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Nanobodies and Nanobody-Based Human Heavy Chain Antibodies As Antitumor Therapeutics
Open accessAbstract
Monoclonal antibodies have revolutionized cancer therapy. However, delivery to tumor cells in vivo is hampered by the large size (150 kDa) of conventional antibodies. The minimal target recognition module of a conventional antibody is composed of two non-covalently associated variable domains (VH and VL). The proper orientation of these domains is mediated by their hydrophobic interface and is stabilized by their linkage to disulfide-linked constant domains (CH1 and CL). VH and VL domains can be fused via a genetic linker into a single chain variable fragment (scFv). scFv modules in turn can be fused to one another, e.g. to generate a bispecific T cell engager (BiTE), or they can be fused in various orientations to antibody hinge and Fc domains to generate bi- and multispecific antibodies. However, the inherent hydrophobic interaction of VH and VL domains limits the stability and solubility of engineered antibodies, often causing aggregation and/or mispairing of V-domains. Nanobodies (15 kDa) and nanobody-based human heavy chain antibodies (75 kDa) can overcome these limitations. Camelids naturally produce antibodies composed only of heavy chains in which the target recognition module is composed of a single variable domain (VHH or nanobody). Advantageous features of nanobodies include their small size, high solubility, high stability, and excellent tissue penetration in vivo. Nanobodies can readily be linked genetically to Fc-domains, other nanobodies, peptide tags, or toxins and can be conjugated chemically at a specific site to drugs, radionuclides, photosensitizers, and nanoparticles. These properties make them particularly suited for specific and efficient targeting of tumors in vivo. Chimeric nanobody-heavy chain antibodies combine advantageous features of nanobodies and human Fc domains in about half the size of a conventional antibody. In this review, we discuss recent developments and perspectives for applications of nanobodies and nanobody-based human heavy chain antibodies as anti-tumor therapeutics.
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“The accumulated methodology of computational antibody protocols could potentially be applied to novel antibody formats with intrinsically better biophysical properties, such as nanobodies [27].”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [27]
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“Single domain antibodies have attracted attention because of their smaller size and better biophysical properties with respect to antibodies (higher stability and lower suspected immunogenicity) [27].”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [27]
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“One of the most promising is the H chain only antibody, or nanobody that are naturally occurring in camelids (llamas, alpacas and camels) [27] and sharks [228, 229] (reviewed by Muyldermans [230] and Bannas et al. [27]).”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [27]
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Citations
Cites
Delivering nanomedicine to solid tumors
Jain, R. K., & Stylianopoulos, T. (2010) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2010.139 · Cited by 3,265
Naturally occurring antibodies devoid of light chains
Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hammers, C., Songa, E. B., Bendahman, N., & Hammers, R. (1993) · Nature · doi:10.1038/363446a0 · Cited by 3,241
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 2,572
Nanobodies: natural single-domain antibodies
Muyldermans, S. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-063011-092449 · Cited by 2,304
Scott, A. M., Wolchok, J. D., & Old, L. J. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3236 · Cited by 2,244
Blinatumomab versus Chemotherapy for Advanced Acute Lymphoblastic Leukemia
Kantarjian, H. M., Stein, A. S., Gökbuget, N., Fielding, A. K., Schuh, A. C., Ribera, J., Wei, A. H., Dombret, H., Foà, R., Bassan, R., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1609783 · Cited by 2,204
Reshaping human antibodies for therapy
Riechmann, L., Clark, M., Waldmann, H., & Winter, G. P. (1988) · Nature · doi:10.1038/332323a0 · Cited by 1,565
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
Adeno-Associated Virus (AAV) as a Vector for Gene Therapy
Naso, M. F., Tomkowicz, B., Perry, W. L., & Strohl, W. R. (2017) · BioDrugs · doi:10.1007/s40259-017-0234-5 · Cited by 1,362
Drug targeting to tumors: Principles, pitfalls and (pre-) clinical progress
Lammers, T., Kiessling, F., Hennink, W. E., & Storm, G. (2012) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.09.063 · Cited by 1,324
Flagged first, then by citations
Cited by
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Items 301–400 of 572
Analysis of EGFR binding hotspots for design of new EGFR inhibitory biologics
Tydings, C. W., Singh, B., Smith, A. W., Ledwitch, K. V., Brown, B. P., Lovly, C. M., Walker, A. S., & Meiler, J. (2024) · Protein Science · doi:10.1002/pro.5141 · Cited by 13
Developing drug-like single-domain antibodies (VHH) from in vitro libraries
Erasmus, M. F., Teixeira, A. A. R., Molina, E., Carnero, L. A. R., Li, J., Knight, D., Niro, R. D., Leal‐Lopes, C., Fanni, A. M., Troell, H. A., et al. (2025) · mAbs · doi:10.1080/19420862.2025.2516676 · Cited by 11
Xu, Z., Qiu, C., Wen, B., Wang, S., Zhu, L., Zhao, L., & Li, H. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.02.059 · Cited by 11
Probing GPCR Dimerization Using Peptides
Farooq, Z., Howell, L. A., & McCormick, P. J. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.843770 · Cited by 11
Site-Specific Modification of Single Domain Antibodies by Enzyme-Immobilized Magnetic Beads
Zhou, S., Fang, X., Lv, J., Yang, Y., Zeng, Y., Liu, Y., Wei, W., Huang, G., Zhang, B., & Wu, C. (2023) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00423 · Cited by 11
Recent progress in antitumor functions of the intracellular antibodies
Lin, Y., Chen, Z., Hu, C., Chen, Z., & Zhang, L. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.02.009 · Cited by 11
Bekesi, A., Abdellaoui, S., Holroyd, N., Delm, W. V., Pardon, E., Pauwels, J., Gevaert, K., Steyaert, J., Derveaux, S., Borysik, A. J., et al. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.09.032 · Cited by 11
A Novel Anti-CD47 Nanobody Tetramer for Cancer Therapy
Ratnikova, N. M., Kravchenko, Y., Ivanova, A. E., Zhuchkov, V. A., Frolova, E. I., & Chumakov, S. P. (2024) · Antibodies · doi:10.3390/antib13010002 · Cited by 10
Sahraoui, P. F., Vadas, O., & Kalia, Y. N. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16040539 · Cited by 10
Gallant, J. P., Hicks, D. M., Shi, K., Moeller, N. H., Hoppe, B., Lake, E. W., Baehr, C., Pravetoni, M., Aihara, H., & LeBeau, A. M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107502 · Cited by 10
Beyond amyloid: nanobody-mediated neuroinflammatory therapy for Alzheimer’s disease
Amniouel, S., Suh, J., Zheng, W. H., & Zhang, Q. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00513-5 · Cited by 11
Introduction of an Aldehyde Handle on Nanobodies by Affinity-Guided Labeling
Mortensen, M. R., Skovsgaard, M. B., Märcher, A., Andersen, V. L., Palmfeldt, J., Nielsen, T. B., Tørring, T., Laursen, N. S., Andersen, K. R., Kjems, J., et al. (2020) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.0c00151 · Cited by 10
Lim, H. T., Kok, B. H., Lim, C. P., Majeed, A. B. A., Leow, C. Y., & Leow, C. Y. (2022) · Biomedical Engineering Advances · doi:10.1016/j.bea.2022.100054 · Cited by 10
Sokolov, P. M., Nifontova, G., Samokhvalov, P. S., Karaulov, A. V., Sukhanova, A. V., & Nabiev, I. R. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030946 · Cited by 10
Zhu, M., Zhang, J., Yang, M., Zhang, H., Xu, T., Kan, F., Zhang, X., Zhang, S., Yin, Y., & Yu, F. (2023) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-023-04793-0 · Cited by 10
Thran, M., Poenisch, M., Danz, H., Horscroft, N., Ichtchenko, K., Tzipori, S. R., & Shoemaker, C. B. (2023) · Scientific Reports · doi:10.1038/s41598-023-41092-7 · Cited by 11
Wiswell, D., Neupane, D., Chen, M., Bowman, E. P., Linn, D. E., Sawant, A., Chackerian, A. A., Zhang, S., & Escandón, E. (2020) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/j.vascn.2020.106872 · Cited by 10
Cable, J., Leonard, J. N., Lu, T. K., Xie, Z., Chang, M. W., Fernández, L. Á., Lora, J. M., Kaufman, H. L., Quintana, F. J., Geiger, R., et al. (2021) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14710 · Cited by 10
Shoari, A., Tahmasebi, M., Khodabakhsh, F., Cohan, R. A., Oghalaie, A., & Behdani, M. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108585 · Cited by 10
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Stähler, T., Danquah, W., Demeules, M., Gondé, H., Hardet, R., Haag, F., Adriouch, S., Koch‐Nolte, F., & Menzel, S. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2384-8_6 · Cited by 10
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Greve, H. D., & Fioravanti, A. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1334829 · Cited by 9
Yang, J., Lin, S., Sun, H., Chen, Z., Yang, F., Lin, X., Guo, L., Wang, L., Wen, A., Zhang, X., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.820336 · Cited by 9
Briolay, T., Fresquet, J., Meyer, D., Kerfélec, B., Chames, P., Ishow, É., & Blanquart, C. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s435787 · Cited by 9
Physicochemical determinants of antibody-protein interactions
Karadag, M., Arslan, M., Kaleli, N. E., & Kalyoncu, S. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.011 · Cited by 9
Single Domain Antibodies as Carriers for Intracellular Drug Delivery: A Proof of Principle Study
Pronk, S. D., Schooten, E., Heinen, J., Helfrich, E., Oliveira, S., & Henegouwen, P. M. P. V. B. E. (2021) · Biomolecules · doi:10.3390/biom11070927 · Cited by 10
Molecular probes for cellular imaging of post-translational proteoforms
Suraritdechachai, S., Lakkanasirorat, B., & Uttamapinant, C. (2022) · RSC Chemical Biology · doi:10.1039/d1cb00190f · Cited by 9
COVID-19-Current Therapeutical Approaches and Future Perspectives
Moisi, R. E., Nedea, M. I., Velescu, B. Ș., Udeanu, D. I., Sultana, C., Ruță, S. M., & Arsene, A. L. (2022) · Processes · doi:10.3390/pr10061053 · Cited by 9
Marine-derived microbes and molecules for drug discovery
Tanaka, Y., Nishikawa, M., Kamisaki, K., Hachiya, S., Nakamura, M., Kuwazuru, T., Tanimura, S., Soyano, K., & Takeda, K. (2022) · Inflammation and Regeneration · doi:10.1186/s41232-022-00207-9 · Cited by 9
Nanobodies: a new potential for prostate cancer treatment
Su, J., Liu, X., Guo, S., Zhang, J., Wei, X., & Li, X. (2023) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-022-04515-y · Cited by 9
Distinct types of VHHs in Alpaca
Wang, X., Zhang, L., Zhang, Y., Li, J., Xu, W., & Zhu, W. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1447212 · Cited by 9
N’Guessan, É., Bacot, S., Raes, F., Leenhardt, J., Guenard, T., Dumas, L. S., Ghezzi, C., Fagret, D., Lombardi, C., Broisat, A., et al. (2025) · EJNMMI Radiopharmacy and Chemistry · doi:10.1186/s41181-025-00380-5 · Cited by 8
Cell-specific mRNA delivery via nanobody-functionalized lipid nanoparticles
Chen, L., der Weken, H. V., Zwaenepoel, O., Okkelman, I. A., Aelvoet, J., Denberghe, E. V., Gettemans, J., Dmitriev, R. I., Geest, B. G. D., Cox, E., et al. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.114365 · Cited by 10
Tandem nanobody: A feasible way to improve the capacity of affinity chromatography
Huang, Y., Fu, J., Zhong, Y., Shuai, W., Zhang, H., Li, Y., He, Q., & Tu, Z. (2021) · Journal of Chromatography B · doi:10.1016/j.jchromb.2021.122678 · Cited by 8
Hansmeier, N. R., Büschlen, I. S., Behncke, R. Y., Ulferts, S., Bisoendial, R. J., & Hägerling, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084369 · Cited by 8
Smith, C. N., Kihn, K. C., Williamson, Z. A., Chow, K. M., Hersh, L. B., Korotkov, K. V., Deredge, D. J., & Blackburn, J. S. (2023) · PLoS ONE · doi:10.1371/journal.pone.0285964 · Cited by 8
Baum, N., Eggers, M., Koenigsdorf, J., Menzel, S., Hambach, J., Stähler, T., Fliegert, R., Kulow, F., Adam, G., Haag, F., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.703574 · Cited by 8
Barroeta, A. B., Marquart, J. A., Bakhtiari, K., Meijer, A. B., Urbanus, R. T., & Meijers, J. C. M. (2022) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.15815 · Cited by 7
Structure determination of an unstable macromolecular complex enabled by nanobody‐peptide bridging
Lorentzen, J., Pedersen, D. V., Gadeberg, T. A. F., & Andersen, G. R. (2022) · Protein Science · doi:10.1002/pro.4432 · Cited by 7
Eshak, F., Pion, L., Scholler, P., Névoltris, D., Chames, P., Rondard, P., Pin, J., Acher, F., & Goupil-Lamy, A. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01620 · Cited by 9
Generation and characterization of antagonistic anti-human CD39 nanobodies
Menzel, S., Duan, Y., Hambach, J., Albrecht, B., Wendt, D., Winzer, R., Tolosa, E., Rissiek, A., Guse, A. H., Haag, F., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1328306 · Cited by 8
Integrated purification of a nanobody using ammonium sulfate precipitation and Capto MMC
Fan, X., Liang, Y., Li, F., Yu, J., Song, H., Feng, D., Xian, M., Liu, W., & Nian, R. (2019) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.6228 · Cited by 8
Next generation single-domain antibodies against respiratory zoonotic RNA viruses
Swart, I. C., Gelder, W. V., de Haan, C. A. M., Bosch, B., & Oliveira, S. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1389548 · Cited by 7
Xie, S., Shi, W., Duan, S., Huang, X., Liu, A., Hou, X., Lin, X., Zhong, D., Sun, S., Ding, Z., et al. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02781-1 · Cited by 7
Talukdar, A., Giri, S., & Doley, R. (2025) · Toxicon · doi:10.1016/j.toxicon.2025.108406 · Cited by 7
Liu, Y., Liu, J., Qiu, Z., Liu, Y., Zhang, J., Ji, X., & Yang, H. (2025) · Microchemical Journal · doi:10.1016/j.microc.2025.114083 · Cited by 7
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Eisa, A. R., Razavi, F. T., Hoseinzadeh, A., Haghmorad, D., & Baharlou, R. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118819 · Cited by 7
Singh, V., Choudhary, S., Bhutkar, M., Nehul, S., Ali, S., Singla, J., Kumar, P., & Tomar, S. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.138751 · Cited by 7
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Eggers, M., Ruhl, F., Haag, F., & Koch-Nolte, F. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114394 · Cited by 6
Li, X., Liu, W., Li, H., Wang, X., & Zhao, Y. (2021) · Protein Expression and Purification · doi:10.1016/j.pep.2021.106030 · Cited by 7
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Jedlitzke, B., Yilmaz, Z., Dörner, W., & Mootz, H. D. (2019) · Angewandte Chemie · doi:10.1002/ange.201912286 · Cited by 7
Mirzaei, M., Mirhosseini, S., Heidari, M., & Khatami, M. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01162-1 · Cited by 7
Khatib, S. E., & Salla, M. (2022) · Leukemia Research Reports · doi:10.1016/j.lrr.2022.100335 · Cited by 8
AAV mediated delivery of a novel anti-BACE1 VHH reduces Abeta in an Alzheimer’s disease mouse modelPreprint
Rincón, M. Y., Zhou, L., Marneffe, C., Voytyuk, I., Wouters, Y., Dewilde, M., Duqué, S. I., Vincke, C., Levites, Y., Golde, T. E., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/698506 · Cited by 7
A SARS-CoV-2 Nanobody Displayed on the Surface of Human Ferritin with High Neutralization Activity
Zhang, W., Wang, H., Wu, T., Gao, X., Shang, Y., Zhang, Z., Liu, X., & Li, Y. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s450829 · Cited by 6
Mihaylova, R., Momekova, D. B., Elincheva, V., & Momekov, G. (2024) · Pharmaceuticals · doi:10.3390/ph17121701 · Cited by 6
Melis, D. R., Segers, C., Wellens, J., de Voorde, M. V., Blacque, O., Ooms, M., Gasser, G., & Opsomer, T. (2025) · Chemical Science · doi:10.1039/d4sc07743a · Cited by 6
Belfakir, S. B., Rodríguez-Rodríguez, E. R., Thrane, S. W., Ljungars, A., Svendsen, W. E., Laustsen, A. H., & Ross, G. M. S. (2025) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2025.137833 · Cited by 6
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Ren, W., Zheng, P., Zhou, Z., Zhou, M., Wu, M., Ding, Y., Jiang, H., Li, P., & Du, J. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c09699 · Cited by 6
Wang, R., Wang, Z., Zhang, H., Liu, X., Zhu, P., Zhou, F., Ma, J., & Hu, Q. (2025) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2025.118526 · Cited by 6
Panchal, J. P., Falk, B. T., Antochshuk, V., & McCoy, M. A. (2022) · mAbs · doi:10.1080/19420862.2022.2124902 · Cited by 6
Ionescu, R. E. (2023) · Micromachines · doi:10.3390/mi14081486 · Cited by 6
ElMaraashly, A. H., Tario, J. D., Hillengaß, J., & Qian, Y. (2023) · American Journal of Clinical Pathology · doi:10.1093/ajcp/aqad086 · Cited by 6
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Wang, L., Dong, J., Wu, C., Yan, C., Bi, C., Xu, C., Wu, Y., Zheng, W., & Xing-yuan, M. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2024.1440150 · Cited by 6
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Teodori, L., Ochoa, S. K., Omer, M., Andersen, V. L., Bech, P., Su, J., Bridoux, J., Nielsen, J. S., Bertelsen, M. B., Hernot, S., et al. (2024) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2024.102305 · Cited by 6
Gless, B. H., Jones, E., Labão‐Almeida, C., Tang, C., Gottscheber, N., Couto, R., & Bernardes, G. J. L. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202502268 · Cited by 6
DI, Z., Wang, Z., Xu, Y., Lin, J., Qiu, M., Liu, J., & Li, X. (2022) · Engineering in Life Sciences · doi:10.1002/elsc.202200028 · Cited by 5
Wang, B., Huang, B., Li, X., Guo, Y., Qi, G., Ding, Y., Gao, H., Zhang, J., Wu, X., & Fang, L. (2022) · Protein Science · doi:10.1002/pro.4461 · Cited by 6
Mendon, N., Ganie, R. A., Kesarwani, S., Dileep, D., Sasi, S., Lama, P., Chandra, A., & Sirajuddin, M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102732 · Cited by 6
Hutton, A. R. J., Kirkby, M., Bogaert, T. V., Casteels, P., Nonne, C., Brabandere, V. D., de Vyver, O. V., Vora, L. K., Tekko, I. A., McCarthy, H. O., et al. (2024) · Macromolecular Materials and Engineering · doi:10.1002/mame.202400029 · Cited by 6
Asadpour, O., & Rahbarizadeh, F. (2020) · Europe PMC (PubMed Central) · doi:10.22074/cellj.2020.6704 · Cited by 6
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Maciorowski, D., Ogaugwu, C., Durvasula, S. R., Durvasula, R. V., & Kunamneni, A. (2020) · SLAS DISCOVERY · doi:10.1177/2472555220979579 · Cited by 6
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Melnyk, I., Das, P., Chenthamarakshan, V., & Lozano, A. C. (2021) · arXiv (Cornell University) · doi:10.48550/arxiv.2111.06801 · Cited by 19
Chen, J., Yao, G., Huang, C., Shen, Q., Miao, J. H., & Jia, L. (2024) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.3c01765 · Cited by 5
de Boissel, P. G. J., Nehmé, R., Fortier, M., Létourneau, M., Guérin, B., Dumulon‐Perreault, V., Aı̈t-Mohand, S., Sarrhini, O., Fuselier, C., Dumoulin, A., et al. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00178 · Cited by 5
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Vijayandran, K., Abdo, A. I. K., Wong, M. T. J., Balakrishnan, V., Nordin, F., Zaman, W. S. W. K., Lim, C. S. Y., & Tye, G. J. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115368 · Cited by 5
Baker, C., Acquah, F. A., Chivukula, L. G., Wu, L., Philippe-Venec, L., Abedi, M., Tao, Y., Ramirez, D. M. C., McCoy, M., Moore, B. D., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01836 · Cited by 7
Tillib, S. V., & Goryainova, O. S. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924050134 · Cited by 5
Kamoshida, G., Yamaguchi, D., Kaya, Y., Yamakado, T., Yamashita, K., Aoyagi, M., Nagai, S., Yamada, N., Kawagishi, Y., Sugano, M., et al. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae328 · Cited by 5
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Sotoudeh, N., Noormohammadi, Z., Habibi‐Anbouhi, M., Kazemi‐Lomedasht, F., & Behdani, M. (2021) · PubMed Central · doi:10.22038/ijbms.2021.57774.12851 · Cited by 5
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Opuni, K. F. M., Ruß, M., Geens, R., Vocht, L. D., Wielendaele, P. V., Debuy, C., Sterckx, Y. G. ‐., & Glocker, M. O. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.08.023 · Cited by 5
Mortaheb, S., Pezeshki, P. S., & Rezaei, N. (2024) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2024.2426636 · Cited by 5
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Hambach, J., Stähler, T., Eden, T. W., Wendt, D., Tode, N., Haag, F., Tolosa, E., Altfeld, M. A., Fathi, A., Dahlke, C., et al. (2021) · Immunity Inflammation and Disease · doi:10.1002/iid3.446 · Cited by 5
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Mahboobi, M., Najafi, A., Kooshki, H., Kheirandish, M., Soofian, S. E., & Sedighian, H. (2025) · Materials Advances · doi:10.1039/d5ma00933b · Cited by 4
Shahmoradipour, P., & Emamzadeh, R. (2026) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118944 · Cited by 4
McIlroy, P. R., Pham, L. T. M., Sheffield, T. Y., Stefan, M. A., Thatcher, C. E., Jaryenneh, J. D., Schwedler, J. L., Sinha, A., Sumner, C. A., Jones, I. K. A., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012903 · Cited by 5
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Metadata
- Authors
- Bannas, P., Hambach, J., & Koch-Nolte, F.
- Affiliations
- University Medical Center Hamburg-Eppendorf (DE)
- Venue
- Frontiers in Immunology
- Publisher
- Frontiers Media SA
- Published
- 2017-11-22
- Volume
- 8
- Pages
- 1603-1603
- ISSN
- 1664-3224 (ISSN-L)
- PMC
- PMC5702627
- OpenAlex
- W2769445535
- Cited by
- 572
- References
- 134
- Citations by year
- 2026: 51 · 2025: 68 · 2024: 93 · 2023: 62 · 2022: 70 · 2021: 85 · 2020: 68 · 2019: 48 · 2018: 27
- FWCI
- 5.92
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Immunology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Wilhelm Sander-Stiftung (2012.113.2)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Radiopharmaceutical Chemistry and Applications
- Keywords
- nanobodies, VHH, camelid antibodies, antibody engineering, tumor targeting, antibody aggregation, bispecific T-cell engagers, antibody-drug conjugates, radionuclide conjugation, photosensitizer conjugation, nanoparticle conjugation, cancer immunotherapy
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