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

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 1,610

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 1,522

The therapeutic monoclonal antibody market

Ecker, D. M., Jones, S. D., & Levine, H. L. (2014) · mAbs · doi:10.4161/19420862.2015.989042 · Cited by 1,369

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

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 1,010

Biopharmaceutical benchmarks 2014

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

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

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 981

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

Saphire, E. O., Parren, P. W. H. I., Pantophlet, R. A., Zwick, M. B., Morris, G. M., Rudd, P. M., Dwek, R. A., Stanfield, R. L., Burton, D. R., & Wilson, I. A. (2001) · Science · doi:10.1126/science.1061692 · Cited by 959

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 18

Fundamentals of protein affinity chromatography: How to prepare and properly use an affinity matrix

Bı́lková, Z., Shabani, E., Moravek, O., Korecká, L., Slováková, M., & Jankovičová, B. (2025) · Journal of Chromatography A · doi:10.1016/j.chroma.2025.466061 · Cited by 16

Characterization of Bispecific Antibody Production in Cell Cultures by Unique Mixed Mode Size Exclusion Chromatography

Jiang, H., Xu, W., Liu, R., Gupta, B., Kilgore, B. R., Du, Z., & Yang, X. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c01641 · Cited by 16

A novel hydrogen peroxide evolved CHO host can improve the expression of difficult to express bispecific antibodies

Mistry, R. K., Kelsall, E. J., Sou, S. N., Barker, H., Jenns, M., Willis, K., Zurlo, F., Hatton, D., & Gibson, S. J. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27744 · Cited by 16

Tetravalent anti-CD20/CD3 bispecific antibody for the treatment of B cell lymphoma

Lu, C.-Y., Chen, G. J., Tai, P., Yang, Y., Hsu, Y.-S., Chang, M., & Hsu, C.-L. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.124 · Cited by 16

Surfaceome interrogation using an RNA-seq approach highlights leukemia initiating cell biomarkers in an LMO2 T cell transgenic model

Pais, H., Ruggero, K., Zhang, J., Al‐Assar, O., Béry, N., Bhuller, R. K., Weston, V., Kearns, P. R., Mecucci, C., Miller, A., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-42214-w · Cited by 14

Greatest Hits—Innovative Technologies for High Throughput Identification of Bispecific Antibodies

Hofmann, T., Krah, S., Sellmann, C., Zielonka, S., & Doerner, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186551 · Cited by 16

Immunodetection of the “brown” spider (Loxosceles intermedia) dermonecrotoxin with an scFv-alkaline phosphatase fusion protein

Jiacomini, I. G., Silva, S. K., Aubrey, N., Muzard, J., Chávez-Olórtegui, C., de Moura, J. F., Billiald, P., & Alvarenga, L. M. (2016) · Immunology Letters · doi:10.1016/j.imlet.2016.03.001 · Cited by 16

High-resolution mass spectrometry confirms the presence of a hydroxyproline (Hyp) post-translational modification in the GGGGP linker of an Fc-fusion protein

Spahr, C. S., Gunasekaran, K., Walker, K. W., & Shi, S. D. ‐. (2017) · mAbs · doi:10.1080/19420862.2017.1325556 · Cited by 16

PSMA-targeted bispecific Fab conjugates that engage T cells

Patterson, J. T., Isaacson, J., Kerwin, L., Atassi, G., Duggal, R., Bresson, D., Zhu, T., Zhou, H., Fu, Y., & Kaufmann, G. F. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.09.065 · Cited by 16

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

High-resolution glycosylation site-engineering method identifies MICA epitope critical for shedding inhibition activity of anti-MICA antibodies

Lombana, T. N., Matsumoto, M. L., Bevers, J. J., Berkley, A. M., Toy, E., Cook, R., Gan, Y., Du, C., Liu, P., Schnier, P. D., et al. (2018) · mAbs · doi:10.1080/19420862.2018.1532767 · Cited by 16

De novo discovery of peptide-based affinity ligands for the fab fragment of human immunoglobulin G

Xiao, X., Kilgore, R., Sarma, S., Chu, W., Menegatti, S., & Hall, C. K. (2022) · Journal of Chromatography A · doi:10.1016/j.chroma.2022.462941 · Cited by 13

Synthesis of Bispecific Antibody Conjugates Using Functionalized Poly-ADP-ribose Polymers

Cheng, Q., Zhang, X., Li, J., Chen, J., Wang, Y., & Zhang, Y. (2023) · Biochemistry · doi:10.1021/acs.biochem.2c00718 · Cited by 15

The impact of expression vector position on transgene transcription allows for rational expression vector design in a targeted integration system

Beal, K. M., Bandara, K., Ali, S. R., Sonak, R. G., Barnes, M. R., Scarcelli, J. J., & Zhang, L. (2023) · Biotechnology Journal · doi:10.1002/biot.202300038 · Cited by 15

A novel bispecific antibody dual-targeting approach for enhanced neutralization against fast-evolving SARS-CoV-2 variants

Kim, J. W., Kim, H. J., Heo, K., Lee, Y., Jang, H. J., Lee, H., Park, J. W., Cho, Y. B., Lee, J. H., Shin, H. G., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1271508 · Cited by 15

Nature as blueprint: Global phenotype engineering of CHO production cells based on a multi-omics comparison with plasma cells

Raab, N., Zeh, N., Kretz, R., Weiß, L., Stadermann, A., Lindner, B., Fischer, S., Stoll, D., & Otte, K. (2024) · Metabolic Engineering · doi:10.1016/j.ymben.2024.03.007 · Cited by 16

Functionalized Protein Binders in Developmental Biology

Schnider, S. T., Viganò, M., Affolter, M., & Aguilar, G. (2024) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-112122-025214 · Cited by 14

Polybodies: Next-generation clinical antibodies

Pande, A. H., Sandeep, & Shinde, S. H. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104198 · Cited by 15

Therapeutic Antibodies: An Overview

Houen, G. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1450-1_1 · Cited by 15

The Role of Bispecific Antibodies in Non-Hodgkin’s Lymphoma: From Structure to Prospective Clinical Use

Tavarozzi, R., & Manzato, E. (2022) · Antibodies · doi:10.3390/antib11010016 · Cited by 15

Direct targeting of cancer cells with antibodies: What can we learn from the successes and failure of unconjugated antibodies for lymphoid neoplasias?

Golay, J. (2017) · Journal of Autoimmunity · doi:10.1016/j.jaut.2017.06.002 · Cited by 15

Mechanically interlocked functionalization of monoclonal antibodies

Bzymek, K. P., Puckett, J. W., Zer, C., Xie, J., Ma, Y., King, J. D., Goodstein, L. H., Avery, K. N., Colcher, D. M., Singh, G. P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03976-5 · Cited by 15

Investigational treatment strategies in glioblastoma: progress made and barriers to success

Nelson, T. A., & Dietrich, J. (2023) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2023.2267982 · Cited by 15

Bispecific Antibody (bsAb) Construct Formats and their Application in Cancer Therapy

Acheampong, D. O. (2019) · Protein and Peptide Letters · doi:10.2174/0929866526666190311163820 · Cited by 14

Bispecific Antibody Therapy for Effective Cardiac Repair through Redirection of Endogenous Stem Cells

Huang, K., Li, Z., Su, T., Shen, D., Hu, S., & Cheng, K. (2019) · Advanced Therapeutics · doi:10.1002/adtp.201900009 · Cited by 14

A cell line development strategy to improve a bispecific antibody expression purity in CHO cells

Ding, M., Shen, L., Xiao, L., Liu, X., & Hu, J. (2020) · Biochemical Engineering Journal · doi:10.1016/j.bej.2020.107857 · Cited by 14

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

bisFabs: Tools for rapidly screening hybridoma IgGs for their activities as bispecific antibodies

Patke, S., Li, J., Wang, P., Slaga, D., Johnston, J., Bhakta, S., Panowski, S. H., Sun, L. L., Junttila, T. T., Scheer, J. M., et al. (2017) · mAbs · doi:10.1080/19420862.2017.1281504 · Cited by 14

Chemically generated IgG2 bispecific antibodies through disulfide bridging

Patterson, J. T., Gros, E., Zhou, H., Atassi, G., Kerwin, L., Carmody, L., Zhu, T., Jones, B., Fu, Y., & Kaufmann, G. F. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.07.021 · Cited by 14

Kinetic mechanism of controlled Fab-arm exchange for the formation of bispecific immunoglobulin G1 antibodies

Goulet, D. R., Orcutt, S. J., Zwolak, A., Rispens, T., Labrijn, A. F., de Jong, R. N., Atkins, W. M., & Chiu, M. L. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000303 · Cited by 14

Fine-tuning bispecific therapeutics

Lim, S. I. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107582 · Cited by 14

Evading pre-existing anti-hinge antibody binding by hinge engineering

Kim, H. S., Kim, I., Zheng, L., Vernes, J.-M., Meng, Y. G., & Spiess, C. (2016) · mAbs · doi:10.1080/19420862.2016.1219006 · Cited by 14

Multispecific Antibodies Targeting PD-1/PD-L1 in Cancer

Chen, M., Zhou, Y., Bao, K., Chen, S., Song, G., & Wang, S.-L. (2025) · BioDrugs · doi:10.1007/s40259-025-00712-6 · Cited by 12

Promises and pitfalls for recombinant oligoclonal antibodies-based therapeutics in cancer and infectious disease

Corti, D., & Kearns, J. D. (2016) · Current Opinion in Immunology · doi:10.1016/j.coi.2016.03.001 · Cited by 13

Design and In Vitro Evaluation of a Cytotoxic Conjugate Based on the Anti-HER2 Affibody Fused to the Fc Fragment of IgG1

Sochaj-Gregorczyk, A. M., Ludzia, P., Kozdrowska, E., Jakimowicz, P., Sokołowska-Wędzina, A., & Otlewski, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081688 · Cited by 13

T-cell Activating Tribodies as a Novel Approach for Efficient Killing of ErbB2-positive Cancer Cells

Riccio, G., Ricardo, A. R., Passariello, M., Saraiva, K., Rubino, V., Cunnah, P., Mertens, N., & Lorenzo, C. D. (2018) · Journal of Immunotherapy · doi:10.1097/cji.0000000000000248 · Cited by 13

When two are better than one: Modeling the mechanisms of antibody mixtures

Einav, T., & Bloom, J. D. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007830 · Cited by 13

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

Current Status of Novel Agents for the Treatment of B Cell Malignancies: What’s Coming Next?

Tannoury, M., Garnier, D., Susín, S. A., & Bauvois, B. (2022) · Cancers · doi:10.3390/cancers14246026 · Cited by 13

Effectively removing the homodimer in bispecific antibodies by weak partitioning mode of anion exchange chromatography

Liang, X., He, Q., Qin, G., Li, G., Li, Q., Tan, H., Wang, Z., Fan, M., & Xu, D. (2023) · Journal of Chromatography B · doi:10.1016/j.jchromb.2023.123767 · Cited by 13

A detergent-based procedure for the preparation of IgG-like bispecific antibodies in high yield

Gupta, J., Hoque, M., Zaman, M., Khan, R. H., & Saleemuddin, M. (2016) · Scientific Reports · doi:10.1038/srep39198 · Cited by 13

Highly flexible, IgG-shaped, trivalent antibodies effectively target tumor cells and induce T cell-mediated killing

Dickopf, S., Lauer, M. E., Ringler, P., Spick, C., Kern, P., & Brinkmann, U. (2018) · Biological Chemistry · doi:10.1515/hsz-2018-0338 · Cited by 13

Targeting Phosphotyrosine in Native Proteins with Conditional, Bispecific Antibody Traps

Zhou, X. X., Bracken, C. J., Zhang, K., Zhou, J., Mou, Y., Wang, L., Cheng, Y., Leung, K., & Wells, J. A. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c08458 · Cited by 13

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

Expression and purification of a novel single-chain diabody (scDb-hERG1/β1) from Pichia pastoris transformants

Duranti, C., Lastraioli, E., Iorio, J., Capitani, C., Carraresi, L., Gonnelli, L., & Arcangeli, A. (2021) · Protein Expression and Purification · doi:10.1016/j.pep.2021.105879 · Cited by 13

Genetic rearrangement during site specific integration event facilitates cell line development of a bispecific molecule

Tevelev, B., Patel, H. K., Shields, K. M., Wei, W., Cooley, C., Zhang, S., Bitzas, G., Duan, W., Lam, K., Jackobek, R., et al. (2021) · Biotechnology Progress · doi:10.1002/btpr.3158 · Cited by 13

A strategy for the efficient construction of anti-PD1-based bispecific antibodies with desired IgG-like properties

Zhao, J., Jiang, L., Yang, H., Deng, L., Meng, X., Ding, J., Yang, S., Zhao, L., Xu, W., Wang, X., et al. (2022) · mAbs · doi:10.1080/19420862.2022.2044435 · Cited by 12

‘In-Format’ screening of a novel bispecific antibody format reveals significant potency improvements relative to unformatted molecules

Scott, M. J., Lee, J. A., Wake, M., Batt, K. V., Wattam, T. A., Hiles, I. D., Batuwangala, T. D., Ashman, C., & Steward, M. (2016) · mAbs · doi:10.1080/19420862.2016.1249078 · Cited by 12

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

The eIg technology to generate Ig-like bispecific antibodies

Kühl, L., Aschmoneit, N., Kontermann, R. E., & Seifert, O. (2022) · mAbs · doi:10.1080/19420862.2022.2063043 · Cited by 12

Antibody aggregation can lead to reduced Protein A binding capacity and low step yield

Yuan, G., Qu, M., Geng, Q., Dong, W., Zhang, X., & Li, Y. (2023) · Protein Expression and Purification · doi:10.1016/j.pep.2023.106315 · Cited by 12

Modulation of protein A binding allows single-step purification of mouse bispecific antibodies that retain FcRn binding

Zwolak, A., Armstrong, A. A., Tam, S. H., Pardinas, J. R., Goulet, D. R., Zheng, S., Brosnan, K., Emmell, E., Luo, J., Gilliland, G. L., et al. (2017) · mAbs · doi:10.1080/19420862.2017.1375639 · Cited by 13

Computational Design of an Allosteric Antibody Switch by Deletion and Rescue of a Complex Structural Constellation

Khowsathit, J., Bazzoli, A., Cheng, H., & Karanicolas, J. (2020) · ACS Central Science · doi:10.1021/acscentsci.9b01065 · Cited by 12

A synonymous codon change alters the drug sensitivity of ΔF508 cystic fibrosis transmembrane conductance regulator

Bali, V., Lazrak, A., Guroji, P., Fu, L., Matalon, S., & Bebok, Z. M. (2015) · The FASEB Journal · doi:10.1096/fj.15-273714 · Cited by 12

Unraveling Antibody Display: Systems Biology and Personalized Medicine

Goulart, L. R., Santos, P. D. S., Carneiro, A. P., Santana, B. A., Vallinoto, A. C. R., & Araújo, T. G. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160923112816 · Cited by 11

Antibody-Recruiting Small Molecules: Synthetic Constructs as Immunotherapeutics

McEnaney, P. J., Parker, C. G., & Zhang, A. X. (2017) · Annual reports in medicinal chemistry · doi:10.1016/bs.armc.2017.08.008 · Cited by 11

Bispecific and Biparatopic Antibody Drug Conjugates

Comer, F. I., Gao, C., & Coats, S. (2018) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-78154-9_11 · Cited by 12

Rapid Identification of Disulfide Bonds and Cysteine-Related Variants in an IgG1 Knob-into-Hole Bispecific Antibody Enhanced by Machine Learning

Baker, J. J., McDaniel, D., Cain, D., Tao, P. L., Li, C., Huang, Y., Liu, H., Zhu-Shimoni, J. X., & Niñonuevo, M. R. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04071 · Cited by 11

Single-Molecule 3D Images of “Hole-Hole” IgG1 Homodimers by Individual-Particle Electron Tomography

Lei, D., Liu, J., Liu, H., Cleveland, T. E., Marino, J. P., Lei, M., & Ren, G. (2019) · Scientific Reports · doi:10.1038/s41598-019-44978-7 · Cited by 11

Modulation of the Biophysical Properties of Bifunctional Antibodies as a Strategy for Mitigating Poor Pharmacokinetics

Datta‐Mannan, A., Brown, R. M., Fitchett, J. R., Heng, A. R., Balasubramaniam, D., Pereira, J. A., & Croy, J. E. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00074 · Cited by 11

Characterization of a single reporter-gene potency assay for T-cell-dependent bispecific molecules

Lee, H., Register, A. C., Shim, J., Contreras, E., Wu, Q., & Jiang, G. (2019) · mAbs · doi:10.1080/19420862.2019.1640548 · Cited by 11

Development and clinical application of bispecific antibody in the treatment of colorectal cancer

Balibegloo, M., & Rezaei, N. (2020) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2020.1783249 · Cited by 11

A roadmap for IgG-like bispecific antibody purification

Li, Y., Wang, Y., Shen, P. S., & Zhou, W. (2020) · Elsevier eBooks · doi:10.1016/b978-0-08-103019-6.00008-4 · Cited by 11

Developability assessment for monoclonal antibody drug candidates: a case study

Garripelli, V. K., Wu, Z. F., & Gupta, S. (2020) · Pharmaceutical Development and Technology · doi:10.1080/10837450.2020.1829641 · Cited by 11

An arrayed CRISPR screen reveals Myc depletion to increase productivity of difficult-to-express complex antibodies in CHO cells

Bauer, N., Oswald, B., Eiche, M., Schiller, L., Langguth, E., Schantz, C., Osterlehner, A., Shen, A. Y., Misaghi, S., Stingele, J., et al. (2022) · Synthetic Biology · doi:10.1093/synbio/ysac026 · Cited by 11

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

A bispecific IgG format containing four independent antigen binding sites

Ljungars, A., Schiött, T., Mattson, U., Steppa, J., Hambe, B., Semmrich, M., Ohlin, M., Tornberg, U., & Mattsson, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-58150-z · Cited by 11

Crystal structure of an L chain optimised 14F7 anti-ganglioside Fv suggests a unique tumour-specificity through an unusual H-chain CDR3 architecture

Bjerregaard-Andersen, K., Johannesen, H., Abdel‐Rahman, N., Heggelund, J. E., Hoås, H. M., Abraha, F., Bousquet, P. A., Høydahl, L. S., Burschowsky, D., Rojas, G., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-28918-5 · Cited by 10

Common light chain chickens produce human antibodies of high affinity and broad epitope coverage for the engineering of bispecifics

Ching, K. H., Berg, K., Reynolds, K., Pedersen, D., Macias, A. T., Abdiche, Y. N., Harriman, W. D., & Leighton, P. A. (2021) · mAbs · doi:10.1080/19420862.2020.1862451 · Cited by 10

A human IgE bispecific antibody shows potent cytotoxic capacity mediated by monocytes

Vukovic, N., Halabi, S., Russo-Cabrera, J. S., Blokhuis, B. R. J., Berraondo, P., Redegeld, F. A., & Zaiss, D. M. W. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102153 · Cited by 10

Manipulating Cell Fates with Protein Conjugates

Wang, Y., Wagner, C. R., & Distefano, M. D. (2022) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.2c00226 · Cited by 10

Physiologically-based pharmacokinetic model for pulmonary disposition of protein therapeutics in humans

Jagdale, P., Sepp, A., & Shah, D. K. (2022) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-022-09824-w · Cited by 10

ImmunoPET Directed to the Brain: A New Tool for Preclinical and Clinical Neuroscience

de Lucas, Á. G., Lamminmäki, U., & Lopez‐Picon, F. R. (2023) · Biomolecules · doi:10.3390/biom13010164 · Cited by 11

Treatment approaches of hard-to-treat non-Hodgkin lymphomas

Nandagopal, L., & Mehta, A. (2017) · Expert Review of Hematology · doi:10.1080/17474086.2017.1283214 · Cited by 10

Modulating Antibody Structure and Function through Directed Mutations and Chemical Rescue

Kaiser, C. E., Pabon, J. P. R., Khowsathit, J., Castaldi, M. P., Kazmirski, S. L., Weis, D. D., Zhang, A. X., & Karanicolas, J. (2018) · ACS Synthetic Biology · doi:10.1021/acssynbio.8b00124 · Cited by 10

Tethering Innate Surface Receptors on Dendritic Cells: A New Avenue for Immune Tolerance Induction?

Lamendour, L., Deluce, N. K.-N., Mouline, C. C., Gouilleux‐Gruart, V., & Velge-Roussel, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155259 · Cited by 10

Designing a new bispecific tandem single-chain variable fragment antibody against tumor necrosis factor-α and interleukin-23 using in silico studies for the treatment of rheumatoid arthritis

Barkhordari, A., Mahnam, K., & Mirmohammad-Sadeghi, H. (2020) · Journal of Molecular Modeling · doi:10.1007/s00894-020-04510-5 · Cited by 10

Relative Contribution of Framework and CDR Regions in Antibody Variable Domains to Multimerisation of Fv- and scFv-Containing Bispecific Antibodies

Bhatta, P., & Humphreys, D. P. (2018) · Antibodies · doi:10.3390/antib7030035 · Cited by 10

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 11

Buffer system improves the removal of host cell protein impurities in monoclonal antibody purification

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