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Alternative molecular formats and therapeutic applications for bispecific antibodies
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Bispecific antibodies are on the cusp of coming of age as therapeutics more than half a century after they were first described. Two bispecific antibodies, catumaxomab (Removab(®), anti-EpCAM×anti-CD3) and blinatumomab (Blincyto(®), anti-CD19×anti-CD3) are approved for therapy, and >30 additional bispecific antibodies are currently in clinical development. Many of these investigational bispecific antibody drugs are designed to retarget T cells to kill tumor cells, whereas most others are intended to interact with two different disease mediators such as cell surface receptors, soluble ligands and other proteins. The modular architecture of antibodies has been exploited to create more than 60 different bispecific antibody formats. These formats vary in many ways including their molecular weight, number of antigen-binding sites, spatial relationship between different binding sites, valency for each antigen, ability to support secondary immune functions and pharmacokinetic half-life. These diverse formats provide great opportunity to tailor the design of bispecific antibodies to match the proposed mechanisms of action and the intended clinical application.
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“Currently, there are over 60 different bsAbs formats with variations in modular structure, size, affinity/avidity, PK behavior, and intended clinical application.84”
From Tutorial on monoclonal antibody pharmacokinetics and its considerations in early development (2018) · cites this paper as [84]
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Cites
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
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
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
Cited by
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Items 501–600 of 607
Rong, Y., Chen, I.-L., Larrabee, L., Sawant, M. S., Fuh, G., & Koenig, P. S. (2024) · Antibodies · doi:10.3390/antib13010014 · Cited by 1
Hussain, H., Ozanne, A. M. S., Patel, T., Vito, D., Ellis, M., Hinchliffe, M., Humphreys, D. P., Stephens, P. E., Sweeney, B., White, J., et al. (2024) · Biotechnology and Bioengineering · doi:10.1002/bit.28879 · Cited by 1
Ligand multimerization effects on binding efficiency of Protein L affinity chromatography resins
Nikzad, J., Khandani, K. K., Talebkhan, Y., Zandi, F., Komijani, S., & Adeli, A. (2025) · Protein Expression and Purification · doi:10.1016/j.pep.2025.106790 · Cited by 1
Targeting the unexplored 'dark proteome': Novel approaches in drug discovery
Singh, D. (2025) · Current Proteomics · doi:10.1016/j.curpro.2025.100020 · Cited by 2
Study on the hole and knob related impurities in the purification of bispecific antibodies
Chen, H., Ji, N., Zhou, M., & Bu, Y. (2025) · Protein Expression and Purification · doi:10.1016/j.pep.2025.106836 · Cited by 1
Secondary antibody deficiencies: what’s around the corner?
Lagnese, G., Messuri, C., Poto, R., Varricchi, G., & Spadaro, G. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1672413 · Cited by 1
Bispecific nanobodies – promising engineered candidates with high therapeutic efficiency
Banerjee, S., Vangapally, S., Mariya, A., & Paidimuddala, B. (2026) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2026.01.010 · Cited by 1
Pothisamutyothin, K., Sathorn, S., Boonmee, R., Thaveekarn, W., & Arunmanee, W. (2026) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0014119 · Cited by 1
Calcium as a molecular switch: Gentle antibody-purification through directed evolution of Protein G
Jönsson, M., Hamnqvist, D., Dieminger, N., Nagy, T. M., Friberg, O., Wolf‐Watz, M., & Hober, S. (2026) · Separation and Purification Technology · doi:10.1016/j.seppur.2026.138115 · Cited by 1
Das, A., Paranandi, M. R., Subbiramani, K., & Reddy, R. (2026) · Biotechnology Progress · doi:10.1002/btpr.88512 · Cited by 1
Bhojnagarwala, P. S., Bordoloi, D., Jose, J. S., Tomirotti, M., Ionescu, C., Sharma, R., 赵姝姝, Kulkarni, A., Ali, A., Frase, D. M., et al. (2026) · Molecular Therapy · doi:10.1016/j.ymthe.2026.05.019 · Cited by 1
Tashima, T. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c00602 · Cited by 1
Antibody based therapy for childhood solid cancers
Birley, K., Chester, K. A., & Anderson, J. (2018) · Current Opinion in Chemical Engineering · doi:10.1016/j.coche.2018.01.005 · Cited by 1
LINGO-1 is a New Therapy Target and Biomarker for Ewing Sarcoma.
Jain, A., Zhang, J., & Rabbitts, T. H. (2017) · PubMed · Cited by 1
Preclinical Development of Monoclonal Antibodies
Meyer-Tamaki, K. B. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803620-4.00023-2 · Cited by 1
Structural arrangement of the VH and VL domains in the COBRA™ T-cell engaging single-chain diabody
Krakow, J. L., Hammel, M., Zhu, Y. J., Hillier, B. J., Paolella, B., Desmarais, A., Wall, R., Chen, T.-H. T., Pei, R., Karunatilake, C., et al. (2021) · Antibody Therapeutics · doi:10.1093/abt/tbab028 · Cited by 1
Zhao, M. K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.06728-5 · Cited by 1
Bispecific antibodies and its applications: a novel approach for targeting SARS-Cov-2
Shukla, A. K., & Misra, S. (2023) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2022-0068 · Cited by 1
Drug discovery processes: When and where the rubber meets the road
Miller, S. M., Moos, W. H., Munk, B. H., Munk, S. A., Hart, C. P., & Spellmeyer, D. C. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-824304-6.00025-0 · Cited by 1
Analysis of pharmaceutically and biologically relevant protein variants
Bobály, B. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-99969-4.00025-5 · Cited by 1
Clinical Application of Therapeutic Bispecific Antibodies
Belachew, G. T. (2023) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2023.49.007880 · Cited by 1
Development of an enabling platform biotechnology for the production of proteins
Aschenbrenner, I., Böckler, M., Franke, F. C., Liebl, K., Catici, D. A. M., Brandl, M., Behnke, J., & Feige, M. J. (2024) · Biological Chemistry · doi:10.1515/hsz-2023-0376 · Cited by 1
Song, M.-S., Cao, W., & Liu, Q. (2024) · Biochemical Engineering Journal · doi:10.1016/j.bej.2024.109462 · Cited by 1
Zhan, L., Xie, L., Lv, F., Huang, J., Chen, Z., Wang, L., & Chen, Z. (2024) · Journal of Chromatography B · doi:10.1016/j.jchromb.2024.124357 · Cited by 1
Synthetic Antibody Engineering: Concepts and Applications
Lai, J. R., Chen, G., & Sidhu, S. S. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-803369-2.00003-6 · Cited by 1
Novel Technologies for Generation of Bispecific Constructs
Fayadat‐Dilman, L. (2018) · Springer eBooks · doi:10.1007/978-981-13-0496-5_6 · Cited by 1
Producing and prospects for the use of bispecific antibodies for the treatment of cancer
Sedykh, S. E., & Nevinsky, G. A. (2019) · Advances in molecular oncology · doi:10.17650/2313-805x-2018-5-4-30-40 · Cited by 1
Monoclonal Antibody-Directed Therapy
Kayser, V., & Datta‐Mannan, A. (2022) · MDPI eBooks · doi:10.3390/books978-3-0365-2872-4 · Cited by 1
Müller‐Späth, T., & Morbidelli, M. (2017) · doi:10.1002/9781119126942.ch18 · Cited by 1
Arathoon, R., Briante, R., O’Connor, A., Tan, S. Y., Klein, P. M., Morgan, J., Ponath, P. D., Presta, L. G., Zhai, Q., Mohanty, S., et al. (2021) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2021-sitc2021.282 · Cited by 1
Self-citationA bioorthogonal antibody-based chemically-induced-dimerization switch for therapeutic applicationPreprint
Martinko, A. J., Tran, H. L., Simonds, E. F., Cooke, A. L., Huang, Z. X., Raguveer, S., Agullet, J. P., Prasad, S., Going, C. C., Marshall, L. A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.11.536272 · Cited by 1
Analytical Characterization of Bispecific Antibodies and Bispecific Molecules
Dillon, M. A., Lombana, T. N., & Spiess, C. (2025) · Wiley eBooks · doi:10.1002/9781394236145.ch2 · Cited by 1
Self-citationSchmittnaegel, M., Klein, C., Levitsky, V., & Knoetgen, H. (2015) · OncoImmunology · doi:10.1080/2162402x.2015.1052930
Future outlook for acute leukemias
Subklewe, M. S. (2016) · Springer eBooks · doi:10.1007/978-3-319-26772-2_8
Therapeutic Applications: Strategies and Molecules Targeting the IL-17/Th17 Pathway
Chu, C. (2016) · Springer eBooks · doi:10.1007/978-3-319-28040-0_5
Cua, S. (2017) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/72381
Characterization of Bispecific or Other Hybrid Molecules
Lombana, T. N., & Spiess, C. (2017) · Wiley eBooks · doi:10.1002/9781119384434.ch8
Self-citationFuture Horizons and New Target Class Opportunities
Wu, H., Webster, C. I., Paterson, J., Guillard, S., Jackson, R., & Minter, R. (2017) · Methods and principles in medicinal chemistry · doi:10.1002/9783527699124.ch21
Immune Therapies in Phase 1 Trials
Postel-Vinay, S. C., & Soria, J. (2017) · Springer eBooks · doi:10.1007/978-3-319-62431-0_32
Rajan, S., Sonoda, J., Tully, T., Williams, A. J., Yang, F., Macchi, F. D., Hudson, T., Chen, M. Z., Liu, S., Valle, N., et al. (2018) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/j.vascn.2018.04.002
Ratanji, K. D. (2017) · Research Explorer (The University of Manchester)
IL-17/TNF-α BISPECIFIC ANTIBODIES AS NEW THERAPEUTIC APPROACH TO RHEUMATOID ARTHRITIS
Adnan, M. (2020) · TURKISH MEDICAL STUDENT JOURNAL · doi:10.4274/tmsj.galenos.2020.07.01.07
Novel Agents Beyond Immunomodulatory Agents and Phosphoinositide-3-Kinase for Follicular Lymphoma
Chin, C. K., & Nastoupil, L. J. (2020) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2020.03.002
High fidelity affinity purification of Fc-fusion molecules from product related impurities
Coyle, B. L., Scanlon, T., Kearns, K., Mohanty, A., Lacki, K. M., & Kett, W. C. (2020) · Elsevier eBooks · doi:10.1016/b978-0-08-103019-6.00003-5
Fcγ receptors—Master regulators of antibody therapy
Beers, S. A., & Frendéus, B. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822028-3.00014-5
Little, M. (2021) · Springer eBooks · doi:10.1007/978-3-030-72599-0_8
Recruiting Killer Cells for Cancer Therapy
Little, M. (2021) · Springer eBooks · doi:10.1007/978-3-030-72599-0_9
Development of Immunotherapeutic Strategies for Early Phase Clinical Trials
Martín-Romano, P., Chabanon, R. M., Procureur, A., Aspeslagh, S., & Postel-Vinay, S. C. (2020) · Springer eBooks · doi:10.1007/978-3-030-47682-3_15
Advanced structural elucidation of new antibody formats by mass spectrometry
Graf, T., Leiß, M., Haberger, M., & Bulau, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822318-5.00005-3
Targeted immunotherapies to consider for B Cell non-hodgkin lymphoma
Namoglu, E. C., Hughes, M. E., & Nasta, S. D. (2021) · Expert Review of Precision Medicine and Drug Development · doi:10.1080/23808993.2021.1967142
Role of Bispecific antibody for Multiple Myeloma; A literature Review
Waleed, M. S. (2021) · Journal of Oncology Research Review & Reports · doi:10.47363/jonrr/2021(2)144
Treatment of Acute Myeloid Leukemia: A Concise Overview
(2020) · Abasyn Journal Life Sciences · doi:10.34091/ajls.3.2.11
Gu, J., McCluskey, A. J., & Ghayur, T. (2017) · Methods and principles in medicinal chemistry · doi:10.1002/9783527699124.ch8
Novel Antibody Interfaces Revealed Through Structural MiningPreprint
Yin, Y., Romei, M. G., Sankar, K., Pal, L. R., Hoi, K. H., Yang, Y., Leonard, B. C., Boenig, G. D. L., Kumar, N., Matsumoto, M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.06.487381
Virgilio, F. D. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732240772.793546180
Faculty Opinions recommendation of Current progress in innovative engineered antibodies.
Abdiche, Y. N. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.729268838.793560915
Paul, S., Planque, S. A., & Massey, R. J. (2015) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0001278.pub3
Tuning the potency and therapeutic window of ImmTAC molecules by affinity modulationPreprint
Robertson, I. B., Mulvaney, R., Dieckmann, N. M. G., Vantellini, A., Canestraro, M., Amicarella, F., O’Dwyer, R., Cole, D. K., Harper, S. J., Dushek, O., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.03.511676
Fuselli, A., Bürgi, M., Kratje, R. B., & Prieto, C. C. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12282-6
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Bansode, M., Deb, K., & Deb, S. (2022) · Methods and principles in medicinal chemistry · doi:10.1002/9783527827855.ch13
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Yasunaga, M. (2023) · Springer eBooks · doi:10.1007/978-3-030-80962-1_200-1
A novel brick for bispecific antibody construction
He, Y., Ma, H., Wang, C., Ai, Z., Wu, Q. Y., Chen, H., & Lu, D. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26492
Vyver, A. J. V. D., Weinzierl, T., Eigenmann, M. J., Frances, N., Herter, S., Buser, R. B., Somandin, J., Diggelmann, S., Limani, F., Lehr, T., et al. (2023) · doi:10.1158/1535-7163.c.6543060.v1
Vyver, A. J. V. D., Weinzierl, T., Eigenmann, M. J., Frances, N., Herter, S., Buser, R. B., Somandin, J., Diggelmann, S., Limani, F., Lehr, T., et al. (2023) · doi:10.1158/1535-7163.22521573
Vyver, A. J. V. D., Weinzierl, T., Eigenmann, M. J., Frances, N., Herter, S., Buser, R. B., Somandin, J., Diggelmann, S., Limani, F., Lehr, T., et al. (2023) · doi:10.1158/1535-7163.c.6543060
Vyver, A. J. V. D., Weinzierl, T., Eigenmann, M. J., Frances, N., Herter, S., Buser, R. B., Somandin, J., Diggelmann, S., Limani, F., Lehr, T., et al. (2023) · doi:10.1158/1535-7163.22521573.v1
Data from Valency of HER2 Targeting Antibodies Influences Tumor Cell Internalization and Penetration
Ramos, M. K., Mandikian, D., Sermeño, L. N., King, A., Dent, A. T., Ho, J., Ulufatu, S., Lombana, T. N., Spiess, C., Go, M. A. T., et al. (2023) · doi:10.1158/1535-7163.c.6542773.v1
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Chasov, V. V., Zmievskaya, E., Ganeeva, I., Gilyazova, E., Davletshin, D., Mirgayazova, R., Khadiullina, R., Valiullina, A., Rizvanov, A. A., & Bulatov, E. (2023) · Preprints.org · doi:10.20944/preprints202309.1136.v1
Monoklonale Anti-Allergen-Antikörper für die Behandlung von Allergien
Pengo, N., Wuillemin, N., Bieli, D., & Gasser, P. (2023) · Allergo Journal · doi:10.1007/s15007-023-5819-3
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Song, M., Cao, W., & Liu, Q. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4809332
Optimization of Mixed-Mode Resins by Integrating Experimental Design and High-Throughput ScreeningPreprint
Song, M., Cao, W., & Liu, Q. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4841900
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Bogdanowicz, A., Wojas‐Krawczyk, K., Krzyżanowska, N., & Krawczyk, P. A. (2024) · Oncology in Clinical Practice · doi:10.5603/ocp.98901
Bispecific Antibodies: An Emerging Concept in Antibody-Based Cancer Therapies
Brandão, R. O., Jiang, X., Selvaraju, S., & Mohapatra, P. (2024) · Interdisciplinary biotechnological advances · doi:10.1007/978-981-97-5508-0_4
Iskra, T., Sacramo, A., & Scarcelli, J. J. (2024) · Springer eBooks · doi:10.1007/978-3-031-62007-2_5
Guarnaccia, A. D., Sandoval, W. N., & Lill, J. R. (2025) · doi:10.1002/9781394236145.ch1
Development of Next-Generation Antibody Therapeutics Using DDS and Molecular Imaging
Yasunaga, M. (2025) · Springer eBooks · doi:10.1007/978-3-032-00767-4_200
Köseoğlu, A. E., Gül, N., Duran, T., Öztürk, C., & Hekim, N. (2026) · Gene · doi:10.1016/j.gene.2026.149999
Modular construction of bispecific antibodies through bioconjugation for T cell-based immunotherapyPreprint
Sun, S.-Q., Wang, L., Xia, J., Li, S., Zhu, J.-M., Cai-wen, D., & Chen, K. (2026) · Research Square · doi:10.21203/rs.3.rs-8371642/v1
Rowe, B., Reese, K. J., McGrath, K., Concannon, A. A., Schwartz, A. M., & Gunn, G. R. (2025) · Bioanalysis · doi:10.1080/17576180.2026.2617254
Bispecifics: The future of therapeutic antibodies
Davis, J. H. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00093-5
Tang, H., McCoy, M., Leonard, A., Mohan, K., Sane, R., Guan, C., Kullolli, M., & Koep, K. (2026) · The AAPS Journal · doi:10.1208/s12248-026-01216-z
Lanshoeft, C. (2017) · theses.fr (ABES) · doi:10.70675/70955a37z9a6cz40f5zbe72z9049aa84a7f0
Développement et évaluation d'anticorps bispécifiques dans le traitement du Myélome multiple
Fayon, M. (2019) · theses.fr (ABES) · doi:10.70675/f357d44fz13a7z4f3bza50cz18ea6c378e17
Développement d’un assemblage multispécifique de Nanofitines à activité anti-tumorale
Jacquot, P. (2022) · theses.fr (ABES) · doi:10.70675/4a1dcc72z0725z4d2ez80d6zf930f0086aa9
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Fenis, A. (2024) · theses.fr (ABES) · doi:10.70675/747c59caz7a79z4064z989cz9dd2bc8bd27e
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Kang, J., Zhang, M., He, Y. B., Chen, J., Liu, X., & Lv, Q. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1746093
Gudavalekar, P. U., Khandave, P. Y., Shalini, S., Selvaraju, S., & Pande, A. H. (2026) · Drug Discovery Today · doi:10.1016/j.drudis.2026.104670
Ramírez-Villarreal, J., & Álvarez-Martínez, R. (2026) · International Journal of Microbiology · doi:10.1155/ijm/5903624
Laboratory-Scale Production of Recombinant IgG Antibodies
Anzai, T., & Yasunaga, M. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5037-0_8
Shi, P., Zheya, Z., He, W., Duan, Y., He, Y., 冯华朋, & Shu, J. (2026) · Frontiers in Veterinary Science · doi:10.3389/fvets.2026.1854176
Ming, K., Hu, Y., Xing, B., Chen, M., Chen, Y., Chen, X., Geng, M., Wu, Z., Liu, Y., Wei, L., et al. (2026) · Materials Today Bio · doi:10.1016/j.mtbio.2026.103336
원혜윤, Park, E., Roh, Y.-G., Kang, M., & Kim, N. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1848290
Pishgahzadeh, E., Mafakher, L., Dabirian, S., Vahidi, H., Kazemi‐Lomedasht, F., Jamshidi, H., & Mohit, E. (2026) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2026.104432
Advancing recombinant protein production in CHO cells through metabolic engineering
Hou, L., Li, W., Li, Z., Geng, S., Wang, T., & Zhang, J. (2026) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2026.1847073
The sweet spot in protein design—Where deep learning meets first principles
Cia, G., Orlando, G., Cianferoni, D., van der Kant, R., Delgado, J., Verschueren, E., Rousseau, F., Serrano, L. G., & Schymkowitz, J. W. H. (2026) · FEBS Letters · doi:10.1002/1873-3468.70429
Spitler, K., Степурська, К. В., Liu, D., Legg, K. M., Hayes, S., Lippold, S., Li, D., Griffitts, T., & Yang, F. (2026) · Talanta · doi:10.1016/j.talanta.2026.130523
Metadata
- Authors
- Spiess, C., Zhai, Q., & Carter, P. J.
- Affiliations
- Genentech (US)
- Corresponding author
- Carter, Paul J.
- Venue
- Molecular Immunology
- Publisher
- Elsevier BV
- Published
- 2015-10
- Volume
- 67
- Issue
- 2
- Pages
- 95-106
- ISSN
- 0161-5890 (ISSN-L)
- OpenAlex
- W1981730803
- Cited by
- 607
- References
- 127
- Citations by year
- 2026: 35 · 2025: 28 · 2024: 49 · 2023: 58 · 2022: 35 · 2021: 61 · 2020: 60 · 2019: 58 · 2018: 69 · 2017: 78 · 2016: 55 · 2015: 21
- FWCI
- 11.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular Immunology (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
- Keywords
- bispecific antibodies, catumaxomab, blinatumomab, T cell redirection, antibody engineering, pharmacokinetics, antibody valency, antibody binding sites, antibody half-life, cancer immunotherapy
- MeSH terms
- Epithelial Cell Adhesion Molecule, Antigens, Neoplasm, Antineoplastic Agents, Humans, Immunotherapy, Neoplasms, Cell Adhesion Molecules, CD3 Complex, Antibodies, Bispecific, Models, Immunological, Antigens, CD19
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