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Volumn 6, Issue , 2016, Pages

A recombinant secondary antibody mimic as a target-specific signal amplifier and an antibody immobilizer in immunoassays

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HORSERADISH PEROXIDASE; HYBRID PROTEIN; IMMUNOGLOBULIN FC FRAGMENT;

EID: 84964393697     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep24159     Document Type: Article
Times cited : (13)

References (22)
  • 1
    • 0036781811 scopus 로고    scopus 로고
    • Ligand-targeted therapeutics in anticancer therapy
    • Allen, T. M. Ligand-targeted therapeutics in anticancer therapy. Nat. Rev. Cancer 2, 750-763 (2002).
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 750-763
    • Allen, T.M.1
  • 2
    • 0035524114 scopus 로고    scopus 로고
    • Improving the efficacy of antibody-based cancer therapies
    • Carter, P. Improving the efficacy of antibody-based cancer therapies. Nat. Rev. Cancer 1, 118-129 (2001).
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 118-129
    • Carter, P.1
  • 3
    • 0026493569 scopus 로고
    • Uranium-loaded apoferritin with antibodies attached: Molecular design for uranium neutron-capture therapy
    • Hainfeld, J. F. Uranium-loaded apoferritin with antibodies attached: molecular design for uranium neutron-capture therapy. Proc. Natl. Acad. Sci. USA 89, 11064-11068 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11064-11068
    • Hainfeld, J.F.1
  • 5
    • 0141839661 scopus 로고    scopus 로고
    • Comparison of antibody functionality using different immobilization methods
    • Danczyk, R. et al. Comparison of antibody functionality using different immobilization methods. Biotechnol. Bioeng. 84, 215-223 (2003).
    • (2003) Biotechnol. Bioeng. , vol.84 , pp. 215-223
    • Danczyk, R.1
  • 6
    • 38349105897 scopus 로고    scopus 로고
    • Controlled antibody immobilization onto immunoanalytical platforms by synthetic peptide
    • Jung, Y. W. et al. Controlled antibody immobilization onto immunoanalytical platforms by synthetic peptide. Anal. Biochem. 374, 99-105 (2008).
    • (2008) Anal. Biochem. , vol.374 , pp. 99-105
    • Jung, Y.W.1
  • 7
    • 0029904435 scopus 로고    scopus 로고
    • Minimizing a binding domain from protein A
    • Braisted, A. C. and Wells, J. A. Minimizing a binding domain from protein A. Proc. Natl. Acad. Sci. USA 93, 5688-5692 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5688-5692
    • Braisted, A.C.1    Wells, J.A.2
  • 8
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8- A resolution
    • Deisenhofer, J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8- A resolution. Biochemistry 20, 2361-2370 (1981).
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 9
    • 84934951314 scopus 로고    scopus 로고
    • An enhanced ascorbate peroxidase 2/antibody-binding domain fusion protein (APEX2-ABD) as a recombinant targetspecific signal amplifier
    • Lee, J. et al. An enhanced ascorbate peroxidase 2/antibody-binding domain fusion protein (APEX2-ABD) as a recombinant targetspecific signal amplifier. Chem. Comm. 51, 10945-10948 (2015).
    • (2015) Chem. Comm. , vol.51 , pp. 10945-10948
    • Lee, J.1
  • 10
    • 84860920261 scopus 로고    scopus 로고
    • Developing an antibody-binding protein cage as a molecular recognition drug modular nanoplatform
    • Kang, H. J. et al. Developing an antibody-binding protein cage as a molecular recognition drug modular nanoplatform. Biomaterials 33, 5423-5430 (2012).
    • (2012) Biomaterials , vol.33 , pp. 5423-5430
    • Kang, H.J.1
  • 11
    • 84882324547 scopus 로고    scopus 로고
    • Fabrication of uniform layer-by-layer assemblies with complementary protein cage nanobuilding blocks via simple His-tag/metal recognition
    • Moon, H. et al. Fabrication of uniform layer-by-layer assemblies with complementary protein cage nanobuilding blocks via simple His-tag/metal recognition. J. Mater. Chem. B 1, 4504-4510 (2013).
    • (2013) J. Mater. Chem. B , vol.1 , pp. 4504-4510
    • Moon, H.1
  • 12
    • 73949126820 scopus 로고    scopus 로고
    • Efficient selection of IgG Fc domain-binding peptides fused to fluorescent protein using E. Coli expression system and dot-blotting assay
    • Jeong, Y. J., Kang, H. J., Bae, K. H., Kim, M. G. and Chung, S. J. Efficient selection of IgG Fc domain-binding peptides fused to fluorescent protein using E. coli expression system and dot-blotting assay. Peptides 31, 202-206 (2010).
    • (2010) Peptides , vol.31 , pp. 202-206
    • Jeong, Y.J.1    Kang, H.J.2    Bae, K.H.3    Kim, M.G.4    Chung, S.J.5
  • 13
    • 0024852342 scopus 로고
    • Catalyzed reporter deposition, a novel method of signal amplification application to immunoassays
    • Bobrow, M. N., Harris, T. D., Shaughnessy, K. J. and Litt, G. J. Catalyzed reporter deposition, a novel method of signal amplification application to immunoassays. J. Immunol. Methods 125, 279-285 (1989).
    • (1989) J. Immunol. Methods , vol.125 , pp. 279-285
    • Bobrow, M.N.1    Harris, T.D.2    Shaughnessy, K.J.3    Litt, G.J.4
  • 14
    • 0033912238 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assay
    • Butler, J. E. Enzyme-Linked Immunosorbent Assay. J. Immunoassay 21, 165-209 (2000).
    • (2000) J. Immunoassay , vol.21 , pp. 165-209
    • Butler, J.E.1
  • 15
    • 0030980643 scopus 로고    scopus 로고
    • Fluorochrome-labeled tyramides: Use in Immunocytochemistry and fluorescence in situ hybridization
    • Gijlswijk, R. P. M. V. et al. Fluorochrome-labeled Tyramides: Use in Immunocytochemistry and Fluorescence In Situ Hybridization. J. Histochem. and Cytochem. 45, 375-382 (1997).
    • (1997) J. Histochem. and Cytochem. , vol.45 , pp. 375-382
    • Gijlswijk, R.P.M.V.1
  • 16
    • 0026625337 scopus 로고
    • The use of catalyzed reporter deposition as a means of signal amplification in a variety of formats
    • Bobrow, M. N., Litt, G. J., Shaughnessy, K. J., Mayer, P. C. and Conlon, J. The use of catalyzed reporter deposition as a means of signal amplification in a variety of formats. J. Immunol. Methods 150, 145-149 (1992).
    • (1992) J. Immunol. Methods , vol.150 , pp. 145-149
    • Bobrow, M.N.1    Litt, G.J.2    Shaughnessy, K.J.3    Mayer, P.C.4    Conlon, J.5
  • 17
    • 33750165279 scopus 로고    scopus 로고
    • Overexpression of epithelial cell adhesion molecule (Ep-CAM) is an independent prognostic marker for reduced survival of patients with epithelial ovarian cancer
    • Spizzo, G. et al. Overexpression of epithelial cell adhesion molecule (Ep-CAM) is an independent prognostic marker for reduced survival of patients with epithelial ovarian cancer. Gynecol. Oncol. 103, 483-488 (2006).
    • (2006) Gynecol. Oncol. , vol.103 , pp. 483-488
    • Spizzo, G.1
  • 18
    • 30644472381 scopus 로고    scopus 로고
    • Frequent high-level expression of the immunotherapeutic target Ep-CAM in colon, stomach, prostate and lung cancers
    • Went, P. et al. Frequent high-level expression of the immunotherapeutic target Ep-CAM in colon, stomach, prostate and lung cancers. Br. J. Cancer 94, 128-135 (2006).
    • (2006) Br. J. Cancer , vol.94 , pp. 128-135
    • Went, P.1
  • 19
    • 77956278335 scopus 로고    scopus 로고
    • High-Magnification in Vivo Imaging of Xenopus Embryos for Cell and Developmental Biology
    • Kieserman, E. K., Lee, C., Gray, R. S., Park, T. J. and Wallingford, J. B. High-Magnification In Vivo Imaging of Xenopus Embryos for Cell and Developmental Biology. CSH protocols 5, doi: 10.1101/pdb.prot5427 (2010).
    • (2010) CSH Protocols , vol.5
    • Kieserman, E.K.1    Lee, C.2    Gray, R.S.3    Park, T.J.4    Wallingford, J.B.5
  • 20
    • 44949229560 scopus 로고    scopus 로고
    • Whole-mount fluorescence immunocytochemistry on Xenopus embryos
    • Lee, C., Kieserman, E., Gray, R. S., Park, T. J. and Wallingford, J. Whole-mount fluorescence immunocytochemistry on Xenopus embryos. CSH protocols 3, doi: 10.1101/pdb.prot4957 (2008).
    • (2008) CSH Protocols , vol.3
    • Lee, C.1    Kieserman, E.2    Gray, R.S.3    Park, T.J.4    Wallingford, J.5
  • 22
    • 84908012108 scopus 로고    scopus 로고
    • Developing genetically engineered encapsulin protein cage nanoparticles as a targeted delivery nanoplatform
    • Moon, H., Lee, J., Min, J. and Kang, S. Developing Genetically Engineered Encapsulin Protein Cage Nanoparticles as a Targeted Delivery Nanoplatform. Biomacromolecules 15, 3794-3801 (2014).
    • (2014) Biomacromolecules , vol.15 , pp. 3794-3801
    • Moon, H.1    Lee, J.2    Min, J.3    Kang, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.