Alternative molecular formats and therapeutic applications for bispecific antibodies

FcRn: the neonatal Fc receptor comes of age

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

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Single-Chain Antigen-Binding Proteins

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The therapeutic monoclonal antibody market

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

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

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Biopharmaceutical benchmarks 2014

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

Macromolecular Modeling with Rosetta

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

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

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Liposomal nanoparticle armed with bivalent bispecific single-domain antibodies, novel weapon in HER2 positive cancerous cell lines targeting

Nikkhoi, S. K., Rahbarizadeh, F., Ranjbar, S., Khaleghi, S., & Farasat, A. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.01.010 · Cited by 29

Chromatographic behavior of bivalent bispecific antibodies on cation exchange columns. I. Experimental observations and phenomenological model

Kimerer, L. K., Pabst, T. M., Hunter, A. K., & Carta, G. (2019) · Journal of Chromatography A · doi:10.1016/j.chroma.2019.04.012 · Cited by 29

PEG Linker Improves Antitumor Efficacy and Safety of Affibody-Based Drug Conjugates

Li, Q., Li, W., Xu, K., Xing, Y., Shi, H., Jing, Z., Li, S., & Hong, Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041540 · Cited by 28

Cancer immunotherapies revisited: state of the art of conventional treatments and next-generation nanomedicines

García-Fernández, C., Saz, A., Fornaguera, C., & Borrós, S. (2021) · Cancer Gene Therapy · doi:10.1038/s41417-021-00333-5 · Cited by 30

Modular Chemical Construction of IgG-like Mono- and Bispecific Synthetic Antibodies (SynAbs)

Thoreau, F., Szijj, P. A., Greene, M. K., Rochet, L. N. C., Thanasi, I. A., Blayney, J. K., Maruani, A., Baker, J. R., Scott, C. J., & Chudasama, V. (2023) · ACS Central Science · doi:10.1021/acscentsci.2c01437 · Cited by 28

CD44v6-Targeted Imaging of Head and Neck Squamous Cell Carcinoma: Antibody-Based Approaches

Spiegelberg, D., & Nilvebrant, J. (2017) · Contrast Media & Molecular Imaging · doi:10.1155/2017/2709547 · Cited by 28

A comparative study of the developability of full-length antibodies, fragments, and bispecific formats reveals higher stability risks for engineered constructs

Morales, I. C., Dingfelder, F., Waibel, I., Turnbull, O. M., Patel, B., Cao, Z., Bjelke, J. R., Grell, S. N., Bennet, A., Hummer, A. M., et al. (2024) · mAbs · doi:10.1080/19420862.2024.2403156 · Cited by 27

Modeling bispecific monoclonal antibody interaction with two cell membrane targets indicates the importance of surface diffusion

Sengers, B. G., McGinty, S., Nouri, F. Z., Argungu, M., Hawkins, E., Hadji, A., Weber, A. D., Taylor, A. R., & Sepp, A. (2016) · mAbs · doi:10.1080/19420862.2016.1178437 · Cited by 30

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

Engaging Cytotoxic T and NK Cells for Immunotherapy in Chronic Lymphocytic Leukemia

Hofland, T., Eldering, E., Kater, A. P., & Tonino, S. H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174315 · Cited by 27

2020 White Paper on Recent Issues in Bioanalysis: BAV Guidance, CLSI H62, Biotherapeutics Stability, Parallelism Testing, CyTOF and Regulatory Feedback ( Part 2A –Recommendations on Biotherapeutics Stability, PK LBA Regulated Bioanalysis, Biomarkers Assays, Cytometry Validation & Innovation Part 2B –Regulatory Agencies’ Inputs on Bioanalysis, Biomarkers, Immunogenicity, Gene & Cell Therapy and Vaccine)

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Multi-attribute method based characterization of antibody drug conjugates (ADC) at the intact and subunit levels

Martelet, A., Garrigue, V., Zhang, Y., Genêt, B., & Guttman, A. (2021) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2021.114094 · Cited by 27

Antibody affinity maturation by computational design

Kuroda, D., & Tsumoto, K. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8648-4_2 · Cited by 26

IGF2 Peptide-Based LYTACs for Targeted Degradation of Extracellular and Transmembrane Proteins

Mikitiuk, M., Barczyński, J., Bielski, P., Arciniega, M., Tyrcha, U., Hec, A., Lipińska, A. D., Rychłowski, M., Holak, T. A., & Sitar, T. (2023) · Molecules · doi:10.3390/molecules28227519 · Cited by 26

Revolutionizing cancer treatment: the power of bi- and tri-specific T-cell engagers in oncolytic virotherapy

Mehrabadi, A. Z., Tat, M., Alvanegh, A. G., Roozbahani, F., & Ghaleh, H. E. G. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1343378 · Cited by 29

Targeting acute myeloid leukemia through antibody engineering: innovations in immunotherapy and combination regimens

Samarkhazan, H. S., Noormohamadi, H., Shafiei, F. S., Taghinejad, Z., Maleknia, M., Raoufi, A., Nouri, S., & Mohammadi, M. H. (2025) · Clinical and Experimental Medicine · doi:10.1007/s10238-025-01764-2 · Cited by 26

Synergistic Neutralization of Pertussis Toxin by a Bispecific Antibody In Vitro and In Vivo

Wagner, E. K., Wang, X., Bui, A., & Maynard, J. A. (2016) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00371-16 · Cited by 27

Dual anti-idiotypic purification of a novel, native-format biparatopic anti-MET antibody with improved in vitro and in vivo efficacy

Godar, M., Morello, V., Sadi, A., Hultberg, A., Jonge, N. D., Basilico, C., Hanssens, V., Saunders, M. J., Lambrecht, B. N., Khattabi, M. E., et al. (2016) · Scientific Reports · doi:10.1038/srep31621 · Cited by 28

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

Multimeric antibodies with increased valency surpassing functional affinity and potency thresholds using novel formats

Miller, A., Carr, S. B., Rabbitts, T. H., & Ali, H. (2020) · mAbs · doi:10.1080/19420862.2020.1752529 · Cited by 26

Production and characterization of a human antisperm monoclonal antibody against CD52g for topical contraception in women

Vaca, G. B., Marathe, J. G., Politch, J. A., Mausser, E., Pudney, J. A., Doud, J., Nador, E., Zeitlin, L., Pauly, M. H., Moench, T. R., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103478 · Cited by 26

Application of mRNA Technology in Cancer Therapeutics

Eralp, Y. (2022) · Vaccines · doi:10.3390/vaccines10081262 · Cited by 27

Application of recombinant antibodies for treatment of Clostridioides difficile infection: Current status and future perspective

Raeisi, H., Azimirad, M., Nabavi-Rad, A., Aghdaei, H. A., Yadegar, A., & Zali, M. R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.972930 · Cited by 28

miR‐143 targets MAPK7 in CHO cells and induces a hyperproductive phenotype to enhance production of difficult‐to‐express proteins

Schoellhorn, M., Fischer, S., Wagner, A., Handrick, R., & Otte, K. (2017) · Biotechnology Progress · doi:10.1002/btpr.2475 · Cited by 26

GingisKHAN™ protease cleavage allows a high-throughput antibody to Fab conversion enabling direct functional assessment during lead identification of human monoclonal and bispecific IgG1 antibodies

Moelleken, J., Endesfelder, M., Gassner, C., Lingke, S., Tomaschek, S., Tyshchuk, O., Lorenz, S. H., Reiff, U., & Mølhøj, M. (2017) · mAbs · doi:10.1080/19420862.2017.1364325 · Cited by 26

An end-to-end automated platform process for high-throughput engineering of next-generation multi-specific antibody therapeutics

Furtmann, N., Schneider, M., Spindler, N., Steinmann, B., Li, Z., Focken, I., Meyer, J., Dimova, D., Kroll, K., Leuschner, W. D., et al. (2021) · mAbs · doi:10.1080/19420862.2021.1955433 · Cited by 25

Bispecific CD3/HER2 Targeting FynomAb Induces Redirected T Cell-Mediated Cytolysis with High Potency and Enhanced Tumor Selectivity

Wuellner, U., Klupsch, K., Buller, F., Attinger-Toller, I., Santimaria, R., Zbinden, I., Henne, P., Grabulovski, D., Bertschinger, J., & Brack, S. (2015) · Antibodies · doi:10.3390/antib4040426 · Cited by 25

The current status of immunotherapy in peritoneal carcinomatosis

Ströhlein, M. A., Heiss, M. M., & Jauch, K. (2016) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2016.1224666 · Cited by 25

BiHC, a T-Cell–Engaging Bispecific Recombinant Antibody, Has Potent Cytotoxic Activity Against Her2 Tumor Cells

Xing, J., Lin, L., Li, J., Liu, J., Zhou, C., Pan, H., Shu, R., Dong, B., Cao, D., Li, Q., et al. (2017) · Translational Oncology · doi:10.1016/j.tranon.2017.07.003 · Cited by 27

Current Considerations on Characterization of Immune Response to Multi-Domain Biotherapeutics

Gorovits, B., Peng, K., & Kromminga, A. (2019) · BioDrugs · doi:10.1007/s40259-019-00389-8 · Cited by 25

Accelerating and de‐risking CMC development with transposon‐derived manufacturing cell lines

Rajendran, S., Balasubramanian, S., Webster, L., Lee, M., Vavilala, D. T., Kulikov, N., Choi, J., Tang, C., Hunter, M., Wang, R., et al. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27742 · Cited by 25

Bispecific antibodies and autologous chimeric antigen receptor T cell therapies for treatment of hematological malignancies

Hadidi, S. A., Heslop, H. E., Brenner, M. K., & Suzuki, M. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.05.039 · Cited by 29

An integrated approach for characterizing immunogenic responses toward a bispecific antibody

Cohen, S., Chung, S., Spiess, C., Lundin, V., Stefanich, E. G., Laing, S. T., Clark, V., Brumm, J., Zhou, Y., Huang, C., et al. (2021) · mAbs · doi:10.1080/19420862.2021.1944017 · Cited by 24

Impact of antibody architecture and paratope valency on effector functions of bispecific NKp30 x EGFR natural killer cell engagers

Boje, A. S., Pekar, L., Koep, K., Lipinski, B., Rabinovich, B. A., Evers, A., Gehlert, C. L., Krohn, S., Xiao, Y., Krah, S., et al. (2024) · mAbs · doi:10.1080/19420862.2024.2315640 · Cited by 24

Transient and stable CHO expression, purification and characterization of novel hetero‐dimeric bispecific I g G antibodies

Rajendra, Y., Peery, R. B., Hougland, M. D., Barnard, G. C., Wu, X., Fitchett, J. R., Bacica, M., & Demarest, S. J. (2016) · Biotechnology Progress · doi:10.1002/btpr.2414 · Cited by 24

A novel synthetic trivalent single chain variable fragment (tri-scFv) construction platform based on the SpyTag/SpyCatcher protein ligase system

Alam, M. K., Brabant, M., Solomon, V. R., Barreto, K., Fonge, H., & Geyer, C. R. (2018) · BMC Biotechnology · doi:10.1186/s12896-018-0466-6 · Cited by 23

Controlled conductivity at low pH in Protein L chromatography enables separation of bispecific and other antibody formats by their binding valency

Chen, C., Wakabayashi, T., Muraoka, M., Feng, S., Shan, C. W., Kun, C. C., Jang, C. T., Soehano, I., Shimizu, Y., Igawa, T., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1583996 · Cited by 23

Predicting Tumor Killing and T-Cell Activation by T-Cell Bispecific Antibodies as a Function of Target Expression: Combining In Vitro Experiments with Systems Modeling

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. (2020) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-20-0269 · Cited by 26

Combination of IM-Based Approaches to Unravel the Coexistence of Two Conformers on a Therapeutic Multispecific mAb

Deslignière, E., Ollivier, S., Ehkirch, A., Martelet, A., Ropartz, D., Lechat, N., Hernandez‐Alba, O., Menet, J.-M., Clavier, S., Rogniaux, H., et al. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c00928 · Cited by 23

Standardized method for mechanistic modeling of multimodal anion exchange chromatography in flow through operation

Hess, R. T., Yun, D., Saleh, D., Briskot, T., Grosch, J., Wang, G., Schwab, T., & Hubbuch, J. J. (2023) · Journal of Chromatography A · doi:10.1016/j.chroma.2023.463789 · Cited by 23

Connected mechanistic process modeling to predict a commercial biopharmaceutical downstream process

Rischawy, F., Briskot, T., Hopf, N., Saleh, D., Wang, G., Kluters, S., Studts, J., & Hubbuch, J. J. (2023) · Computers & Chemical Engineering · doi:10.1016/j.compchemeng.2023.108292 · Cited by 23

Diabody-Ig: a novel platform for the generation of multivalent and multispecific antibody molecules

Seifert, O., Rau, A., Beha, N., Richter, F., & Kontermann, R. E. (2019) · mAbs · doi:10.1080/19420862.2019.1603024 · Cited by 23

Characterization of a Novel Bispecific Antibody With Improved Conformational and Chemical Stability

Manikwar, P., Mulagapati, S. H. R., Kasturirangan, S., Moez, K., Rainey, G. J., & Lobo, B. A. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.06.025 · Cited by 23

An update on antibody-based immunotherapies for Clostridium difficile infection

Tanha, J., & Hussack, G. (2016) · Clinical and Experimental Gastroenterology · doi:10.2147/ceg.s84017 · Cited by 22

Targeting Solid Tumors Using CD3 Bispecific Antibodies

Crawford, A., & Chiu, D. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0073 · Cited by 22

Regulatory considerations in the design, development and quality of monoclonal antibodies and related products for the diagnosis and treatment of cancer

Shapiro, M. A. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1379738 · Cited by 22

Recombinant Antibodies to Arm Cytotoxic Lymphocytes in Cancer Immunotherapy

Koch, J., & Tesar, M. (2017) · Transfusion Medicine and Hemotherapy · doi:10.1159/000479981 · Cited by 22

Molecular engineering strategies and methods for the expression and purification of IgG1-based bispecific bivalent antibodies

Dimasi, N., Fleming, R. L., Wu, H., & Gao, C. (2018) · Methods · doi:10.1016/j.ymeth.2018.08.004 · Cited by 22

Targeting acute myeloid leukemia stem cells: Current therapies in development and potential strategies with new dimensions

Tan, Y., Wu, Q., & Zhou, F. (2020) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2020.102993 · Cited by 20

Combined Anti-Cancer Strategies Based on Anti-Checkpoint Inhibitor Antibodies

Golay, J., & Andrea, A. E. (2020) · Antibodies · doi:10.3390/antib9020017 · Cited by 24

Discovery Strategies to Maximize the Clinical Potential of T-Cell Engaging Antibodies for the Treatment of Solid Tumors

Voynov, V., Adam, P. J., Nixon, A. E., & Scheer, J. M. (2020) · Antibodies · doi:10.3390/antib9040065 · Cited by 22

Development of a Trispecific Antibody Designed to Simultaneously and Efficiently Target Three Different Antigens on Tumor Cells

Dimasi, N., Fleming, R. L., Hay, C. M., Woods, R., XU, L. L., Wu, H., & Gao, C. (2015) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5b00268 · Cited by 22

Monitoring removal of hole-hole homodimer by analytical hydrophobic interaction chromatography in purifying a bispecific antibody

Chen, T., Han, J.-Y., Guo, G., Wang, Q., Wang, Y., & Li, Y. (2019) · Protein Expression and Purification · doi:10.1016/j.pep.2019.105457 · Cited by 21

Multiscale modeling of protein membrane interactions for nanoparticle targeting in drug delivery

Eckmann, D. M., Bradley, R. P., Kandy, S. K., Patil, K., Janmey, P. A., & Radhakrishnan, R. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.06.023 · Cited by 21

A Comprehensive Review of Biological Agents for Lupus: Beyond Single Target

Yang, B., Zhao, M., Wu, H., & Lu, Q. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.539797 · Cited by 21

Tuning the potency and selectivity of ImmTAC molecules by affinity modulation

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. (2023) · Clinical & Experimental Immunology · doi:10.1093/cei/uxad120 · Cited by 22

Targeting Human-Cytomegalovirus-Infected Cells by Redirecting T Cells Using an Anti-CD3/Anti-Glycoprotein B Bispecific Antibody

Meng, W., Tang, A., Ye, X., Gui, X., Li, L., Fan, X., Schultz, R. D., Freed, D. C., Ha, S., Wang, D., et al. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01719-17 · Cited by 21

Current strategies in the non-clinical safety assessment of biologics: New targets, new molecules, new challenges

Brennan, F. R., Andrews, L., Arulanandam, A. R. N., Blümel, J., Fikes, J., Grimaldi, C. M., Lansita, J. A., Loberg, L. I., MacLachlan, T. K., Milton, M., et al. (2018) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2018.07.009 · Cited by 21

Toward a Combinatorial Approach for the Prediction of IgG Half-Life and Clearance

Goulet, D. R., Watson, M. J., Tam, S. H., Zwolak, A., Chiu, M. L., Atkins, W. M., & Nath, A. (2018) · Drug Metabolism and Disposition · doi:10.1124/dmd.118.081893 · Cited by 21

Generation of bispecific antibodies using chemical conjugation methods

Dimasi, N., Kumar, A., & Gao, C. (2021) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2021.08.006 · Cited by 20

Simultaneous evaluation of treatment efficacy and toxicity for bispecific T‐cell engager therapeutics in a humanized mouse model

Yang, J., Jiao, J., Draheim, K., Yang, G., Yang, H., Yao, L., Shultz, L. D., Greiner, D. L., Rajagopal, D., Vessillier, S., et al. (2023) · The FASEB Journal · doi:10.1096/fj.202300040r · Cited by 20

Detection of a phosphorylated glycine-serine linker in an IgG-based fusion protein

Tyshchuk, O., Völger, H. R., Ferrara, C., Bulau, P., Koll, H., & Mølhøj, M. (2016) · mAbs · doi:10.1080/19420862.2016.1236165 · Cited by 20

Novel multispecific heterodimeric antibody format allowing modular assembly of variable domain fragments

Egan, T. J., Diem, D., Weldon, R., Neumann, T., Meyer, S., & Urech, D. (2016) · mAbs · doi:10.1080/19420862.2016.1248012 · Cited by 20

Influence of Escherichia coli chaperone DnaK on protein immunogenicity

Ratanji, K. D., Derrick, J. P., Kimber, I., Thorpe, R., Wadhwa, M., & Dearman, R. J. (2016) · Immunology · doi:10.1111/imm.12689 · Cited by 20

IgG light chain-independent secretion of heavy chain dimers: consequence for therapeutic antibody production and design

Stoyle, C. L., Stephens, P. E., Humphreys, D. P., Heywood, S. P., Cain, K., & Bulleid, N. J. (2017) · Biochemical Journal · doi:10.1042/bcj20170342 · Cited by 20

Decomposing Dynamical Couplings in Mutated scFv Antibody Fragments into Stabilizing and Destabilizing Effects

Ramaprasad, A. S. E., Uddin, S., Casas‐Finet, J. R., & Jacobs, D. J. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09268 · Cited by 21

Hydrogel Formulations for biologicals: Current Spotlight From a Commercial Perspective

Ickenstein, L. M., & Garidel, P. (2018) · Therapeutic Delivery · doi:10.4155/tde-2017-0085 · Cited by 20

Viscosities and Protein Interactions of Bispecific Antibodies and Their Monospecific Mixtures

Woldeyes, M. A., Josephson, L. L., Leiske, D. L., Galush, W. J., Roberts, C. J., & Furst, E. M. (2018) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.8b00706 · Cited by 20

Editorial overview: Special section: New concepts in antibody therapeutics: What's in store for antibody therapy?

Schuurman, J., & Parren, P. W. H. I. (2016) · Current Opinion in Immunology · doi:10.1016/j.coi.2016.04.001 · Cited by 20

Engineered Bifunctional Proteins for Targeted Cancer Therapy: Prospects and Challenges

Du, Y., & Xu, J. (2021) · Advanced Materials · doi:10.1002/adma.202103114 · Cited by 19

Generation of a Novel SORT1×HER2 Bispecific Antibody–Drug Conjugate Targeting HER2-Low-Expression Tumor

Zhuang, W., Zhang, W., Wang, L., Xie, L., Feng, J., Zhang, B., & Hu, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216056 · Cited by 19

Engineering of Immunoglobulin Fc Heterodimers Using Yeast Surface-Displayed Combinatorial Fc Library Screening

Choi, H., Kim, Y., Choi, D.-K., & Kim, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145349 · Cited by 19

Insertion of scFv into the hinge domain of full-length IgG1 monoclonal antibody results in tetravalent bispecific molecule with robust properties

Bezabeh, B. Z., Fleming, R. L., Fazenbaker, C. A., Zhong, H., Coffman, K. T., Yu, X., Leow, C. C., Gibson, N., Wilson, S. D., Stover, C. K., et al. (2016) · mAbs · doi:10.1080/19420862.2016.1270492 · Cited by 19

NKG2D ligand targeted Bispecific T Cell Engagers lead to robust antitumor activity against diverse human tumors

Godbersen, C., Coupet, T. A., Huehls, A., Zhang, T., Battles, M., Fisher, J., Ernstoff, M., & Sentman, C. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0846 · Cited by 20

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 18

Nanobody stability engineering by employing the ΔTm shift; a comparison with apparent rate constants of heat-induced aggregation

Kunz, P., Ortale, A., Mücke, N., Zinner, K., & Hoheisel, J. D. (2019) · Protein Engineering Design and Selection · doi:10.1093/protein/gzz017 · Cited by 19

The biological activity of bispecific trastuzumab/pertuzumab plant biosimilars may be drastically boosted by disulfiram increasing formaldehyde accumulation in cancer cells

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