메뉴 건너뛰기




Volumn 65, Issue 5, 2013, Pages 677-688

Controlled antibody/(bio-) conjugation of inorganic nanoparticles for targeted delivery

Author keywords

Antibodies; Bioconjugation; Colloidal nanoparticles; Controlled targeting; Drug delivery; Gold nanoparticles; Magnetic nanoparticles; Molecular recognition; Quantum dots

Indexed keywords

BIO-CONJUGATION; COLLOIDAL NANOPARTICLES; CONTROLLED TARGETING; GOLD NANOPARTICLES; MAGNETIC NANO-PARTICLES;

EID: 84878408367     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2012.12.003     Document Type: Review
Times cited : (173)

References (154)
  • 1
    • 0037017738 scopus 로고    scopus 로고
    • Direct on air sampling filter quantification of cat allergen
    • Holmquist L., Vesterberg O. Direct on air sampling filter quantification of cat allergen. J. Biochem. Biophys. Methods 2002, 51:17-25.
    • (2002) J. Biochem. Biophys. Methods , vol.51 , pp. 17-25
    • Holmquist, L.1    Vesterberg, O.2
  • 2
    • 1542297653 scopus 로고    scopus 로고
    • Recombinant immunotoxins and retargeted killer cells: employing engineered antibody fragments for tumor-specific targeting of cytotoxic effectors
    • Wels W., Biburger M., Muller T., Dalken B., Giesubel U., Tonn T., Uherek C. Recombinant immunotoxins and retargeted killer cells: employing engineered antibody fragments for tumor-specific targeting of cytotoxic effectors. Cancer Immunol. Immunother. 2004, 53:217-226.
    • (2004) Cancer Immunol. Immunother. , vol.53 , pp. 217-226
    • Wels, W.1    Biburger, M.2    Muller, T.3    Dalken, B.4    Giesubel, U.5    Tonn, T.6    Uherek, C.7
  • 3
    • 77953147424 scopus 로고    scopus 로고
    • Simultaneous multiplex detection and confirmation of the proteinaceous toxins abrin, ricin, botulinum toxins, and Staphylococcus enterotoxins A, B, and C in food
    • Garber E., Venkateswaran K., O'Brien T. Simultaneous multiplex detection and confirmation of the proteinaceous toxins abrin, ricin, botulinum toxins, and Staphylococcus enterotoxins A, B, and C in food. J. Agric. Food Chem. 2010, 58:6600-6607.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 6600-6607
    • Garber, E.1    Venkateswaran, K.2    O'Brien, T.3
  • 4
    • 0017584586 scopus 로고
    • Analysis of cell-surfaces by xenogeneic myeloma-hybrid antibodies - Differentiation antigens of rat lymphocytes
    • Williams A., Galfre G., Milstein C. Analysis of cell-surfaces by xenogeneic myeloma-hybrid antibodies - Differentiation antigens of rat lymphocytes. Cell 1977, 12:663-673.
    • (1977) Cell , vol.12 , pp. 663-673
    • Williams, A.1    Galfre, G.2    Milstein, C.3
  • 5
  • 6
    • 7644220935 scopus 로고    scopus 로고
    • Laboratory measurement of growth hormone
    • Popii V., Baumann G. Laboratory measurement of growth hormone. Clin. Chim. Acta 2004, 350:1-16.
    • (2004) Clin. Chim. Acta , vol.350 , pp. 1-16
    • Popii, V.1    Baumann, G.2
  • 7
    • 77954868973 scopus 로고    scopus 로고
    • Preparation of monoclonal antibody for melamine and development of an indirect competitive ELISA for melamine detection in raw milk, milk powder, and animal feeds
    • Yin W., Liu J., Zhang T., Li W., Liu W., Meng M., He F., Wan Y., Feng C., Wang S., Lu X., Xi R. Preparation of monoclonal antibody for melamine and development of an indirect competitive ELISA for melamine detection in raw milk, milk powder, and animal feeds. J. Agric. Food Chem. 2010, 58:8152-8157.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 8152-8157
    • Yin, W.1    Liu, J.2    Zhang, T.3    Li, W.4    Liu, W.5    Meng, M.6    He, F.7    Wan, Y.8    Feng, C.9    Wang, S.10    Lu, X.11    Xi, R.12
  • 8
    • 80053387466 scopus 로고    scopus 로고
    • Generation and characterization of antibodies specific for caspase-cleaved neo-epitopes: a novel approach
    • Ai X., Butts B., Vora K., Li W., Tache-Talmadge C., Fridman A., Mehmet H. Generation and characterization of antibodies specific for caspase-cleaved neo-epitopes: a novel approach. Cell Death Dis. 2011, 2.
    • (2011) Cell Death Dis. , vol.2
    • Ai, X.1    Butts, B.2    Vora, K.3    Li, W.4    Tache-Talmadge, C.5    Fridman, A.6    Mehmet, H.7
  • 9
    • 68649127138 scopus 로고    scopus 로고
    • Gold nanorod based selective identification of Escherichia coli bacteria using two-photon Rayleigh scattering spectroscopy
    • Singh A., Senapati D., Wang S., Griffin J., Neely A., Candice P., Naylor K., Varisli B., Kalluri J., Ray P. Gold nanorod based selective identification of Escherichia coli bacteria using two-photon Rayleigh scattering spectroscopy. ACS Nano 2009, 3:1906-1912.
    • (2009) ACS Nano , vol.3 , pp. 1906-1912
    • Singh, A.1    Senapati, D.2    Wang, S.3    Griffin, J.4    Neely, A.5    Candice, P.6    Naylor, K.7    Varisli, B.8    Kalluri, J.9    Ray, P.10
  • 10
    • 0035238791 scopus 로고    scopus 로고
    • Estrogen receptor antibodies: specificity and utility in detection, localization and analyses of estrogen receptor alpha and beta
    • Pavao M., Traish A. Estrogen receptor antibodies: specificity and utility in detection, localization and analyses of estrogen receptor alpha and beta. Steroids 2001, 66:1-16.
    • (2001) Steroids , vol.66 , pp. 1-16
    • Pavao, M.1    Traish, A.2
  • 11
    • 0001654969 scopus 로고    scopus 로고
    • Antigen/antibody immunocomplex from CdTe nanoparticle bioconjugates
    • Wang S., Mamedova N., Kotov N.A., Chen W., Studer J. Antigen/antibody immunocomplex from CdTe nanoparticle bioconjugates. Nano Lett. 2002, 2:817-822.
    • (2002) Nano Lett. , vol.2 , pp. 817-822
    • Wang, S.1    Mamedova, N.2    Kotov, N.A.3    Chen, W.4    Studer, J.5
  • 12
    • 78651375475 scopus 로고    scopus 로고
    • Detection of respiratory syncytial virus using nanoparticle amplified immuno-polymerase chain reaction
    • Perez J., Vargis E., Russ P., Haselton F., Wright D. Detection of respiratory syncytial virus using nanoparticle amplified immuno-polymerase chain reaction. Anal. Biochem. 2011, 410:141-148.
    • (2011) Anal. Biochem. , vol.410 , pp. 141-148
    • Perez, J.1    Vargis, E.2    Russ, P.3    Haselton, F.4    Wright, D.5
  • 13
    • 34548407734 scopus 로고    scopus 로고
    • Rapid detection of Listeria monocytogenes by nanoparticle-based immunomagnetic separation and real-time PCR
    • Yang H., Qu L., Wimbrow A., Jiang X., Sun Y. Rapid detection of Listeria monocytogenes by nanoparticle-based immunomagnetic separation and real-time PCR. Int. J. Food Microbiol. 2007, 118:132-138.
    • (2007) Int. J. Food Microbiol. , vol.118 , pp. 132-138
    • Yang, H.1    Qu, L.2    Wimbrow, A.3    Jiang, X.4    Sun, Y.5
  • 15
    • 70449134139 scopus 로고    scopus 로고
    • Integrated multifunctional nanosystems for medical diagnosis and treatment
    • Shi D. Integrated multifunctional nanosystems for medical diagnosis and treatment. Adv. Funct. Mater. 2009, 19:3356-3373.
    • (2009) Adv. Funct. Mater. , vol.19 , pp. 3356-3373
    • Shi, D.1
  • 17
    • 11044222650 scopus 로고    scopus 로고
    • Synthesis and surface engineering of iron oxide nanoparticles for biomedical applications
    • Gupta A.K., Gupta M. Synthesis and surface engineering of iron oxide nanoparticles for biomedical applications. Biomaterials 2005, 26:3995-4021.
    • (2005) Biomaterials , vol.26 , pp. 3995-4021
    • Gupta, A.K.1    Gupta, M.2
  • 19
    • 19944401541 scopus 로고    scopus 로고
    • Surface plasmon resonance scattering and absorption of anti-EGFR antibody conjugated gold nanoparticles in cancer diagnostics: applications in oral cancer
    • El-Sayed I.H., Huang X., El-Sayed M.A. Surface plasmon resonance scattering and absorption of anti-EGFR antibody conjugated gold nanoparticles in cancer diagnostics: applications in oral cancer. Nano Lett. 2005, 5:829-834.
    • (2005) Nano Lett. , vol.5 , pp. 829-834
    • El-Sayed, I.H.1    Huang, X.2    El-Sayed, M.A.3
  • 20
    • 39149086684 scopus 로고    scopus 로고
    • Nanoparticles synthesis using supercritical fluid technology - towards biomedical applications
    • Byrappa K., Ohara S., Adschiri T. Nanoparticles synthesis using supercritical fluid technology - towards biomedical applications. Adv. Drug Deliv. Rev. 2008, 60:299-327.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 299-327
    • Byrappa, K.1    Ohara, S.2    Adschiri, T.3
  • 21
    • 33846797814 scopus 로고    scopus 로고
    • Recent advances in nanoparticle synthesis with reversed micelles
    • Eastoe J., Hollamby M., Hudson L. Recent advances in nanoparticle synthesis with reversed micelles. Adv. Colloid Interface Sci. 2006, 128:5-15.
    • (2006) Adv. Colloid Interface Sci. , vol.128 , pp. 5-15
    • Eastoe, J.1    Hollamby, M.2    Hudson, L.3
  • 22
    • 34447101222 scopus 로고    scopus 로고
    • Toward greener nanosynthesis
    • Dahl J., Maddux B., Hutchison J. Toward greener nanosynthesis. Chem. Rev. 2007, 107:2228-2269.
    • (2007) Chem. Rev. , vol.107 , pp. 2228-2269
    • Dahl, J.1    Maddux, B.2    Hutchison, J.3
  • 23
    • 4644287020 scopus 로고    scopus 로고
    • Recent advances in the liquid-phase syntheses of inorganic nanoparticles
    • Cushing B., Kolesnichenko V., O'Connor C. Recent advances in the liquid-phase syntheses of inorganic nanoparticles. Chem. Rev. 2004, 104:3893-3946.
    • (2004) Chem. Rev. , vol.104 , pp. 3893-3946
    • Cushing, B.1    Kolesnichenko, V.2    O'Connor, C.3
  • 24
    • 77950207533 scopus 로고    scopus 로고
    • Surface modification, functionalization and bioconjugation of colloidal inorganic nanoparticles
    • Sperling R.A., Parak W.J. Surface modification, functionalization and bioconjugation of colloidal inorganic nanoparticles. Phil. Trans. R. Soc. A 2010, 368:1333-1383.
    • (2010) Phil. Trans. R. Soc. A , vol.368 , pp. 1333-1383
    • Sperling, R.A.1    Parak, W.J.2
  • 25
    • 34247179477 scopus 로고    scopus 로고
    • Magnetic nanoparticles: synthesis, protection, functionalization, and application
    • Lu A.H., Salabas E.L., Schuth F. Magnetic nanoparticles: synthesis, protection, functionalization, and application. Angew. Chem. Int. Ed. 2007, 46:1222-1244.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 1222-1244
    • Lu, A.H.1    Salabas, E.L.2    Schuth, F.3
  • 26
    • 0037459989 scopus 로고    scopus 로고
    • Chemical synthesis of magnetic nanoparticles
    • Hyeon T. Chemical synthesis of magnetic nanoparticles. Chem. Commun. 2003, 8:927-934.
    • (2003) Chem. Commun. , vol.8 , pp. 927-934
    • Hyeon, T.1
  • 29
    • 80051538645 scopus 로고    scopus 로고
    • Preparation of peptide-functionalized gold nanoparticles using one pot EDC/Sulfo-NHS coupling
    • Bartczak D., Kanaras A. Preparation of peptide-functionalized gold nanoparticles using one pot EDC/Sulfo-NHS coupling. Langmuir 2011, 27:10119-10123.
    • (2011) Langmuir , vol.27 , pp. 10119-10123
    • Bartczak, D.1    Kanaras, A.2
  • 31
    • 2942744602 scopus 로고    scopus 로고
    • One molecule per particle method for functionalising nanoparticles
    • Wilson R., Chen Y., Aveyard J. One molecule per particle method for functionalising nanoparticles. Chem. Commun. (Camb.) 2004, 1156-1157.
    • (2004) Chem. Commun. (Camb.) , pp. 1156-1157
    • Wilson, R.1    Chen, Y.2    Aveyard, J.3
  • 32
    • 33645776706 scopus 로고    scopus 로고
    • A generic approach to monofunctionalized protein-like gold nanoparticles based on immobilized metal ion affinity chromatography
    • Levy R., Wang Z.X., Duchesne L., Doty R.C., Cooper A.I., Brust M., Fernig D.G. A generic approach to monofunctionalized protein-like gold nanoparticles based on immobilized metal ion affinity chromatography. ChemBioChem 2006, 7:592-594.
    • (2006) ChemBioChem , vol.7 , pp. 592-594
    • Levy, R.1    Wang, Z.X.2    Duchesne, L.3    Doty, R.C.4    Cooper, A.I.5    Brust, M.6    Fernig, D.G.7
  • 34
    • 0030009986 scopus 로고    scopus 로고
    • Monolayers in three dimensions: synthesis and electrochemistry of -functionalized alkanethiolate-stabilized gold cluster compounds
    • Hostetler M.J., Green S.J., Stokes J.J., Murray R.W. Monolayers in three dimensions: synthesis and electrochemistry of -functionalized alkanethiolate-stabilized gold cluster compounds. J. Am. Chem. Soc. 1996, 118:4212-4213.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 4212-4213
    • Hostetler, M.J.1    Green, S.J.2    Stokes, J.J.3    Murray, R.W.4
  • 35
    • 20444376973 scopus 로고    scopus 로고
    • A "nanonecklace" synthesized from monofunctionalized gold nanoparticles
    • Dai Q., Worden J.G., Trullinger J., Huo Q. A "nanonecklace" synthesized from monofunctionalized gold nanoparticles. J. Am. Chem. Soc. 2005, 127:8008-8009.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8008-8009
    • Dai, Q.1    Worden, J.G.2    Trullinger, J.3    Huo, Q.4
  • 36
    • 18444395282 scopus 로고    scopus 로고
    • Preparative manipulation of gold nanoparticles by reversible binding to a polymeric solid support
    • Abed O., Vaskevich A., Arad-Yellin R., Shanzer A., Rubinstein I. Preparative manipulation of gold nanoparticles by reversible binding to a polymeric solid support. Chem. Eur. J. 2005, 11:2836-2841.
    • (2005) Chem. Eur. J. , vol.11 , pp. 2836-2841
    • Abed, O.1    Vaskevich, A.2    Arad-Yellin, R.3    Shanzer, A.4    Rubinstein, I.5
  • 37
    • 4544371165 scopus 로고    scopus 로고
    • Monofunctional group-modified gold nanoparticles from solid phase synthesis approach: solid support and experimental condition effect
    • Worden J.G., Dai Q., Shaffer A.W., Huo Q. Monofunctional group-modified gold nanoparticles from solid phase synthesis approach: solid support and experimental condition effect. Chem. Matter. 2004, 16:3746-3755.
    • (2004) Chem. Matter. , vol.16 , pp. 3746-3755
    • Worden, J.G.1    Dai, Q.2    Shaffer, A.W.3    Huo, Q.4
  • 38
    • 33748579253 scopus 로고    scopus 로고
    • Monofunctional gold nanoparticles prepared via a noncovalent-interaction-based solid-phase modification approach
    • Liu X., Worden J.G., Dai Q., Zou J., Wang J., Huo Q. Monofunctional gold nanoparticles prepared via a noncovalent-interaction-based solid-phase modification approach. Small 2006, 2:1126-1129.
    • (2006) Small , vol.2 , pp. 1126-1129
    • Liu, X.1    Worden, J.G.2    Dai, Q.3    Zou, J.4    Wang, J.5    Huo, Q.6
  • 39
    • 1642418270 scopus 로고    scopus 로고
    • Controlled functionalization of gold nanoparticles through a solid phase synthesis approach
    • Worden J.G., Shaffer A.W., Huo Q. Controlled functionalization of gold nanoparticles through a solid phase synthesis approach. Chem. Commun. 2004, 2004:518-519.
    • (2004) Chem. Commun. , vol.2004 , pp. 518-519
    • Worden, J.G.1    Shaffer, A.W.2    Huo, Q.3
  • 40
    • 4644265229 scopus 로고    scopus 로고
    • Comparison study of the solution phase versus solid phase place exchange reactions in the controlled functionalization of gold nanoparticles
    • Shaffer A.W., Worden J.G., Huo G. Comparison study of the solution phase versus solid phase place exchange reactions in the controlled functionalization of gold nanoparticles. Langmuir 2004, 20:8343-8351.
    • (2004) Langmuir , vol.20 , pp. 8343-8351
    • Shaffer, A.W.1    Worden, J.G.2    Huo, G.3
  • 41
    • 1942456849 scopus 로고    scopus 로고
    • Synthesis of monofunctionalized gold nanoparticles by Fmoc solid-phase reactions
    • Sung K.M., Mosley D.W., Peelle B.R., Zhang S.G., Jacobson J.M. Synthesis of monofunctionalized gold nanoparticles by Fmoc solid-phase reactions. J. Am. Chem. Soc. 2004, 126:5064-5065.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5064-5065
    • Sung, K.M.1    Mosley, D.W.2    Peelle, B.R.3    Zhang, S.G.4    Jacobson, J.M.5
  • 43
    • 40949138273 scopus 로고    scopus 로고
    • Stoichiometric functionalization of gold nanoparticles in solution through a free radical polymerization approach
    • Krüger C., Agarwal S., Greiner A. Stoichiometric functionalization of gold nanoparticles in solution through a free radical polymerization approach. J. Am. Chem. Soc. 2008, 130:2710-2711.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2710-2711
    • Krüger, C.1    Agarwal, S.2    Greiner, A.3
  • 45
  • 46
    • 33646494891 scopus 로고    scopus 로고
    • Electrophoretic separation of nanoparticles with a discrete number of functional groups
    • Sperling R.A., Pellegrino T., Li J.K., Chang W.H., Parak W.J. Electrophoretic separation of nanoparticles with a discrete number of functional groups. Adv. Funct. Mater. 2006, 16:943-948.
    • (2006) Adv. Funct. Mater. , vol.16 , pp. 943-948
    • Sperling, R.A.1    Pellegrino, T.2    Li, J.K.3    Chang, W.H.4    Parak, W.J.5
  • 54
    • 77649110057 scopus 로고    scopus 로고
    • A quantitative assessment of nanoparticle-ligand distributions: implications for targeted drug and imaging delivery in dendrimer conjugates
    • Mullen D.G., Fang M., Desai A., Baker J.R., Orr B.G., Banaszak Holl M.M. A quantitative assessment of nanoparticle-ligand distributions: implications for targeted drug and imaging delivery in dendrimer conjugates. ACS Nano 2010, 4:657-670.
    • (2010) ACS Nano , vol.4 , pp. 657-670
    • Mullen, D.G.1    Fang, M.2    Desai, A.3    Baker, J.R.4    Orr, B.G.5    Banaszak Holl, M.M.6
  • 57
    • 80053255666 scopus 로고    scopus 로고
    • Precisely designed gold nanoparticles by surface polymerization - artificial molecules as building blocks for novel materials
    • Bokern S., Gries K., Agarwal S., Görtz H.-H., Warzelhan V., Greiner A. Precisely designed gold nanoparticles by surface polymerization - artificial molecules as building blocks for novel materials. Adv. Funct. Mater. 2011, 21:3753-3759.
    • (2011) Adv. Funct. Mater. , vol.21 , pp. 3753-3759
    • Bokern, S.1    Gries, K.2    Agarwal, S.3    Görtz, H.-H.4    Warzelhan, V.5    Greiner, A.6
  • 59
    • 0033548686 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single biomolecules
    • Weiss S. Fluorescence spectroscopy of single biomolecules. Science 1999, 283:1676-1683.
    • (1999) Science , vol.283 , pp. 1676-1683
    • Weiss, S.1
  • 60
    • 84865781741 scopus 로고    scopus 로고
    • Quantitative characterization of fluorophores in multi-component nanoprobes by single-molecule fluorescence
    • Bumb A., Sarkar S.K., Wu X.S., Brechbiel M.W., Neuman K.C. Quantitative characterization of fluorophores in multi-component nanoprobes by single-molecule fluorescence. Biomed. Opt. Express 2011, 2:2761-2769.
    • (2011) Biomed. Opt. Express , vol.2 , pp. 2761-2769
    • Bumb, A.1    Sarkar, S.K.2    Wu, X.S.3    Brechbiel, M.W.4    Neuman, K.C.5
  • 61
    • 84857510454 scopus 로고    scopus 로고
    • Signal amplification using functional nanomaterials for biosensing
    • Lei J., Ju H. Signal amplification using functional nanomaterials for biosensing. Chem. Soc. Rev. 2012, 41:2122-2134.
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 2122-2134
    • Lei, J.1    Ju, H.2
  • 62
    • 79451473902 scopus 로고    scopus 로고
    • Nanoparticles for the development of improved (bio)sensing systems
    • Pérez-López B., Merkoçi A. Nanoparticles for the development of improved (bio)sensing systems. Anal. Bioanal. Chem. 2011, 399:1577-1590.
    • (2011) Anal. Bioanal. Chem. , vol.399 , pp. 1577-1590
    • Pérez-López, B.1    Merkoçi, A.2
  • 63
    • 1542315410 scopus 로고    scopus 로고
    • Labeling of fusion proteins of O-6-alkylguanine-DNA alkyltransferase with small molecules in vivo and in vitro
    • Keppler A., Kindermann M., Gendreizig S., Pick H., Vogel H., Johnsson K. Labeling of fusion proteins of O-6-alkylguanine-DNA alkyltransferase with small molecules in vivo and in vitro. Methods 2004, 32:437-444.
    • (2004) Methods , vol.32 , pp. 437-444
    • Keppler, A.1    Kindermann, M.2    Gendreizig, S.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 64
    • 84861167694 scopus 로고    scopus 로고
    • Protein oriented ligation on nanoparticles exploiting O6-Alkylguanine-DNA Transferase (SNAP) genetically encoded fusion
    • Colombo M., Mazzucchelli S., Montenegro J.M., Galbiati E., Corsi F., Parak W.J., Prosperi D. Protein oriented ligation on nanoparticles exploiting O6-Alkylguanine-DNA Transferase (SNAP) genetically encoded fusion. Small 2012, 8:1492-1497.
    • (2012) Small , vol.8 , pp. 1492-1497
    • Colombo, M.1    Mazzucchelli, S.2    Montenegro, J.M.3    Galbiati, E.4    Corsi, F.5    Parak, W.J.6    Prosperi, D.7
  • 65
    • 0022519337 scopus 로고
    • 3-Dimensional structure of an antigen-antibody complex at 2.8-A resolution
    • Amit A., Mariuzza R., Phillips S., Poljak R. 3-Dimensional structure of an antigen-antibody complex at 2.8-A resolution. Science 1986, 233:747-753.
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.1    Mariuzza, R.2    Phillips, S.3    Poljak, R.4
  • 66
    • 0035873513 scopus 로고    scopus 로고
    • Inhibition of antigen-induced mediator release from IgE-sensitized cells by a monoclonal anti-Fc epsilon RI alpha-chain receptor antibody: implications for the involvement of the membrane-proximal alpha-chain region in Fc epsilon RI-mediated cell activation
    • Nechansky A., Robertson M., Albrecht B., Apgar J., Kricek F. Inhibition of antigen-induced mediator release from IgE-sensitized cells by a monoclonal anti-Fc epsilon RI alpha-chain receptor antibody: implications for the involvement of the membrane-proximal alpha-chain region in Fc epsilon RI-mediated cell activation. J. Immunol. 2001, 166:5979-5990.
    • (2001) J. Immunol. , vol.166 , pp. 5979-5990
    • Nechansky, A.1    Robertson, M.2    Albrecht, B.3    Apgar, J.4    Kricek, F.5
  • 67
    • 82455210227 scopus 로고    scopus 로고
    • Vitellogenin mediates phagocytosis through interaction with FcgammaR
    • Liu M., Pan J., Ji H., Zhao B., Zhang S. Vitellogenin mediates phagocytosis through interaction with FcgammaR. Mol. Immunol. 2011, 49:211-218.
    • (2011) Mol. Immunol. , vol.49 , pp. 211-218
    • Liu, M.1    Pan, J.2    Ji, H.3    Zhao, B.4    Zhang, S.5
  • 68
    • 34249310057 scopus 로고    scopus 로고
    • Platelet-bound lipopolysaccharide enhances Fc receptor-mediated phagocytosis of IgG-opsonized platelets
    • Semple J., Aslam R., Kim M., Speck E., Freedman J. Platelet-bound lipopolysaccharide enhances Fc receptor-mediated phagocytosis of IgG-opsonized platelets. Blood 2007, 109:4803-4805.
    • (2007) Blood , vol.109 , pp. 4803-4805
    • Semple, J.1    Aslam, R.2    Kim, M.3    Speck, E.4    Freedman, J.5
  • 69
    • 0344420075 scopus 로고    scopus 로고
    • Enhanced phagocytosis of Candida species mediated by opsonization with a recombinant human antibody single-chain variable fragment
    • Wellington M., Bliss J., Haidaris C. Enhanced phagocytosis of Candida species mediated by opsonization with a recombinant human antibody single-chain variable fragment. Infect. Immun. 2003, 71:7228-7231.
    • (2003) Infect. Immun. , vol.71 , pp. 7228-7231
    • Wellington, M.1    Bliss, J.2    Haidaris, C.3
  • 71
    • 33845385609 scopus 로고    scopus 로고
    • Surfactant protein A binds to IgG and enhances phagocytosis of IgG-opsonized erythrocytes
    • Lin P., Wright J. Surfactant protein A binds to IgG and enhances phagocytosis of IgG-opsonized erythrocytes. Am. J. Physiol. Lung Cell. Mol. Physiol. 2006, 291:L1199-L1206.
    • (2006) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.291
    • Lin, P.1    Wright, J.2
  • 72
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan E.A. Anatomy of the antibody molecule. Mol. Immunol. 1994, 31:169-217.
    • (1994) Mol. Immunol. , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 73
    • 34547579309 scopus 로고    scopus 로고
    • Characterization of the functional binding properties of antibody conjugated quantum dots
    • Pathak S., Davidson M.C., Silva G.A. Characterization of the functional binding properties of antibody conjugated quantum dots. Nano Lett. 2007, 7:1839-1845.
    • (2007) Nano Lett. , vol.7 , pp. 1839-1845
    • Pathak, S.1    Davidson, M.C.2    Silva, G.A.3
  • 74
    • 84859025228 scopus 로고    scopus 로고
    • Role of antibodies in cancer targeting
    • Attarwala H. Role of antibodies in cancer targeting. J. Nat. Sci. Biol. Med. 2010, 1:53-56.
    • (2010) J. Nat. Sci. Biol. Med. , vol.1 , pp. 53-56
    • Attarwala, H.1
  • 75
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P., Hudson P. Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 2005, 23:1126-1136.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.2
  • 76
    • 84878378182 scopus 로고    scopus 로고
    • Bio-Rad Protein Assay, in, Bio-Rad.
    • Bio-Rad Protein Assay, in, Bio-Rad.
  • 77
    • 84908582232 scopus 로고    scopus 로고
    • Engineering of ultra-small diagnostic nanoprobes through oriented conjugation of single-domain antibodies and quantum dots
    • Sukhanova A., Even-Desrumeaux K., Chames P., Baty D., Artemyev M., Oleinikov V., Nabiev I. Engineering of ultra-small diagnostic nanoprobes through oriented conjugation of single-domain antibodies and quantum dots. Nat. Protoc. Exch. 2012, 10.1038/protex.2012.042.
    • (2012) Nat. Protoc. Exch.
    • Sukhanova, A.1    Even-Desrumeaux, K.2    Chames, P.3    Baty, D.4    Artemyev, M.5    Oleinikov, V.6    Nabiev, I.7
  • 78
    • 0033057177 scopus 로고    scopus 로고
    • The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues
    • Hammarstrom S. The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues. Semin. Cancer Biol. 1999, 9:67-81.
    • (1999) Semin. Cancer Biol. , vol.9 , pp. 67-81
    • Hammarstrom, S.1
  • 79
    • 0023481357 scopus 로고
    • Transport of molecules across tumor vasculature
    • Jain R.K. Transport of molecules across tumor vasculature. Cancer Metastasis Rev. 1987, 6:559-593.
    • (1987) Cancer Metastasis Rev. , vol.6 , pp. 559-593
    • Jain, R.K.1
  • 80
    • 69949120445 scopus 로고    scopus 로고
    • Interfacial assembly of proteins and peptides: recent examples studied by neutron reflection
    • Zhao X., Pan F., Lu J. Interfacial assembly of proteins and peptides: recent examples studied by neutron reflection. J. R. Soc. Interface 2009, 6:S659-S670.
    • (2009) J. R. Soc. Interface , vol.6
    • Zhao, X.1    Pan, F.2    Lu, J.3
  • 81
    • 79959212598 scopus 로고    scopus 로고
    • Interfacial immobilization of monoclonal antibody and detection of human prostate-specific antigen
    • Zhao X., Pan F., Cowsill B., Lu J. Interfacial immobilization of monoclonal antibody and detection of human prostate-specific antigen. Langmuir 2011, 27:7654-7662.
    • (2011) Langmuir , vol.27 , pp. 7654-7662
    • Zhao, X.1    Pan, F.2    Cowsill, B.3    Lu, J.4
  • 83
    • 69949172399 scopus 로고    scopus 로고
    • Colorimetric multiplexed immunoassay for sequential detection of tumor markers
    • Wang J., Cao Y., Xu Y., Li G. Colorimetric multiplexed immunoassay for sequential detection of tumor markers. Biosens. Bioelectron. 2009, 25:532-536.
    • (2009) Biosens. Bioelectron. , vol.25 , pp. 532-536
    • Wang, J.1    Cao, Y.2    Xu, Y.3    Li, G.4
  • 85
    • 66149103634 scopus 로고    scopus 로고
    • Nanoparticle-target interactions parallel antibody-protein interactions
    • Koh I., Hong R., Weissleder R., Josephson L. Nanoparticle-target interactions parallel antibody-protein interactions. Anal. Chem. 2009, 81:3618-3622.
    • (2009) Anal. Chem. , vol.81 , pp. 3618-3622
    • Koh, I.1    Hong, R.2    Weissleder, R.3    Josephson, L.4
  • 86
    • 69849105542 scopus 로고    scopus 로고
    • Role of nanoparticle valency in the nondestructive magnetic-relaxation-mediated detection and magnetic isolation of cells in complex media
    • Kaittanis C., Santra S., Perez J.M. Role of nanoparticle valency in the nondestructive magnetic-relaxation-mediated detection and magnetic isolation of cells in complex media. J. Am. Chem. Soc. 2009, 131:12780-12791.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12780-12791
    • Kaittanis, C.1    Santra, S.2    Perez, J.M.3
  • 87
    • 77953152498 scopus 로고    scopus 로고
    • Rapid detection and differentiation of antibodies to HIV-1 and HIV-2 using multivalent antigens and magnetic immunochromatography testing
    • Granade T.C., Workman S., Wells S.K., Holder A.N., Owen S.M., Pau C.-P. Rapid detection and differentiation of antibodies to HIV-1 and HIV-2 using multivalent antigens and magnetic immunochromatography testing. Clin. Vaccine Immunol. 2010, 17:1034-1039.
    • (2010) Clin. Vaccine Immunol. , vol.17 , pp. 1034-1039
    • Granade, T.C.1    Workman, S.2    Wells, S.K.3    Holder, A.N.4    Owen, S.M.5    Pau, C.-P.6
  • 89
    • 77956707999 scopus 로고    scopus 로고
    • Two-step in vivo tumor targeting by biotin-conjugated antibodies and superparamagnetic nanoparticles assessed by magnetic resonance imaging at 1.5 T
    • Baio G., Fabbi M., Salvi S., de Totero D., Truini M., Ferrini S., Neumaier C.E. Two-step in vivo tumor targeting by biotin-conjugated antibodies and superparamagnetic nanoparticles assessed by magnetic resonance imaging at 1.5 T. Mol. Imaging Biol. 2010, 12:305-315.
    • (2010) Mol. Imaging Biol. , vol.12 , pp. 305-315
    • Baio, G.1    Fabbi, M.2    Salvi, S.3    de Totero, D.4    Truini, M.5    Ferrini, S.6    Neumaier, C.E.7
  • 91
    • 34548591376 scopus 로고    scopus 로고
    • Self-directed and self-oriented immobilization of antibody by protein G-DNA conjugate
    • Jung Y., Lee J., Jung H., Chung B. Self-directed and self-oriented immobilization of antibody by protein G-DNA conjugate. Anal. Biochem. 2007, 79:6534-6541.
    • (2007) Anal. Biochem. , vol.79 , pp. 6534-6541
    • Jung, Y.1    Lee, J.2    Jung, H.3    Chung, B.4
  • 92
    • 39049135903 scopus 로고    scopus 로고
    • Directional conjugation of antibodies to nanoparticles for synthesis of multiplexed optical contrast agents with both delivery and targeting moieties
    • Kumar S., Aaron J., Sokolov K. Directional conjugation of antibodies to nanoparticles for synthesis of multiplexed optical contrast agents with both delivery and targeting moieties. Nat. Protoc. 2008, 3:314-320.
    • (2008) Nat. Protoc. , vol.3 , pp. 314-320
    • Kumar, S.1    Aaron, J.2    Sokolov, K.3
  • 93
    • 44049097500 scopus 로고    scopus 로고
    • Recent advances in immobilization methods of antibodies on solid supports
    • Jung Y., Jeong J., Chung B. Recent advances in immobilization methods of antibodies on solid supports. Analyst 2008, 133:697-701.
    • (2008) Analyst , vol.133 , pp. 697-701
    • Jung, Y.1    Jeong, J.2    Chung, B.3
  • 94
    • 2042468821 scopus 로고    scopus 로고
    • Advances in recombinant antibody microarrays
    • Pavlickova P., Schneider E., Hug H. Advances in recombinant antibody microarrays. Clin. Chim. Acta 2004, 343:17-35.
    • (2004) Clin. Chim. Acta , vol.343 , pp. 17-35
    • Pavlickova, P.1    Schneider, E.2    Hug, H.3
  • 96
  • 98
    • 25444523999 scopus 로고    scopus 로고
    • Studies on fluorescence resonance energy transfer between dyes and water-soluble quantum dots
    • Wang X.-Y., Ma Q., Li Y.-B., Li B., Su X.-G., Jin Q.-H. Studies on fluorescence resonance energy transfer between dyes and water-soluble quantum dots. Luminescence 2005, 20:251-255.
    • (2005) Luminescence , vol.20 , pp. 251-255
    • Wang, X.-Y.1    Ma, Q.2    Li, Y.-B.3    Li, B.4    Su, X.-G.5    Jin, Q.-H.6
  • 99
    • 13844308235 scopus 로고    scopus 로고
    • A continuous displacement immunoassay for human heart-type fatty acid-binding protein in plasma
    • van der Voort D., Pelsers M., Korf J., Hermens W., Glatz J. A continuous displacement immunoassay for human heart-type fatty acid-binding protein in plasma. J. Immunol. Methods 2004, 295:1-8.
    • (2004) J. Immunol. Methods , vol.295 , pp. 1-8
    • van der Voort, D.1    Pelsers, M.2    Korf, J.3    Hermens, W.4    Glatz, J.5
  • 100
    • 47149115539 scopus 로고    scopus 로고
    • Imaging breast cancer cells and tissues using peptide-labeled fluorescent silica nanoparticles
    • Wu P., He X., Wang K., Tan W., Ma D., Yang W., He C. Imaging breast cancer cells and tissues using peptide-labeled fluorescent silica nanoparticles. J. Nanosci. Nanotechnol. 2008, 8:2483-2487.
    • (2008) J. Nanosci. Nanotechnol. , vol.8 , pp. 2483-2487
    • Wu, P.1    He, X.2    Wang, K.3    Tan, W.4    Ma, D.5    Yang, W.6    He, C.7
  • 101
    • 79959790851 scopus 로고    scopus 로고
    • Taking advantage of unspecific interactions to produce highly active magnetic nanoparticle-antibody conjugates
    • Puertas S., Batalla P., Moros M., Polo E., del Pino P., Guisan J.M., Grazu V., de la Fuente J.M. Taking advantage of unspecific interactions to produce highly active magnetic nanoparticle-antibody conjugates. ACS Nano 2011, 5:4521-4528.
    • (2011) ACS Nano , vol.5 , pp. 4521-4528
    • Puertas, S.1    Batalla, P.2    Moros, M.3    Polo, E.4    del Pino, P.5    Guisan, J.M.6    Grazu, V.7    de la Fuente, J.M.8
  • 102
    • 44349128319 scopus 로고    scopus 로고
    • Synthesis of functionalized Au nanoparticles for protein detection
    • Jana N.R., Ying J.Y. Synthesis of functionalized Au nanoparticles for protein detection. Adv. Mater. 2008, 20:430-434.
    • (2008) Adv. Mater. , vol.20 , pp. 430-434
    • Jana, N.R.1    Ying, J.Y.2
  • 104
    • 54849429975 scopus 로고    scopus 로고
    • One-step preparation of antibody and oligonucleotide dual-labeled gold nanoparticle bio-probes and their properties
    • Kong X., Qiao F., Qi H., Li F. One-step preparation of antibody and oligonucleotide dual-labeled gold nanoparticle bio-probes and their properties. Biotechnol. Lett. 2008, 30:2071-2077.
    • (2008) Biotechnol. Lett. , vol.30 , pp. 2071-2077
    • Kong, X.1    Qiao, F.2    Qi, H.3    Li, F.4
  • 105
    • 33645933271 scopus 로고    scopus 로고
    • A real-time PCR-based method for determining the surface coverage of thiol-capped oligonucleotides bound onto gold nanoparticles
    • Kim E., Stanton J., Vega R., Kunstman K., Mirkin C., Wolinsky S. A real-time PCR-based method for determining the surface coverage of thiol-capped oligonucleotides bound onto gold nanoparticles. Nucleic Acids Res. 2006, 34.
    • (2006) Nucleic Acids Res. , vol.34
    • Kim, E.1    Stanton, J.2    Vega, R.3    Kunstman, K.4    Mirkin, C.5    Wolinsky, S.6
  • 106
    • 77957363662 scopus 로고    scopus 로고
    • Ultrasensitive electrochemical detection of biotin using electrically addressable site-oriented antibody immobilization approach via aminophenyl boronic acid
    • Ho J., Hsu W., Liao W., Chiu J., Chen M., Chang H., Li C. Ultrasensitive electrochemical detection of biotin using electrically addressable site-oriented antibody immobilization approach via aminophenyl boronic acid. Biosens. Bioelectron. 2010, 26:1021-1027.
    • (2010) Biosens. Bioelectron. , vol.26 , pp. 1021-1027
    • Ho, J.1    Hsu, W.2    Liao, W.3    Chiu, J.4    Chen, M.5    Chang, H.6    Li, C.7
  • 108
    • 0031148662 scopus 로고    scopus 로고
    • Multistep denaturation and hierarchy of disulfide bond cleavage of a monoclonal antibody
    • Brody T. Multistep denaturation and hierarchy of disulfide bond cleavage of a monoclonal antibody. Anal. Biochem. 1997, 247:247-256.
    • (1997) Anal. Biochem. , vol.247 , pp. 247-256
    • Brody, T.1
  • 109
    • 0029954457 scopus 로고    scopus 로고
    • Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor (TGF) activity: the relationship between intramolecular disulfide bridges and TGF activity
    • Yamaoka K., Ingendoh A., Tsubuki S., Nagai Y., Sanai Y. Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor (TGF) activity: the relationship between intramolecular disulfide bridges and TGF activity. J. Biochem. 1996, 119:878-886.
    • (1996) J. Biochem. , vol.119 , pp. 878-886
    • Yamaoka, K.1    Ingendoh, A.2    Tsubuki, S.3    Nagai, Y.4    Sanai, Y.5
  • 110
    • 33646125185 scopus 로고    scopus 로고
    • Oriented immobilisation of engineered single-chain antibodies to develop biosensors for virus detection
    • Torrance L., Ziegler A., Pittman H., Paterson M., Toth R., Eggleston I. Oriented immobilisation of engineered single-chain antibodies to develop biosensors for virus detection. J. Virol. Methods 2006, 134:164-170.
    • (2006) J. Virol. Methods , vol.134 , pp. 164-170
    • Torrance, L.1    Ziegler, A.2    Pittman, H.3    Paterson, M.4    Toth, R.5    Eggleston, I.6
  • 111
    • 0034229423 scopus 로고    scopus 로고
    • Gold-sulfur bonding in 2D and 3D self-assembled monolayers: XPS characterization
    • Bourg M.-C., Badia A., Lennox R.B. Gold-sulfur bonding in 2D and 3D self-assembled monolayers: XPS characterization. J. Phys. Chem. B 2000, 104:6562-6567.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 6562-6567
    • Bourg, M.-C.1    Badia, A.2    Lennox, R.B.3
  • 112
    • 33846960727 scopus 로고
    • Molecular-level control over surface order in self-assembled monolayer films of thiols on gold
    • Bain C.D., Whitesides G.M. Molecular-level control over surface order in self-assembled monolayer films of thiols on gold. Science 1988, 240:62-63.
    • (1988) Science , vol.240 , pp. 62-63
    • Bain, C.D.1    Whitesides, G.M.2
  • 113
    • 0042076872 scopus 로고
    • Self-assembled monolayers and multilayers of conjugated thiols, alpha, omega-dithiols, and thioacetyl-containing adsorbates - Understanding attachments between potential molecular wires and gold surfaces
    • Tour J.M., Jones L., Pearson D.L., Lamba J.J.S., Burgin T.P., Whitesides G.M., Allara D.L., Parikh A.N., Atre S.V. Self-assembled monolayers and multilayers of conjugated thiols, alpha, omega-dithiols, and thioacetyl-containing adsorbates - Understanding attachments between potential molecular wires and gold surfaces. J. Am. Chem. Soc. 1995, 117:9529-9534.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9529-9534
    • Tour, J.M.1    Jones, L.2    Pearson, D.L.3    Lamba, J.J.S.4    Burgin, T.P.5    Whitesides, G.M.6    Allara, D.L.7    Parikh, A.N.8    Atre, S.V.9
  • 114
    • 1942481178 scopus 로고
    • Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold
    • Bain C.D., Troughton E.B., Tao Y.-T., Evall J., Whitesides G.M., Nuzzo R.G. Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold. J. Am. Chem. Soc. 1989, 111:321-335.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 321-335
    • Bain, C.D.1    Troughton, E.B.2    Tao, Y.-T.3    Evall, J.4    Whitesides, G.M.5    Nuzzo, R.G.6
  • 115
    • 77953317927 scopus 로고    scopus 로고
    • Direct observation of adsorption-induced inactivation of antibody fragments surrounded by mixed-PEG layer on a gold surface
    • Yoshimoto K., Nishio M., Sugasawa H., Nagasaki Y. Direct observation of adsorption-induced inactivation of antibody fragments surrounded by mixed-PEG layer on a gold surface. J. Am. Chem. Soc. 2010, 132:7982-7989.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7982-7989
    • Yoshimoto, K.1    Nishio, M.2    Sugasawa, H.3    Nagasaki, Y.4
  • 117
    • 77951275912 scopus 로고    scopus 로고
    • Synthesis of pyridyl disulfide-functionalized nanoparticles for conjugating thiol-containing small molecules, peptides, and proteins
    • van der Vlies A.J., O'Neil C.P., Hasegawa U., Hammond N., Hubbell J.A. Synthesis of pyridyl disulfide-functionalized nanoparticles for conjugating thiol-containing small molecules, peptides, and proteins. Bioconjug. Chem. 2010, 21:653-662.
    • (2010) Bioconjug. Chem. , vol.21 , pp. 653-662
    • van der Vlies, A.J.1    O'Neil, C.P.2    Hasegawa, U.3    Hammond, N.4    Hubbell, J.A.5
  • 118
    • 33646012980 scopus 로고    scopus 로고
    • Preparation of very reactive thiol-protected gold nanoparticles: revisiting the Brust-Schiffrin method
    • Araki K., Mizuguchi E., Tanaka H., Takuji O. Preparation of very reactive thiol-protected gold nanoparticles: revisiting the Brust-Schiffrin method. J. Nanosci. Nanotechnol. 2006, 6:708-712.
    • (2006) J. Nanosci. Nanotechnol. , vol.6 , pp. 708-712
    • Araki, K.1    Mizuguchi, E.2    Tanaka, H.3    Takuji, O.4
  • 119
    • 79953162642 scopus 로고    scopus 로고
    • Direct observation of chemokine receptors 5 on T-lymphocyte cell surfaces using fluorescent metal nanoprobes 2: approximation of CCR5 populations
    • Zhang J., Fu Y., Li G., Zhao R., Lakowicz J. Direct observation of chemokine receptors 5 on T-lymphocyte cell surfaces using fluorescent metal nanoprobes 2: approximation of CCR5 populations. Biochem. Biophys. Res. Commun. 2011, 407:63-67.
    • (2011) Biochem. Biophys. Res. Commun. , vol.407 , pp. 63-67
    • Zhang, J.1    Fu, Y.2    Li, G.3    Zhao, R.4    Lakowicz, J.5
  • 120
    • 79955562207 scopus 로고    scopus 로고
    • Targeted photodynamic therapy of breast cancer cells using antibody-phthalocyanine-gold nanoparticle conjugates
    • Stuchinskaya T., Moreno M., Cook M., Edwards D., Russell D. Targeted photodynamic therapy of breast cancer cells using antibody-phthalocyanine-gold nanoparticle conjugates. Photochem. Photobiol. Sci. 2011, 10:822-831.
    • (2011) Photochem. Photobiol. Sci. , vol.10 , pp. 822-831
    • Stuchinskaya, T.1    Moreno, M.2    Cook, M.3    Edwards, D.4    Russell, D.5
  • 121
    • 67349211070 scopus 로고    scopus 로고
    • Selective immobilization of proteins on gold dot arrays and characterization using chemical force microscopy
    • Kim H., Park J., Cho I., Kim S., Paek S., Lee H. Selective immobilization of proteins on gold dot arrays and characterization using chemical force microscopy. J. Colloid Interface Sci. 2009, 334:161-166.
    • (2009) J. Colloid Interface Sci. , vol.334 , pp. 161-166
    • Kim, H.1    Park, J.2    Cho, I.3    Kim, S.4    Paek, S.5    Lee, H.6
  • 122
    • 80755143196 scopus 로고    scopus 로고
    • Using engineered single-chain antibodies to correlate molecular binding properties and nanoparticle adhesion dynamics
    • Haun J., Pepper L., Boder E., Hammer D. Using engineered single-chain antibodies to correlate molecular binding properties and nanoparticle adhesion dynamics. Langmuir 2011, 27:13701-13712.
    • (2011) Langmuir , vol.27 , pp. 13701-13712
    • Haun, J.1    Pepper, L.2    Boder, E.3    Hammer, D.4
  • 123
    • 33845595417 scopus 로고    scopus 로고
    • A nanocatalyst-based assay for proteins: DNA-free ultrasensitive electrochemical detection using catalytic reduction of p-nitrophenol by gold-nanoparticle labels
    • Das J., Aziz M., Yang H. A nanocatalyst-based assay for proteins: DNA-free ultrasensitive electrochemical detection using catalytic reduction of p-nitrophenol by gold-nanoparticle labels. J. Am. Chem. Soc. 2006, 128:16022-16023.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16022-16023
    • Das, J.1    Aziz, M.2    Yang, H.3
  • 124
    • 20444375424 scopus 로고    scopus 로고
    • Selective targeting of antibody-conjugated nanoparticles to leukemic cells and primary T-lymphocytes
    • Dinauer N., Balthasar S., Weber C., Kreuter J., Langer K., von Briesen H. Selective targeting of antibody-conjugated nanoparticles to leukemic cells and primary T-lymphocytes. Biomaterials 2005, 26:5898-5906.
    • (2005) Biomaterials , vol.26 , pp. 5898-5906
    • Dinauer, N.1    Balthasar, S.2    Weber, C.3    Kreuter, J.4    Langer, K.5    von Briesen, H.6
  • 125
    • 0029797773 scopus 로고    scopus 로고
    • Streptavidins with intersubunit crosslinks have enhanced stability
    • Reznik G., Vajda S., Smith C., Cantor C., Sano T. Streptavidins with intersubunit crosslinks have enhanced stability. Nat. Biotechnol. 1996, 14:1007-1011.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1007-1011
    • Reznik, G.1    Vajda, S.2    Smith, C.3    Cantor, C.4    Sano, T.5
  • 127
    • 0343941543 scopus 로고    scopus 로고
    • Extremely high thermal stability of streptavidin and avidin upon biotin binding
    • Gonzalez M., Argarana C., Fidelio G. Extremely high thermal stability of streptavidin and avidin upon biotin binding. Biomol. Eng. 1999, 16:67-72.
    • (1999) Biomol. Eng. , vol.16 , pp. 67-72
    • Gonzalez, M.1    Argarana, C.2    Fidelio, G.3
  • 128
    • 6344253039 scopus 로고    scopus 로고
    • Controlled surface functionalization of silica nanospheres by covalent conjugation reactions and preparation of high density streptavidin nanoparticles
    • Schiestel T., Brunner H., Tovar G.E.M. Controlled surface functionalization of silica nanospheres by covalent conjugation reactions and preparation of high density streptavidin nanoparticles. J. Nanosci. Nanotechnol. 2004, 4:504-511.
    • (2004) J. Nanosci. Nanotechnol. , vol.4 , pp. 504-511
    • Schiestel, T.1    Brunner, H.2    Tovar, G.E.M.3
  • 129
    • 79952117209 scopus 로고    scopus 로고
    • Covalent binding of streptavidin on gold magnetic nanoparticles for bead array fabrication
    • Li S., Liu H., He N. Covalent binding of streptavidin on gold magnetic nanoparticles for bead array fabrication. J. Nanosci. Nanotechnol. 2010, 10:4875-4882.
    • (2010) J. Nanosci. Nanotechnol. , vol.10 , pp. 4875-4882
    • Li, S.1    Liu, H.2    He, N.3
  • 130
    • 80053591961 scopus 로고    scopus 로고
    • Engineered streptavidin monomer and dimer with improved stability and function
    • Lim K., Huang H., Pralle A., Park S. Engineered streptavidin monomer and dimer with improved stability and function. Biochemistry 2011, 50:8682-8691.
    • (2011) Biochemistry , vol.50 , pp. 8682-8691
    • Lim, K.1    Huang, H.2    Pralle, A.3    Park, S.4
  • 131
    • 78951473593 scopus 로고    scopus 로고
    • ToF-SIMS and PCA of surface-immobilized antibodies with different orientations
    • Park J., Cho I., Moon D., Paek S., Lee T. ToF-SIMS and PCA of surface-immobilized antibodies with different orientations. Surf. Interface Anal. 2011, 43:285-289.
    • (2011) Surf. Interface Anal. , vol.43 , pp. 285-289
    • Park, J.1    Cho, I.2    Moon, D.3    Paek, S.4    Lee, T.5
  • 132
    • 34247381635 scopus 로고    scopus 로고
    • Site-directed biotinylation of antibodies for controlled immobilization of solid surfaces
    • Cho I., Paek E., Lee H., Kang J., Kim T., Paek S. Site-directed biotinylation of antibodies for controlled immobilization of solid surfaces. Anal. Biochem. 2007, 365:14-23.
    • (2007) Anal. Biochem. , vol.365 , pp. 14-23
    • Cho, I.1    Paek, E.2    Lee, H.3    Kang, J.4    Kim, T.5    Paek, S.6
  • 133
    • 34247112358 scopus 로고    scopus 로고
    • Direct immobilization of protein G variants with various numbers of cysteine residues on a gold surface
    • Lee J., Park H., Jung Y., Kim J., Jung S., Chung B. Direct immobilization of protein G variants with various numbers of cysteine residues on a gold surface. Anal. Chem. 2007, 79:2680-2687.
    • (2007) Anal. Chem. , vol.79 , pp. 2680-2687
    • Lee, J.1    Park, H.2    Jung, Y.3    Kim, J.4    Jung, S.5    Chung, B.6
  • 134
    • 34547784409 scopus 로고    scopus 로고
    • Self-assembled monolayers for MALDI-TOF mass spectrometry for immunoassays of human protein antigens
    • Patrie S., Mrksich M. Self-assembled monolayers for MALDI-TOF mass spectrometry for immunoassays of human protein antigens. Anal. Chem. 2007, 79:5878-5887.
    • (2007) Anal. Chem. , vol.79 , pp. 5878-5887
    • Patrie, S.1    Mrksich, M.2
  • 135
    • 33846231069 scopus 로고    scopus 로고
    • Self-assembled layer of thiolated Protein G as an immunosensor scaffold
    • Fowler J., Stuart M., Wong D. Self-assembled layer of thiolated Protein G as an immunosensor scaffold. Anal. Chem. 2007, 79:350-354.
    • (2007) Anal. Chem. , vol.79 , pp. 350-354
    • Fowler, J.1    Stuart, M.2    Wong, D.3
  • 136
    • 31444456883 scopus 로고    scopus 로고
    • Fabrication of antibody arrays using thermally responsive elastin fusion proteins
    • Gao D., McBean N., Schultz J., Yan Y., Mulchandani A., Chen W. Fabrication of antibody arrays using thermally responsive elastin fusion proteins. J. Am. Chem. Soc. 2006, 128:676-677.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 676-677
    • Gao, D.1    McBean, N.2    Schultz, J.3    Yan, Y.4    Mulchandani, A.5    Chen, W.6
  • 137
    • 84878378740 scopus 로고    scopus 로고
    • Protein A/G Recombinant PROSPEC.
    • Protein A/G Recombinant PROSPEC.
  • 138
    • 84878407108 scopus 로고    scopus 로고
    • Protein A/G Biovision, in.
    • Protein A/G Biovision, in.
  • 139
    • 84878389230 scopus 로고    scopus 로고
    • Pierce Recombinant Protein A/G and Conjugates, in.
    • Pierce Recombinant Protein A/G and Conjugates, in.
  • 140
    • 80052356118 scopus 로고    scopus 로고
    • Enhancing immunoassay detection of antigens with multimeric protein Gs
    • Lee J.H., Choi H.K., Lee S.Y., Lim M.-W., Chang J.H. Enhancing immunoassay detection of antigens with multimeric protein Gs. Biosens. Bioelectron. 2011, 28:146-151.
    • (2011) Biosens. Bioelectron. , vol.28 , pp. 146-151
    • Lee, J.H.1    Choi, H.K.2    Lee, S.Y.3    Lim, M.-W.4    Chang, J.H.5
  • 142
    • 27744445693 scopus 로고    scopus 로고
    • Sensitive detection of proteins using difunctional DNA-gold nanoparticles
    • Hazarika P., Ceyhan B., Niemeyer C.M. Sensitive detection of proteins using difunctional DNA-gold nanoparticles. Small 2005, 1:844-848.
    • (2005) Small , vol.1 , pp. 844-848
    • Hazarika, P.1    Ceyhan, B.2    Niemeyer, C.M.3
  • 143
    • 0035476388 scopus 로고    scopus 로고
    • DNA-directed functionalization of colloidal gold with proteins
    • Niemeyer C.M., Ceyhan B. DNA-directed functionalization of colloidal gold with proteins. Angew. Chem. Int. Ed. 2001, 40:3685-3688.
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 3685-3688
    • Niemeyer, C.M.1    Ceyhan, B.2
  • 144
    • 50849089350 scopus 로고    scopus 로고
    • Antibody fragments as probe in biosensor development
    • Saerens D., Huang L., Bonroy K., Muyldermans S. Antibody fragments as probe in biosensor development. Sensors 2008, 8:4669-4686.
    • (2008) Sensors , vol.8 , pp. 4669-4686
    • Saerens, D.1    Huang, L.2    Bonroy, K.3    Muyldermans, S.4
  • 145
    • 78650818528 scopus 로고    scopus 로고
    • Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance
    • Hernandez K., Fernandez-Lafuente R. Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance. Enzyme Microb. Technol. 2011, 48:107-122.
    • (2011) Enzyme Microb. Technol. , vol.48 , pp. 107-122
    • Hernandez, K.1    Fernandez-Lafuente, R.2
  • 147
    • 52749088977 scopus 로고    scopus 로고
    • Covalent immobilization of antibodies on finally inert support surfaces through their surface regions having the highest densities in carboxyl groups
    • Batalla P., Fuentes M., Mateo C., Grazu V., Fernandez-Lafuente R., Guisan J.M. Covalent immobilization of antibodies on finally inert support surfaces through their surface regions having the highest densities in carboxyl groups. Biomacromolecules 2008, 9:2230-2236.
    • (2008) Biomacromolecules , vol.9 , pp. 2230-2236
    • Batalla, P.1    Fuentes, M.2    Mateo, C.3    Grazu, V.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 148
    • 67650507243 scopus 로고    scopus 로고
    • Impact of surface defects and denaturation of capture surface proteins on nonspecific binding in immunoassays using antibody-coated polystyrene nanoparticle labels
    • Nareoja T., Maattanen A., Peltonen J., Hanninen P., Harma H. Impact of surface defects and denaturation of capture surface proteins on nonspecific binding in immunoassays using antibody-coated polystyrene nanoparticle labels. J. Immunol. Methods 2009, 347:24-30.
    • (2009) J. Immunol. Methods , vol.347 , pp. 24-30
    • Nareoja, T.1    Maattanen, A.2    Peltonen, J.3    Hanninen, P.4    Harma, H.5
  • 150
    • 79952302512 scopus 로고    scopus 로고
    • Physical-chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles
    • Monopoli M.P., Walczyk D., Campbell A., Elia G., Lynch I., Bombelli F.B., Dawson K.A. Physical-chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles. J. Am. Chem. Soc. 2011, 133:2525-2534.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2525-2534
    • Monopoli, M.P.1    Walczyk, D.2    Campbell, A.3    Elia, G.4    Lynch, I.5    Bombelli, F.B.6    Dawson, K.A.7
  • 151
    • 58049196998 scopus 로고    scopus 로고
    • Composite nanoparticles take aim at cancer
    • Rivera Gil P., Parak W.J. Composite nanoparticles take aim at cancer. ACS Nano 2008, 2:2200-2205.
    • (2008) ACS Nano , vol.2 , pp. 2200-2205
    • Rivera Gil, P.1    Parak, W.J.2
  • 153
    • 79951898882 scopus 로고    scopus 로고
    • Interactions of nanoparticles with plasma proteins: implication on clearance and toxicity of drug delivery systems
    • Karmali P.P., Simberg D. Interactions of nanoparticles with plasma proteins: implication on clearance and toxicity of drug delivery systems. Expert Opin. Drug Deliv. 2011, 8:343-357.
    • (2011) Expert Opin. Drug Deliv. , vol.8 , pp. 343-357
    • Karmali, P.P.1    Simberg, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.