus 로고
    • Nanogold-plasmon-resonance-based glucose sensing
    • Aslan K., Lakowicz J.R., and Geddes C.D. Nanogold-plasmon-resonance-based glucose sensing. Anal. Biochem. 330 (2004) 145-155
    • (2004) Anal. Biochem. , vol.330 , pp. 145-155
    • Aslan, K.1    Lakowicz, J.R.2    Geddes, C.D.3
  • 122
    • 3042813670 scopus 로고    scopus 로고
    • Saccharide sensing using gold and silver nanoparticles-A review
    • Aslan K., Zhang J., Lakowicz J.R., and Geddes C.D. Saccharide sensing using gold and silver nanoparticles-A review. J. Fluoresc. 14 (2004) 391-400
    • (2004) J. Fluoresc. , vol.14 , pp. 391-400
    • Aslan, K.1    Zhang, J.2    Lakowicz, J.R.3    Geddes, C.D.4
  • 125
    • 0001469077 scopus 로고    scopus 로고
    • Self-assembled nanostructured materials
    • Fendler J.H. Self-assembled nanostructured materials. Chem. Mater. 8 (1996) 1616-1624
    • (1996) Chem. Mater. , vol.8 , pp. 1616-1624
    • Fendler, J.H.1
  • 126
    • 0342914504 scopus 로고    scopus 로고
    • Fabrication of ordered two-dimensional arrays of micro- and nanoparticles using patterned self-assembled monolayers as templates
    • Quin D., Xia Y., Xu B., Yang H., Zhu C., and Whitesides G.M. Fabrication of ordered two-dimensional arrays of micro- and nanoparticles using patterned self-assembled monolayers as templates. Adv. Mater. 11 (1999) 1433-1437
    • (1999) Adv. Mater. , vol.11 , pp. 1433-1437
    • Quin, D.1    Xia, Y.2    Xu, B.3    Yang, H.4    Zhu, C.5    Whitesides, G.M.6
  • 127
    • 0034023478 scopus 로고    scopus 로고
    • Use of a steroid cyclic disulfide anchor in constructing gold nanoparticle-oligonucleotide conjugates
    • Letsinger R.L., Elghanian R.V.G., and Mirkin C.A. Use of a steroid cyclic disulfide anchor in constructing gold nanoparticle-oligonucleotide conjugates. Bioconj. Chem. 11 (2000) 289-291
    • (2000) Bioconj. Chem. , vol.11 , pp. 289-291
    • Letsinger, R.L.1    Elghanian, R.V.G.2    Mirkin, C.A.3
  • 128
    • 0033585584 scopus 로고    scopus 로고
    • Hybrid nanoparticles with block copolymer shell structures
    • Watson K.J., Zhu J., Nguyen S.-B.T., and Mirkin C.A. Hybrid nanoparticles with block copolymer shell structures. J. Am. Chem. Soc. 121 (1999) 462-463
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 462-463
    • Watson, K.J.1    Zhu, J.2    Nguyen, S.-B.T.3    Mirkin, C.A.4
  • 129
    • 0032486787 scopus 로고    scopus 로고
    • pH-gated single-electron tunneling in chemically modified gold nanoclusters
    • Brousseau L.C., Zhao Q., Shultz D.A., and Feldheim D.L. pH-gated single-electron tunneling in chemically modified gold nanoclusters. J. Am. Chem. Soc. 120 (1998) 7645-7646
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7645-7646
    • Brousseau, L.C.1    Zhao, Q.2    Shultz, D.A.3    Feldheim, D.L.4
  • 131
    • 0035925126 scopus 로고    scopus 로고
    • Competitive photochemical reactivity in a self-assembled monolayer on a colloidal gold cluster
    • Hu J., Zhang J., Liu F., Kitteredge K., Whiteshell J.K., and Fox M.A. Competitive photochemical reactivity in a self-assembled monolayer on a colloidal gold cluster. J. Am. Chem. Soc. 123 (2001) 1464-1470
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1464-1470
    • Hu, J.1    Zhang, J.2    Liu, F.3    Kitteredge, K.4    Whiteshell, J.K.5    Fox, M.A.6
  • 133
    • 0030084093 scopus 로고    scopus 로고
    • Semiconductor clusters, nanocrystals, and quantum dots
    • Alivisatos A.P. Semiconductor clusters, nanocrystals, and quantum dots. Science 27 (1996) 933-937
    • (1996) Science , vol.27 , pp. 933-937
    • Alivisatos, A.P.1
  • 134
    • 0032215542 scopus 로고    scopus 로고
    • Gold nanoclusters reductively deposited on porous silicon: morphology and electronic structures
    • Coulthard I., Degen S., Zhu Y.-J., and Sham T.K. Gold nanoclusters reductively deposited on porous silicon: morphology and electronic structures. Can. J. Phys. 76 (1998) 1707-1716
    • (1998) Can. J. Phys. , vol.76 , pp. 1707-1716
    • Coulthard, I.1    Degen, S.2    Zhu, Y.-J.3    Sham, T.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.