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

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works

Sequences of proteins of immunological interest

Kabat, B. E. A. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90805-4 · Cited by 3,387 · see citing works

Rapid generation of functional human IgG antibodies derived from Fab-on-phage display libraries

Jostock, T., Vanhove, M., Brepoels, E., van Gool, R., Daukandt, M., Wehnert, A., van Hegelsom, R., Dransfield, D., Sexton, D., Devlin, M., et al. (2004) · Journal of Immunological Methods · doi:10.1016/j.jim.2004.03.014 · Cited by 2,562 · see citing works

Humanization of an anti-p185HER2 antibody for human cancer therapy.

Carter, P., Presta, L., Gorman, C., Ridgway, J., Henner, D., Wong, W., Rowland, A., Kotts, C., Carver, M. E., & Shepard, H. (1992) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.89.10.4285 · Cited by 1,958 · see citing works

Untitled work

Leaver-Fay (2011) · doi:10.1016/b978-0-12-381270-4.00019-6 · Cited by 1,904 · see citing works

Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab

Cho, H., Mason, K., Ramyar, K. X., Stanley, A. M., Gabelli, S. B., Denney, D. W., & Leahy, D. J. (2003) · Nature · doi:10.1038/nature01392 · Cited by 1,615 · see citing works

Human Antibodies with Sub-nanomolar Affinities Isolated from a Large Non-immunized Phage Display Library

Vaughan, T. J., Williams, A. J., Pritchard, K., Osbourn, J. K., Pope, A. R., Earnshaw, J. C., McCafferty, J., Hodits, R. A., Wilton, J., & Johnson, K. S. (1996) · Nature Biotechnology · doi:10.1038/nbt0396-309 · Cited by 1,028 · 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

THE COVALENT STRUCTURE OF AN ENTIRE γG IMMUNOGLOBULIN MOLECULE

Edelman, G. M., Cunningham, B. A., Gall, W. E., Gottlieb, P. D., Rutishauser, U. S., & Waxdal, M. J. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.63.1.78 · Cited by 903 · 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

RosettaScripts: A Scripting Language Interface to the Rosetta Macromolecular Modeling Suite

Fleishman, S. J., Leaver‐Fay, A., Corn, J. E., Strauch, E., Khare, S. D., Koga, N., Ashworth, J. R., Murphy, P. M., Richter, F. M., Lemmon, G., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020161 · Cited by 659 · see citing works

Alternative molecular formats and therapeutic applications for bispecific antibodies

Spiess, C., Zhai, Q., & Carter, P. J. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.01.003 · Cited by 607 · see citing works

Computational Alanine Scanning of Protein-Protein Interfaces

Kortemme, T., Kim, D. E., & Baker, D. A. (2004) · Science s STKE · doi:10.1126/stke.2192004pl2 · Cited by 586 · see citing works

Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region.

Tao, M., & Morrison, S. L. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.143.8.2595 · Cited by 531 · 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

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

Hydrogen bonds and salt bridges across protein-protein interfaces

Xu, D., Tsai, C.-J., & Nussinov, R. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.9.999 · Cited by 457 · see citing works

Selection and analysis of an optimized anti-VEGF antibody: crystal structure of an affinity-matured fab in complex with antigen 1 1Edited by I. A. Wilson

Chen, Y., Wiesmann, C., Fuh, G., Li, B., Christinger, H. W., McKay, P., de Vos, A. M., & Lowman, H. B. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3192 · Cited by 447 · 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

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

Contribution of Variable Domains to the Stability of Humanized IgG1 Monoclonal Antibodies

Ionescu, R. M., Vlasak, J., Price, C. E., & Kirchmeier, M. J. (2007) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21104 · Cited by 315 · 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

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

On the Role of Electrostatic Interactions in the Design of Protein–Protein Interfaces

Sheinerman, F. B., & Honig, B. H. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00030-x · Cited by 252 · see citing works

An Unfolded CH1 Domain Controls the Assembly and Secretion of IgG Antibodies

Feige, M. J., Groscurth, S., Marcinowski, M., Shimizu, Y., Kessler, H., Hendershot, L. M., & Büchner, J. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.028 · Cited by 237 · 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

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

How antibodies fold

Feige, M. J., Hendershot, L. M., & Buchner, J. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.11.005 · Cited by 196 · see citing works

Scientific Benchmarks for Guiding Macromolecular Energy Function Improvement

Leaver‐Fay, A., O’Meara, M. J., Tyka, M., Jacak, R., Song, Y., Kellogg, E. H., Thompson, J., Davis, I., Pache, R. A., Lyskov, S., et al. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-394292-0.00006-0 · Cited by 189 · see citing works

X-ray Structures of the Antigen-binding Domains from Three Variants of Humanized anti-p185HER2 Antibody 4D5 and Comparison with Molecular Modeling

Eigenbrot, C. W., Randal, M., Presta, L., Carter, P. M., & Kossiakoff, A. A. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1099 · Cited by 186 · 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

[17] Bispecific monoclonal antibodies from hybrid hybridomas

Suresh, M. R., Cuello, A. C., & Milstein, C. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)21019-8 · Cited by 160 · see citing works

Kinetics of Irreversible Protein Aggregation: Analysis of Extended Lumry−Eyring Models and Implications for Predicting Protein Shelf Life

Roberts, C. J. (2003) · The Journal of Physical Chemistry B · doi:10.1021/jp026827s · Cited by 159 · see citing works

Examination of Thermal Unfolding and Aggregation Profiles of a Series of Developable Therapeutic Monoclonal Antibodies

Brader, M. L., Estey, T., Bai, S., Alston, R. W., Lucas, K. K., Lantz, S. R., Landsman, P., & Maloney, K. M. (2015) · Molecular Pharmaceutics · doi:10.1021/mp400666b · Cited by 159 · see citing works

Antitumor Efficacy of a Bispecific Antibody That Targets HER2 and Activates T Cells

Junttila, T. T., Li, J., Johnston, J., Hristopoulos, M. L., Clark, R. A., Ellerman, D. A., Wang, B.-E., Li, Y., Mathieu, M. A., Li, G., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3622-t · Cited by 157 · see citing works

Improving target cell specificity using a novel monovalent bispecific IgG design

Mazor, Y., Oganesyan, V., Yang, C., Hansen, A. M., Wang, J., Liu, H., Sachsenmeier, K. F., Marcia, C., Gadre, D., Borrok, M. J., et al. (2015) · mAbs · doi:10.1080/19420862.2015.1007816 · Cited by 150 · 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

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

Influence of immunoglobulin isotype on therapeutic antibody function

Beers, S. A., Glennie, M. J., & White, A. L. (2016) · Blood · doi:10.1182/blood-2015-09-625343 · Cited by 119 · see citing works

Human Antibody Production in Transgenic Animals

Brüggemann, M., Osborn, M. J., Ma, B., Hayre, J. K., Avis, S., Lundstrom, B., & Buelow, R. (2014) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-014-0322-x · Cited by 114 · see citing works

High-Level Production of Recombinant Proteins in CHO Cells Using a Dicistronic DHFR Intron Expression Vector

Lucas, B. K., Giere, L., DeMarco, R., Shen, A., Chisholm, V., & Crowley, C. W. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.9.1774 · Cited by 98 · see citing works

Knobs-into-holes antibody production in mammalian cell lines reveals that asymmetric afucosylation is sufficient for full antibody-dependent cellular cytotoxicity

Shatz-Binder, W., Chung, S., Li, B., Marshall, B., Tejada, M. L., Phung, W., Sandoval, W. N., Kelley, R. F., & Scheer, J. M. (2013) · mAbs · doi:10.4161/mabs.26307 · Cited by 88 · see citing works

Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life

Roberts, C. J., Darrington, R. T., & Whitley, M. B. (2003) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.10377 · Cited by 88 · see citing works

Immunoglobulin isotype knowledge and application to Fc engineering

Brezski, R. J., & Georgiou, G. (2016) · Current Opinion in Immunology · doi:10.1016/j.coi.2016.03.002 · Cited by 82 · see citing works

Amplification and cloning of the Chinese hamster glutamine synthetase gene.

Sanders, P. G., & Wilson, R. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01762.x · Cited by 80 · 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

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

Phase I Dose-Escalation Study of Onartuzumab as a Single Agent and in Combination with Bevacizumab in Patients with Advanced Solid Malignancies

Salgia, R., Patel, P. H., Bothos, J. G., Yu, W., Eppler, S., Hegde, P. S., Bai, S., Kaur, S., Nijem, I., Catenacci, D. V. T., et al. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2070 · Cited by 66 · 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

Conformational selection in substrate recognition by Hsp70 chaperones.

Marcinowski, M., Rosam, M., Seitz, C., Elferich, J., Behnke, J., Bello, C., Feige, M., Becker, C. F. W., Antes, I., & Buchner, J. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.11.030 · Cited by 48 · see citing works

Characterization of Chain Pairing Variants of Bispecific IgG Expressed in a Single Host Cell by High-Resolution Native and Denaturing Mass Spectrometry

Schachner, L. F., Han, G., Dillon, M. A., Zhou, J., McCarty, L., Ellerman, D. A., Yin, Y., Spiess, C., Lill, J. R., Carter, P. J., et al. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02866 · Cited by 48 · see citing works

Optimization and automation of an end‐to‐end high throughput microscale transient protein production process

Bos, A. B., Luan, P., Duque, J. N., Reilly, D. E., Harms, P. D., & Wong, A. W. (2015) · Biotechnology and Bioengineering · doi:10.1002/bit.25601 · Cited by 47 · see citing works

Chinese hamster ovary K1 host cell enables stable cell line development for antibody molecules which are difficult to express in DUXB11‐derived dihydrofolate reductase deficient host cell

Hu, Z., Guo, D., Yip, S. S. M., Zhan, D., Misaghi, S., Joly, J. C., Snedecor, B. R., & Shen, A. Y. (2013) · Biotechnology Progress · doi:10.1002/btpr.1730 · Cited by 42 · see citing works

Precise quantification of mixtures of bispecific IgG produced in single host cells by liquid chromatography-Orbitrap high-resolution mass spectrometry

Yin, Y., Han, G., Zhou, J., Dillon, M. A., McCarty, L., Gavino, L., Ellerman, D. A., Spiess, C., Sandoval, W. N., & Carter, P. J. (2016) · mAbs · doi:10.1080/19420862.2016.1232217 · Cited by 39 · see citing works

Engineering a humanized bispecific F(ab')2 fragment for improved binding to T cells.

Rodrigues, M. L., Shalaby, M. R., Werther, W., Presta, L. G., & Carter, P. M. (1992) · PubMed · Cited by 38 · 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

Heavy and light chain pairing of bivalent quadroma and knobs-into-holes antibodies analyzed by UHR-ESI-QTOF mass spectrometry

Schäfer, W. M., Völger, H. R., Lorenz, S. H., Imhof-Jung, S., Regula, J. T., Klein, C., & Mølhøj, M. (2015) · mAbs · doi:10.1080/19420862.2015.1111498 · Cited by 35 · see citing works

Optimizing antibody expression by using the naturally occurring framework diversity in a live bacterial antibody display system

Lombana, T. N., Dillon, M. A., Bevers, J. J., & Spiess, C. (2015) · Scientific Reports · doi:10.1038/srep17488 · Cited by 26 · 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

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

Design and Production of Bispecific Antibodies

Wang, Q., Chen, Y., Park, J., Liu, X., Hu, Y., Wang, T., McFarland, K. S., & Betenbaugh, M. J. (2019) · Antibodies · doi:10.3390/antib8030043 · Cited by 280 · see citing works

Bispecific Antibodies and Antibody–Drug Conjugates for Cancer Therapy: Technological Considerations

Shim, H. (2020) · Biomolecules · doi:10.3390/biom10030360 · Cited by 167 · see citing works

Avidity-based binding to HER2 results in selective killing of HER2-overexpressing cells by anti-HER2/CD3

Slaga, D., Ellerman, D. A., Lombana, T. N., Vij, R., Li, J., Hristopoulos, M. L., Clark, R., Johnston, J., Shelton, A., Mai, E., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aat5775 · Cited by 138 · see citing works

Bispecific T-Cell Redirection versus Chimeric Antigen Receptor (CAR)-T Cells as Approaches to Kill Cancer Cells

Strohl, W. R., & Naso, M. F. (2019) · Antibodies · doi:10.3390/antib8030041 · Cited by 136 · 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

Biology drives the discovery of bispecific antibodies as innovative therapeutics

Nie, S., Wang, Z., Moscoso‐Castro, M., D'Souza, P., Lei, C., Xu, J., & Gu, J. (2020) · Antibody Therapeutics · doi:10.1093/abt/tbaa003 · Cited by 95 · see citing works

Ten years in the making: application of CrossMab technology for the development of therapeutic bispecific antibodies and antibody fusion proteins

Surowka, M., Schäfer, W. M., & Klein, C. (2021) · mAbs · doi:10.1080/19420862.2021.1967714 · Cited by 92 · 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

Toward Drug-Like Multispecific Antibodies by Design

Sawant, M. S., Streu, C. N., Wu, L., & Tessier, P. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207496 · Cited by 74 · see citing works

Maximizing antibody production in a targeted integration host by optimization of subunit gene dosage and position

Carver, J., Ng, D., Zhou, M., Ko, P., Zhan, D., Yim, M., Shaw, D., Snedecor, B., Laird, M. W., Lang, S. E., et al. (2020) · Biotechnology Progress · doi:10.1002/btpr.2967 · Cited by 63 · see citing works

Engineering an anti-HER2 biparatopic antibody with a multimodal mechanism of action

Kast, F., Schwill, M., Stüber, J. C., Pfundstein, S., Nagy‐Davidescu, G., Rodríguez, J. M. M., Seehusen, F., Richter, C. P., Honegger, A., Hartmann, K. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23948-6 · Cited by 60 · see citing works

Next generation of multispecific antibody engineering

Kéri, D., Walker, M., Singh, I., Nishikawa, K. K., & Garcés, F. (2023) · Antibody Therapeutics · doi:10.1093/abt/tbad027 · Cited by 57 · see citing works

High-throughput antibody screening from complex matrices using intact protein electrospray mass spectrometry

Sawyer, W. S., Srikumar, N., Carver, J., Chu, P. Y., Shen, A., Xu, A., Williams, A. J., Spiess, C., Wu, C., Liu, Y., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917383117 · Cited by 55 · see citing works

A brief introduction of IgG-like bispecific antibody purification: Methods for removing product-related impurities

Li, Y. (2018) · Protein Expression and Purification · doi:10.1016/j.pep.2018.11.011 · Cited by 55 · see citing works

Dual antibody inhibition of KLK5 and KLK7 for Netherton syndrome and atopic dermatitis

Chavarría‐Smith, J., Chiu, C., Jackman, J. K., Yin, J., Zhang, J., Hackney, J. A., Lin, W., Tyagi, T., Sun, Y., Tao, J., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abp9159 · Cited by 52 · see citing works

Tetravalent biepitopic targeting enables intrinsic antibody agonism of tumor necrosis factor receptor superfamily members

Yang, Y., Yeh, S. H., Madireddi, S., Matochko, W. L., Gu, C., Sanchez, P. P., Ultsch, M. H., Boenig, G. D. L., Harris, S. F., Leonard, B. C., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1625662 · Cited by 46 · see citing works

Productive common light chain libraries yield diverse panels of high affinity bispecific antibodies

Blarcom, T. J. V., Lindquist, K. C., Melton, Z., Cheung‐Lee, W. L., Wagstrom, C., McDonough, D., Oseguera, C. A. V., Ding, S., Rossi, A., Potluri, S., et al. (2017) · mAbs · doi:10.1080/19420862.2017.1406570 · Cited by 43 · see citing works

Building blocks for bispecific and trispecific antibodies

Wu, X., & Demarest, S. J. (2018) · Methods · doi:10.1016/j.ymeth.2018.08.010 · Cited by 42 · see citing works

Novel CH1:CL interfaces that enhance correct light chain pairing in heterodimeric bispecific antibodies

Bönisch, M., Sellmann, C., Maresch, D., Halbig, C., Becker, S., Toleikis, L., Hock, B. M., & Rüker, F. (2017) · Protein Engineering Design and Selection · doi:10.1093/protein/gzx044 · Cited by 39 · see citing works

Development of a targeted integration Chinese hamster ovary host directly targeting either one or two vectors simultaneously to a single locus using the Cre/Lox recombinase‐mediated cassette exchange system

Ng, D., Zhou, M., Zhan, D., Yip, S. S. M., Ko, P., Yim, M., Modrusan, Z. D., Joly, J. C., Snedecor, B., Laird, M. W., et al. (2021) · Biotechnology Progress · doi:10.1002/btpr.3140 · Cited by 38 · see citing works

Structural and functional characterization of MBS301, an afucosylated bispecific anti-HER2 antibody

Huang, S., Li, F., Liu, H., Ye, P., Fan, X., Xinqiu, Y., Zhi-Dan, W. U., Chen, J., Jin, C., Shen, B., et al. (2018) · mAbs · doi:10.1080/19420862.2018.1486946 · Cited by 37 · see citing works

Format chain exchange (FORCE) for high-throughput generation of bispecific antibodies in combinatorial binder-format matrices

Dengl, S., Mayer, K., Bormann, F., Dürr, H., Hoffmann, E., Nussbaum, B., Tischler, M., Wagner, M., Kuglstatter, A., Leibrock, L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18477-7 · Cited by 33 · see citing works

Tailoring translational strength using Kozak sequence variants improves bispecific antibody assembly and reduces product‐related impurities in CHO cells

Blanco, N., Williams, A. J., Tang, D., Zhan, D., Misaghi, S., Kelley, R. F., & Simmons, L. C. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27347 · Cited by 32 · see citing works

Computational design of a specific heavy chain/κ light chain interface for expressing fully IgG bispecific antibodies

Froning, K., Leaver‐Fay, A., Wu, X., Phan, S., Gao, L., Huang, F., Pustilnik, A., Bacica, M., Houlihan, K., Chai, Q., et al. (2017) · Protein Science · doi:10.1002/pro.3240 · Cited by 30 · see citing works

Development of in silico models to predict viscosity and mouse clearance using a comprehensive analytical data set collected on 83 scaffold-consistent monoclonal antibodies

Mock, M. L., Jacobitz, A. W., LANGMEAD, C. J., Sudom, A. M., Yoo, D., Humphreys, S. C., Alday, M., Alekseychyk, L., Angell, N., Bi, V., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2256745 · Cited by 29 · see citing works

Elucidating heavy/light chain pairing preferences to facilitate the assembly of bispecific IgG in single cells

Joshi, K. K., Phung, W., Han, G., Yin, Y., Kim, I., Sandoval, W. N., & Carter, P. J. (2019) · mAbs · doi:10.1080/19420862.2019.1640549 · Cited by 27 · see citing works

Nonclinical immunogenicity risk assessment for knobs-into-holes bispecific IgG 1 antibodies

Tsai, W. K., Li, Y., Yin, Z., Tran, P., Phung, Q. T., Zhou, Z., Peng, K., Qin, D., Tam, S., Spiess, C., et al. (2024) · mAbs · doi:10.1080/19420862.2024.2362789 · Cited by 24 · see citing works

Development of T-cell engagers selective for cells co-expressing two antigens

DiCara, D. M., Bhakta, S., Go, M. A. T., Ziai, J. M., Firestein, R., Forrest, B., Gu, C., Leong, S. R., Lee, G., Yu, S., et al. (2022) · mAbs · doi:10.1080/19420862.2022.2115213 · Cited by 24 · see citing works

Efficient production of bispecific antibody by FAST-Ig TM and its application to NXT007 for the treatment of hemophilia A

Koga, H., Yamano, T., Betancur, J., Nagatomo, S., Ikeda, Y., Yamaguchi, K., Nabuchi, Y., Sato, K., Teranishi-Ikawa, Y., Sato, M., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2222441 · Cited by 23 · see citing works

High-Throughput Generation of Bipod (Fab × scFv) Bispecific Antibodies Exploits Differential Chain Expression and Affinity Capture

Nesspor, T., Kinealy, K., Mazzanti, N., Diem, M. D., Boye, K., Hoffman, H., Springer, C., Sprenkle, J., Powers, G. D., Jiang, H., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-64536-w · Cited by 21 · see citing works

Characterization and Monitoring of a Novel Light-heavy-light Chain Mispair in a Therapeutic Bispecific Antibody

Cao, M., Parthemore, C., Jiao, Y., Korman, S. A., Aspelund, M. T., Hunter, A. K., Kilby, G. W., & Chen, X. (2021) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2021.04.010 · Cited by 20 · see citing works

Automated middle-up approach for the characterization of biotherapeutic products by combining on-line hinge-specific digestion with RPLC-HRMS analysis

Camperi, J., Guillarme, D., Lei, M., & Stella, C. (2020) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2020.113130 · Cited by 20 · see citing works

Culture temperature modulates half antibody and aggregate formation in a Chinese hamster ovary cell line expressing a bispecific antibody

Gomez, N. V., Wieczorek, A., Lu, F., Bruno, R., Diaz, L., Agrawal, N. J., & Daris, K. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26803 · Cited by 19 · see citing works

Generation of dual specific bivalent BiTEs (dbBIspecific T-cell engaging antibodies) for cellular immunotherapy

Kujawski, M., Li, L., Bhattacharya, S., Wong, P. W., Lee, W.-H., Williams, L., Li, H., Chea, J., Poku, K., Bowles, N., et al. (2019) · BMC Cancer · doi:10.1186/s12885-019-6056-8 · Cited by 17 · see citing works

EFab domain substitution as a solution to the light-chain pairing problem of bispecific antibodies

Cooke, H. A., Arndt, J. W., Quan, C., Shapiro, R. I., Wen, D., Foley, S. F., Vecchi, M. M., & Preyer, M. (2018) · mAbs · doi:10.1080/19420862.2018.1519631 · Cited by 17 · see citing works

Influence of the bispecific antibody IgG subclass on T cell redirection

Kapelski, S., Cleiren, E., Attar, R. M., Philippar, U., Häsler, J., & Chiu, M. L. (2019) · mAbs · doi:10.1080/19420862.2019.1624464 · Cited by 17 · see citing works

Trends and challenges in bispecific antibody production

Karbyshev, M. S., Kalashnikova, I. V., Dubrovskaya, V. V., Baskakova, K. O., Kuzmichev, P. K., & Sandig, V. (2025) · Journal of Chromatography A · doi:10.1016/j.chroma.2025.465722 · Cited by 16 · see citing works

Single cell-produced and in vitro-assembled anti-FcRH5/CD3 T-cell dependent bispecific antibodies have similar in vitro and in vivo properties

Ovacik, A. M., Li, J., Lemper, M., Danilenko, D. M., Stagg, N. J., Mathieu, M. A., Ellerman, D. A., Gupta, V., Kalia, N., Nguy, T., et al. (2018) · mAbs · doi:10.1080/19420862.2018.1551676 · Cited by 16 · see citing works

Characterization of bispecific and mispaired IgGs by native charge-variant mass spectrometry

Phung, W., Han, G., Polderdijk, S. G. I., Dillon, M. A., Shatz-Binder, W., Liu, P., Wei, B., Suresh, P., Fischer, D., Spiess, C., et al. (2019) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2019.116229 · Cited by 16 · see citing works

IgG-like bispecific antibody platforms with built-in purification-facilitating elements

Li, Y. (2021) · Protein Expression and Purification · doi:10.1016/j.pep.2021.105955 · Cited by 14 · see citing works

A comprehensive analysis of novel disulfide bond introduction site into the constant domain of human Fab

Nakamura, H., Yoshikawa, M., Oda‐Ueda, N., Ueda, T., & Ohkuri, T. (2021) · Scientific Reports · doi:10.1038/s41598-021-92225-9 · Cited by 13 · see citing works

CDR loop interactions can determine heavy and light chain pairing preferences in bispecific antibodies

Fernández‐Quintero, M. L., Kroell, K. B., Grunewald, L., Fischer, A.-L. M., Riccabona, J. R., & Liedl, K. R. (2022) · mAbs · doi:10.1080/19420862.2021.2024118 · Cited by 13 · see citing works

High-Throughput Mass Spectrometry for Biopharma: A Universal Modality and Target Independent Analytical Method for Accurate Biomolecule Characterization

Campuzano, I. D. G., Pelegri-O’Day, E. M., Srinivasan, N., Lippens, J. L., Egea, P. F., Umeda, A., Aral, J., Zhang, T., Laganowsky, A. D., & Netirojjanakul, C. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00138 · Cited by 13 · see citing works

Rational selection of building blocks for the assembly of bispecific antibodies

Gong, D., Riley, T. P., Bzymek, K. P., Correia, A. R., Li, D., Spahr, C. S., Robinson, J. H., Case, R. B., Wang, Z., & Garcés, F. (2021) · mAbs · doi:10.1080/19420862.2020.1870058 · Cited by 13 · see citing works

Emerging trends in bispecific antibody and scaffold protein therapeutics

Verdino, P., Atwell, S., & Demarest, S. J. (2018) · Current Opinion in Chemical Engineering · doi:10.1016/j.coche.2018.01.004 · Cited by 12 · see citing works

Efficient production of bispecific antibodies—optimization of transfection strategy leads to high-level stable cell line generation of a Fabs-in-tandem immunoglobin

Gong, S., & Wu, C. (2023) · Antibody Therapeutics · doi:10.1093/abt/tbad013 · Cited by 11 · see citing works

Design of orthogonal constant domain interfaces to aid proper heavy/light chain pairing of bispecific antibodies

Barlow, K. A., Battles, M. B., Brown, M. E., Canfield, K., Lu, X., Lynaugh, H., Morrill, M. B., Rappazzo, C. G., Reyes, S. P., Sandberg, C., et al. (2025) · mAbs · doi:10.1080/19420862.2025.2479531 · Cited by 11 · see citing works

Tethered-variable CL bispecific IgG: an antibody platform for rapid bispecific antibody screening

Kim, H. S., Dunshee, D. R., Yee, A., Tong, R. K., Kim, I., Farahi, F., Hongo, J.-A., Ernst, J. A., Sonoda, J., & Spiess, C. (2017) · Protein Engineering Design and Selection · doi:10.1093/protein/gzx034 · Cited by 11 · see citing works

Bioanalytical Challenges and Unique Considerations to Support Pharmacokinetic Characterization of Bispecific Biotherapeutics

Ma, M., Colletti, K. S., Yang, T., Leung, S. S., Pederson, S. M., Hottenstein, C. S., Xu, X., Warrino, D. E., & Wakshull, E. (2019) · Bioanalysis · doi:10.4155/bio-2018-0146 · Cited by 10 · see citing works

Robust production of monovalent bispecific IgG antibodies through novel electrostatic steering mutations at the C H 1-C λ interface

Bagert, J. D., Oganesyan, V., Chiang, C.-I., Iannotti, M., Lin, J., Yang, C., Payne, S. R., McMahon, W., Edwards, S., Dippel, A. B., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2273449 · Cited by 9 · see citing works

RUBY® – a tetravalent (2+2) bispecific antibody format with excellent functionality and IgG-like stability, pharmacology and developability properties

Nyesiga, B., Levin, M., Säll, A., Rosén, A., Jansson, K., Fritzell, S., Hägerbrand, K., Weilguny, D., & von Schantz, L. (2024) · mAbs · doi:10.1080/19420862.2024.2330113 · Cited by 8 · see citing works

Mechanism-Driven Design of Multispecific Antibodies for Targeted Disease Treatment

Fine, J., Meksiriporn, B., Tan, J., & Spangler, J. B. (2024) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-100522-102155 · Cited by 7 · see citing works

Modular design of bi- and multi-specific knob domain fusions

Kuravsky, M. L., Gibbons, G. F., Joyce, C., Scott-Tucker, A., Macpherson, A., & Lawson, A. D. G. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1384467 · Cited by 7 · see citing works

Comparing Antibody Interfaces to Inform Rational Design of New Antibody Formats

Fernández‐Quintero, M. L., Quoika, P. K., Wedl, F. S., Seidler, C. A., Kroell, K. B., Loeffler, J. R., Pomarici, N. D., Hoerschinger, V. J., Bujotzek, A., Georges, G. J., et al. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.812750 · Cited by 8 · see citing works

Concurrent transfection of randomized transgene configurations into targeted integration CHO host is an advantageous and cost‐effective method for expression of complex molecules

Dong, E., Lam, C., Tang, D., Louie, S., Yim, M., Williams, A. J., Sawyer, W. S., Yip, S. S. M., Carver, J. O., AlBarakat, A., et al. (2020) · Biotechnology Journal · doi:10.1002/biot.202000230 · Cited by 6 · see citing works

Development of a 10 g/L process for a difficult-to-express multispecific antibody format using a holistic process development approach

Peltret, M., Vetsch, P., Farvaque, E., Mette, R., Tsachaki, M., Duarte, L., Duret, A., Vaxelaire, E., Frank, J., Moritz, B., et al. (2024) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2024.04.017 · Cited by 6 · see citing works

Structural study of a light chain mispaired bispecific predicts mechanism of downstream separation

Cha, M., Xu, A., & Williams, A. J. (2024) · Journal of Chromatography A · doi:10.1016/j.chroma.2024.465117 · Cited by 6 · see citing works

Evaluation of Human Anti Igg Polyclonal Antibody Production Conjugated with Peroxidase in Egg Yolk

Abdolmaleki, F., Zamani, Z., & Talebi, S. (2020) · Iranian Journal of Public Health · doi:10.18502/ijph.v48i7.2962 · Cited by 6 · see citing works

Analysis of thermostability for seven Phe to Ala and six Pro to Gly mutants in the Fab constant region of adalimumab

Yoshikawa, M., Nakamura, H., Oda‐Ueda, N., & Ohkuri, T. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad047 · Cited by 5 · see citing works

Stellabody: A novel hexamer‐promoting mutation for improved IgG potency

Whitehead, C. A., Wines, B. D., Davies, A. M., McDonnell, J. M., Trist, H. M., Esparon, S. E., & Hogarth, P. M. (2024) · Immunological Reviews · doi:10.1111/imr.13400 · Cited by 4 · see citing works

Characterization of free light chain impurity in a bispecific antibody

Sadek, M., Mantha, N., Lippold, S., Li, D., Spitler, K., Li, R., Spinosa, P. C., Liu, B., Luu, S., Woon, N., et al. (2025) · mAbs · doi:10.1080/19420862.2025.2527689 · Cited by 3 · see citing works

Rapid Generation of Murine Bispecific Antibodies Using FAST-IgTM for Preclinical Screening of HER2/CD3 T-Cell Engagers

Koga, H., Kuroi, H., Hirano, R., Hirayama, H., Nabuchi, Y., & Kuramochi, T. (2024) · Antibodies · doi:10.3390/antib13010003 · Cited by 3 · see citing works

High-Throughput Analyses of Therapeutic Antibodies Using High-Field Asymmetric Waveform Ion Mobility Spectrometry Combined with SampleStream and Intact Protein Mass Spectrometry

Shi, L., Dillon, M. A., Compton, P. D., Sawyer, W. S., Thorup, J. R., Kwong, M., Chan, P., Chiu, C., Li, R., Yadav, R., et al. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c03158 · Cited by 3 · see citing works

Chapter 4: Production Strategies and Challenges with IgG-Based Bispecific Ab Formats

Gu, C., & Ellerman, D. A. (2020) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-030-31415-6_4 · Cited by 3 · see citing works

An Engineered Mouse Model That Generates a Diverse Repertoire of Endogenous, High-Affinity Common Light Chain Antibodies

Rong, Y., Chen, I.-L., Larrabee, L., Sawant, M. S., Fuh, G., & Koenig, P. S. (2024) · Antibodies · doi:10.3390/antib13010014 · Cited by 1 · see citing works

Age-Related Macular Degeneration and its Current Treatment Strategies: An Updated Review

Gelat, B., Trivedi, K., Malaviya, P. B., Rathaur, P., Patel, B., Gelat, R., & Johar, K. (2024) · IntechOpen eBooks · doi:10.5772/intechopen.1004075 · Cited by 1 · see citing works

Folding-mediated secretion of pure bispecific antibodies

Tilegenova, C., Liu, T., Zhao, Q., Are, M., Zhao, Y., Choi, W. S., Bhaumik, A., Steele, R. A., Manieri, N. A., Turegun, B., et al. (2025) · Nature Biotechnology · doi:10.1038/s41587-025-02842-2 · Cited by 1 · see citing works

Identification of engineered IMGT Fc variants in IMGT/mAb-DB, a database of therapeutic antibodies and fusion proteins

Manso, T., Sanou, G., Nousias, C., Maalem, I., Boutin, F., Giudicelli, V., Duroux, P., Lefranc, M., & Κοσσίδα, Σ. (2025) · mAbs · doi:10.1080/19420862.2025.2594260 · Cited by 1 · see citing works

Capillary gel electrophoresis for the analysis of heterodimer purity in a highly glycosylated, bispecific Fc fusion protein

Daniels, C., Jones, K., Makani, V. S., Schmidt, C., Pate, J., Wu, D., Schreiber, T. H., de Silva, S., Shukla, A. A., & Oien, N. P. (2026) · Frontiers in Analytical Science · doi:10.3389/frans.2026.1739382 · Cited by 1 · see citing works

Analytical Characterization of Bispecific Antibodies and Bispecific Molecules

Dillon, M. A., Lombana, T. N., & Spiess, C. (2025) · doi:10.1002/9781394236145.ch2 · Cited by 1 · see citing works

Identification of Engineered IMGT Fc Variants in IMGT/mAb-DB Therapeutic Antibodies and Fusion proteinsPreprint

Manso, T., Sanou, G., Nousias, C., Maalem, I., Boutin, F., Giudicelli, V., Duroux, P., Lefranc, M., & Κοσσίδα, Σ. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.03.673706

Generation of Bispecific Antibodies Using FAST-Ig™

Yeo, C. Y., & Feng, S. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5037-0_3

T cell–mediated depletion of intratumoral regulatory T cells using a CCR8xCD3 T cell–engaging bispecific antibody (TCB) promotes antitumor immunity in preclinical mouse models

Wang, B., Ishizuka, I. E., Esen, E., Li, J., Chiu, C., Sun, Y., Lin, Z., Seshasayee, D., Kusi, A., Zhong, Y., et al. (2026) · Science Translational Medicine · doi:10.1126/scitranslmed.aea7127

Elucidating heavy/light chain pairing preferences to facilitate the assembly of bispecific IgG in single cells

Joshi, K. K., Phung, W., Han, G., Yin, Y., Kim, I., Sandoval, W. N., & Carter, P. J. (2019) · mAbs · doi:10.1080/19420862.2019.1640549 · Cited by 27 · see citing works

An efficient route to bispecific antibody production using single-reactor mammalian co-culture

Shatz-Binder, W., Ng, D., Dutina, G., Wong, A. W., Dunshee, D. R., Sonoda, J., Shen, A. Y., & Scheer, J. M. (2016) · mAbs · doi:10.1080/19420862.2016.1234569 · Cited by 26 · see citing works

An efficient route to the production of an IgG-like bispecific antibody

Zuo, Z., Jimenez, X., Witte, L., & Zhu, Z. (2000) · Protein Engineering Design and Selection · doi:10.1093/protein/13.5.361 · Cited by 39 · 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

Computational design of a specific heavy chain/κ light chain interface for expressing fully IgG bispecific antibodies

Froning, K., Leaver‐Fay, A., Wu, X., Phan, S., Gao, L., Huang, F., Pustilnik, A., Bacica, M., Houlihan, K., Chai, Q., et al. (2017) · Protein Science · doi:10.1002/pro.3240 · Cited by 30 · see citing works