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Exploring the next generation of antibody–drug conjugates
Abstract
Antibody-drug conjugates (ADCs) are a promising cancer treatment modality that enables the selective delivery of highly cytotoxic payloads to tumours. However, realizing the full potential of this platform necessitates innovative molecular designs to tackle several clinical challenges such as drug resistance, tumour heterogeneity and treatment-related adverse effects. Several emerging ADC formats exist, including bispecific ADCs, conditionally active ADCs (also known as probody-drug conjugates), immune-stimulating ADCs, protein-degrader ADCs and dual-drug ADCs, and each offers unique capabilities for tackling these various challenges. For example, probody-drug conjugates can enhance tumour specificity, whereas bispecific ADCs and dual-drug ADCs can address resistance and heterogeneity with enhanced activity. The incorporation of immune-stimulating and protein-degrader ADCs, which have distinct mechanisms of action, into existing treatment strategies could enable multimodal cancer treatment. Despite the promising outlook, the importance of patient stratification and biomarker identification cannot be overstated for these emerging ADCs, as these factors are crucial to identify patients who are most likely to derive benefit. As we continue to deepen our understanding of tumour biology and refine ADC design, we will edge closer to developing truly effective and safe ADCs for patients with treatment-refractory cancers. In this Review, we highlight advances in each ADC component (the monoclonal antibody, payload, linker and conjugation chemistry) and provide more-detailed discussions on selected examples of emerging novel ADCs of each format, enabled by engineering of one or more of these components.
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“Thirteen FDA-approved ADCs are currently on the market, with over 200 ADCs in various stages of clinical development (Table 1)6,8,9.”
From The evolving landscape of antibody-drug conjugates (ADCs) for treatment of prostate cancer (2025) · cites this paper as [8]
In the citing paper
“To date, 11 ADCs have been Food and Drug Administration (FDA)-approved for 20 specific indications”
From Current and emerging concepts for systemic treatment of metastatic colorectal cancer (2025) · cites this paper as [59]
Citations
Cites
Tumour heterogeneity and resistance to cancer therapies
Dagogo-Jack, I., & Shaw, A. T. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2017.166 · Cited by 3,846
PROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395
Strategies and challenges for the next generation of antibody–drug conjugates
Beck, A., Goetsch, L., Dumontet, C., & Corvaïa, N. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.268 · Cited by 2,271
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
STING-Dependent Cytosolic DNA Sensing Mediates Innate Immune Recognition of Immunogenic Tumors
Woo, S.-R., Fuertes, M. B., Corrales, L., Spranger, S., Furdyna, M. J., Leung, M. Y. K., Duggan, R., Wang, Y., Barber, G. N., Fitzgerald, K. A., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.10.017 · Cited by 1,917
Prodrugs: design and clinical applications
Rautio, J., Kumpulainen, H., Heimbach, T., Oliyai, R., Oh, D.-M., Järvinen, T., & Savolainen, J. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2468 · Cited by 1,681
Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index
Junutula, J. R., Raab, H. E., Clark, S., Bhakta, S., Leipold, D. D., Weir, S., Chen, Y., Simpson, M., Tsai, S. P., Dennis, M. S., et al. (2008) · Nature Biotechnology · doi:10.1038/nbt.1480 · Cited by 1,388
Anti-PD-1 and Anti-CTLA-4 Therapies in Cancer: Mechanisms of Action, Efficacy, and Limitations
Seidel, J. A., Otsuka, A., & Kabashima, K. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00086 · Cited by 1,360
Ogitani, Y., Aida, T., Hagihara, K., Yamaguchi, J., Ishii, C., Harada, N., Soma, M., Okamoto, H., Oitate, M., Arakawa, S., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-2822 · Cited by 1,228
Unlocking the potential of antibody–drug conjugates for cancer therapy
Drago, J. Z., Modi, S., & Chandarlapaty, S. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-021-00470-8 · Cited by 1,209
Research works printed but not linked: 1
- CytomX Therapeutics Inc. CytomX therapeutics presents overview of conditionally-activated antibody-drug conjugate (ADC) programs including next generation EpCAM-targeting CX-2051. CytomX Press Release Details https://ir.cytomx.com/news-releases/news-release-details/cytomx-therapeutics-presents-overview-conditionally-activated/ (2022).
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Antibody–Drug Conjugates (ADCs): current and future biopharmaceuticals
Wang, R., Hu, B., Pan, Z., Mo, C., Zhao, X., Liu, G., Hou, P., Cui, Q., Zhao, X., Wang, W., et al. (2025) · Journal of Hematology & Oncology · doi:10.1186/s13045-025-01704-3 · Cited by 331
Xu, G., Jin, J., Fu, Z., Wang, G., Lei, X., Xu, J., & Wang, J. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02312-w · Cited by 320
Cancer therapy with antibodies
Paul, S., Konig, M. F., Pardoll, D. M., Bettegowda, C., Papadopoulos, N., Wright, K. M., Gabelli, S. B., Ho, M., van Elsas, A., & Zhou, S. (2024) · Nature reviews. Cancer · doi:10.1038/s41568-024-00690-x · Cited by 292
The Journey of Antibody–Drug Conjugates: Lessons Learned from 40 Years of Development
Colombo, R., Tarantino, P., Rich, J. R., LoRusso, P. M., & de Vries, E. G. E. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-0708 · Cited by 254
Targeted protein degradation for cancer therapy
Hinterndorfer, M., Spiteri, V. A., Ciulli, A., & Winter, G. E. (2025) · Nature reviews. Cancer · doi:10.1038/s41568-025-00817-8 · Cited by 263
Advances in molecular pathology and therapy of non-small cell lung cancer
Huang, Q., Li, Y., Huang, Y., Wu, J., Bao, W., Xue, C., Li, X., Dong, S., Dong, Z., & Hu, S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02243-6 · Cited by 197
Next-generation combination approaches for immune checkpoint therapy
Goswami, S., Pauken, K. E., Wang, L., & Sharma, P. (2024) · Nature Immunology · doi:10.1038/s41590-024-02015-4 · Cited by 114
Antibody–drug conjugates in cancer therapy: current landscape, challenges, and future directions
Chen, B., Zheng, X., Wu, J., Chen, G., Yu, J. Q., Xu, Y. X., Wu, W. K. K., Tse, G. M.-K., To, K. F., & Kang, W. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02489-2 · Cited by 121
Synthetic Biology in Natural Product Biosynthesis
Seshadri, K., Abad, A. N. D., Nagasawa, K. K., Yost, K. M., Johnson, C. W., Dror, M. J., & Tang, Y. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00567 · Cited by 94
Resistance to antibody–drug conjugates: A review
Li, S., Zhao, X., Fu, K., Zhu, S., Pan, C., Yang, C., Wang, F., To, K. K. W., & Fu, L. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.12.036 · Cited by 100
Tumour and microenvironment crosstalk in NSCLC progression and response to therapy
Rahal, Z., Darzi, R. E., Moghaddam, S. J., Cascone, T., & Kadara, H. N. (2025) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-025-01021-1 · Cited by 105
Trop2-targeted therapies in solid tumors: advances and future directions
Liu, X., Ma, L., Li, J., Sun, L., Yang, Y., Liu, T., Xing, D., Yan, S., & Zhang, M. (2024) · Theranostics · doi:10.7150/thno.98178 · Cited by 89
The next generation of immunotherapies for lung cancers
Zhao, S., Zhao, H., Yang, W., & Zhang, L. (2025) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-025-01035-9 · Cited by 96
Wen, P. Y., Weller, M., Lee, E. Q., Touat, M., Khasraw, M., Rahman, R. M., Platten, M., Lim, M. K., Winkler, F., Horbinski, C., et al. (2025) · Neuro-Oncology · doi:10.1093/neuonc/noaf177 · Cited by 113
From cell-SELEX to tissue-SELEX for targeted drug delivery and aptamer nanomedicine
Wong, K., Wong, M., Lee, J. H., & Liu, J. (2025) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2025.115646 · Cited by 82
Digestive cancers: mechanisms, therapeutics and management
Zhan, T., Betge, J., Schulte, N., Dreikhausen, L., Hirth, M., Li, M., Weidner, P., Leipertz, A., Teufel, A., & Ebert, M. P. A. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02097-4 · Cited by 90
Unveiling the molecular and immunological drivers of antibody–drug conjugates in cancer treatment
Zippelius, A., Tolaney, S. M., Tarantino, P., Balthasar, J. P., & Thurber, G. M. (2025) · Nature reviews. Cancer · doi:10.1038/s41568-025-00869-w · Cited by 87
Linker Design for the Antibody Drug Conjugates: A Comprehensive Review
Lei, Y., Zheng, M., Chen, P., Chen, P., Loh, T., & Liu, H. (2025) · ChemMedChem · doi:10.1002/cmdc.202500262 · Cited by 69
Receptor-ligand interactions for optimized endocytosis in targeted therapies
Sung, Y., Choi, Y., Kim, E. S., Ryu, J. H., & Kwon, I. C. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.01.060 · Cited by 64
Zhao, S., Cheng, Y., Wang, Q. J., Li, X., Liao, J., Rodon, J. A., Meng, X., Luo, Y., Chen, Z., Wang, W., et al. (2025) · Nature Medicine · doi:10.1038/s41591-025-03638-2 · Cited by 67
A pivotal decade for bispecific antibodies?
Surowka, M., & Klein, C. (2024) · mAbs · doi:10.1080/19420862.2024.2321635 · Cited by 64
Antibody–drug conjugates in cancer therapy: mechanisms and clinical studies
He, J., Zeng, X., Wang, C., Wang, E., & Li, Y. (2024) · MedComm · doi:10.1002/mco2.671 · Cited by 60
Antibody-Drug Conjugates: A promising breakthrough in cancer therapy
Parit, S., Manchare, A., Gholap, A. D., Mundhe, P., Hatvate, N. T., Rojekar, S. V., & Patravale, V. B. (2024) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.124211 · Cited by 59
Antibody–drug conjugates: prospects for the next generation
Grairi, M., & Borgne, M. L. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104241 · Cited by 61
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Primac, I., Tabury, K., Tasdogan, A., Baatout, S., & Herrmann, K. (2025) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-025-01069-z · Cited by 63
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Hu, Y., Zhu, Y., Qi, D., Tang, C., & Zhang, W. (2024) · Biomarker Research · doi:10.1186/s40364-024-00633-6 · Cited by 54
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Reck, M., Frost, N., Peters, S., Fox, B. A., Ferrara, R., Savai, R., & Barlési, F. (2025) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-025-01061-7 · Cited by 62
Antibody-drug conjugates in cancer therapy: applications and future advances
Long, R., Zuo, H., Tang, G., Zhang, C., Yue, X., Yang, J., Luo, X., Deng, Y., Qiu, J.-Y., Li, J., et al. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1516419 · Cited by 56
Dong, Y., Zhang, Z., Luan, S., Zheng, M., Wang, Z., Chen, Y., Chen, X., Tong, A., & Yang, H. (2024) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2024-009710 · Cited by 49
Antibody-drug conjugates for targeted cancer therapy: Recent advances in potential payloads
Xi, M., Zhu, J., Zhang, F., Shen, H., Chen, J., Xiao, Z., Huangfu, Y., Wu, C., Sun, H., & Xia, G. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116709 · Cited by 47
Dual-payload antibody–drug conjugates: Taking a dual shot
Tao, J., Gu, Y., Zhou, W., & Wang, Y. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116995 · Cited by 47
Zhou, K., Liu, X., & Zhu, H. (2025) · Journal of Hematology & Oncology · doi:10.1186/s13045-025-01752-9 · Cited by 52
Technological advancements in antibody-based therapeutics for treatment of diseases
Lu, R., Chiang, H.-L., Yuan, J. P., Wang, H.-H., Chen, C.-Y., Panda, S. S., Liang, K.-H., Peng, H., Ko, S.-H., Hsu, H.-J., et al. (2025) · Journal of Biomedical Science · doi:10.1186/s12929-025-01190-2 · Cited by 59
Engineered multi-domain lipid nanoparticles for targeted delivery
Liu, Z., Chen, J., Xu, M., Ho, S., Wei, Y., Ho, H., & Yong, K. (2025) · Chemical Society Reviews · doi:10.1039/d4cs00891j · Cited by 63
Homogeneous antibody-drug conjugates with dual payloads: potential, methods and considerations
Wen, M., Yu, A., Park, Y. J., Calarese, D. A., Gerber, H. P., & Yin, G. (2025) · mAbs · doi:10.1080/19420862.2025.2498162 · Cited by 42
Targeted protein degradation in the transmembrane and extracellular space
Zhu, R., Zhang, H., & Chen, P. R. (2025) · Science · doi:10.1126/science.adx5094 · Cited by 43
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Shimozaki, K., Fukuoka, S., Ooki, A., & Yamaguchi, K. (2024) · ESMO Open · doi:10.1016/j.esmoop.2024.103679 · Cited by 43
Applications of cell penetrating peptide-based drug delivery system in immunotherapy
Du, J., Zhang, R., Jiang, S., Xiao, S., Liu, Y., Niu, Y., Zhao, W.-X., Wang, D., & Ma, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1540192 · Cited by 42
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Steup, C., Kennel, K. B., Neurath, M. F., Fichtner-Feigl, S., & Greten, F. R. (2025) · Gut · doi:10.1136/gutjnl-2025-335412 · Cited by 39
Single-Domain Antibodies as Antibody–Drug Conjugates: From Promise to Practice—A Systematic Review
Pérez, V. M. M., Baselga, M., & Schuhmacher, A. J. (2024) · Cancers · doi:10.3390/cancers16152681 · Cited by 43
Mao, K., Chen, P., Sun, H., Zhong, S., Zheng, H., & Xu, L. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1425617 · Cited by 38
Engineered Proteins and Chemical Tools to Probe the Cell Surface Proteome
Leung, K., Schaefer, K., Lin, Z., Yao, Z. W., & Wells, J. A. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00554 · Cited by 44
Zhang, J., Liu, R., Wang, S., Feng, Z. C., Yang, H., Gao, S., Li, X., Yao, X., Chen, J., Gong, Z., et al. (2025) · Annals of Oncology · doi:10.1016/j.annonc.2025.04.009 · Cited by 37
Lu, Y., Huang, W., Li, Y., Xu, Y., Wei, Q., Sha, C., & Guo, P. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-01159-2 · Cited by 44
Tong, Y., Fan, X., Liu, H., & Liang, T. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1495675 · Cited by 36
Valle, I., Grinda, T., Antonuzzo, L., & Pistilli, B. (2025) · npj Breast Cancer · doi:10.1038/s41523-025-00829-5 · Cited by 43
Tang, S., Wynn, C., Le, T., McCandless, M. G., Zhang, Y., Patel, R., Maihle, N. J., & Hillegass, W. B. (2024) · Cancer and Metastasis Reviews · doi:10.1007/s10555-024-10231-5 · Cited by 40
Dernbach, G., Eich, M., Dragomir, M. P., Anders, P., Jurczok, N., Stief, C. G., Jurmeister, P. S., Schlomm, T., Klauschen, F., Horst, D. A., et al. (2025) · Modern Pathology · doi:10.1016/j.modpat.2025.100753 · Cited by 35
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Mundhara, N., & Sadhukhan, P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168899 · Cited by 37
Precision-engineered PROTACs minimize off-tissue effects in cancer therapy
Shi, J., Wang, L., Zeng, X., Xie, C., Meng, Z., Campbell, A., Wang, L., Fan, H., & Sun, H. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1505255 · Cited by 35
Recent Advances in Peptide Linkers for Antibody-Drug Conjugates
Li, S., Guo, Y., Che, J., Dai, H., & Dong, X. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01982 · Cited by 35
Understanding the Toxicity Profile of Approved ADCs
Martinez, P. B., de Sá, A. L., Díaz‐Tejeiro, C., Paniagua‐Herranz, L., Sanvicente, A., López-Cade, I., Pérez‐Segura, P., Alonso‐Moreno, C., Nieto‐Jiménez, C., & Ocaña, A. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17020258 · Cited by 34
Evolving roles of MET as a therapeutic target in NSCLC and beyond
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Emerging paradigms and recent progress in targeting ErbB in cancers
Stoup, N., Liberelle, M., Lebègue, N., & SEUNINGEN, I. V. (2024) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2024.04.009 · Cited by 33
RNA modifications in the tumor microenvironment: insights into the cancer-immunity cycle and beyond
Ding, Y.-P., Liu, C., & Yu, K. (2025) · Experimental Hematology and Oncology · doi:10.1186/s40164-025-00648-1 · Cited by 34
Poudel, Y. B., Thakore, R. R., & Chekler, E. P. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01289 · Cited by 29
Galloylated liposomes enable targeted drug delivery by overcoming protein corona shielding
Li, J., Yu, J., Song, J. T., Zhang, Y., Li, N., Wang, Z., Qin, M., Zhao, M., Zhang, B., Huang, R., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63198-4 · Cited by 33
Tardito, S., Matis, S., Zocchi, M. R., Benelli, R., & Poggi, A. D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137131 · Cited by 30
Nadal‐Bufí, F., Salomon, P. L., Moliner, F. D., Sarris, K., Wang, Z., Wills, R. D., Marin, V. L., Shi, X., Zhou, K., Wang, Z., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c16842 · Cited by 28
Lv, Y., Cui, X., Li, T., Liu, C., Wang, A., Wang, T., Zhou, X., Li, R., Zhang, F., Hu, Y., et al. (2025) · Clinical and Experimental Medicine · doi:10.1007/s10238-025-01655-6 · Cited by 29
Lin, J., Chen, Z., Zhang, D., Zhang, N., Chen, H., & Guo, D. (2025) · Macromolecular Rapid Communications · doi:10.1002/marc.202401051 · Cited by 28
Cheng, H., Yang, C., Wang, J., Liu, H., Zhang, K., Wu, R., Li, J., Fang, Y., Hu, R., Jeong, H., et al. (2025) · Chem · doi:10.1016/j.chempr.2025.102624 · Cited by 29
Chemical diversity of reagents that modify RNA 2′-OH in water: a review
Shioi, R., & Kool, E. T. (2024) · Chemical Science · doi:10.1039/d4sc05317f · Cited by 25
Programmable Circular Multispecific Aptamer-Drug Engager to Broadly Boost Antitumor Immunity
Chen, J., Chi, H., Wang, C., Du, Y., Wang, Y., Yang, S., Jiang, S., Lv, X., He, J., Chen, J., et al. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c06189 · Cited by 25
Cheng, Y., Lü, J., Zhang, C., Yan, W., Zhu, P., Qin, Q., & Gong, L. (2025) · Antibody Therapeutics · doi:10.1093/abt/tbaf004 · Cited by 25
Shi, X., Tang, K., Zhang, Q., Han, Q., Quan, L., Li, Y., Cui, J., Feng, N., Gong, J., Shang, B., et al. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1556245 · Cited by 24
Dong, S., Li, X., Huang, Q., Li, Y., Li, J., Zhu, X., Xue, C., Chen, R., Zeng, Y., Wu, J., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101215 · Cited by 25
Tumor-Agnostic Therapies in Practice: Challenges, Innovations, and Future Perspectives
Wu, S., & Thawani, R. (2025) · Cancers · doi:10.3390/cancers17050801 · Cited by 26
Leung, Y., Llauradó, M., Cameron, A., Da-Anoy, A., Cook, L. S., Hoenisch, J., Ghesquiere, C., Gaillard, S. L., Schmid, J., Dawson, A., et al. (2025) · Journal of Gynecologic Oncology · doi:10.3802/jgo.2025.36.e74 · Cited by 24
Xu, X., Yu, T., & Wang, Z. (2025) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2025.103012 · Cited by 23
Antibody-drug conjugates: Current challenges and innovative solutions for precision cancer therapy
Zhou, X., Han, Y., Fang, Y., Ma, P., Zhou, J., Jiang, Y., Xing, S., Tang, Q., Hou, Y., Wang, S., et al. (2025) · Med · doi:10.1016/j.medj.2025.100849 · Cited by 26
Hong, J., Li, K., He, J., & Liang, M. (2024) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.4c00254 · Cited by 23
Therapeutic potential of cis-targeting bispecific antibodies
Oslund, R., Holland, P. M., Lesley, S. A., & Fadeyi, O. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.07.004 · Cited by 23
Aliaga, P. T., Spitaleri, G., Attili, I., Corvaja, C., Battaiotto, E., Angelopoulos, P. A., Signore, E. D., Passaro, A., & de Marinis, F. (2025) · Molecules · doi:10.3390/molecules30122645 · Cited by 22
Antibody-drug conjugates as multimodal therapies against hard-to-treat cancers
Armstrong, G. B., Graham, H., Cheung, A., Montaseri, H., Burley, G. A., Karagiannis, S. N., & Rattray, Z. (2025) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2025.115648 · Cited by 23
How multispecific molecules are transforming pharmacotherapy
Deshaies, R. J. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01262-w · Cited by 25
Shapiro, M. A. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1379738 · Cited by 22
Zhang, L., Yan, Y., Gao, Y., Chen, Y., Yu, J., Ren, N., & Sun, L. (2024) · Scientific Reports · doi:10.1038/s41598-024-68311-z · Cited by 27
Zhang, B., Zhang, Z., Gao, J., Lu, S., Pang, R., Li, D., Huang, X., Qin, N., Liu, L., & Wang, Z. (2024) · iScience · doi:10.1016/j.isci.2024.111536 · Cited by 24
Programmable protein ligation on cell surfaces
Kofoed, C., Erkalo, G., Tay, N. E. S., Ye, X., Lin, Y., & Muir, T. W. (2025) · Nature · doi:10.1038/s41586-025-09287-2 · Cited by 27
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Evers, A., Guarnera, E., Pekar, L., & Zielonka, S. (2025) · mAbs · doi:10.1080/19420862.2025.2583210 · Cited by 23
The evolving landscape of antibody-drug conjugates (ADCs) for treatment of prostate cancer
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Self-citationKrueger, J. I., Dieskau, A. P., Hassfeld, J., Gries, J., Block, O., Weinmann, H., Kaufmann, D., Hildbrand, S., Kraft, V., Moeckel, R., et al. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202420719 · Cited by 18
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177Lu-Labeled Antibody–Drug Conjugate: A Dual-Mechanistic Treatment Modality in Solid Tumors
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Self-citationRecent developments in bioconjugation: From strategies to design and clinical applications
Samieipour, F., Dianat‐Moghadam, H., & Khanahmad, H. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118593 · Cited by 20
Metadata
- Authors
- Tsuchikama, K., Anami, Y., Ha, S. Y. Y., & Yamazaki, C. M.
- Affiliations
- Brown Foundation Institute of Molecular Medicine for the Prevention of Human Diseases (US)
- Corresponding author
- Tsuchikama, Kyoji
- Venue
- Nature Reviews Clinical Oncology
- Published
- 2024-01-08
- Volume
- 21
- Issue
- 3
- Pages
- 203-223
- ISSN
- 1759-4774 (ISSN-L)
- 1759-4782
- OpenAlex
- W4390673654
- Cited by
- 659
- References
- 248
- Citations by year
- 2026: 282 · 2025: 270 · 2024: 106
- FWCI
- 42.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Nature Reviews Clinical Oncology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Defense (W81XWH1910598, W81XWH)
- National Institutes of Health (W81XWH)
- 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 › Toxin Mechanisms and Immunotoxins
- Keywords
- antibody-drug conjugates, drug resistance, tumor heterogeneity, linker chemistry, chemical conjugation, payload design, patient stratification, biomarkers, treatment-refractory cancer, multimodal cancer therapy
- MeSH terms
- Antibodies, Monoclonal, Antineoplastic Agents, Pharmaceutical Preparations, Humans, Neoplasms, Immunoconjugates
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