The DOI matches its Crossref record; 134 of the 134 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Sorted by citations
Items 401–500 of 572
Pitino, M., Fleites, L. A., Shrum, L., Heck, M. L., & Shatters, R. G. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.1045337 · Cited by 4
Rapid and Wash-Free Anti-Drug Antibody Assay Enabled by a Complementary Nanoluciferase Biosensor
Sun, R., Qian, M. G., & Zhang, X. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c01017 · Cited by 4
Lü, H., Ji, P., Liu, S., Zhang, Z., Wang, L., Sun, Y., Liu, B., Wang, L., & Zhao, Q. (2023) · Journal of Integrative Agriculture · doi:10.1016/j.jia.2023.09.033 · Cited by 4
La bioproduction des anticorps monoclonaux
Joubert, S., Dodelet, V. C., Béliard, R., & Durocher, Y. (2019) · médecine/sciences · doi:10.1051/medsci/2019219 · Cited by 6
Organic nanocarriers for targeted delivery of anticancer agents
Dahiya, S., & Dahiya, R. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85503-7.00010-9 · Cited by 4
Creating a Selective Nanobody Against 3-Nitrotyrosine Containing Proteins
Fossen, E. M. V., Grutzius, S., Ruby, C. E., Mourich, D. V., Cebra, C., Bracha, S., Karplus, P. A., Cooley, R. B., & Mehl, R. A. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.835229 · Cited by 4
Hu, X., Fan, J., Ma, Q., Han, L., Cao, Z., Xu, C., Luan, J., Nan, Y., Wu, T., Zhang, Y., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1242140/v1 · Cited by 4
Zhou, Y., Li, J., Gao, G., Li, Y., & Zhang, C. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e24340 · Cited by 3
ENPP1/CD203a-targeting heavy-chain antibody reveals cell-specific expression on human immune cells
Lorenz, H., Menzel, S., Roshchyna, N., Albrecht, B., Gebhardt, A. J., Schneider, E., Haag, F., Rissiek, B., Oheim, R., Koch‐Nolte, F., et al. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05539-y · Cited by 3
Sherbaevna, S. R. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115552 · Cited by 3
An adaptive autoregressive diffusion approach to design active humanized antibodies and nanobodies
Ma, J., Wu, F., Xu, T., Xu, S., Liu, W., Yan, L., Qu, M., Yang, X., Bai, Q., Xiao, J., et al. (2025) · Nature Machine Intelligence · doi:10.1038/s42256-025-01120-9 · Cited by 8
Shen, W., Xu, J., Chen, Z., Wei, Y., Wang, Q., Wang, X., Zhang, X., Zhu, Q., & Xu, S. (2025) · Journal of Virology · doi:10.1128/jvi.01478-25 · Cited by 3
Jung, D., Jo, S.-G., Gong, E.-Y., Kim, J.-H., Ha, K., Wee, G., Huh, S. J., Jeoung, Y.-H., & Kim, S.-H. (2026) · Genes & Genomics · doi:10.1007/s13258-025-01733-9 · Cited by 3
Asano, R., Takeuchi, M., Nakakido, M., Itô, S., Aikawa, C., Yokoyama, T., Senoo, A., Ueno, G., Nagatoishi, S., Tanaka, Y., et al. (2024) · Protein Science · doi:10.1002/pro.5017 · Cited by 4
Nanoparticle targeting strategies for traumatic brain injury
Flores-Prieto, D. E. E., & Stabenfeldt, S. E. (2024) · Journal of Neural Engineering · doi:10.1088/1741-2552/ad995b · Cited by 5
PET imaging of HIV-1 envelope protein gp120 using 18F-labeled nanobodies
Martínez‐Orengo, N., Shah, S., Lai, J., Basuli, F., Lyndaker, A., Turner, M. L., Peiravi, M., Sourabh, S., Sampson, K., Zhang, P., et al. (2025) · iScience · doi:10.1016/j.isci.2025.111795 · Cited by 3
Chen, Y., & Duong, F. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00793 · Cited by 3
Dual-acting therapeutic proteins for intraocular use
Collins, M., Awwad, S., Ibeanu, N., Khaw, P. T., Guiliano, D. B., Brocchini, S., & Khalili, H. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.10.025 · Cited by 3
Wu, X., Zhang, J., & Fang, L. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3926-9_10 · Cited by 3
Light-responsive monobodies for dynamic control of customizable protein bindingPreprint
Carrasco‐López, C., Zhao, E. M., Gil, A. A., Alam, N., Toettcher, J. E., & Avalos, J. L. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.08.831909 · Cited by 3
An adaptive autoregressive diffusion approach to design active humanized antibody and nanobodyPreprint
Ma, J., Wu, F., Xu, T., Xu, S., Liu, W., Yan, D., Bai, Q., & Yao, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.22.619416 · Cited by 3
Therapeutic antibodies against cancer—A step toward the treatment
Panwar, U., Khan, M. A., Selvaraj, C., & Singh, S. K. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-19200-5.00001-4 · Cited by 2
Najafi, A., Valadan, R., Asgarian‐Omran, H., Rafiei, A., & Tehrani, M. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110999 · Cited by 2
Characteristics and Genomic Localization of Nurse Shark (Ginglymostoma cirratum) IgNAR
Tang, W., Zheng, K., Sun, S., Zhong, B., Luo, Z., Yang, J., Jia, L., Yang, L., Shang, W., Jiang, X., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312879 · Cited by 2
Pape, L. J., Gebhardt, A. J., Dannenberg, M., Risch, H., Duttmann, A., Weisel, K., Hambach, J., Koch-Nolte, F., & Bannas, P. (2025) · Scientific Reports · doi:10.1038/s41598-025-25194-y · Cited by 1
Niemelä, L. R. K., Kirjavainen, L.-M., Kozlowski, H. C. J., Salminen, H., & Frey, A. D. (2026) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-025-13700-1 · Cited by 2
Design strategies for fluorescent biosensors and their application to mycotoxin detection in food
Ma, J., Wu, L., Hu, X. L., Zhao, Q., Zhao, W., & Wu, H. (2026) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2026.217915 · Cited by 2
Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation
Cao, C.-K., Xu, X.-Y., Liang, F., Yao, M., Chen, Y., Li, X.-K., & Su, Z. (2026) · Military Medical Research · doi:10.1016/j.mmr.2026.100009 · Cited by 2
Kozani, P. S., Kozani, P. S., & Rahbarizadeh, F. (2021) · Trends in Medical Sciences · doi:10.5812/tms.114888 · Cited by 2
Keller, L., Tardy, C., Ligat, L., Pennec, S. L., Béry, N., Koraïchi, F., Chinestra, P., David, M., Gence, R., Favre, G., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.980539 · Cited by 2
Site-specific drug delivery utilizing monoclonal antibodies
Marson, D., Russi, M., Fermeglia, A., Laurini, E., & Pricl, S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91668-4.00007-1 · Cited by 2
Photoimmuno-antimicrobial therapy for Staphylococcus aureus implant infection
van Dijk, B., Oliveira, S., van Duyvenbode, J. F. F. H., Nurmohamed, F. R. H. A., Mashayekhi, V., Hernández, I. B., van Strijp, J. A. G., de Vor, L., Aerts, P. C., Vogely, H. C., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0300069 · Cited by 2
Screening, expression and anti-tumor functional identification of anti-LAG-3 nanobodies
Jiang, D., Chen, R., Wang, L., & Xu, G. (2024) · Protein Expression and Purification · doi:10.1016/j.pep.2024.106522 · Cited by 2
Kang, L., Dong, Y., Wang, W., Li, Z., Wang, Y., Yan, L., Yin, C., Zhang, X., Dai, H., Wu, B., et al. (2024) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2623 · Cited by 2
The process using a synthetic library that generates multiple diverse human single domain antibodies
Tornetta, M. A., Whitaker, B., Cantwell, O. M., Pisors, E. D., Han, L., MacWilliams, M. P., Jiang, H., Zhou, F., & Chiu, M. L. (2024) · Antibody Therapeutics · doi:10.1093/abt/tbae020 · Cited by 2
Innovative CDR grafting and computational methods for PD-1 specific nanobody design
Devasani, J. R., Guntuku, G., Panatula, N., Muthyala, M. K. K., Palla, M. S., & Siahaan, T. J. (2025) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2024.1488331 · Cited by 2
Pang, G., Wang, R., Yang, H., Chai, M., Gao, Y., Chen, S., Mao, T., Du, L., Lan, Y., Li, S., et al. (2025) · Protein Science · doi:10.1002/pro.70090 · Cited by 2
Arafiles, J. V. V., Hirose, H., Hirai, Y., Kuriyama, M., Sakyiamah, M. M., Nomura, W., Sonomura, K., Imanishi, M., Otaka, A., Tamamura, H., et al. (2021) · Angewandte Chemie · doi:10.1002/ange.202016754 · Cited by 2
Optical image-guided therapy of pancreatic cancer with an ultra-small bispecific protein
Song, W., Hsu, J. C., Lan, X., & Cai, W. (2023) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-023-06186-4 · Cited by 2
Construction of Semisynthetic Shark vNAR Yeast Surface Display Antibody Libraries
Kolmar, H., Grzeschik, J., Könning, D., Krah, S., & Zielonka, S. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3381-6_11 · Cited by 2
Li, Y., & Wang, J. (2023) · Journal of Labelled Compounds and Radiopharmaceuticals · doi:10.1002/jlcr.4069 · Cited by 2
Characterization of plant produced VHH antibodies against cobra venom toxins for antivenom therapy
Vitayathikornnasak, S., Rattanapisit, K., Malla, A., Suwanchaikasem, P., Strasser, R., Khorattanakulchai, N., Pothisamutyothin, K., Arunmanee, W., & Phoolcharoen, W. (2024) · Biotechnology Reports · doi:10.1016/j.btre.2024.e00841 · Cited by 2
Enzyme responsive delivery of engineered antibody fragments
Zhong, L. (2023) · doi:10.3990/1.9789036559706 · Cited by 2
Singh, V., Bhutkar, M., Choudhary, S., Nehul, S., Kumar, R., Singla, J., Kumar, P., & Tomar, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.13.593833 · Cited by 2
Qassas, M. K., Skhal, D., Nattouf, A. H., & Abbady, A. Q. (2021) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2022.2044381 · Cited by 1
The construction of long-acting exendin-4 analog and its hypoglycemic effect in diabetic mice
Cai, J., Zang, L., Wu, X., Liang, Z., Zheng, K., Zhao, L., & Li, H. (2023) · Protein Expression and Purification · doi:10.1016/j.pep.2023.106373 · Cited by 1
Engineering high affinity antigen-binders: Beyond conventional antibodies
Pandey, R. K., & Mehrotra, S. (2024) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2023.12.014 · Cited by 1
Sun, Y., Martinez-Ramos, C., Chen, E., Osawa, Y., & Zhang, H. (2024) · Biomedicines · doi:10.3390/biomedicines12081863 · Cited by 1
Sultana, S., & Geyer, C. R. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150956 · Cited by 1
Contribution of CDR3 in characterization of camelid VHH and its aflatoxin B1-binding interaction
Mukhtar, H., Ma, L., Pang, Q., Wang, X., & Wang, J. (2025) · Food Chemistry Advances · doi:10.1016/j.focha.2025.100885 · Cited by 1
Leleux, J. A., Rosenberg, J. N., Sonzogni, O., Walker, R. L., Venkitaraman, A., Garrison, S. M., Jin, N., Gregory, P. D., & Jarjour, J. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.02.026 · Cited by 1
Lemmex, A. C. D., Allred, J. R., Ostergaard, J., Trask, J., Bui, H. N., Anderson, M. J. M., Kopp, B., Streeter, O., Smiley, A. T., Babilonia-Díaz, N. S., et al. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.4c00803 · Cited by 1
Neutralization of the Pandemic Influenza A/H1N1 Virus with Lama glama Humanized Nanobodies (VHH)
Páez-Hernández, Z. Y., Stephano-Hornedo, J. L., Prats, J. A. B., Córdova‐Guerrero, I., Macías-Alonso, M., Marrero, J. G., Capiz, A. P., & García‐González, V. (2025) · Antibodies · doi:10.3390/antib14020042 · Cited by 1
Kotel'nikov, D. D., Tatarinova, K. S., & Zhdanov, D. D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26199262 · Cited by 1
Enzyme‐Linked Immunosorbent Assay‐Derived Methods for Biomarker Detection
Lu, K., Yi, Y., Liu, L., & Wu, H. (2025) · Analysis & Sensing · doi:10.1002/anse.202500180 · Cited by 1
Structural mechanisms and insights on multiple nanobodies binding diverse SOD1 epitopes
Cheng, S., Zhong, C., Zhu, H., Mu, K., Jiang, H., Zhong, P., Ma, Z., Liu, X., Wang, Z., Liu, R., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-09293-0 · Cited by 1
Aria, H., Bakherad, H., Mehdipour, A. R., Azizi, M., & Rezaei, M. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116174 · 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
Nanobodies for inflammatory bowel disease: Miniaturizing solutions
Tang, Y.-T., Ding, N., Li, H.-S., Zhou, Y., Jin, Z., Zha, J., & He, W.-Q. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.114713 · Cited by 1
Li, J., Lu, Q., Zhu, Z., Wang, X., Chen, Y., Zhang, Z., Yu, Z., Wang, Z., Chen, Y., Xie, H., et al. (2026) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2025-013986 · Cited by 1
Zhu, Z., Li, J., Lu, Q., Zeng, W., Yu, Z., Liu, N., Zhang, Z., Wang, Z., Yang, N., Chen, Y., et al. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04319-z · Cited by 2
Targeting purinergic receptors in glioblastoma with nanobody-displaying AAV vectors
Jargalsaikhan, S., Schäfer, W., Zapf, N., Reetz, M., Rodríguez, D. G., Malatesta, P., Bannas, P., Dührsen, L., Mohme, M., Lamszus, K., et al. (2026) · Neuropharmacology · doi:10.1016/j.neuropharm.2026.110955 · Cited by 1
Humanized synthetic nanobody library for antivenom development
Jia, Y. Y., Coronado, F., & Garcia, C. (2026) · Toxicon · doi:10.1016/j.toxicon.2026.109092 · Cited by 1
State of the art and novel treatments in psoriatic arthritis
Hackett, S., Al‐Mossawi, H., & Coates, L. C. (2026) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2026.102135 · Cited by 1
Smekenov, I., Tleumbetova, N., Bektasov, S., & Bissenbaev, A. K. (2026) · Microorganisms · doi:10.3390/microorganisms14040863 · Cited by 1
Adedokun, K. A., Fayemo, H. T., Oyeniyi, G. M., Bello, A., Orugun, O. A., Imodoye, S. O., Ogunlakin, A. D., Eziagu, U. B., Dewan, S. M. R., Khan, S. A., et al. (2026) · Next Materials · doi:10.1016/j.nxmate.2026.102232 · Cited by 2
NanoBind: Mechanism-Driven Deep Learning of Nanobody–Antigen Molecular Recognition
Zhao, S., Zhu, Y., Li, R., Xu, Z., Han, M., Han, J., Li, Q., Guan, M., Wang, L., Liu, J., et al. (2026) · Research · doi:10.34133/research.1327 · Cited by 1
Boisgard, R., MacFarland, D., Goubard, A., Castellano, R., Chames, P., & Kerfélec, B. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.115129 · Cited by 1
Mestiri, S., Assami, L., Yoosuf, Z. S. K. M., Fernandes, Q., El-Ella, D. M. A., Elsabah, H., Merhi, M., Makni‐Maalej, K., Cherif, H., Dermime, S., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1822508 · Cited by 1
Functional Characteristics Derived from the Structural Design of Bispecific Antibodies
Han, J., Lim, S. Y., Kim, Y., Jeong, D.-H., Kim, H., Ha, S., Park, J., Won, Y., & Lim, K. S. (2026) · Pharmaceuticals · doi:10.3390/ph19081245 · Cited by 1
Engineering Homogeneous Photoactive Antibody Fragments
Bridge, T., & Sachdeva, A. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3251-2_2 · Cited by 1
Functionalized nanobody-based delivery systems for cancer diagnosis and therapeutic applications
Kumar, G. V., Manicum, A.-L. E., Makwikwi, T., Chakafana, G., Agwamba, E. C., & Katerere, D. R. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15518-5.00026-4 · Cited by 1
Construction of Synthetic Probiotic Bacteria for In Situ Delivery of Anti-SARS-CoV-2 Nanobodies
Portero, C. E., Smith, C., Zhou, Y., Marchán-Rivadeneira, M. R., Wu, S., & Han, Y. H. (2025) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-025-10758-1 · Cited by 1
Study review of camelid and shark antibodies for biomedical and biotechnological applications
Alcivar, E. I. M., & Maily, S. (2021) · Bionatura · doi:10.21931/rb/2021.06.04.31 · Cited by 1
McKennan, C. G., Sang, Z., & Shi, Y. (2025) · The Annals of Applied Statistics · doi:10.1214/24-aoas1975 · Cited by 1
Zümrütdal, E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.14.503886 · Cited by 1
A Comprehensive Review on Therapeutic Potential of NanobodiesPreprint
Haddad, F., Dokmak, G., Kanwal, S., & Karaman, R. (2023) · Preprints.org · doi:10.20944/preprints202310.1583.v1 · Cited by 1
Tong, Y., Chen, R., Lu, X., Chen, C., Sun, G.-Q., Yu, X., Lyu, S., Feng, M., Long, Y., Gong, L., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.05.597674 · Cited by 1
Periprosthetic joint infections
van Dijk, B. (2024) · doi:10.33540/2310 · Cited by 1
Mapping the intracellular molecular mechanisms of chemokine signalling within cancer
Keil, G. (2019) · UEA Digital Repository (University of East Anglia)
Zhao, Y., Tong, X., Zhang, C., & Li, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.21.912907
Oral Presentation Full Texts & Abstracts
(2019) · Turkish Journal of Biochemistry · doi:10.1515/tjb-2019-44s206
Smith, C. N., Kihn, K. C., Williamson, Z. A., Chow, K. M., Hersh, L. B., Korotkov, K. V., Deredge, D. J., & Blackburn, J. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.02.311787
Moura Paiva, I. (2020) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3-5141-r867
Tandem Nanobody: a feasible way to improve the capacity of affinity chromatographyPreprint
Fu, J., Huang, Y., Zhong, Y., Shuai, W., Zhang, H., Li, Y., He, Q., & Tu, Z. (2020) · doi:10.22541/au.160690863.36576552/v1
Seeking a Magic Bullet–the search for new Parkinson’s disease therapeutic agents
Gruschus, J. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85707-9.00009-5
The Design and Development of Antibody–Drug Conjugates (ADC s ) for the Treatment of Cancer
Tumey, L. N. (2021) · Burger's Medicinal Chemistry and Drug Discovery · doi:10.1002/0471266949.bmc283
Gibson, R. S., Porter, M. L., & Kimball, A. B. (2021) · International Journal of Women’s Dermatology · doi:10.1016/j.ijwd.2021.07.007
Ban, D., Rice, C., & McCoy, M. A. (2021) · mAbs · doi:10.1080/19420862.2021.1978132
Nassiri, M., Behnam-Rasouli, R., Azghandi, M. V., Gopalan, V., Dolati, P., & Nourmohammadi, R. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.120222
Effects of CD105 Nb68 on Biological Behaviors of CD105 Positive Tumor Cells
(2022) · Journal of Contemporary Medical Practice · doi:10.53469/jcmp.2022.04(03).07
Peptide derived nanobody inhibits entry of SARS-CoV-2 variantsPreprint
Mendon, N., Ganie, R. A., Kesarwani, S., Dileep, D., Sasi, S., Lama, P., Chandra, A., & Sirajuddin, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.21.489021
Kuhn, B. T. (2022) · doi:10.21248/gups.68614
Philipp, M., Müller, L., Andrée, M., Hussnaetter, K. P., Schaal, H., Feldbrügge, M., & Schipper, K. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.11.516239
Innovative strategies to study epigenetic regulation and advance precision medicine
Suris, A., Zhou, Y., & Huang, Y. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-824010-6.00036-8
Application of Nano-Antibodies for Cancer Immunotherapy
Singh, S., Singh, S. P., & Parihar, A. S. (2023) · Current Tissue Microenvironment Reports · doi:10.1007/s43152-023-00044-z
Novel Targeting Carriers in Antibody-Drug Conjugates
Wei, X., & Chen, S. (2023) · Springer eBooks · doi:10.1007/978-981-19-5638-6_7
Ortega, C., Intriago, L. M. R., & Trujillo, L. E. (2023) · Bionatura · doi:10.21931/rb/2023.08.02.13
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review