Alternative molecular formats and therapeutic applications for bispecific antibodies

FcRn: the neonatal Fc receptor comes of age

Roopenian, D. C., & Akilesh, S. (2007) · Nature Reviews Immunology · doi:10.1038/nri2155 · Cited by 2,346 · see citing works

Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli.

Huston, J. S., Levinson, D., Mudgett-Hunter, M., Tai, M. S., Novotný, J., Margolies, M. N., Ridge, R. J., Bruccoleri, R. E., Haber, E., & Crea, R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.16.5879 · Cited by 1,594 · see citing works

Single-Chain Antigen-Binding Proteins

Bird, R. E., Hardman, K. D., Jacobson, J. W., Johnson, S., Kaufman, B. M., Lee, S., Lee, T. T., Pope, S. H., Riordan, G. S., & Whitlow, M. D. (1988) · Science · doi:10.1126/science.3140379 · Cited by 1,509 · see citing works

The therapeutic monoclonal antibody market

Ecker, D. M., Jones, S. D., & Levine, H. L. (2014) · mAbs · doi:10.4161/19420862.2015.989042 · Cited by 1,292 · see citing works

Tumor Regression in Cancer Patients by Very Low Doses of a T Cell–Engaging Antibody

Bargou, R., Leo, E., Zugmaier, G., Klinger, M., Goebeler, M., Knop, S., Noppeney, R., Viardot, A., Hess, G., Schuler, M., et al. (2008) · Science · doi:10.1126/science.1158545 · Cited by 1,078 · see citing works

Biopharmaceutical benchmarks 2014

Walsh, G. (2014) · Nature Biotechnology · doi:10.1038/nbt.3040 · Cited by 1,008 · see citing works

Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli

Ward, E. S., Güssow, D., Griffiths, A. D., Jones, P., & Winter, G. P. (1989) · Nature · doi:10.1038/341544a0 · Cited by 1,003 · see citing works

Macromolecular Modeling with Rosetta

Das, R., & Baker, D. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062906.171838 · Cited by 995 · see citing works

Crystal Structure of a Neutralizing Human IgG Against HIV-1: A Template for Vaccine Design

Saphire, E., Parren, P., Pantophlet, R., Zwick, M., Morris, G., Rudd, P., Dwek, R., Stanfield, R., Burton, D., & Wilson, I. A. G. (2001) · Science · doi:10.1126/science.1061692 · Cited by 985 · see citing works

Anti-Inflammatory Activity of Human IgG4 Antibodies by Dynamic Fab Arm Exchange

Kolfschoten, M. V. D. N., Schuurman, J., Losen, M. H., Bleeker, W. K., Martínez‐Martínez, P., Vermeulen, E., den Bleker, T. H., Wiegman, L., Vink, T., Aarden, L. A., et al. (2007) · Science · doi:10.1126/science.1144603 · Cited by 972 · see citing works

"Diabodies": small bivalent and bispecific antibody fragments.

Holliger, P., Prospero, T. D., & Winter, G. P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6444 · Cited by 879 · see citing works

Therapeutic antibodies for autoimmunity and inflammation

Chan, A. C., & Carter, P. J. (2010) · Nature reviews. Immunology · doi:10.1038/nri2761 · Cited by 840 · see citing works

‘Knobs-into-holes’ engineering of antibody C H 3 domains for heavy chain heterodimerization

Ridgway, J. B., Presta, L. G., & Carter, P. M. (1996) · Protein Engineering Design and Selection · doi:10.1093/protein/9.7.617 · Cited by 816 · see citing works

Boosting Brain Uptake of a Therapeutic Antibody by Reducing Its Affinity for a Transcytosis Target

Yu, Y. J., Zhang, Y., Kenrick, M., Hoyte, K., Luk, W., Lu, Y., Atwal, J., Elliott, J. M., Prabhu, S., Watts, R. J., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002230 · Cited by 794 · see citing works

Industrialization of mAb production technology: The bioprocessing industry at a crossroads

Kelley, B. D. (2009) · mAbs · doi:10.4161/mabs.1.5.9448 · Cited by 668 · see citing works

Increased Brain Penetration and Potency of a Therapeutic Antibody Using a Monovalent Molecular Shuttle

Niewoehner, J., Bohrmann, B., Collin, L., Urich, E., Sade, H., Maier, P., Rueger, P., Stracke, J. O., Lau, W., Tissot, A. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2013.10.061 · Cited by 622 · see citing works

Strategies for extended serum half-life of protein therapeutics

Kontermann, R. E. (2011) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2011.06.012 · Cited by 576 · see citing works

The trifunctional antibody catumaxomab for the treatment of malignant ascites due to epithelial cancer: Results of a prospective randomized phase II/III trial

Heiss, M. M., Murawa, P., Koralewski, P., Kutarska, E., Kolesnik, O., Ivanchenko, V. V., Dudnichenko, A. S., Aleknavičienė, B., Razbadauskas, A., Gore, M. E., et al. (2010) · International Journal of Cancer · doi:10.1002/ijc.25423 · Cited by 548 · see citing works

Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme

Desmyter, A., Transue, T. R., Ghahroudi, M. A., Thi, M. H. D., Poortmans, F., HAMERS, R., Muyldermans, S., & Wyns, L. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0996-803 · Cited by 525 · see citing works

An efficient route to human bispecific IgG

Merchant, A. M., Zhu, Z., Yuan, J. Q., Goddard, A. D., Adams, C. W., Presta, L. G., & Carter, P. M. (1998) · Nature Biotechnology · doi:10.1038/nbt0798-677 · Cited by 513 · see citing works

A bispecific antibody to factors IXa and X restores factor VIII hemostatic activity in a hemophilia A model

Kitazawa, T., Igawa, T., Sampei, Z., Muto, A., Kojima, T., Soeda, T., Yoshihashi, K., Okuyama-Nishida, Y., Saito, H., Tsunoda, H., et al. (2012) · Nature Medicine · doi:10.1038/nm.2942 · Cited by 509 · see citing works

Hybrid antibodies can target sites for attack by T cells

Staerz, U. D., Kanagawa, O., & Bevan, M. J. (1985) · Nature · doi:10.1038/314628a0 · Cited by 492 · see citing works

Immunoglobulin domain crossover as a generic approach for the production of bispecific IgG antibodies

Schäfer, W. M., Regula, J. T., Bähner, M., Schanzer, J., Croasdale, R., Dürr, H., Gassner, C., Georges, G. J., Kettenberger, H., Imhof-Jung, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019002108 · Cited by 485 · see citing works

Dual targeting strategies with bispecific antibodies

Kontermann, R. E. (2012) · mAbs · doi:10.4161/mabs.4.2.19000 · Cited by 438 · see citing works

Variants of the Antibody Herceptin That Interact with HER2 and VEGF at the Antigen Binding Site

Boström, J., Yu, S., Kan, D., Appleton, B. A., Lee, C. V., Billeci, K. L., Man, W., Peale, F. V., Jr., Ross, S., Wiesmann, C., et al. (2009) · Science · doi:10.1126/science.1165480 · Cited by 372 · see citing works

Blinatumomab: A historical perspective

Nagorsen, D., Kufer, P., Baeuerle, P. A., & Bargou, R. C. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.07.013 · Cited by 356 · see citing works

A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity.

Mack, M., Riethmüller, G., & Kufer, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.15.7021 · Cited by 351 · see citing works

Simultaneous targeting of multiple disease mediators by a dual-variable-domain immunoglobulin

Wu, C., Hua, Y., Grinnell, C. M., Bryant, S. H., Miller, R., Clabbers, A., Bose, S., McCarthy, D., Zhu, R.-R., Santora, L. C., et al. (2007) · Nature Biotechnology · doi:10.1038/nbt1345 · Cited by 344 · see citing works

A Two-in-One Antibody against HER3 and EGFR Has Superior Inhibitory Activity Compared with Monospecific Antibodies

Schaefer, G., Haber, L., Crocker, L., Shia, S., Shao, L., Dowbenko, D. J., Tótpál, K., Wong, A., Lee, C. V., Stawicki, S. S., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.003 · Cited by 341 · see citing works

Efficient generation of stable bispecific IgG1 by controlled Fab-arm exchange

Labrijn, A. F., Meesters, J. I., de Goeij, B. E. C. G., van den Bremer, E. T. J., Neijssen, J., van Kampen, M. D., Strumane, K., Verploegen, S. A. B. W., Kundu, A., Gramer, M. J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220145110 · Cited by 340 · see citing works

Identification and Multidimensional Optimization of an Asymmetric Bispecific IgG Antibody Mimicking the Function of Factor VIII Cofactor Activity

Sampei, Z., Igawa, T., Soeda, T., Okuyama-Nishida, Y., Moriyama, C., Wakabayashi, T., Tanaka, E., Muto, A., Kojima, T., Kitazawa, T., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057479 · Cited by 338 · see citing works

Potent neutralization of botulinum neurotoxin by recombinant oligoclonal antibody

Nowakowski, A., Wang, C., Powers, D. B., Amersdorfer, P., Smith, T. J., Montgomery, V. A., Sheridan, R., Blake, R., Smith, L. A., & Marks, J. D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172229899 · Cited by 331 · see citing works

Improved tumor targeting of anti–epidermal growth factor receptor Nanobodies through albumin binding: taking advantage of modular Nanobody technology

Tijink, B. M., Laeremans, T., Budde, M., van Walsum, M., Dreier, T., de Haard, H., Leemans, C. R., & van Dongen, G. A. M. S. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2384 · Cited by 306 · see citing works

Formatted anti–tumor necrosis factor α VHH proteins derived from camelids show superior potency and targeting to inflamed joints in a murine model of collagen‐induced arthritis

Coppieters, K. T., Dreier, T., Silence, K., de Haard, H., Lauwereys, M., Casteels, P., Beirnaert, E., Jonckheere, H., de Wiele, C. V., Staelens, L., et al. (2006) · Arthritis & Rheumatism · doi:10.1002/art.21827 · Cited by 303 · see citing works

Camel Single-domain Antibodies as Modular Building Units in Bispecific and Bivalent Antibody Constructs

Conrath, K., Lauwereys, M., Wyns, L., & Muyldermans, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007734200 · Cited by 301 · see citing works

Selective costimulation modulation using abatacept in patients with active rheumatoid arthritis while receiving etanercept: a randomised clinical trial

Weinblatt, M. E., Schiff, M., Goldman, A. L., Kremer, J. M., Luggen, M. E., Li, T., Chen, D., & Becker, J.-C. (2006) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2006.055111 · Cited by 300 · see citing works

Therapeutic IgG4 antibodies engage in Fab-arm exchange with endogenous human IgG4 in vivo

Labrijn, A. F., Buijsse, A. O., van den Bremer, E. T. J., Verwilligen, A., Bleeker, W. K., Thorpe, S. J., Killestein, J., Polman, C. H., Aalberse, R. C., Schuurman, J., et al. (2009) · Nature Biotechnology · doi:10.1038/nbt.1553 · Cited by 297 · see citing works

Enhancing Antibody Fc Heterodimer Formation through Electrostatic Steering Effects

Gunasekaran, K., Pentony, M., Shen, M., Garrett, L., Forte, C. P., Woodward, A., Ng, S. B., Born, T. L., Retter, M. W., Manchulenko, K., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.117382 · Cited by 281 · see citing works

Recombination of a mixture of univalent antibody fragments of different specificity

Nisonoff, A., & Rivers, M. M. (1961) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(61)90296-x · Cited by 280 · see citing works

Addressing Safety Liabilities of TfR Bispecific Antibodies That Cross the Blood-Brain Barrier

Couch, J. A., Yu, Y. J., Zhang, Y., Tarrant, J. M., Fuji, R. N., Meilandt, W. J., Solanoy, H. O., Tong, R. K., Hoyte, K., Luk, W., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3005338 · Cited by 270 · see citing works

Preparation and performance of bispecific F(ab' gamma)2 antibody containing thioether-linked Fab' gamma fragments.

Glennie, M. J., McBride, H. M., Worth, A. T., & Stevenson, G. T. (1987) · The Journal of Immunology · doi:10.4049/jimmunol.139.7.2367 · Cited by 263 · see citing works

Stable heterodimers from remodeling the domain interface of a homodimer using a phage display library

Atwell, S., Ridgway, J. B., Wells, J. A., & Carter, P. M. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1116 · Cited by 262 · see citing works

Preparation of Bispecific Antibodies by Chemical Recombination of Monoclonal Immunoglobulin G 1 Fragments

Brennan, M., Davison, P. F., & Paulus, H. (1985) · Science · doi:10.1126/science.3925553 · Cited by 252 · see citing works

Monovalent antibody design and mechanism of action of onartuzumab, a MET antagonist with anti-tumor activity as a therapeutic agent

Merchant, M. A., Ma, X., Maun, H. R., Zheng, Z., Peng, J., Romero, M., Huang, A. J. Y., Yang, N.-Y., Nishimura, M. C., Greve, J. M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302725110 · Cited by 236 · see citing works

Generation of bispecific IgG antibodies by structure-based design of an orthogonal Fab interface

Lewis, S. M., Wu, X., Pustilnik, A., Sereno, A., Huang, F., Rick, H. L., Guntas, G., Leaver‐Fay, A., Smith, E. M., Ho, C., et al. (2014) · Nature Biotechnology · doi:10.1038/nbt.2797 · Cited by 234 · see citing works

Improved Pharmacokinetics of Recombinant Bispecific Antibody Molecules by Fusion to Human Serum Albumin

Müller, D., Karle, A. C., Meißburger, B., Höfig, I., Stork, R., & Kontermann, R. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700820200 · Cited by 222 · see citing works

Advances in the production and downstream processing of antibodies

Chon, J. H., & Zarbis‐Papastoitsis, G. (2011) · New Biotechnology · doi:10.1016/j.nbt.2011.03.015 · Cited by 220 · see citing works

Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting

Rossi, E. A., Goldenberg, D. M., Cardillo, T. M., McBride, W. J., Sharkey, R. M., & Chang, C.-H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600982103 · Cited by 209 · see citing works

Bispecific tandem diabody for tumor therapy with improved antigen binding and pharmacokinetics

Kipriyanov, S. M., Moldenhauer, G., Schuhmacher, J., Cochlovius, B., von der Lieth, C., Matys, E., & Little, M. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3156 · Cited by 202 · see citing works

Effector Cell Recruitment with Novel Fv-based Dual-affinity Re-targeting Protein Leads to Potent Tumor Cytolysis and in Vivo B-cell Depletion

Johnson, S., Burke, S., Huang, L., Gorlatov, S. N., Li, H., Wang, W., Zhang, W., Tuaillon, N., Rainey, G. J., Barat, B., et al. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.04.001 · Cited by 198 · see citing works

Bispecific antibodies with natural architecture produced by co-culture of bacteria expressing two distinct half-antibodies

Spiess, C., Merchant, M. A., Huang, A. J. Y., Zheng, Z., Yang, N.-Y., Peng, J., Ellerman, D. A., Shatz-Binder, W., Reilly, D. E., Yansura, D. G., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2621 · Cited by 197 · see citing works

SEEDbodies: fusion proteins based on strand-exchange engineered domain (SEED) CH3 heterodimers in an Fc analogue platform for asymmetric binders or immunofusions and bispecific antibodies†

Davis, J. H., Aperlo, C., Li, Y., Kurosawa, E., Lan, Y., Lo, K.-M., & Huston, J. S. (2010) · Protein Engineering Design and Selection · doi:10.1093/protein/gzp094 · Cited by 194 · see citing works

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. R., Balderes, P. J., Prewett, M. C., Corcoran, E., Mangalampalli, V. R. M., Bassi, R., Anselma, D. J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500815200 · Cited by 180 · see citing works

Development of humanized bispecific antibodies reactive with cytotoxic lymphocytes and tumor cells overexpressing the HER2 protooncogene.

Shalaby, M. R., Shepard, H. M., Presta, L. G., Rodrigues, M. L., Beverley, P. C. L., Feldmann, M., & Carter, P. M. (1992) · The Journal of Experimental Medicine · doi:10.1084/jem.175.1.217 · Cited by 176 · see citing works

Targeting T cells to tumor cells using bispecific antibodies

Frankel, S. R., & Baeuerle, P. A. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.03.029 · Cited by 166 · see citing works

A tale of two specificities: bispecific antibodies for therapeutic and diagnostic applications

Byrne, H., Conroy, P. J., Whisstock, J. C., & O’Kennedy, R. J. (2013) · Trends in biotechnology · doi:10.1016/j.tibtech.2013.08.007 · Cited by 159 · see citing works

A novel platform for engineering blood‐brain barrier‐crossing bispecific biologics

Farrington, G. K., Caram‐Salas, N. L., Haqqani, A. S., Brunette, E., Eldredge, J. K., Pepinsky, B., Antognetti, G., Baumann, E., Ding, W., Garber, E. A., et al. (2014) · The FASEB Journal · doi:10.1096/fj.14-253369 · Cited by 148 · see citing works

Signal amplification in molecular imaging by pretargeting a multivalent, bispecific antibody

Sharkey, R. M., Cardillo, T. M., Rossi, E. A., Chang, C., Karacay, H., McBride, W. J., Hansen, H. J., Horak, I. D., & Goldenberg, D. M. (2005) · Nature Medicine · doi:10.1038/nm1322 · Cited by 148 · see citing works

Structural and functional characterization of the trifunctional antibody catumaxomab

Chelius, D., Ruf, P., Gruber, P., Plöscher, M., Liedtke, R., Gansberger, E., Heß, J., Wasiliu, M., & Lindhofer, H. (2010) · mAbs · doi:10.4161/mabs.2.3.11791 · Cited by 145 · see citing works

Generating Bispecific Human IgG1 and IgG2 Antibodies from Any Antibody Pair

Strop, P., Ho, W.-H., Boustany, L. M., Abdiche, Y. N., Lindquist, K. C., Farias, S., Rickert, M., Appah, C. T., Pascua, E., Radcliffe, T., et al. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.04.020 · Cited by 144 · see citing works

Antibody VH Domains as Small Recognition Units

Davies, J., & Riechmann, L. (1995) · Nature Biotechnology · doi:10.1038/nbt0595-475 · Cited by 141 · see citing works

Phase I trial of 2B1, a bispecific monoclonal antibody targeting c-erbB-2 and Fc gamma RIII.

Weiner, L. M., Clark, J. I., Davey, M., Li, W. S., de Palazzo, I. G., Ring, D. B., & Alpaugh, R. K. (1995) · PubMed · Cited by 139 · see citing works

Antibody therapeutics, antibody engineering, and the merits of protein stability.

Demarest, S. J., & Glaser, S. (2008) · PubMed · Cited by 131 · see citing works

Chemical generation of bispecific antibodies

Doppalapudi, V. R., Huang, J., Liu, D., Jin, P., Liu, B., Li, L., Desharnais, J., van Hagen, C., Levin, N. J., Shields, M. J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016478108 · Cited by 124 · see citing works

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. L., Persaud, A., Jimenez, X., Burtrum, D. B., Balderes, P. J., Liu, M., Böhlen, P., Witte, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310132200 · Cited by 124 · see citing works

Improving biophysical properties of a bispecific antibody scaffold to aid developability

von Kreudenstein, T. S., Escobar-Cabrera, E., Lario, P. I., D’Angelo, I., Brault, K., Kelly, J. F., Durocher, Y., Baardsnes, J., Woods, R. J., Xie, M. H., et al. (2013) · mAbs · doi:10.4161/mabs.25632 · Cited by 123 · see citing works

Advantages of bispecific hybridomas in one-step immunocytochemistry and immunoassays.

Suresh, M. R., Cuello, A. C., & Milstein, C. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.20.7989 · Cited by 117 · see citing works

Human Domain Antibodies against Virulence Traits ofCandida albicansInhibit Fungus Adherence to Vaginal Epithelium and Protect against Experimental Vaginal Candidiasis

Bernardis, F. D., Liu, H., O’Mahony, R., Valle, R. L., Bartollino, S., Sandini, S., Grant, S., Brewis, N., Tomlinson, I. M., Basset, R. C., et al. (2006) · The Journal of Infectious Diseases · doi:10.1086/509891 · Cited by 114 · see citing works

Engineering Aggregation-Resistant Antibodies

Perchiacca, J. M., & Tessier, P. M. (2012) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-062011-081052 · Cited by 114 · see citing works

A novel tri-functional antibody fusion protein with improved pharmacokinetic properties generated by fusing a bispecific single-chain diabody with an albumin-binding domain from streptococcal protein G

Stork, R., Müller, D., & Kontermann, R. E. (2007) · Protein Engineering Design and Selection · doi:10.1093/protein/gzm061 · Cited by 111 · see citing works

Bispecific Designed Ankyrin Repeat Proteins (DARPins) Targeting Epidermal Growth Factor Receptor Inhibit A431 Cell Proliferation and Receptor Recycling

Boersma, Y. L., Chao, G., Steiner, D., Wittrup, K. D., & Plückthun, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.293266 · Cited by 111 · see citing works

Sustained protection against Ebola virus infection following treatment of infected nonhuman primates with ZMAb

Qiu, X., Audet, J., Wong, G., Fernando, L., Bello, A., Pillet, S., Alimonti, J. B., & Kobinger, G. P. (2013) · Scientific Reports · doi:10.1038/srep03365 · Cited by 106 · see citing works

Engineered proteins with desired specificity: DARPins, other alternative scaffolds and bispecific IgGs

Jost, C., & Plückthun, A. (2014) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.05.011 · Cited by 105 · see citing works

A novel bispecific antibody format enables simultaneous bivalent and monovalent co-engagement of distinct target antigens

Moore, G. L., Bautista, C., Pong, E., Nguyen, D.-H. T., Jacinto, J. M., Eivazi, A., Muchhal, U. S., Karki, S., Chu, S. Y., & Lazar, G. A. (2011) · mAbs · doi:10.4161/mabs.3.6.18123 · Cited by 104 · see citing works

A modular IgG-scFv bispecific antibody topology

Orcutt, K. D., Ackerman, M. E., Cieslewicz, M., Quiroz, E., Slusarczyk, A. L., Frangioni, J. V., & Wittrup, K. D. (2009) · Protein Engineering Design and Selection · doi:10.1093/protein/gzp077 · Cited by 101 · see citing works

Molecular construction and optimization of anti-human IL-1α/β dual variable domain immunoglobulin (DVD-IgTM) molecules

Wu, C., Hua, Y., Bose, S., Miller, R., Medina, L., Santora, L. C., & Ghayur, T. (2009) · mAbs · doi:10.4161/mabs.1.4.8755 · Cited by 94 · see citing works

Cure of Burkitt's lymphoma in severe combined immunodeficiency mice by T cells, tetravalent CD3 x CD19 tandem diabody, and CD28 costimulation.

Cochlovius, B., Kipriyanov, S. M., Stassar, M. J. J. G., Schuhmacher, J., Benner, A., Moldenhauer, G., & Little, M. (2000) · PubMed · Cited by 91 · see citing works

Rational identification of an optimal antibody mixture for targeting the epidermal growth factor receptor

Koefoed, K., Steinaa, L., Søderberg, J. N., Kjær, I., Jacobsen, H. J., Meijer, P., Haurum, J. S., Jensen, A. D., Kragh, M., Andersen, P. S., et al. (2011) · mAbs · doi:10.4161/mabs.3.6.17955 · Cited by 91 · see citing works

Development of a Two-part Strategy to Identify a Therapeutic Human Bispecific Antibody That Inhibits IgE Receptor Signaling

Jackman, J. K., Chen, Y., Huang, A. J. Y., Moffat, B., Scheer, J. M., Leong, S. R., Lee, W. P., Zhang, J., Sharma, N., Lu, Y., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113910 · Cited by 91 · see citing works

The Design and Characterization of Oligospecific Antibodies for Simultaneous Targeting of Multiple Disease Mediators

Dimasi, N., Gao, C., Fleming, R. L., Woods, R. M., Yao, X.-T., Shirinian, L., Kiener, P. A., & Wu, H. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.08.032 · Cited by 90 · see citing works

Recombinant approaches to IgG-like bispecific antibodies

Marvin, J. S., & Zhu, Z. (2005) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2005.00119.x · Cited by 87 · see citing works

Remodeling domain interfaces to enhance heterodimer formation

Zhu, Z., Presta, L. G., Zapata, G. A., & Carter, P. M. (1997) · Protein Science · doi:10.1002/pro.5560060404 · Cited by 87 · see citing works

Symmetry breaking: bispecific antibodies, the beginnings, and 50 years on.

Riethmüller, G. (2012) · Europe PMC (PubMed Central) · Cited by 85 · see citing works

A Bispecific Diabody That Mediates Natural Killer Cell Cytotoxicity Against Xenotransplantated Human Hodgkin’s Tumors

Arndt, M. A. E., Krauß, J., Kipriyanov, S. M., Pfreundschuh, M. G., & Little, M. (1999) · Blood · doi:10.1182/blood.v94.8.2562.420k20_2562_2568 · Cited by 85 · see citing works

ImmTAC-redirected tumour cell killing induces and potentiates antigen cross-presentation by dendritic cells

Bossi, G., Buisson, S., Oates, J., Jakobsen, B. K., & Hassan, N. J. (2014) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-014-1525-z · Cited by 80 · see citing works

Four-in-One Antibodies Have Superior Cancer Inhibitory Activity against EGFR, HER2, HER3, and VEGF through Disruption of HER/MET Crosstalk

Hu, S., Fu, W., Xu, W., Yang, Y., Cruz, M., Berezov, S. D., Jorissen, D., Takeda, H., & Zhu, W. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-1670 · Cited by 80 · see citing works

Retargeting serum immunoglobulin with bispecific diabodies

Holliger, P., Wing, M. G., Pound, J. D., Bohlen, H., & Winter, G. P. (1997) · Nature Biotechnology · doi:10.1038/nbt0797-632 · Cited by 79 · see citing works

The Dock and Lock Method: A Novel Platform Technology for Building Multivalent, Multifunctional Structures of Defined Composition with Retained Bioactivity

Chang, C., Rossi, E. A., & Goldenberg, D. M. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1217 · Cited by 78 · see citing works

Novel tetravalent and bispecific IgG‐like antibody molecules combining single‐chain diabodies with the immunoglobulin γ1 Fc or CH3 region

Alt, M., Müller, R., & Kontermann, R. E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00782-6 · Cited by 77 · see citing works

Recombinant Bispecific Monoclonal Antibodies Prepared by the Dock-and-Lock Strategy for Pretargeted Radioimmunotherapy

Sharkey, R. M., Rossi, E. A., McBride, W. J., Chang, C., & Goldenberg, D. M. (2010) · Seminars in Nuclear Medicine · doi:10.1053/j.semnuclmed.2009.12.002 · Cited by 77 · see citing works

Humoral response to catumaxomab correlates with clinical outcome: Results of the pivotal phase II/III study in patients with malignant ascites

Ott, M., Marmé, F., Moldenhauer, G., Lindhofer, H., Hennig, M., Spannagl, R., Essing, M. M., Linke, R., & Seimetz, D. (2011) · International Journal of Cancer · doi:10.1002/ijc.26258 · Cited by 77 · see citing works

A Novel Antibody Engineering Strategy for Making Monovalent Bispecific Heterodimeric IgG Antibodies by Electrostatic Steering Mechanism

Liu, Z., Leng, E. C., Gunasekaran, K., Pentony, M., Shen, M., Howard, M., Stoops, J. D., Manchulenko, K., Razinkov, V. I., Liu, H., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.620260 · Cited by 75 · see citing works

Bispecific antibodies for delivery into the brain

Watts, R. J., & Dennis, M. S. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.03.023 · Cited by 74 · see citing works

Novel asymmetrically engineered antibody Fc variant with superior FcγR binding affinity and specificity compared with afucosylated Fc variant

Mimoto, F., Igawa, T., Kuramochi, T., Katada, H., Kadono, S., Kamikawa, T., Shida-Kawazoe, M., & Hattori, K. (2013) · mAbs · doi:10.4161/mabs.23452 · Cited by 74 · see citing works

A fibronectin scaffold approach to bispecific inhibitors of epidermal growth factor receptor and insulin-like growth factor-I receptor

Emanuel, S. L., Engle, L. J., Chao, G., Zhu, R.-R., Cao, C., Lin, Z., Yamniuk, A. P., Hosbach, J., Brown, J. M., Fitzpatrick, E., et al. (2011) · mAbs · doi:10.4161/mabs.3.1.14168 · Cited by 72 · see citing works

Hexavalent bispecific antibodies represent a new class of anticancer therapeutics: 1. Properties of anti-CD20/CD22 antibodies in lymphoma

Rossi, E. A., Goldenberg, D. M., Cardillo, T. M., Stein, R., & Chang, C. (2009) · Blood · doi:10.1182/blood-2008-10-187138 · Cited by 72 · see citing works

Structure reveals function of the dual variable domain immunoglobulin (DVD-Ig™) molecule

Jakob, C. G., Edalji, R. P., Judge, R. A., DiGiammarino, E. L., Li, Y., Gu, J., & Ghayur, T. (2013) · mAbs · doi:10.4161/mabs.23977 · Cited by 72 · see citing works

Development of a Human IgG4 Bispecific Antibody for Dual Targeting of Interleukin-4 (IL-4) and Interleukin-13 (IL-13) Cytokines

Spiess, C., Bevers, J. J., Jackman, J. K., Chiang, N., Nakamura, G. R., Dillon, M. A., Liu, H., Molina, P., Elliott, J. M., Shatz-Binder, W., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.480483 · Cited by 71 · see citing works

Bispecific digoxigenin-binding antibodies for targeted payload delivery

Metz, S., Haas, A. K., Daub, K., Croasdale, R., Stracke, J. O., Lau, W., Georges, G. J., Josel, H., Dziadek, S., Hopfner, K., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018565108 · Cited by 68 · see citing works

Engineering and characterization of a bispecific HER2 × EGFR‐binding affibody molecule

Friedman, M., Lindström, S., Ekerljung, L., Svahn, H. A., Carlsson, J., Brismar, H., Gedda, L., Frejd, F. Y., & Ståhl, S. (2009) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20090096 · Cited by 65 · see citing works

Safety and Pharmacokinetics of XOMA 3AB, a Novel Mixture of Three Monoclonal Antibodies against Botulinum Toxin A

Nayak, S., Griffiss, J. M., McKenzie, R., Fuchs, E. J., Jurao, R. A., An, A. T., Ahene, A. B., Tomic, M. T., Hendrix, C. W., & Zenilman, J. M. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02830-14 · Cited by 62 · see citing works

Chemically programmed antibodies: Endothelin receptor targeting CovX-Bodies™

Doppalapudi, V. R., Tryder, N., Li, L., Aja, T., Griffith, D. A., Liao, F., Roxas, G., Ramprasad, M. P., Bradshaw, C. W., & Barbas, C. F. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.10.009 · Cited by 59 · see citing works

Engineering of stable bispecific antibodies targeting IL-17A and IL-23

Mabry, R., Lewis, K. E., Moore, M. D., McKernan, P. A., Bukowski, T. R., Bontadelli, K., Brender, T., Okada, S. L., Lum, K. D., West, J. W., et al. (2009) · Protein Engineering Design and Selection · doi:10.1093/protein/gzp073 · Cited by 59 · see citing works

A Novel Glycoengineered Bispecific Antibody Format for Targeted Inhibition of Epidermal Growth Factor Receptor (EGFR) and Insulin-like Growth Factor Receptor Type I (IGF-1R) Demonstrating Unique Molecular Properties

Schanzer, J. M., Wartha, K., Croasdale, R., Moser, S., Künkele, K., Ries, C. H., Scheuer, W., Dürr, H., Pompiati, S., Pollman, J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.528109 · Cited by 58 · see citing works

DARPins as Bispecific Receptor Antagonists Analyzed for Immunoglobulin E Receptor Blockage

Eggel, A., Baumann, M. J., Amstutz, P., Stadler, B. M., & Vogel, M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.08.014 · Cited by 58 · see citing works

World Bispecific Antibody Summit, September 27–28, 2011, Boston, MA

Dhimolea, E., & Reichert, J. M. (2012) · mAbs · doi:10.4161/mabs.4.1.18821 · Cited by 56 · see citing works

Building novel binding ligands to B7.1 and B7.2 based on human antibody single variable light chain domains 1 1Edited by I. A. Wilson

van den Beucken, T., van Neer, N., Sablon, E., Desmet, J., Celis, L., Hoogenboom, H. R., & Hufton, S. E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4703 · Cited by 54 · see citing works

Contributions of a Highly Conserved VH/VL Hydrogen Bonding Interaction to scFv Folding Stability and Refolding Efficiency

Tan, P., Sandmaier, B. M., & Stayton, P. S. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)74066-4 · Cited by 52 · see citing works

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. L., Böhlen, P., Witte, L., & Zhu, Z. (2001) · PubMed · Cited by 49 · see citing works

Development of tetravalent IgG1 dual targeting IGF-1R–EGFR antibodies with potent tumor inhibition

Croasdale, R., Wartha, K., Schanzer, J. M., Kuenkele, K. P., Ries, C. H., Mayer, K., Gassner, C., Wagner, M., Dimoudis, N., Herter, S., et al. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.03.016 · Cited by 48 · see citing works

Monoclonal antibody therapeutics with up to five specificities: Functional enhancement through fusion of target-specific peptides

LaFleur, D. W., Abramyan, D., Kanakaraj, P., Smith, R. G., Shah, R. R., Wang, G., Yao, X.-T., Kankanala, S., Boyd, E., Zaritskaya, L., et al. (2013) · mAbs · doi:10.4161/mabs.23043 · Cited by 48 · see citing works

ImmTACs

Oates, J., & Jakobsen, B. K. (2013) · OncoImmunology · doi:10.4161/onci.22891 · Cited by 45 · see citing works

A Bispecific Antibody-IFNα2b Immunocytokine Targeting CD20 and HLA-DR Is Highly Toxic to Human Lymphoma and Multiple Myeloma Cells

Rossi, E. A., Rossi, D. L., Stein, R., Goldenberg, D. M., & Chang, C. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2126 · Cited by 45 · see citing works

The structure of dual-variable-domain immunoglobulin molecules alone and bound to antigen

Correia, I., Sung, J. J., Burton, R. E., Jakob, C. G., Carragher, B. O., Ghayur, T., & Radziejewski, C. H. (2013) · mAbs · doi:10.4161/mabs.24258 · Cited by 43 · see citing works

Consistent manufacturing and quality control of a highly complex recombinant polyclonal antibody product for human therapeutic use

Frandsen, T. P., Næsted, H., Rasmussen, S. K., Hauptig, P., Wiberg, F. C., Rasmussen, L. K., Jensen, A. M. V., Persson, P., Wikén, M., Engström, A., et al. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.23166 · Cited by 43 · see citing works

LUZ-Y, a Novel Platform for the Mammalian Cell Production of Full-length IgG-bispecific Antibodies

Wranik, B. J., Christensen, E., Schaefer, G., Jackman, J. K., Vendel, A. C., & Eaton, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.397869 · Cited by 40 · see citing works

Recombinant Human Polyclonal Antibodies: A New Class of Therapeutic Antibodies Against Viral Infections

Bregenholt, S., Jensen, A. D., Lantto, J., Hyldig, S. M. W., & Haurum, J. S. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206777442173 · Cited by 39 · see citing works

VH/VL interface engineering to promote selective expression and inhibit conformational isomerization of thrombopoietin receptor agonist single-chain diabody

Igawa, T., Tsunoda, H., Kikuchi, Y., Yoshida, M., Tanaka, M., Koga, A., Sekimori, Y., Orita, T., Aso, Y., Hattori, K., et al. (2010) · Protein Engineering Design and Selection · doi:10.1093/protein/gzq034 · Cited by 36 · see citing works

Monospecific bivalent scFv-SH: Effects of linker length and location of an engineered cysteine on production, antigen binding activity and free SH accessibility

Albrecht, H., DeNardo, G. L., & DeNardo, S. J. (2006) · Journal of Immunological Methods · doi:10.1016/j.jim.2005.12.012 · Cited by 35 · see citing works

Crystal Structure of an Anti-Ang2 CrossFab Demonstrates Complete Structural and Functional Integrity of the Variable Domain

Fenn, S., Schiller, C., Griese, J. J., Dürr, H., Imhof-Jung, S., Gassner, C., Moelleken, J., Regula, J. T., Schäfer, W. M., Thomas, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061953 · Cited by 34 · see citing works

Sequential affinity purification of peroxidase tagged bispecific anti-SARS-CoV antibodies on phenylboronic acid agarose

Bhatnagar, P. K., Das, D., & Suresh, M. R. (2008) · Journal of Chromatography B · doi:10.1016/j.jchromb.2008.01.003 · Cited by 25 · see citing works

Treatment of refractory Hodgkin's disease with an anti-CD16/CD30 bispecific antibody

Renner, C., Hartmann, F., & Pfreundschuh, M. G. (1997) · Cancer Immunology Immunotherapy · doi:10.1007/s002620050428 · Cited by 24 · see citing works

A New Method to Generate Quadromas by Electrofusion and FACS Sorting

Kreutz, F., XU, D. Z., & Suresh, M. R. (1998) · Hybridoma · doi:10.1089/hyb.1998.17.267 · Cited by 18 · see citing works

Radiocurability by Targeting Tumor Necrosis Factor-α Using a Bispecific Antibody in Carcinoembryonic Antigen Transgenic Mice

Larbouret, C., Robert, B., Linard, C., Navarro‐Teulon, I., Gourgou, S., Bibeau, F., Martineau, P., Santoro, L., Pouget, J., Pèlegrin, A., et al. (2007) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2007.07.2372 · Cited by 14 · see citing works

Bispecific antibodies: a mechanistic review of the pipeline

Labrijn, A. F., Janmaat, M. L., Reichert, J. M., & Parren, P. W. H. I. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0028-1 · Cited by 1,303 · see citing works

The making of bispecific antibodies

Brinkmann, U., & Kontermann, R. E. (2017) · mAbs · doi:10.1080/19420862.2016.1268307 · Cited by 933 · see citing works

Next generation antibody drugs: pursuit of the 'high-hanging fruit'

Carter, P. J., & Lazar, G. A. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.227 · Cited by 760 · see citing works

Immunotherapy for glioma: Current management and future application

Xu, S., Tang, L., Li, X., Fan, F., & Liu, Z. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.02.002 · Cited by 747 · see citing works

T cell-engaging therapies — BiTEs and beyond

Goebeler, M.-E., & Bargou, R. C. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0347-5 · Cited by 658 · see citing works

Antibody Structure and Function: The Basis for Engineering Therapeutics

Chiu, M. L., Goulet, D. R., Teplyakov, A., & Gilliland, G. L. (2019) · Antibodies · doi:10.3390/antib8040055 · Cited by 646 · see citing works

NK cell-mediated antibody-dependent cellular cytotoxicity in cancer immunotherapy

Wang, W. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00368 · Cited by 573 · see citing works

Nanobodies and nanobody-based human heavy chain antibodies as antitumor therapeutics

Bannas, P., Hambach, J., & Koch-Nolte, F. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01603 · Cited by 572 · see citing works

Multifunctional Natural Killer Cell Engagers Targeting NKp46 Trigger Protective Tumor Immunity

Gauthier, L., Morel, A., Anceriz, N., Rossi, B., Blanchard-Alvarez, A., Grondin, G., Trichard, S., Cesari, C., Sapet, M., Bosco, F., et al. (2019) · Cell · doi:10.1016/j.cell.2019.04.041 · Cited by 444 · see citing works

mRNA therapeutics in cancer immunotherapy

Beck, J. D., Reidenbach, D., Salomon, N., Sahin, U., Türeci, Ö., Vormehr, M., & Kranz, L. M. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01348-0 · Cited by 385 · see citing works

Effector-attenuating Substitutions That Maintain Antibody Stability and Reduce Toxicity in Mice

Lo, M., Kim, H. S., Tong, R. K., Bainbridge, T. W., Vernes, J.-M., Zhang, Y., Lin, Y. L., Chung, S., Dennis, M. S., Zuchero, Y. J. Y., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.767749 · Cited by 312 · see citing works

Considerations for the Design of Antibody-Based Therapeutics

Goulet, D. R., & Atkins, W. M. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.05.031 · Cited by 305 · see citing works

Tutorial on monoclonal antibody pharmacokinetics and its considerations in early development

Ovacik, M., & Lin, K. (2018) · Clinical and Translational Science · doi:10.1111/cts.12567 · Cited by 299 · see citing works

Bispecific antibodies: design, therapy, perspectives

Sedykh, S. E., Prinz, V. Y., Buneva, V. N., & Nevinsky, G. A. (2018) · Drug Design Development and Therapy · doi:10.2147/dddt.s151282 · Cited by 292 · see citing works

Elimination of large tumors in mice by mRNA-encoded bispecific antibodies

Stadler, C. R., Bähr-Mahmud, H., Celik, L., Hebich, B., Roth, A. S., Roth, R. P., Karikó, K., Türeci, Ö., & Sahin, U. (2017) · Nature Medicine · doi:10.1038/nm.4356 · Cited by 290 · see citing works

Antibody or Antibody Fragments: Implications for Molecular Imaging and Targeted Therapy of Solid Tumors

Xenaki, K. T., Oliveira, S., & Henegouwen, P. M. P. V. B. E. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01287 · Cited by 290 · see citing works

Bispecific antibodies and their applications

Fan, G., Wang, Z., Hao, M., & Li, J. (2015) · Journal of Hematology & Oncology · doi:10.1186/s13045-015-0227-0 · Cited by 289 · see citing works

Catch me if you can: Leukemia Escape after CD19-Directed T Cell Immunotherapies

Ruella, M., & Maus, M. V. (2016) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2016.09.003 · Cited by 285 · see citing works

Current progress in innovative engineered antibodies

Strohl, W. R. (2017) · Protein & Cell · doi:10.1007/s13238-017-0457-8 · Cited by 282 · see citing works

NK-mediated antibody-dependent cell-mediated cytotoxicity in solid tumors: biological evidence and clinical perspectives

Nigro, C. L., Macagno, M., Sangiolo, D., Bertolaccini, L., Aglietta, M., & Merlano, M. C. (2019) · Annals of Translational Medicine · doi:10.21037/atm.2019.01.42 · Cited by 273 · see citing works

CARs versus BiTEs: A Comparison between T Cell–Redirection Strategies for Cancer Treatment

Slaney, C. Y., Wang, P., Darcy, P. K., & Kershaw, M. H. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0297 · Cited by 231 · see citing works

Monoclonal antibody therapy of solid tumors: clinical limitations and novel strategies to enhance treatment efficacy

Cruz, E., & Kayser, V. (2019) · Biologics · doi:10.2147/btt.s166310 · Cited by 233 · see citing works

Challenges and opportunities for non-antibody scaffold drugs

Vazquez-Lombardi, R., Phan, T. G., Zimmermann, C., Lowe, D., Jermutus, L., & Christ, D. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.09.004 · Cited by 226 · see citing works

New immune cell engagers for cancer immunotherapy

Fenis, A., Demaria, O., Gauthier, L., Vivier, É., & Narni-Mancinelli, É. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-023-00982-7 · Cited by 212 · see citing works

How mRNA therapeutics are entering the monoclonal antibody field

Van Hoecke, L., & Roose, K. (2019) · Journal of Translational Medicine · doi:10.1186/s12967-019-1804-8 · Cited by 205 · see citing works

Opportunities for therapeutic antibodies directed at G-protein-coupled receptors

Hutchings, C. J., Koglin, M., Olson, W. C., & Marshall, F. H. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.91 · Cited by 198 · see citing works

Bispecific T-cell engagers: Towards understanding variables influencing the in vitro potency and tumor selectivity and their modulation to enhance their efficacy and safety

Ellerman, D. A. (2018) · Methods · doi:10.1016/j.ymeth.2018.10.026 · Cited by 197 · see citing works

Emerging Strategies for Developing Next-Generation Protein Therapeutics for Cancer Treatment

Kintzing, J. R., Interrante, M. V. F., & Cochran, J. R. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.10.005 · Cited by 192 · see citing works

The use of CrossMAb technology for the generation of bi- and multispecific antibodies

Klein, C., Schäfer, W. M., & Regula, J. T. (2016) · mAbs · doi:10.1080/19420862.2016.1197457 · Cited by 186 · see citing works

Redirecting T cells to hematological malignancies with bispecific antibodies

Velasquez, M. P., Bonifant, C. L., & Gottschalk, S. M. (2017) · Blood · doi:10.1182/blood-2017-06-741058 · Cited by 174 · see citing works

Antibody therapeutics and immunoregulation in cancer and autoimmune disease

Yasunaga, M. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.06.001 · Cited by 164 · see citing works

A novel, native-format bispecific antibody triggering T-cell killing of B-cells is robustly active in mouse tumor models and cynomolgus monkeys

Smith, E., Olson, K., Haber, L., Varghese, B., Duramad, P., Tustian, A. D., Oyejide, A., Kirshner, J. R., Canova, L., Menon, J., et al. (2015) · Scientific Reports · doi:10.1038/srep17943 · Cited by 167 · see citing works

Engineering antibody therapeutics

Chiu, M. L., & Gilliland, G. L. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.07.012 · Cited by 165 · see citing works

Bi-specific and tri-specific antibodies- the next big thing in solid tumor therapeutics

Runcie, K. D., Budman, D. R., John, V. S., & Seetharamu, N. (2018) · Molecular Medicine · doi:10.1186/s10020-018-0051-4 · Cited by 161 · see citing works

Antibody Engineering for Pursuing a Healthier Future

Saeed, A. F. U. H., Wang, R., Ling, S., & Wang, S. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00495 · Cited by 154 · see citing works

T cell engaging bispecific antibody (T-BsAb): From technology to therapeutics

Wu, Z., & Cheung, N. V. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.08.005 · Cited by 151 · see citing works

Recent advances of bispecific antibodies in solid tumors

Yu, S., Li, A., Liu, Q., Yuan, X., Xu, H., Jiao, D., Pestell, R. G., Han, X., & Wu, K. (2017) · Journal of Hematology & Oncology · doi:10.1186/s13045-017-0522-z · Cited by 151 · see citing works

Selective Blockade of the Ubiquitous Checkpoint Receptor CD47 Is Enabled by Dual-Targeting Bispecific Antibodies

Dheilly, E., Moine, V., Broyer, L., Salgado-Pires, S., Johnson, Z., Papaioannou, A., Cons, L., Calloud, S., Majocchi, S., Nelson, R. J., et al. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2016.11.006 · Cited by 146 · see citing works

Bispecific Anti-HIV-1 Antibodies with Enhanced Breadth and Potency

Bournazos, S., Gazumyan, A., Seaman, M. S., Nussenzweig, M. C., & Ravetch, J. V. (2016) · Cell · doi:10.1016/j.cell.2016.04.050 · Cited by 146 · see citing works

Engineering therapeutic bispecific antibodies using CrossMab technology

Klein, C., Schäfer, W. M., Regula, J. T., Dumontet, C., Brinkmann, U., Bacac, M., & Umaña, P. (2018) · Methods · doi:10.1016/j.ymeth.2018.11.008 · Cited by 145 · see citing works

Current methods for the synthesis of homogeneous antibody–drug conjugates

Sochaj, A. M., Świderska, K. W., & Otlewski, J. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.05.001 · Cited by 142 · see citing works

Natural killer cell engagers in cancer immunotherapy: Next generation of immuno‐oncology treatments

Demaria, O., Gauthier, L., Debroas, G., & Vivier, É. (2021) · European Journal of Immunology · doi:10.1002/eji.202048953 · Cited by 144 · see citing works

Decoding mechanisms by which silent codon changes influence protein biogenesis and function

Bali, V., & Bebok, Z. M. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.03.011 · Cited by 133 · see citing works

mRNA as novel technology for passive immunotherapy

Schlake, T., Theß, A., Thran, M., & Jordan, I. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2935-4 · Cited by 132 · see citing works

Increased Tumor Penetration of Single-Domain Antibody–Drug Conjugates Improves <i>In Vivo</i> Efficacy in Prostate Cancer Models

Nessler, I., Khera, E., Vance, S., Kopp, A., Qiu, Q., Keating, T. A., Abu-Yousif, A. O., Sandal, T., Legg, J., Thompson, L., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-2295 · Cited by 128 · see citing works

Enhanced tumor-targeting selectivity by modulating bispecific antibody binding affinity and format valence

Mazor, Y., Sachsenmeier, K. F., Yang, C., Hansen, A. M., Filderman, J. N., Mulgrew, K. A., Wu, H., & Dall’Acqua, W. F. (2017) · Scientific Reports · doi:10.1038/srep40098 · Cited by 128 · see citing works

Antibody Fragments as Potential Biopharmaceuticals for Cancer Therapy: Success and Limitations

Kholodenko, R. V., Kalinovsky, D. V., Doronin, I. I., Ponomarev, E. D., & Kholodenko, I. V. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867324666170817152554 · Cited by 126 · see citing works

Antibody and antibody fragments for cancer immunotherapy

Chen, W., Yang, Y., & Jiang, X. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.08.021 · Cited by 120 · see citing works

Comparison of biosensor platforms in the evaluation of high affinity antibody-antigen binding kinetics

Yang, D., Singh, A., Wu, H., & Kroe-Barrett, R. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.06.024 · Cited by 120 · see citing works

Generation of T-cell-redirecting bispecific antibodies with differentiated profiles of cytokine release and biodistribution by CD3 affinity tuning

Haber, L., Olson, K., Kelly, M. P., Crawford, A., DiLillo, D. J., Tavaré, R., Ullman, E., Mao, S., Canova, L., Sineshchekova, O., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-93842-0 · Cited by 120 · see citing works

Metal-Organic Framework Nanoparticle-Based Biomineralization: A New Strategy toward Cancer Treatment

Chu, C., Su, M., Zhu, J. X., Li, D., Cheng, H., Chen, X. S., & Liu, G. (2019) · Theranostics · doi:10.7150/thno.33539 · Cited by 118 · see citing works

Expanding the Boundaries of Biotherapeutics with Bispecific Antibodies

Husain, B., & Ellerman, D. A. (2018) · BioDrugs · doi:10.1007/s40259-018-0299-9 · Cited by 116 · see citing works

A “Trojan horse” bispecific-antibody strategy for broad protection against ebolaviruses

Wec, A. Z., Nyakatura, E. K., Herbert, A. S., Howell, K. A., Holtsberg, F. W., Bakken, R. R., Mittler, E., Christin, J. R., Shulenin, S., Jangra, R. K., et al. (2016) · Science · doi:10.1126/science.aag3267 · Cited by 113 · see citing works

An FDA oncology analysis of CD3 bispecific constructs and first-in-human dose selection

Saber, H., Valle, P. D., Ricks, T. K., & Leighton, J. K. (2017) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2017.09.001 · Cited by 108 · see citing works

The development of bispecific antibodies and their applications in tumor immune escape

Zhang, X., Yang, Y., Fan, D., & Xiong, D. (2017) · Experimental Hematology and Oncology · doi:10.1186/s40164-017-0072-7 · Cited by 108 · see citing works

When liposomes met antibodies: Drug delivery and beyond

Di, J., Xie, F., & Xu, Y. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.09.003 · Cited by 107 · see citing works

Fc Engineering for Developing Therapeutic Bispecific Antibodies and Novel Scaffolds

Liu, H.-Y., Saxena, A., Sidhu, S., & Wu, D.-H. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00038 · Cited by 109 · see citing works

Limitations and opportunities for immune checkpoint inhibitors in pediatric malignancies

Park, J. A., & Cheung, N. V. (2017) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2017.05.006 · Cited by 103 · see citing works

New emerging targets in cancer immunotherapy: the role of TIM3

Friedlaender, A., Addeo, A., & Banna, G. L. (2019) · ESMO Open · doi:10.1136/esmoopen-2019-000497 · Cited by 103 · see citing works

Cellular cytotoxicity is a form of immunogenic cell death

Minute, L., Teijeira, Á., Sánchez-Paulete, A. R., Ochoa, M. C., Álvarez, M., Otano, I., Etxeberría, I., Bolaños, E., Azpilikueta, A., Garasa, S., et al. (2020) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2019-000325 · Cited by 101 · see citing works

Breast cancer immunotherapy: Current and novel approaches

Barzaman, K., Moradi‐Kalbolandi, S., Hosseinzadeh, A., Kazemi, M. H., Khorramdelazad, H., Safari, E., & Farahmand, L. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107886 · Cited by 100 · see citing works

Principles and Current Clinical Landscape of Multispecific Antibodies against Cancer

Elshiaty, M., Schindler, H., & Christopoulos, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115632 · Cited by 98 · see citing works

PD-L1/LAG-3 bispecific antibody enhances tumor-specific immunity

Jiang, H., Ni, H., Zhang, P., Guo, X., Wu, M., Shen, H., Wang, J., Wu, W., Wu, Z., Ding, J., et al. (2021) · OncoImmunology · doi:10.1080/2162402x.2021.1943180 · Cited by 99 · see citing works

Dengue virus neutralizing antibody: a review of targets, cross-reactivity, and antibody-dependent enhancement

Sarker, A., Dhama, N., & Gupta, T. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1200195 · Cited by 104 · see citing works

Coming-of-Age of Antibodies in Cancer Therapeutics

Ayyar, B. V., Arora, S., & O’Kennedy, R. J. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.09.005 · Cited by 96 · see citing works

High concentration formulation developability approaches and considerations

Zarzar, J., Khan, T. A., Bhagawati, M., Weiche, B., Sydow-Andersen, J., & Sreedhara, A. (2023) · mAbs · doi:10.1080/19420862.2023.2211185 · Cited by 94 · see citing works

Immunoglobulin Fc Heterodimer Platform Technology: From Design to Applications in Therapeutic Antibodies and Proteins

Ha, J.-H., Kim, J.-E., & Kim, Y. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00394 · Cited by 92 · see citing works

Fifty years of monoclonals: the past, present and future of antibody therapeutics

Chan, A. C., Martyn, G. D., & Carter, P. J. (2025) · Nature reviews. Immunology · doi:10.1038/s41577-025-01207-9 · Cited by 96 · see citing works

Recent advances and challenges of bispecific antibodies in solid tumors

Wu, Y., Yi, M., Zhu, S., Wang, H., & Wu, K. (2021) · Experimental Hematology and Oncology · doi:10.1186/s40164-021-00250-1 · Cited by 89 · see citing works

Bispecific, T-Cell-Recruiting Antibodies in B-Cell Malignancies

Lejeune, M., Köse, M. C., Duray, E., Einsele, H., Beguin, Y. P., & Caers, J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00762 · Cited by 87 · see citing works

Perspective: Designing T-Cell Engagers With Better Therapeutic Windows

Vafa, O., & Trinklein, N. D. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00446 · Cited by 82 · see citing works

Combination Therapy with Bispecific Antibodies and PD-1 Blockade Enhances the Antitumor Potency of T Cells

Chang, C., Wang, Y., Li, R., Rossi, D. L., Liu, D., Rossi, E. A., Cardillo, T. M., & Goldenberg, D. M. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-3431 · Cited by 86 · see citing works

Bispecific antibodies and CARs: generalized immunotherapeutics harnessing T cell redirection

Zhukovsky, E. A., Morse, R. J., & Maus, M. V. (2016) · Current Opinion in Immunology · doi:10.1016/j.coi.2016.02.006 · Cited by 85 · see citing works

Structural basis of a novel heterodimeric Fc for bispecific antibody production

Wei, H., Cai, H., Jin, Y., Wang, P., Zhang, Q., Lin, Y., Wang, W., Cheng, J., Zeng, N., Xu, T., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.17558 · Cited by 84 · see citing works

Format and geometries matter: Structure-based design defines the functionality of bispecific antibodies

Dickopf, S., Georges, G. J., & Brinkmann, U. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.05.006 · Cited by 84 · see citing works

Monoclonal antibody therapy for the treatment of asthma and chronic obstructive pulmonary disease with eosinophilic inflammation

Nixon, J. V., Newbold, P., Mustelin, T., Anderson, G. P., & Kolbeck, R. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.10.016 · Cited by 82 · see citing works

Cell-surface proteomics for the identification of novel therapeutic targets in cancer

Kuhlmann, L., Cummins, E., Samudio, I. J., & Kislinger, T. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2018.1429924 · Cited by 80 · see citing works

Interdomain spacing and spatial configuration drive the potency of IgG-[L]-scFv T cell bispecific antibodies

Santich, B. H., Park, J. A., Tran, H., Guo, H.-F., Huse, M., & Cheung, N. V. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aax1315 · Cited by 81 · see citing works

Treatment Options for Primary Autoimmune Hemolytic Anemia: A Short Comprehensive Review

Salama, A. (2015) · Transfusion Medicine and Hemotherapy · doi:10.1159/000438731 · Cited by 80 · see citing works

Checkpoint Antibodies but not T Cell–Recruiting Diabodies Effectively Synergize with TIL-Inducing γ-Irradiation

Hettich, M., Lahoti, J., Prasad, S., & Niedermann, G. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-3451 · Cited by 78 · see citing works

Bispecific Antibodies in the Treatment of Hematologic Malignancies

Duell, J., Lammers, P. E., Djuretic, I. M., Chunyk, A. G., Alekar, S., Jacobs, I. A., & Gill, S. I. (2019) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.1396 · Cited by 77 · see citing works

CD28 co-stimulation: novel insights and applications in cancer immunotherapy

Lotze, M. T., Olejniczak, S. H., & Skokos, D. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01061-1 · Cited by 77 · see citing works

Immuno-targeting the multifunctional CD38 using nanobody

Li, T., Qi, S., Unger, M., Hou, Y. N., Deng, Q. W., Liu, J., Lam, C. M. C., Wang, X. W., Du, X., Zhang, P., et al. (2016) · Scientific Reports · doi:10.1038/srep27055 · Cited by 75 · see citing works

Clinical Pharmacology and Translational Aspects of Bispecific Antibodies

Trivedi, A., Stienen, S., Zhu, M., Li, H., Yuraszeck, T., Gibbs, J., Heath, T., Loberg, R., & Kasichayanula, S. (2017) · Clinical and Translational Science · doi:10.1111/cts.12459 · Cited by 76 · see citing works

Bispecific monoclonal antibodies for targeted immunotherapy of solid tumors: Recent advances and clinical trials

Hosseini, S. S., Khalili, S., Baradaran, B., Bidar, N., Shahbazi, M., Mosafer, J., Hashemzaei, M., Mokhtarzadeh, A., & Hamblin, M. R. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.058 · Cited by 76 · see citing works

Emerging Trends in Immunotherapy for Cancer

Mishra, A., Ali, A., Dutta, S., Banday, S., & Malonia, S. K. (2022) · Diseases · doi:10.3390/diseases10030060 · Cited by 75 · see citing works

Design and engineering of bispecific antibodies: insights and practical considerations

Madsen, A. V., Pedersen, L. E., Kristensen, P. K., & Goletz, S. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2024.1352014 · Cited by 76 · see citing works

Single-Chain Variable Fragment-Based Bispecific Antibodies: Hitting Two Targets with One Sophisticated Arrow

Ahamadi-Fesharaki, R., Fateh, A., Vaziri, F., Solgi, G., Siadat, S. D., Mahboudi, F., & Jamnani, F. R. (2019) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2019.02.004 · Cited by 76 · see citing works

Efficient production of bispecific IgG of different isotypes and species of origin in single mammalian cells

Dillon, M., Yin, Y., Zhou, J., McCarty, L., Ellerman, D., Slaga, D., Junttila, T. T., Han, G., Sandoval, W., Ovacik, M. A., et al. (2017) · mAbs · doi:10.1080/19420862.2016.1267089 · Cited by 75 · see citing works

2015 White Paper on Recent Issues in Bioanalysis: Focus on New Technologies and Biomarkers (Part 3 – Lba, Biomarkers and Immunogenicity)

Amaravadi, L. S., Song, A., Myler, H. A., Thway, T. M., Kirshner, S., Devanarayan, V., Ni, Y. G., Garofolo, F., Birnboeck, H., Richards, S. M., et al. (2015) · Bioanalysis · doi:10.4155/bio.15.226 · Cited by 74 · see citing works

Antibody–drug conjugates and bispecific antibodies targeting cancers: applications of click chemistry

Hong, Y., Nam, S.-M., & Moon, A. (2023) · Archives of Pharmacal Research · doi:10.1007/s12272-023-01433-6 · Cited by 74 · see citing works

Good modeling practice for industrial chromatography: Mechanistic modeling of ion exchange chromatography of a bispecific antibody

Rischawy, F., Saleh, D., Hahn, T., Oelmeier, S. A., Spitz, J., & Kluters, S. (2019) · Computers & Chemical Engineering · doi:10.1016/j.compchemeng.2019.106532 · Cited by 71 · see citing works

T Cell–Activating Bispecific Antibodies in Cancer Therapy

Trabolsi, A., Arumov, A., & Schatz, J. H. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900496 · Cited by 70 · see citing works

Combination therapy in inflammatory bowel disease – from traditional immunosuppressors towards the new paradigm of dual targeted therapy

Privitera, G., Pugliese, D., Onali, S., Petito, V., Scaldaferri, F., Gasbarrini, A., Danese, S., & Armuzzi, A. (2021) · Autoimmunity Reviews · doi:10.1016/j.autrev.2021.102832 · Cited by 70 · see citing works

Silencing Fc Domains in T cell–Engaging Bispecific Antibodies Improves T-cell Trafficking and Antitumor Potency

Wang, L., Hoseini, S. S., Xu, H., Ponomarev, V., & Cheung, N. V. (2019) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-19-0121 · Cited by 69 · see citing works

Bispecific Targeting of PD-1 and PD-L1 Enhances T-cell Activation and Antitumor Immunity

Kotanides, H., Li, Y. H., Malabunga, M., Carpenito, C., Eastman, S. W., Shen, Y., Wang, G., Inigo, I. V., Surguladze, D., Pennello, A. L., et al. (2020) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-20-0304 · Cited by 65 · see citing works

Bispecific antibodies in haematological malignancies

Viardot, A., & Bargou, R. C. (2018) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2018.04.002 · Cited by 67 · see citing works

Bridging the gap with multispecific immune cell engagers in cancer and infectious diseases

Rolin, C., Zimmer, J., & Seguin‐Devaux, C. (2024) · Cellular and Molecular Immunology · doi:10.1038/s41423-024-01176-4 · Cited by 66 · see citing works

Redirected optimized cell killing (ROCK®): A highly versatile multispecific fit-for-purpose antibody platform for engaging innate immunity

Ellwanger, K., Reusch, U., Fucek, I., Wingert, S., Ross, T., Müller, T. R., Schniegler‐Mattox, U., Haneke, T., Rajkovic, E., Koch, J., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1616506 · Cited by 65 · see citing works

Evolution of phage display technology: from discovery to application

Rahbarnia, L., Farajnia, S., Babaei, H., Majidi, J., Veisi, K., Ahmadzadeh, V., & Akbari, B. (2016) · Journal of drug targeting · doi:10.1080/1061186x.2016.1258570 · Cited by 65 · see citing works

283 The trifunctional antibody catumaxomab: mode of action

Seimetz, D., Linke, R., Atz, J., Essing, M. M., & Klein, A. (2010) · European Journal of Cancer Supplements · doi:10.1016/s1359-6349(10)71088-0

Bispecific antibodies and their applications

Fan, G., Wang, Z., Hao, M., & Li, J. (2015) · Journal of Hematology & Oncology · doi:10.1186/s13045-015-0227-0 · Cited by 289 · see citing works

Bispecific Antibodies: Progress and Application

Habeeb, A., & Hajree, S. (2018) · International Journal of Health Sciences and Research

Bispecific and Multivalent Antibodies - New Swords to Combat Hematological Malignancies

Stanglmaier, M., & Heß, J. (2016) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781681081816116020004

Recombinant Bispecific Antibodies for Cancer Therapy

Müller, D., & Kontermann, R. E. (2011) · Cell engineering · doi:10.1007/978-94-007-1257-7_11 · Cited by 2 · see citing works