메뉴 건너뛰기




Volumn 31, Issue 9, 2010, Pages 1198-1207

Research and development of next generation of antibody-based therapeutics

Author keywords

antibody design; antibody efficacy enhancement; antibody engineering; antibody therapeutics; next generation of antibody; novel antibody format

Indexed keywords

ABCIXIMAB; ADALIMUMAB; ALEMTUZUMAB; ANKYRIN; ANTIBODY CONJUGATE; ARZERRA; AVE 9633; BASILIXIMAB; BEVACIZUMAB; BRENTUXIMAB VEDOTIN; C 326; CANAKINUMAB; CD16 ANTIGEN; CDX 011; CERTOLIZUMAB PEGOL; CETUXIMAB; COTARA; CT 322; DACLIZUMAB; ECULIZUMAB; EDRECOLOMAB; EFALIZUMAB; FC RECEPTOR; GEMTUZUMAB OZOGAMICIN; IBRITUMOMAB TIUXETAN; IMGN 242; IMMUNOGLOBULIN ANTIBODY; INFLIXIMAB; INOTUZUMAB OZOGAMICIN; INTERLEUKIN 1 RECEPTOR BLOCKING AGENT; MDX 1203; MEDI 547; MP 0112; NATALIZUMAB; NIMOTUZUMAB; OMALIZUMAB; ORTHOCLONE; PALIVIZUMAB; PANITUMUMAB; PROLIA; RANIBIZUMAB; REMOVAB; RITUXIMAB; SGN 33; SIMPONI; TOCILIZUMAB; TOSITUMOMAB I 131; TRASTUZUMAB; TRASTUZUMAB DM1; TUMOR NECROSIS FACTOR INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; USTEKINUMAB; VASCULOTROPIN INHIBITOR;

EID: 77956381860     PISSN: 16714083     EISSN: 17457254     Source Type: Journal    
DOI: 10.1038/aps.2010.120     Document Type: Review
Times cited : (111)

References (105)
  • 1
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G, Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975; 256: 495-497
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 2
    • 0021716682 scopus 로고
    • Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region domains
    • Morrison SL, Johnson MJ, Herzenberg LA, Oi VT. Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc Natl Acad Sci USA 1984; 81: 6851-6855
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 6851-6855
    • Morrison, S.L.1    Johnson, M.J.2    Herzenberg, L.A.3    Oi, V.T.4
  • 3
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones PT, Dear PH, Foote J, Neuberger MS, Winter G. Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 1986; 321: 522-525
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 6
    • 0027089852 scopus 로고
    • A transgenic mouse that expresses a diversity of human sequence heavy and light chain immunoglobulins
    • Taylor LD, Carmack CE, Schramm SR, Mashayekh R, Higgins KM, Kuo CC, et al. A transgenic mouse that expresses a diversity of human sequence heavy and light chain immunoglobulins. Nucleic Acids Res 1992; 20: 6287-6295
    • (1992) Nucleic Acids Res , vol.20 , pp. 6287-6295
    • Taylor, L.D.1    Carmack, C.E.2    Schramm, S.R.3    Mashayekh, R.4    Higgins, K.M.5    Kuo, C.C.6
  • 7
    • 0028222932 scopus 로고
    • Antigen-specific human antibodies from mice comprising four distinct genetic modifications
    • Lonberg N, Taylor LD, Harding FA, Trounstine M, Higgins KM, Schramm SR, et al. Antigen-specific human antibodies from mice comprising four distinct genetic modifications. Nature 1994; 368: 856-859
    • (1994) Nature , vol.368 , pp. 856-859
    • Lonberg, N.1    Taylor, L.D.2    Harding, F.A.3    Trounstine, M.4    Higgins, K.M.5    Schramm, S.R.6
  • 8
    • 0027963484 scopus 로고
    • Antigen-specific human monoclonal antibodies from mice engineered with human Ig heavy and light chain YACs
    • Green LL, Hardy MC, Maynard-Currie CE, Tsuda H, Louie DM, Mendez MJ, et al. Antigen-specific human monoclonal antibodies from mice engineered with human Ig heavy and light chain YACs. Nat Genet 1994; 7: 13-21.
    • (1994) Nat Genet , vol.7 , pp. 13-21
    • Green, L.L.1    Hardy, M.C.2    Maynard-Currie, C.E.3    Tsuda, H.4    Louie, D.M.5    Mendez, M.J.6
  • 9
    • 17644378667 scopus 로고    scopus 로고
    • Immunogenicity of engineered antibodies
    • Hwang WYK, Foote J. Immunogenicity of engineered antibodies. Methods 2005; 36: 3-10.
    • (2005) Methods , vol.36 , pp. 3-10
    • Hwang, W.Y.K.1    Foote, J.2
  • 10
    • 38449099720 scopus 로고    scopus 로고
    • An update on treatment advances for the first-line therapy of metastatic colorectal cancer
    • Lee JJ, Chu E. An update on treatment advances for the first-line therapy of metastatic colorectal cancer. Cancer J 2007; 13: 276-281
    • (2007) Cancer J , vol.13 , pp. 276-281
    • Lee, J.J.1    Chu, E.2
  • 11
    • 55849128896 scopus 로고    scopus 로고
    • Durable complete responses from therapy with combined epratuzumab and rituximab: Final results from an international multicenter, phase 2 study in recurrent, indolent, non-Hodgkin lymphoma
    • Leonard JP, Schuster SJ, Emmanouilides C, Couture F, Teoh N, Wegener WA, et al. Durable complete responses from therapy with combined epratuzumab and rituximab: final results from an international multicenter, phase 2 study in recurrent, indolent, non-Hodgkin lymphoma. Cancer 2008; 113: 2714-2723
    • (2008) Cancer , vol.113 , pp. 2714-2723
    • Leonard, J.P.1    Schuster, S.J.2    Emmanouilides, C.3    Couture, F.4    Teoh, N.5    Wegener, W.A.6
  • 12
    • 33645054805 scopus 로고    scopus 로고
    • Bispecific antibodies for dual-modality cancer therapy: Killing two signaling cascades with one stone
    • Marvin JS, Zhu Z. Bispecific antibodies for dual-modality cancer therapy: Killing two signaling cascades with one stone. Curr Opin Drug Discov Devel 2006; 9: 184-193
    • (2006) Curr Opin Drug Discov Devel , vol.9 , pp. 184-193
    • Marvin, J.S.1    Zhu, Z.2
  • 13
    • 0025348891 scopus 로고
    • Targeting human T-lymphocytes with bispecific antibodies to react against human ovarian carcinoma cells growing in nu/nu mice
    • Garrido MA, Valdayo MJ, Winkler DF, Titus JA, Hecht TT, Perez P, et al. Targeting human T-lymphocytes with bispecific antibodies to react against human ovarian carcinoma cells growing in nu/nu mice. Cancer Res 1990; 50: 4227-4232
    • (1990) Cancer Res , vol.50 , pp. 4227-4232
    • Garrido, M.A.1    Valdayo, M.J.2    Winkler, D.F.3    Titus, J.A.4    Hecht, T.T.5    Perez, P.6
  • 14
    • 67449156132 scopus 로고    scopus 로고
    • Bispecific T-cell engaging antibodies for cancer therapy
    • Baeuerle PA, Reinhardt C. Bispecific T-cell engaging antibodies for cancer therapy. Cancer Res 2009; 69: 4941-4944
    • (2009) Cancer Res , vol.69 , pp. 4941-4944
    • Baeuerle, P.A.1    Reinhardt, C.2
  • 15
    • 0035476882 scopus 로고    scopus 로고
    • Complete inhibition of vascular endothelial growth factor (VEGF) activities with a bifunctional diabody directed against both VEGF kinase receptors, fms-like tyrosine kinase receptor and kinase insert domain-containing receptor
    • Lu D, Jimenez X, Zhang H, Wu Y, Bohlen P, Witte L, et al. Complete inhibition of vascular endothelial growth factor (VEGF) activities with a bifunctional diabody directed against both VEGF kinase receptors, fms-like tyrosine kinase receptor and kinase insert domain-containing receptor. Cancer Res 2001; 61: 7002-7008
    • (2001) Cancer Res , vol.61 , pp. 7002-7008
    • Lu, D.1    Jimenez, X.2    Zhang, H.3    Wu, Y.4    Bohlen, P.5    Witte, L.6
  • 16
    • 9144256621 scopus 로고    scopus 로고
    • Simultaneous blockade of both the epidermal growth factor receptor and the insulin-like growth factor receptor signaling pathways in cancer cells with a fully human recombinant bispecific antibody
    • Lu D, Zhang H, Ludwig D, Persaud A, Jimenez X, Burtrum D, et al. Simultaneous blockade of both the epidermal growth factor receptor and the insulin-like growth factor receptor signaling pathways in cancer cells with a fully human recombinant bispecific antibody. J Biol Chem 2004; 279: 2856-2865
    • (2004) J Biol Chem , vol.279 , pp. 2856-2865
    • Lu, D.1    Zhang, H.2    Ludwig, D.3    Persaud, A.4    Jimenez, X.5    Burtrum, D.6
  • 17
    • 21244441508 scopus 로고    scopus 로고
    • A fully human recombinant igg-like bispecific antibody to both the epidermal growth factor receptor and the insulin-like growth factor receptor for enhanced antitumor activity
    • Lu D, Zhang H, Koo H, Tonra J, Balderes P, Prewett M, et al. A fully human recombinant igg-like bispecific antibody to both the epidermal growth factor receptor and the insulin-like growth factor receptor for enhanced antitumor activity. J Biol Chem 2005; 280: 19665-19672
    • (2005) J Biol Chem , vol.280 , pp. 19665-19672
    • Lu, D.1    Zhang, H.2    Koo, H.3    Tonra, J.4    Balderes, P.5    Prewett, M.6
  • 18
    • 55249104916 scopus 로고    scopus 로고
    • Targeting ErbB2 and ErbB3 with a bispecific single-chain Fv enhances targeting selectivity and induces a therapeutic effect in vitro
    • Robinson MK, Hodge KM, Horak E, Sundberg AL, Russeva M, Shaller CC, et al. Targeting ErbB2 and ErbB3 with a bispecific single-chain Fv enhances targeting selectivity and induces a therapeutic effect in vitro. Br J Cancer 2008; 99: 1415-1425
    • (2008) Br J Cancer , vol.99 , pp. 1415-1425
    • Robinson, M.K.1    Hodge, K.M.2    Horak, E.3    Sundberg, A.L.4    Russeva, M.5    Shaller, C.C.6
  • 19
    • 66449132035 scopus 로고    scopus 로고
    • Development of a fully human anti-PDGFRbeta antibody that suppresses growth of human tumor xenografts and enhances antitumor activity of an anti-VEGFR2 antibody
    • Shen J, Vil MD, Prewett M, Damoci C, Zhang H, Li H, et al. Development of a fully human anti-PDGFRbeta antibody that suppresses growth of human tumor xenografts and enhances antitumor activity of an anti-VEGFR2 antibody. Neoplasia 2009; 11: 594-604.
    • (2009) Neoplasia , vol.11 , pp. 594-604
    • Shen, J.1    Vil, M.D.2    Prewett, M.3    Damoci, C.4    Zhang, H.5    Li, H.6
  • 20
    • 0032737901 scopus 로고    scopus 로고
    • Acquired antagonistic activity of a bispecific diabody directed against two different epitopes on vascular endothelial growth factor receptor 2
    • Lu D, Kotanides H, Jimenez X, Zhou Q, Persaud K, Bohlen P, et al. Acquired antagonistic activity of a bispecific diabody directed against two different epitopes on vascular endothelial growth factor receptor 2. J Immunol Methods 1999; 230: 159-171
    • (1999) J Immunol Methods , vol.230 , pp. 159-171
    • Lu, D.1    Kotanides, H.2    Jimenez, X.3    Zhou, Q.4    Persaud, K.5    Bohlen, P.6
  • 22
    • 0028786757 scopus 로고
    • Toward the production of bispecific antibody fragments for clinical applications
    • Carter P, Ridgway J, Zhu Z. Toward the production of bispecific antibody fragments for clinical applications. J Hematother 1995; 4: 463-470
    • (1995) J Hematother , vol.4 , pp. 463-470
    • Carter, P.1    Ridgway, J.2    Zhu, Z.3
  • 23
    • 0035251453 scopus 로고    scopus 로고
    • Bispecific human IgG by design
    • Carter P. Bispecific human IgG by design. J Immunol Methods 2001; 248: 7-15.
    • (2001) J Immunol Methods , vol.248 , pp. 7-15
    • Carter, P.1
  • 24
    • 20444380008 scopus 로고    scopus 로고
    • Recombinant approaches to IgG-like bispecific antibodies
    • Marvin JS, Zhu Z. Recombinant approaches to IgG-like bispecific antibodies. Acta Pharmacol Sin 2005; 26: 649-658
    • (2005) Acta Pharmacol Sin , vol.26 , pp. 649-658
    • Marvin, J.S.1    Zhu, Z.2
  • 25
    • 4143149984 scopus 로고    scopus 로고
    • Recent advances in the generation of bispecific antibodies for tumor immunotherapy
    • Kipriyanov SM, Le GF. Recent advances in the generation of bispecific antibodies for tumor immunotherapy. Curr Opin Drug Discov Devel 2004; 7: 233-242
    • (2004) Curr Opin Drug Discov Devel , vol.7 , pp. 233-242
    • Kipriyanov, S.M.1    Le, G.F.2
  • 26
    • 0344654890 scopus 로고    scopus 로고
    • Novel tetravalent and bispecific IgGlike antibody molecules combining single-chain diabodies with the immunoglobulin gamma1 Fc or CH3 region
    • Alt M, Muller R, Kontermann RE. Novel tetravalent and bispecific IgGlike antibody molecules combining single-chain diabodies with the immunoglobulin gamma1 Fc or CH3 region. FEBS Lett 1999; 454: 90-94
    • (1999) FEBS Lett , vol.454 , pp. 90-94
    • Alt, M.1    Muller, R.2    Kontermann, R.E.3
  • 28
    • 1642633148 scopus 로고    scopus 로고
    • Radiolabeled antibody therapy in non-Hodgkins lymphoma: Radiation protection, isotope comparisons and quality of life issues
    • Silverman DH, Delpassand ES, Torabi F, Goy A, McLaughlin P, Murray JL. Radiolabeled antibody therapy in non-Hodgkins lymphoma: radiation protection, isotope comparisons and quality of life issues. Cancer Treat Rev 2004; 30: 165-172
    • (2004) Cancer Treat Rev , vol.30 , pp. 165-172
    • Silverman, D.H.1    Delpassand, E.S.2    Torabi, F.3    Goy, A.4    McLaughlin, P.5    Murray, J.L.6
  • 29
    • 33646352962 scopus 로고    scopus 로고
    • Potent antibody therapeutics by design
    • Carter PJ. Potent antibody therapeutics by design. Nat Rev Immunol 2006; 6: 343-357
    • (2006) Nat Rev Immunol , vol.6 , pp. 343-357
    • Carter, P.J.1
  • 30
    • 56449129810 scopus 로고    scopus 로고
    • Targeting HER2-positive breast cancer with trastuzumab-dm1, an antibody-cytotoxic drug conjugate
    • Lewis Phillips GD, Li G, Dugger DL, Crocker LM, Parsons KL, Mai E, et al. Targeting HER2-positive breast cancer with trastuzumab-dm1, an antibody-cytotoxic drug conjugate. Cancer Res 2008; 68: 9280-9290
    • (2008) Cancer Res , vol.68 , pp. 9280-9290
    • Lewis Phillips, G.D.1    Li, G.2    Dugger, D.L.3    Crocker, L.M.4    Parsons, K.L.5    Mai, E.6
  • 31
    • 49449119098 scopus 로고    scopus 로고
    • Antibody-drug conjugates for cancer therapy
    • Carter PJ, Senter PD. Antibody-drug conjugates for cancer therapy. Cancer J 2008; 14: 154-169
    • (2008) Cancer J , vol.14 , pp. 154-169
    • Carter, P.J.1    Senter, P.D.2
  • 32
    • 74849092615 scopus 로고    scopus 로고
    • Antibody-drug conjugate targets
    • Teicher BA. Antibody-drug conjugate targets. Curr Cancer Drug Targets 2009; 9: 982-1004.
    • (2009) Curr Cancer Drug Targets , vol.9 , pp. 982-1004
    • Teicher, B.A.1
  • 33
    • 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, et al. Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene. Blood 2002; 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
  • 34
    • 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, et al. 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 2008; 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
  • 35
    • 56749096598 scopus 로고    scopus 로고
    • Evidence for linkage disequilibrium between fc{gamma}RIIIa-v158f and fc{gamma}riia-h131r polymorphisms in white patients, and for an fc{gamma}riiia-restricted influence on the response to therapeutic antibodies
    • Lejeune J, Thibault G, Ternant D, Cartron G, Watier H, Ohresser M. Evidence for linkage disequilibrium between fc{gamma}RIIIa-v158f and fc{gamma}riia-h131r polymorphisms in white patients, and for an fc{gamma}riiia-restricted influence on the response to therapeutic antibodies. J Clin Oncol 2008; 26: 5489-5491
    • (2008) J Clin Oncol , vol.26 , pp. 5489-5491
    • Lejeune, J.1    Thibault, G.2    Ternant, D.3    Cartron, G.4    Watier, H.5    Ohresser, M.6
  • 36
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • Shields RL, Namenuk AK, Hong K, Meng YG, Rae J, Briggs J, et al. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R. J Biol Chem 2001; 276: 6591-6604
    • (2001) J Biol Chem , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6
  • 38
    • 35748949531 scopus 로고    scopus 로고
    • Optimizing engagement of the immune system by anti-tumor antibodies: An engineers perspective
    • Desjarlais JR, Lazar GA, Zhukovsky EA, Chu SY. Optimizing engagement of the immune system by anti-tumor antibodies: an engineers perspective. Drug Discov Today 2007; 12: 898-910.
    • (2007) Drug Discov Today , vol.12 , pp. 898-910
    • Desjarlais, J.R.1    Lazar, G.A.2    Zhukovsky, E.A.3    Chu, S.Y.4
  • 39
    • 77956372262 scopus 로고    scopus 로고
    • Variant Fc regions. ed. PCT/US2006/025276 Ref Type: Patent
    • Allan B. Variant Fc regions. ed. Applied Molecular Evolution. PCT/US2006/025276. 2010. Ref Type: Patent
    • (2010) Applied Molecular Evolution
    • Allan, B.1
  • 41
    • 33747339717 scopus 로고    scopus 로고
    • Molecular aspects of human FcgammaR interactions with IgG: Functional and therapeutic consequences
    • Siberil S, Dutertre CA, Boix C, Bonnin E, Mnez R, Stura E, et al. Molecular aspects of human FcgammaR interactions with IgG: functional and therapeutic consequences. Immunol Lett 2006; 106: 111-118
    • (2006) Immunol Lett , vol.106 , pp. 111-118
    • Siberil, S.1    Dutertre, C.A.2    Boix, C.3    Bonnin, E.4    Mnez, R.5    Stura, E.6
  • 42
    • 54249100952 scopus 로고    scopus 로고
    • Potent in vitro and in vivo activity of an fc-engineered anti-cd19 monoclonal antibody against lymphoma and leukemia
    • Horton HM, Bernett MJ, Pong E, Peipp M, Karki S, Chu SY, et al. Potent in vitro and in vivo activity of an fc-engineered anti-cd19 monoclonal antibody against lymphoma and leukemia. Cancer Res 2008; 68: 8049-8057
    • (2008) Cancer Res , vol.68 , pp. 8049-8057
    • Horton, H.M.1    Bernett, M.J.2    Pong, E.3    Peipp, M.4    Karki, S.5    Chu, S.Y.6
  • 43
    • 45549090117 scopus 로고    scopus 로고
    • Engineered antibodies of IgG1/IgG3 mixed isotype with enhanced cytotoxic activities
    • Natsume A, In M, Takamura H, Nakagawa T, Shimizu Y, Kitajima K, et al. Engineered antibodies of IgG1/IgG3 mixed isotype with enhanced cytotoxic activities. Cancer Res 2008; 68: 3863-3872
    • (2008) Cancer Res , vol.68 , pp. 3863-3872
    • Natsume, A.1    In, M.2    Takamura, H.3    Nakagawa, T.4    Shimizu, Y.5    Kitajima, K.6
  • 44
    • 4644245850 scopus 로고    scopus 로고
    • Establishment of FUT8 knockout Chinese hamster ovary cells: An ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity
    • Yamane-Ohnuki N, Kinoshita S, Inoue-Urakubo M, Kusunoki M, Iida S, Nakano R, et al. Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnol Bioeng 2004; 87: 614-622
    • (2004) Biotechnol Bioeng , vol.87 , pp. 614-622
    • Yamane-Ohnuki, N.1    Kinoshita, S.2    Inoue-Urakubo, M.3    Kusunoki, M.4    Iida, S.5    Nakano, R.6
  • 45
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibodydependent cellular cytotoxic activity
    • Umana P, Jean-Mairet J, Moudry R, Amstutz H, Bailey JE. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibodydependent cellular cytotoxic activity. Nat Biotech 1999; 17: 176-180
    • (1999) Nat Biotech , vol.17 , pp. 176-180
    • Umana, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5
  • 48
    • 33751322142 scopus 로고    scopus 로고
    • Compensation of endogenous IgG mediated inhibition of antibodydependent cellular cytotoxicity by glyco-engineering of therapeutic antibodies
    • Nechansky A, Schuster M, Jost W, Siegl P, Wiederkum S, Gorr G, et al. Compensation of endogenous IgG mediated inhibition of antibodydependent cellular cytotoxicity by glyco-engineering of therapeutic antibodies. Mol Immunol 2007; 44: 1815-1817
    • (2007) Mol Immunol , vol.44 , pp. 1815-1817
    • Nechansky, A.1    Schuster, M.2    Jost, W.3    Siegl, P.4    Wiederkum, S.5    Gorr, G.6
  • 49
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006; 313: 670-673
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 50
    • 33747631571 scopus 로고    scopus 로고
    • Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn)
    • DallAcqua WF, Kiener PA, Wu H. Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn). J Biol Chem 2006; 281: 23514-23524
    • (2006) J Biol Chem , vol.281 , pp. 23514-23524
    • Dallacqua, W.F.1    Kiener, P.A.2    Wu, H.3
  • 51
    • 64149121224 scopus 로고    scopus 로고
    • Structural characterization of a human Fc fragment engineered for extended serum half-life
    • Oganesyan V, Damschroder MM, Woods RM, Cook KE, Wu H, Dallacqua WF. Structural characterization of a human Fc fragment engineered for extended serum half-life. Mol Immunol 2009; 46: 1750-1755
    • (2009) Mol Immunol , vol.46 , pp. 1750-1755
    • Oganesyan, V.1    Damschroder, M.M.2    Woods, R.M.3    Cook, K.E.4    Wu, H.5    Dallacqua, W.F.6
  • 52
    • 77951027408 scopus 로고    scopus 로고
    • A therapeutic anti-VEGF antibody with increased potency independent of pharmacokinetic half-life
    • Yeung YA, Wu X, Reyes AE 2nd, Vernes JM, Lien S, Lowe J, et al. A therapeutic anti-VEGF antibody with increased potency independent of pharmacokinetic half-life. Cancer Res 2010; 70: 3269-3277
    • (2010) Cancer Res , vol.70 , pp. 3269-3277
    • Yeung, Y.A.1    Wu, X.2    Reyes, I.I.A.E.3    Vernes, J.M.4    Lien, S.5    Lowe, J.6
  • 57
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P, Hudson PJ. 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.J.2
  • 59
    • 0027197493 scopus 로고
    • Diabodies: Small bivalent and bispecific antibody fragments
    • Holliger P, Prospero T, Winter G. "Diabodies": small bivalent and bispecific antibody fragments. Proc Natl Acad Sci USA 1993; 90: 6444-6448
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6444-6448
    • Holliger, P.1    Prospero, T.2    Winter, G.3
  • 60
    • 0027923826 scopus 로고
    • Protein engineering. Making of the minibody
    • Quiocho FA. Protein engineering. Making of the minibody. Nature 1993; 362: 293-294
    • (1993) Nature , vol.362 , pp. 293-294
    • Quiocho, F.A.1
  • 62
    • 0042195979 scopus 로고    scopus 로고
    • Selection and characterization of naturally occurring single-domain (IgNAR) antibody fragments from immunized sharks by phage display
    • Dooley H, Flajnik MF, Porter AJ. Selection and characterization of naturally occurring single-domain (IgNAR) antibody fragments from immunized sharks by phage display. Mol Immunol 2003; 40: 25-33.
    • (2003) Mol Immunol , vol.40 , pp. 25-33
    • Dooley, H.1    Flajnik, M.F.2    Porter, A.J.3
  • 64
    • 34249718925 scopus 로고    scopus 로고
    • Certolizumab pegol: In crohns disease
    • Blick SK, Curran MP. Certolizumab Pegol: In Crohns Disease. BioDrugs 2007; 21: 195-201 .
    • (2007) BioDrugs , vol.21 , pp. 195-201
    • Blick, S.K.1    Curran, M.P.2
  • 65
    • 34250361507 scopus 로고    scopus 로고
    • Improved pharmacokinetics of recombinant bispecific antibody molecules by fusion to human serum albumin
    • Muller,D. Karle A, Meissburger B, Höfig I, Stork R, Kontermann RE, et al. Improved pharmacokinetics of recombinant bispecific antibody molecules by fusion to human serum albumin. J Biol Chem 2007; 282: 12650-12660
    • (2007) J Biol Chem , vol.282 , pp. 12650-12660
    • Mullerd. Karle, A.1    Meissburger, B.2    Höfig, I.3    Stork, R.4    Kontermann, R.E.5
  • 66
    • 33745712861 scopus 로고    scopus 로고
    • The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin
    • Nguyen A, Reyes AE 2nd, Zhang M, McDonald P, Wong WL, Damico LA, et al. The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin. Protein Eng Des Sel 2006; 19: 291-297
    • (2006) Protein Eng des Sel , vol.19 , pp. 291-297
    • Nguyen, A.1    Reyes, I.I.A.E.2    Zhang, M.3    McDonald, P.4    Wong, W.L.5    Damico, L.A.6
  • 69
    • 0344033650 scopus 로고    scopus 로고
    • Imitating the humoral immune response
    • Skerra A. Imitating the humoral immune response. Curr Opin Chem Biol 2003; 7: 683-693
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 683-693
    • Skerra, A.1
  • 70
    • 33646740974 scopus 로고    scopus 로고
    • Antagonists to human and mouse vascular endothelial growth factor receptor 2 generated by directed protein evolution in vitro
    • Getmanova EV, Chen Y, Bloom L, Gokemeijer J, Shamah S, Warikoo V, et al. Antagonists to human and mouse vascular endothelial growth factor receptor 2 generated by directed protein evolution in vitro. Chem Biol 2006; 13: 549-556
    • (2006) Chem Biol , vol.13 , pp. 549-556
    • Getmanova, E.V.1    Chen, Y.2    Bloom, L.3    Gokemeijer, J.4    Shamah, S.5    Warikoo, V.6
  • 71
    • 28644436100 scopus 로고    scopus 로고
    • Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains
    • Silverman J, Liu Q, Bakker A, To W, Duguay A, Alba BM, et al. Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains. Nat Biotechnol 2005; 23: 1556-1561
    • (2005) Nat Biotechnol , vol.23 , pp. 1556-1561
    • Silverman, J.1    Liu, Q.2    Bakker, A.3    To, W.4    Duguay, A.5    Alba, B.M.6
  • 72
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • Binz HK, Stumpp MT, Forrer P, Amstutz P, Plnckthun A. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J Mol Biol 2003; 332: 489-503.
    • (2003) J Mol Biol , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Plnckthun, A.5
  • 74
    • 2342624119 scopus 로고    scopus 로고
    • High-affinity binders selected from designed ankyrin repeat protein libraries
    • Binz HK, Amstutz P, Kohl A, Stumpp MT, Briand C, Forrer P, et al. High-affinity binders selected from designed ankyrin repeat protein libraries. Nat Biotechnol 2004; 22: 575-582
    • (2004) Nat Biotechnol , vol.22 , pp. 575-582
    • Binz, H.K.1    Amstutz, P.2    Kohl, A.3    Stumpp, M.T.4    Briand, C.5    Forrer, P.6
  • 75
    • 43549101411 scopus 로고    scopus 로고
    • Alternative binding proteins: Affibody binding proteins developed from a small three-helix bundle scaffold
    • Nygren PA. Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold. FEBS J 2008; 275: 2668-2676
    • (2008) FEBS J , vol.275 , pp. 2668-2676
    • Nygren, P.A.1
  • 76
    • 12844276589 scopus 로고    scopus 로고
    • Lipocalins in drug discovery: From natural ligand-binding proteins to "anticalins"
    • Schlehuber S, Skerra A. Lipocalins in drug discovery: from natural ligand-binding proteins to "anticalins". Drug Discov Today 2005; 10: 23-33.
    • (2005) Drug Discov Today , vol.10 , pp. 23-33
    • Schlehuber, S.1    Skerra, A.2
  • 77
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
    • Colas P, Cohen B, Jessen T, Grishina I, McCoy J, Brent R, et al. Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2. Nature 1996; 380: 548-550
    • (1996) Nature , vol.380 , pp. 548-550
    • Colas, P.1    Cohen, B.2    Jessen, T.3    Grishina, I.4    McCoy, J.5    Brent, R.6
  • 78
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz HK, Amstutz P, Pluckthun A. Engineering novel binding proteins from nonimmunoglobulin domains. Nat Biotechnol 2005; 23: 1257-1268
    • (2005) Nat Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pluckthun, A.3
  • 79
    • 0029785574 scopus 로고    scopus 로고
    • Intra-and extracellular immunization against HIV-1 infection with lymphocytes transduced with an AAV vector expressing a human anti-gp120 antibody
    • Chen JD, Yang Q, Yang AG, Marasco WA, Chen SY. Intra-and extracellular immunization against HIV-1 infection with lymphocytes transduced with an AAV vector expressing a human anti-gp120 antibody. Hum Gene Ther 1996; 7: 1515-1525
    • (1996) Hum Gene Ther , vol.7 , pp. 1515-1525
    • Chen, J.D.1    Yang, Q.2    Yang, A.G.3    Marasco, W.A.4    Chen, S.Y.5
  • 80
    • 0043123378 scopus 로고    scopus 로고
    • Single domain intracellular antibodies: A minimal fragment for direct in vivo selection of antigenspecific Intrabodies
    • Tanaka T, Lobato MN, Rabbitts TH. Single domain intracellular antibodies: a minimal fragment for direct in vivo selection of antigenspecific Intrabodies. J Mol Biol 2003; 331: 1109-1120
    • (2003) J Mol Biol , vol.331 , pp. 1109-1120
    • Tanaka, T.1    Lobato, M.N.2    Rabbitts, T.H.3
  • 81
    • 20444391361 scopus 로고    scopus 로고
    • Phenotypic knockout of VEGF-R2 and Tie-2 with an intradiabody reduces tumor growth and angiogenesis in vivo
    • Jendreyko N, Popkov M, Rader C, Barbas CF. Phenotypic knockout of VEGF-R2 and Tie-2 with an intradiabody reduces tumor growth and angiogenesis in vivo. Proc Natl Acad Sci USA 2005; 102: 8293-8298 .
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8293-8298
    • Jendreyko, N.1    Popkov, M.2    Rader, C.3    Barbas, C.F.4
  • 82
    • 0036359198 scopus 로고    scopus 로고
    • Intrabodies Targeting scFv expression to eukaryotic intracellular compartments
    • Cohen PA. Intrabodies. Targeting scFv expression to eukaryotic intracellular compartments. Methods Mol Biol 2002; 178: 367-378
    • (2002) Methods Mol Biol , vol.178 , pp. 367-378
    • Cohen, P.A.1
  • 83
    • 20444368797 scopus 로고    scopus 로고
    • Novel highly efficient intrabody mediates complete inhibition of cell surface expression of the human vascular endothelial growth factor receptor-2 (VEGFR-2/KDR)
    • Boldicke T, Weber H, Mueller PP, Barleon B, Bernal M. Novel highly efficient intrabody mediates complete inhibition of cell surface expression of the human vascular endothelial growth factor receptor-2 (VEGFR-2/KDR). J Immunol Methods 2005; 300: 146-159
    • (2005) J Immunol Methods , vol.300 , pp. 146-159
    • Boldicke, T.1    Weber, H.2    Mueller, P.P.3    Barleon, B.4    Bernal, M.5
  • 84
    • 0029812091 scopus 로고    scopus 로고
    • Intracellular expression of a single-chain antibody directed to the EGFR leads to growth inhibition of tumor cells
    • Jannot CB, Beerli RR, Mason S, Gullick WJ, Hynes NE. Intracellular expression of a single-chain antibody directed to the EGFR leads to growth inhibition of tumor cells. Oncogene 1996; 13: 275-282
    • (1996) Oncogene , vol.13 , pp. 275-282
    • Jannot, C.B.1    Beerli, R.R.2    Mason, S.3    Gullick, W.J.4    Hynes, N.E.5
  • 85
    • 16844381988 scopus 로고    scopus 로고
    • Proapoptotic activity of cell-permeable anti-Akt single-chain antibodies
    • Shin I, Edl J, Biswas S, Lin PC, Mernaugh R, Arteaga CL, et al. Proapoptotic activity of cell-permeable anti-Akt single-chain antibodies. Cancer Res 2005; 65: 2815-2824
    • (2005) Cancer Res , vol.65 , pp. 2815-2824
    • Shin, I.1    Edl, J.2    Biswas, S.3    Lin, P.C.4    Mernaugh, R.5    Arteaga, C.L.6
  • 86
    • 28044459831 scopus 로고    scopus 로고
    • Human single-domain neutralizing intrabodies directed against Etk kinase: A novel approach to impair cellular transformation
    • Paz K, Brennan LA, Iacolina M, Doody J, Hadari YR, Zhu Z, et al. Human single-domain neutralizing intrabodies directed against Etk kinase: a novel approach to impair cellular transformation. Mol Cancer Ther 2005; 4: 1801-1809
    • (2005) Mol Cancer Ther , vol.4 , pp. 1801-1809
    • Paz, K.1    Brennan, L.A.2    Iacolina, M.3    Doody, J.4    Hadari, Y.R.5    Zhu, Z.6
  • 87
    • 0036570976 scopus 로고    scopus 로고
    • Characterization of anti-cyclin e single-chain Fv antibodies and intrabodies in breast cancer cells: Enhanced intracellular stability of novel sFv-Fc intrabodies
    • Strube RW, Chen SY. Characterization of anti-cyclin E single-chain Fv antibodies and intrabodies in breast cancer cells: enhanced intracellular stability of novel sFv-Fc intrabodies. J Immunol Methods 2002; 263: 149-167
    • (2002) J Immunol Methods , vol.263 , pp. 149-167
    • Strube, R.W.1    Chen, S.Y.2
  • 88
    • 33646495989 scopus 로고    scopus 로고
    • Intrabody-based approaches to cancer therapy: Status and prospects
    • Williams BR, Zhu Z. Intrabody-based approaches to cancer therapy: status and prospects. Curr Med Chem 2006; 13: 1473-1480
    • (2006) Curr Med Chem , vol.13 , pp. 1473-1480
    • Williams, B.R.1    Zhu, Z.2
  • 89
    • 0033542388 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 replication in vitro in acutely and persistently infected human CD4+ mononuclear cells expressing Murine and humanized anti-human immunodeficiency virus type 1 Tat single-chain variable fragment intrabodies
    • Mhashilkar AM, LaVecchio J, Eberhardt B, Porter-Brooks J, Boisot S, Dove JH, et al. Inhibition of human immunodeficiency virus type 1 replication in vitro in acutely and persistently infected human CD4+ mononuclear cells expressing Murine and humanized anti-human immunodeficiency virus type 1 Tat single-chain variable fragment intrabodies. Human Gene Ther 1999; 10: 1453-1467
    • (1999) Human Gene Ther , vol.10 , pp. 1453-1467
    • Mhashilkar, A.M.1    Lavecchio, J.2    Eberhardt, B.3    Porter-Brooks, J.4    Boisot, S.5    Dove, J.H.6
  • 90
    • 0034681197 scopus 로고    scopus 로고
    • Functional deletion of the CCR5 receptor by intracellular immunization produces cells that are refractory to CCR5-dependent HIV-1 infection and cell fusion
    • Steinberger P, Andris-Widhopf J, Bühler B, Torbett BE, Barbas CF. Functional deletion of the CCR5 receptor by intracellular immunization produces cells that are refractory to CCR5-dependent HIV-1 infection and cell fusion. Proc Natl Acad Sci USA 2000; 97: 805-810
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 805-810
    • Steinberger, P.1    Andris-Widhopf, J.2    Bühler, B.3    Torbett, B.E.4    Barbas, C.F.5
  • 91
    • 34248143972 scopus 로고    scopus 로고
    • Intrabody strategies for the treatment of human papillomavirus-associated disease
    • Doorbar J, Griffin H. Intrabody strategies for the treatment of human papillomavirus-associated disease. Expert Opin Biol Ther 2007; 7: 677-689
    • (2007) Expert Opin Biol Ther , vol.7 , pp. 677-689
    • Doorbar, J.1    Griffin, H.2
  • 92
    • 68949159773 scopus 로고    scopus 로고
    • Developing intrabodies for the therapeutic suppression of neurodegenerative pathology
    • Messer A, Lynch SM, Butler DC. Developing intrabodies for the therapeutic suppression of neurodegenerative pathology. Expert Opin Biol Ther 2009; 9: 1189-1197
    • (2009) Expert Opin Biol Ther , vol.9 , pp. 1189-1197
    • Messer, A.1    Lynch, S.M.2    Butler, D.C.3
  • 93
    • 85047699270 scopus 로고    scopus 로고
    • Intrabody-mediated phenotypic knockout of major histocompatibility complex class i expression in human and monkey cell lines and in primary human keratinocytes
    • Mhashilkar AM, Doebis C, Seifert M, Busch A, Zani C, Soo Hoo J, et al. Intrabody-mediated phenotypic knockout of major histocompatibility complex class I expression in human and monkey cell lines and in primary human keratinocytes. Gene Ther 2002; 9: 307-319
    • (2002) Gene Ther , vol.9 , pp. 307-319
    • Mhashilkar, A.M.1    Doebis, C.2    Seifert, M.3    Busch, A.4    Zani, C.5    Soo Hoo, J.6
  • 94
    • 18544408628 scopus 로고    scopus 로고
    • A cancer gene therapy approach utilizing an anti-erbB-2 single-chain antibody-encoding adenovirus (AD21): A phase i trial
    • Alvarez RD, Barnes MN, Gomez-Navarro J, Wang M, Strong TV, Arafat W, et al. A cancer gene therapy approach utilizing an anti-erbB-2 single-chain antibody-encoding adenovirus (AD21): a phase I trial. Clin Cancer Res 2000; 6: 3081-3087
    • (2000) Clin Cancer Res , vol.6 , pp. 3081-3087
    • Alvarez, R.D.1    Barnes, M.N.2    Gomez-Navarro, J.3    Wang, M.4    Strong, T.V.5    Arafat, W.6
  • 95
    • 24644445065 scopus 로고    scopus 로고
    • Nucleic acid modulation of gene expression: Approaches for nucleic acid therapeutics against cancer
    • Nakata Y, Kim TK, Shetzline S, Gewirtz AM. Nucleic acid modulation of gene expression: approaches for nucleic acid therapeutics against cancer. Crit Rev Eukaryot Gene Expr 2005; 15: 163-182
    • (2005) Crit Rev Eukaryot Gene Expr , vol.15 , pp. 163-182
    • Nakata, Y.1    Kim, T.K.2    Shetzline, S.3    Gewirtz, A.M.4
  • 96
    • 0347623204 scopus 로고    scopus 로고
    • Nonspecific, concentrationdependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs)
    • Persengiev SP, Zhu X, Green MR. Nonspecific, concentrationdependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs). RNA 2004; 10: 12-18
    • (2004) RNA , vol.10 , pp. 12-18
    • Persengiev, S.P.1    Zhu, X.2    Green, M.R.3
  • 99
    • 1042290308 scopus 로고    scopus 로고
    • Improved Therapeutic Responses in a Xenograft Model of Human B Lymphoma (Namalwa) for Liposomal Vincristine versus Liposomal Doxorubicin Targeted via Anti-CD19 IgG2a or Fab fragments
    • Sapra P, Moase EH, Ma J, Allen TM. Improved Therapeutic Responses in a Xenograft Model of Human B Lymphoma (Namalwa) for Liposomal Vincristine versus Liposomal Doxorubicin Targeted via Anti-CD19 IgG2a or Fab fragments. Clin Cancer Res 2004; 10: 1100-1111
    • (2004) Clin Cancer Res , vol.10 , pp. 1100-1111
    • Sapra, P.1    Moase, E.H.2    Ma, J.3    Allen, T.M.4
  • 100
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a Herpesvirus structural protein
    • Elliott G, OHare P. Intercellular trafficking and protein delivery by a Herpesvirus structural protein. Cell 1997; 88: 223-233
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    Ohare, P.2
  • 101
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel AD, Pabo CO. Cellular uptake of the tat protein from human immunodeficiency virus. Cell 1988; 55: 1189-1193
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 102
    • 0036299007 scopus 로고    scopus 로고
    • Intracellular antibody capture technology: Application to selection of intracellular antibodies recognising the BCR-ABL oncogenic protein
    • Tse E, Lobato MN, Forster A, Tanaka T, Chung GT, Rabbitts TH. Intracellular antibody capture technology: application to selection of intracellular antibodies recognising the BCR-ABL oncogenic protein. J Mol Biol 2002; 317; 85-94.
    • (2002) J Mol Biol , vol.317 , pp. 85-94
    • Tse, E.1    Lobato, M.N.2    Forster, A.3    Tanaka, T.4    Chung, G.T.5    Rabbitts, T.H.6
  • 103
    • 0345549465 scopus 로고    scopus 로고
    • Direct phage to intrabody screening (DPIS): Demonstration by isolation of cytosolic intrabodies against the TES1 site of Epstein Barr virus latent membrane protein 1 (LMP1) that block NF-[kappa]B transactivation
    • Gennari F, Mehta S, Wang Y, St Clair Tallarico A, Palu G, et al. Direct phage to intrabody screening (DPIS): demonstration by isolation of cytosolic intrabodies against the TES1 site of Epstein Barr virus latent membrane protein 1 (LMP1) that block NF-[kappa]B transactivation. J Mol Biol 2004; 335: 193-207.
    • (2004) J Mol Biol , vol.335 , pp. 193-207
    • Gennari, F.1    Mehta, S.2    Wang, Y.3    St Clair Tallarico, A.4    Palu, G.5
  • 104
    • 0347997286 scopus 로고    scopus 로고
    • Direct in vivo screening of intrabody libraries constructed on a highly stable single-chain framework
    • der Maur AA, Zahnd C, Fischer F, Spinelli S, Honegger A, Cambillau C, et al. Direct in vivo screening of intrabody libraries constructed on a highly stable single-chain framework. J Biol Chem 2002; 277: 45075-45085
    • (2002) J Biol Chem , vol.277 , pp. 45075-45085
    • Der Maur, A.A.1    Zahnd, C.2    Fischer, F.3    Spinelli, S.4    Honegger, A.5    Cambillau, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.