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Volumn 282, Issue 22, 2015, Pages 4389-4401

Development of a bispecific antibody tetramerized through hetero-associating peptides

Author keywords

bispecific antibody; cancer therapy; CD16; epidermal growth factor receptor; self associating peptide

Indexed keywords

BISPECIFIC ANTIBODY; EPIDERMAL GROWTH FACTOR RECEPTOR; FC RECEPTOR;

EID: 84954527495     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13505     Document Type: Article
Times cited : (11)

References (46)
  • 1
    • 79952377840 scopus 로고    scopus 로고
    • Developing the next generation of monoclonal antibodies for the treatment of rheumatoid arthritis
    • Campbell J, Lowe D, &, Sleeman MA, (2011) Developing the next generation of monoclonal antibodies for the treatment of rheumatoid arthritis. Br J Pharmacol 162, 1470-1484.
    • (2011) Br J Pharmacol , vol.162 , pp. 1470-1484
    • Campbell, J.1    Lowe, D.2    Sleeman, M.A.3
  • 2
    • 65549152525 scopus 로고    scopus 로고
    • Monoclonal antibody therapies for solid tumors
    • Tassev DV, &, Cheung NK, (2009) Monoclonal antibody therapies for solid tumors. Expert Opin Biol Ther 9, 341-353.
    • (2009) Expert Opin Biol Ther , vol.9 , pp. 341-353
    • Tassev, D.V.1    Cheung, N.K.2
  • 3
    • 79959382429 scopus 로고    scopus 로고
    • Engineering antibodies for cancer therapy
    • Boder ET, &, Jiang W, (2011) Engineering antibodies for cancer therapy. Annu Rev Chem Biomol Eng 2, 53-75.
    • (2011) Annu Rev Chem Biomol Eng , vol.2 , pp. 53-75
    • Boder, E.T.1    Jiang, W.2
  • 4
    • 77951523463 scopus 로고    scopus 로고
    • Bispecific antibodies for cancer therapy: The light at the end of the tunnel?
    • Chames P, &, Baty D, (2009) Bispecific antibodies for cancer therapy: the light at the end of the tunnel? MAbs 1, 539-547.
    • (2009) MAbs , vol.1 , pp. 539-547
    • Chames, P.1    Baty, D.2
  • 5
    • 79958187876 scopus 로고    scopus 로고
    • Therapeutic potential of anticancer immunotoxins
    • Choudhary S, Mathew M, &, Verma RS, (2011) Therapeutic potential of anticancer immunotoxins. Drug Discov Today 16, 495-503.
    • (2011) Drug Discov Today , vol.16 , pp. 495-503
    • Choudhary, S.1    Mathew, M.2    Verma, R.S.3
  • 6
    • 84884828581 scopus 로고    scopus 로고
    • Immunocytokines: A review of molecules in clinical development for cancer therapy
    • List T, &, Neri D, (2013) Immunocytokines: a review of molecules in clinical development for cancer therapy. Clin Pharmacol 5, 29-45.
    • (2013) Clin Pharmacol , vol.5 , pp. 29-45
    • List, T.1    Neri, D.2
  • 10
    • 0026567963 scopus 로고
    • Formation of a bispecific antibody by the use of leucine zippers
    • Kostelny SA, Cole MS, &, Tso JY, (1992) Formation of a bispecific antibody by the use of leucine zippers. J Immunol 148, 1547-1553.
    • (1992) J Immunol , vol.148 , pp. 1547-1553
    • Kostelny, S.A.1    Cole, M.S.2    Tso, J.Y.3
  • 12
    • 84863337696 scopus 로고    scopus 로고
    • The dock-and-lock method combines recombinant engineering with site-specific covalent conjugation to generate multifunctional structures
    • Rossi EA, Goldenberg DM, &, Chang CH, (2012) The dock-and-lock method combines recombinant engineering with site-specific covalent conjugation to generate multifunctional structures. Bioconjug Chem 23, 309-323.
    • (2012) Bioconjug Chem , vol.23 , pp. 309-323
    • Rossi, E.A.1    Goldenberg, D.M.2    Chang, C.H.3
  • 14
  • 15
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • Arbabi-Ghahroudi M, Desmyter A, Wyns L, Hamers R, &, Muyldermans S, (1997) Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett 414, 521-526.
    • (1997) FEBS Lett , vol.414 , pp. 521-526
    • Arbabi-Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 16
    • 0036179747 scopus 로고    scopus 로고
    • A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia
    • Lee S, Fan S, Makarova O, Straight S, &, Margolis B, (2002) A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia. Mol Cell Biol 22, 1778-1791.
    • (2002) Mol Cell Biol , vol.22 , pp. 1778-1791
    • Lee, S.1    Fan, S.2    Makarova, O.3    Straight, S.4    Margolis, B.5
  • 18
    • 3543040058 scopus 로고    scopus 로고
    • Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes
    • Li Y, Karnak D, Demeler B, Margolis B, &, Lavie A, (2004) Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes. EMBO J 23, 2723-2733.
    • (2004) EMBO J , vol.23 , pp. 2723-2733
    • Li, Y.1    Karnak, D.2    Demeler, B.3    Margolis, B.4    Lavie, A.5
  • 19
    • 0024818499 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • Sowdhamini R, Srinivasan N, Shoichet B, Santi DV, Ramakrishnan C, &, Balaram P, (1989) Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. Protein Eng 3, 95-103.
    • (1989) Protein Eng , vol.3 , pp. 95-103
    • Sowdhamini, R.1    Srinivasan, N.2    Shoichet, B.3    Santi, D.V.4    Ramakrishnan, C.5    Balaram, P.6
  • 20
    • 84896689696 scopus 로고    scopus 로고
    • KRAS mutation confers resistance to antibody-dependent cellular cytotoxicity of cetuximab against human colorectal cancer cells
    • Nakadate Y, Kodera Y, Kitamura Y, Shirasawa S, Tachibana T, Tamura T, &, Koizumi F, (2014) KRAS mutation confers resistance to antibody-dependent cellular cytotoxicity of cetuximab against human colorectal cancer cells. Int J Cancer 134, 2146-2155.
    • (2014) Int J Cancer , vol.134 , pp. 2146-2155
    • Nakadate, Y.1    Kodera, Y.2    Kitamura, Y.3    Shirasawa, S.4    Tachibana, T.5    Tamura, T.6    Koizumi, F.7
  • 28
    • 0021860882 scopus 로고
    • Preparation of bispecific antibodies by chemical recombination of monoclonal immunoglobulin G1 fragments
    • Brennan M, Davison PF, &, Paulus H, (1985) Preparation of bispecific antibodies by chemical recombination of monoclonal immunoglobulin G1 fragments. Sience 229, 81-83.
    • (1985) Sience , vol.229 , pp. 81-83
    • Brennan, M.1    Davison, P.F.2    Paulus, H.3
  • 29
    • 0022555989 scopus 로고
    • Bispecific monoclonal antibodies from hybrid hybridomas
    • Suresh MR, Cuello AC, &, Milstein C, (1986) Bispecific monoclonal antibodies from hybrid hybridomas. Methods Enzymol 121, 210-228.
    • (1986) Methods Enzymol , vol.121 , pp. 210-228
    • Suresh, M.R.1    Cuello, A.C.2    Milstein, C.3
  • 30
    • 33646477258 scopus 로고    scopus 로고
    • Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting
    • Rossi EA, Goldenberg DM, Cardillo TM, McBride WJ, Sharkey RM, &, Chang CH, (2006) Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting. Proc Natl Acad Sci USA 103, 6841-6846.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6841-6846
    • Rossi, E.A.1    Goldenberg, D.M.2    Cardillo, T.M.3    McBride, W.J.4    Sharkey, R.M.5    Chang, C.H.6
  • 31
    • 18744382488 scopus 로고    scopus 로고
    • A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins
    • Feng W, Long JF, &, Zhang M, (2005) A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins. Proc Natl Acad Sci USA 102, 6861-6866.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6861-6866
    • Feng, W.1    Long, J.F.2    Zhang, M.3
  • 32
    • 84876564677 scopus 로고    scopus 로고
    • Domain order of a bispecific diabody dramatically enhances its antitumor activity beyond structural format conversion: The case of the hEx3 diabody
    • Asano R, Kumagai T, Nagai K, Taki S, Shimomura I, Arai K, Ogata H, Okada M, Hayasaka F, Sanada H, et al,. (2013) Domain order of a bispecific diabody dramatically enhances its antitumor activity beyond structural format conversion: the case of the hEx3 diabody. Protein Eng Des Sel 26, 359-367.
    • (2013) Protein Eng des Sel , vol.26 , pp. 359-367
    • Asano, R.1    Kumagai, T.2    Nagai, K.3    Taki, S.4    Shimomura, I.5    Arai, K.6    Ogata, H.7    Okada, M.8    Hayasaka, F.9    Sanada, H.10
  • 33
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P, &, Hudson PJ, (2005) Engineered antibody fragments and the rise of single domains. Nat Biotechnol 23, 1126-1136.
    • (2005) Nat Biotechnol , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 35
    • 0030611643 scopus 로고    scopus 로고
    • Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-48L/R/H phenotype
    • Koene HR, Kleijer M, Algra J, Roos D, von dem Borne AE, &, de Haas M, (1997) Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-48L/R/H phenotype. Blood 90, 1109-1114.
    • (1997) Blood , vol.90 , pp. 1109-1114
    • Koene, H.R.1    Kleijer, M.2    Algra, J.3    Roos, D.4    Von Dem Borne, A.E.5    De Haas, M.6
  • 36
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene
    • Cartron G, Dacheux L, Salles G, Solal-Celigny P, Bardos P, Colombat P, &, Watier H, (2002) Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene. Blood 99, 754-758.
    • (2002) Blood , vol.99 , pp. 754-758
    • Cartron, G.1    Dacheux, L.2    Salles, G.3    Solal-Celigny, P.4    Bardos, P.5    Colombat, P.6    Watier, H.7
  • 37
    • 0642373290 scopus 로고    scopus 로고
    • Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma
    • Weng WK, &, Levy R, (2003) Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma. J Clin Oncol 21, 3940-3947.
    • (2003) J Clin Oncol , vol.21 , pp. 3940-3947
    • Weng, W.K.1    Levy, R.2
  • 38
    • 42949157368 scopus 로고    scopus 로고
    • Immunoglobulin G fragment C receptor polymorphisms and clinical efficacy of trastuzumab-based therapy in patients with HER-2/neu-positive metastatic breast cancer
    • Musolino A, Naldi N, Bortesi B, Pezzuolo D, Capelletti M, Missale G, Laccabue D, Zerbini A, Camisa R, Bisagni G, et al,. (2008) Immunoglobulin G fragment C receptor polymorphisms and clinical efficacy of trastuzumab-based therapy in patients with HER-2/neu-positive metastatic breast cancer. J Clin Oncol 26, 1789-1796.
    • (2008) J Clin Oncol , vol.26 , pp. 1789-1796
    • Musolino, A.1    Naldi, N.2    Bortesi, B.3    Pezzuolo, D.4    Capelletti, M.5    Missale, G.6    Laccabue, D.7    Zerbini, A.8    Camisa, R.9    Bisagni, G.10
  • 39
    • 84906241263 scopus 로고    scopus 로고
    • A FcγRIII-engaging bispecific antibody expands the range of HER2-expressing breast tumors eligible to antibody therapy
    • Turini M, Chames P, Bruhns P, Baty D, &, Kerfelec B, (2014) A FcγRIII-engaging bispecific antibody expands the range of HER2-expressing breast tumors eligible to antibody therapy. Oncotarget 5, 5304-5319.
    • (2014) Oncotarget , vol.5 , pp. 5304-5319
    • Turini, M.1    Chames, P.2    Bruhns, P.3    Baty, D.4    Kerfelec, B.5
  • 40
    • 0024362504 scopus 로고
    • Expression vector system based on the chicken beta-actin promoter directs efficient production of interleukin-5
    • Miyazaki J, Takaki S, Araki K, Tashiro F, Tominaga A, Takatsu K, &, Yamamura K, (1989) Expression vector system based on the chicken beta-actin promoter directs efficient production of interleukin-5. Gene 79, 269-277.
    • (1989) Gene , vol.79 , pp. 269-277
    • Miyazaki, J.1    Takaki, S.2    Araki, K.3    Tashiro, F.4    Tominaga, A.5    Takatsu, K.6    Yamamura, K.7
  • 45
    • 0035831483 scopus 로고    scopus 로고
    • Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs
    • Els Conrath K, Lauwereys M, Wyns L, &, Muyldermans S, (2001) Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs. J Biol Chem 276, 7346-7350.
    • (2001) J Biol Chem , vol.276 , pp. 7346-7350
    • Els Conrath, K.1    Lauwereys, M.2    Wyns, L.3    Muyldermans, S.4
  • 46
    • 0028819660 scopus 로고
    • Biological efficacy of a chimeric antibody to the epidermal growth factor receptor in a human tumor xenograft model
    • Goldstein NI, Prewett M, Zuklys K, Rockwell P, &, Mendelsohn J, (1995) Biological efficacy of a chimeric antibody to the epidermal growth factor receptor in a human tumor xenograft model. Clin Cancer Res 1, 1311-1318.
    • (1995) Clin Cancer Res , vol.1 , pp. 1311-1318
    • Goldstein, N.I.1    Prewett, M.2    Zuklys, K.3    Rockwell, P.4    Mendelsohn, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.