Exploring the next generation of antibody–drug conjugates

Tsuchikama, Kyoji; Anami, Yasuaki; Ha, Summer Y. Y.; Yamazaki, Chisato M.

doi:10.1038/s41571-023-00850-2

Cited by 660Monoclonal and Polyclonal Antibodies ResearchProtein Degradation and InhibitorsToxin Mechanisms and Immunotoxins

Exploring the next generation of antibody–drug conjugates

Tsuchikama, Kyoji, Anami, Yasuaki, Ha, Summer Y. Y., Yamazaki, Chisato M.·2024·Nature Reviews Clinical Oncology

DOI 10.1038/s41571-023-00850-2

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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.
“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]
To date, 11 antibody-drug conjugates have been FDA-approved for 20 specific indications.
“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]

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Sulfatase-cleavable linkers for antibody-drug conjugates
Bargh, J. D., Walsh, S. J., Isidro‐Llobet, A., Omarjee, S., Carroll, J. S., & Spring, D. R. (2020) · Chemical Science · doi:10.1039/c9sc06410a · Cited by 80 · see citing works
Tandem-Cleavage Linkers Improve the In Vivo Stability and Tolerability of Antibody–Drug Conjugates
Chuprakov, S., Ogunkoya, A. O., Barfield, R. M., Bauzon, M., Hickle, C., Kim, Y. C., Yeo, D., Zhang, F., Rabuka, D., & Drake, P. M. (2021) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.1c00029 · Cited by 80 · see citing works
Highly homogeneous antibody modification through optimisation of the synthesis and conjugation of functionalised dibromopyridazinediones
Bahou, C., Richards, D. A., Maruani, A., Love, E. A., Javaid, F., Caddick, S., Baker, J. R., & Chudasama, V. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob03138f · Cited by 80 · see citing works
Dual-mechanistic antibody-drug conjugate via site-specific selenocysteine/cysteine conjugation
Nilchan, N., Li, X., Pedzisa, L., Nanna, A. R., Roush, W. R., & Rader, C. M. (2019) · Antibody Therapeutics · doi:10.1093/abt/tbz009 · Cited by 80 · see citing works
First-in-Human Phase I Study of Aprutumab Ixadotin, a Fibroblast Growth Factor Receptor 2 Antibody–Drug Conjugate (BAY 1187982) in Patients with Advanced Cancer
Kim, S., Meric‐Bernstam, F., Kalyan, A., Babich, A., Liu, R., Tanigawa, T., Sommer, A., Osada, M., Reetz, F., Laurent, D., et al. (2019) · Targeted Oncology · doi:10.1007/s11523-019-00670-4 · Cited by 77 · see citing works
Praluzatamab Ravtansine, a CD166-Targeting Antibody–Drug Conjugate, in Patients with Advanced Solid Tumors: An Open-Label Phase I/II Trial
Boni, V., Fidler, M. J., Arkenau, H., Spira, A., Meric‐Bernstam, F., Uboha, N., Sanborn, R. E., Sweis, R. F., LoRusso, P. M., Nagasaka, M., et al. (2022) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-3656 · Cited by 76 · see citing works
Regioselective and Stoichiometrically Controlled Conjugation of Photodynamic Sensitizers to a HER2 Targeting Antibody Fragment
Bryden, F., Maruani, A., Savoie, H., Chudasama, V., Smith, M. E. B., Caddick, S., & Boyle, R. W. (2014) · Bioconjugate Chemistry · doi:10.1021/bc5000324 · Cited by 75 · see citing works
Inhibition of Megakaryocyte Differentiation by Antibody–Drug Conjugates (ADCs) is Mediated by Macropinocytosis: Implications for ADC-induced Thrombocytopenia
Zhao, H., Gulesserian, S., Ganesan, S. K., Ou, J. W., Morrison, K. J. M., Zeng, Z., Robles, V., Snyder, J., Do, L., Aviña, H., et al. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0710 · Cited by 73 · see citing works
Site‐Specific Protein Labeling via Sortase‐Mediated Transpeptidation
Antos, J. M., Ingram, J. R., Fang, T., Pishesha, N., Truttmann, M. C., & Ploegh, H. L. (2017) · Current Protocols in Protein Science · doi:10.1002/cpps.38 · Cited by 73 · see citing works
Phase I, First-in-Human Study of the Probody Therapeutic CX-2029 in Adults with Advanced Solid Tumor Malignancies
Johnson, M., El-Khoueiry, A., Hafez, N., Lakhani, N., Mamdani, H., Rodon, J., Sanborn, R. E., Garcia-Corbacho, J., Boni, V., Stroh, M., et al. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-0194 · Cited by 72 · see citing works
Structural insights into the mechanism of action of a biparatopic anti-HER2 antibody
Oganesyan, V., Li, P., Bee, J. S., Li, J., Perry, S. R., Comer, F. I., XU, L. L., Cook, K. E., Senthil, K., Clarke, L., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.818013 · Cited by 72 · see citing works
Optimization of Tubulysin Antibody?Drug Conjugates: A Case Study in Addressing ADC Metabolism
Tumey, L. N., Leverett, C. A., Vetelino, B. C., Li, F., Rago, B., Han, X., Loganzo, F., Musto, S., Bai, G., Sukuru, S. C. K., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00195 · Cited by 71 · see citing works
Synthesis of a heterotrifunctional linker for the site-specific preparation of antibody-drug conjugates with two distinct warheads
Kumar, A., Kinneer, K., Masterson, L. A., Ezeadi, E., Howard, P. W., Wu, H., Gao, C., & Dimasi, N. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.10.043 · Cited by 71 · see citing works
Bispecific antibodies for targeted delivery of anti-cancer therapeutic agents: A review
Beishenaliev, A., Loke, Y. L., Goh, S. J., Geo, H. N., Mugila, M., Misran, M., Chung, L. Y., Kiew, L. V., Roffler, S. R., & Teo, Y. Y. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.05.032 · Cited by 71 · see citing works
Liver Microvascular Injury and Thrombocytopenia of Antibody–Calicheamicin Conjugates in Cynomolgus Monkeys—Mechanism and Monitoring
Guffroy, M., Falahatpisheh, H., Biddle, K. E., Kreeger, J., Obert, L., Walters, K. M., Goldstein, R., Boucher, G., Coskran, T., Reagan, W. J., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-0939 · Cited by 70 · see citing works
Duocarmycin-based antibody–drug conjugates as an emerging biotherapeutic entity for targeted cancer therapy: Pharmaceutical strategy and clinical progress
Yao, H.-P., Zhao, H., Hudson, R., Tong, X.-M., & Wang, M.-H. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.06.012 · Cited by 70 · see citing works
Site-specific targeting of antibody activity in vivo mediated by disease-associated proteases
Erster, O., Thomas, J. M., Hamzah, J., Jabaiah, A. M., Getz, J. A., Schoep, T. D., Hall, S. S., Ruoslahti, E. I., & Daugherty, P. S. (2012) · Journal of Controlled Release · doi:10.1016/j.jconrel.2012.05.035 · Cited by 70 · see citing works
Improved Lysosomal Trafficking Can Modulate the Potency of Antibody Drug Conjugates
DeVay, R. M., Delaria, K., Zhu, G., Holz, C., Foletti, D. L., Sutton, J. E., Bolton, G. L., Dushin, R. G., Bee, C., Pons, J., et al. (2017) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.7b00013 · Cited by 68 · see citing works
Exatecan Antibody Drug Conjugates Based on a Hydrophilic Polysarcosine Drug-Linker Platform
Conilh, L., Fournet, G., Fourmaux, E., Murcia, A., Matera, E., Joseph, B., Dumontet, C., & Viricel, W. (2021) · Pharmaceuticals · doi:10.3390/ph14030247 · Cited by 67 · see citing works
Cellular-Resolution Imaging of Bystander Payload Tissue Penetration from Antibody-Drug Conjugates
Khera, E., Dong, S., Huang, H., de Bever, L., van Delft, F. L., & Thurber, G. M. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0580 · Cited by 67 · see citing works
Characterization of proprotein convertase subtilisin/kexin type 9 (PCSK9) trafficking reveals a novel lysosomal targeting mechanism via amyloid precursor-like protein 2 (APLP2)
DeVay, R. M., Shelton, D. L., & Liang, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.453373 · Cited by 66 · see citing works
Homogeneous antibody-drug conjugates via site-selective disulfide bridging
Forte, N., Chudasama, V., & Baker, J. R. (2018) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2018.09.004 · Cited by 66 · see citing works
Trop‐2 cleavage by ADAM10 is an activator switch for cancer growth and metastasis
Trerotola, M., Guerra, E., Ali, Z., Aloisi, A. L., Ceci, M., Simeone, P., Acciarito, A., Zanna, P. T., Vacca, G., D’Amore, A., et al. (2021) · Neoplasia · doi:10.1016/j.neo.2021.03.006 · Cited by 65 · see citing works
AJICAP Second Generation: Improved Chemical Site-Specific Conjugation Technology for Antibody–Drug Conjugate Production
Fujii, T., Matsuda, Y., Seki, T., Shikida, N., Iwai, Y., Ooba, Y., Takahashi, K., Isokawa, M., Kawaguchi, S., Hatada, N., et al. (2023) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00040 · Cited by 64 · see citing works
460MO Preliminary results from a phase I study using the bispecific, human epidermal growth factor 2 (HER2)-targeting antibody-drug conjugate (ADC) zanidatamab zovodotin (ZW49) in solid cancers
Jhaveri, K. L., Han, H. S., Dotan, E., Oh, D.-Y., Ferrario, C., Tolcher, A. W., Lee, K.-W., Liao, C.-Y. A., Kang, Y.-K., Kim, Y. H., et al. (2022) · Annals of Oncology · doi:10.1016/j.annonc.2022.07.589 · Cited by 61 · see citing works
Phase I/IIa Trial of BMS-986148, an Anti-mesothelin Antibody–drug Conjugate, Alone or in Combination with Nivolumab in Patients with Advanced Solid Tumors
Rottey, S., Clarke, J., Aung, K. L., Machiels, J.-P., Markman, B., Heinhuis, K. M., Millward, M., Lolkema, M. P., Patel, S. P., de Souza, P., et al. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-1181 · Cited by 59 · see citing works
The Role of Toll-like Receptor Agonists and Their Nanomedicines for Tumor Immunotherapy
Huang, L., Ge, X., Liu, Y., Li, H., & Zhang, Z. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14061228 · Cited by 56 · see citing works
Abstract P6-17-13: ZW49, a HER2 targeted biparatopic antibody drug conjugate for the treatment of HER2 expressing cancers
Hamblett, K., Barnscher, S. D., Davies, R., Hammond, P., Hernandez, A., Wickman, G., Fung, V., Ding, T., Garnett, G. A. E., Galey, A., et al. (2019) · Cancer Research · doi:10.1158/1538-7445.sabcs18-p6-17-13 · Cited by 53 · see citing works
Generating tumor-selective conditionally active biologic anti-CTLA4 antibodies via protein-associated chemical switches
Chang, H. W., Frey, G., Liu, H., Xing, C., Steinman, L., Boyle, W. J., & Short, J. M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2020606118 · Cited by 52 · see citing works
Design and Characterization of Immune-Stimulating Imidazo[4,5-c]quinoline Antibody-Drug Conjugates
Fang, S., Brems, B. M., Olawode, E. O., Miller, J. T. G., Brooks, T. A., & Tumey, L. N. (2022) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.2c00392 · Cited by 52 · see citing works
A phase 1/2 study of a first-in-human immune-stimulating antibody conjugate (ISAC) BDC-1001 in patients with advanced HER2-expressing solid tumors.
Li, B. T., Pegram, M. D., Lee, K., Sharma, M. R., Lee, J., Spira, A. I., Hanna, G. J., Kang, Y., Rasco, D. W., Moore, K. N., et al. (2023) · Journal of Clinical Oncology · doi:10.1200/jco.2023.41.16_suppl.2538 · Cited by 52 · see citing works
A Biparatopic Antibody–Drug Conjugate to Treat MET-Expressing Cancers, Including Those that Are Unresponsive to MET Pathway Blockade
DaSilva, J. O., Yang, K., Surriga, O., Nittoli, T., Kunz, A., Franklin, M. C., Delfino, F. J., Mao, S., Zhao, F. H., Giurleo, J. T., et al. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0009 · Cited by 51 · see citing works
An Enzymatically Cleavable Tripeptide Linker for Maximizing the Therapeutic Index of Antibody–Drug Conjugates
Ha, S. Y. Y., Anami, Y., Yamazaki, C. M., Xiong, W., Haase, C. M., Olson, S. D., Lee, J., Ueno, N. T., Zhang, N., An, Z., et al. (2022) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-22-0362 · Cited by 50 · see citing works
Self-citation
Imaging a functional tumorigenic biomarker in the transformed epithelium
LeBeau, A. M., Lee, M., Murphy, S. T., Hann, B. C., Warren, R. S., Santos, R. D., Kurhanewicz, J. V., Hanash, S., VanBrocklin, H. F., & Craik, C. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218694110 · Cited by 48 · see citing works
Enzyme-Agnostic Lysosomal Screen Identifies New Legumain-Cleavable ADC Linkers
Miller, J. T. G., Vitro, C. N., Fang, S., Benjamin, S. R., & Tumey, L. N. (2021) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.1c00124 · Cited by 48 · see citing works
Sortase A‐Generated Highly Potent Anti‐CD20‐MMAE Conjugates for Efficient Elimination of B‐Lineage Lymphomas
Pan, L., Zhao, W., Lai, J., Ding, D., Zhang, Q. Y., Yang, X., Huang, M., Jin, S., Xu, Y., Zeng, S., et al. (2016) · Small · doi:10.1002/smll.201602267 · Cited by 46 · see citing works
Characterization of Antibody Products Obtained through Enzymatic and Nonenzymatic Glycosylation Reactions with a Glycan Oxazoline and Preparation of a Homogeneous Antibody–Drug Conjugate via Fc N -Glycan
Manabe, S., Yamaguchi, Y., Matsumoto, K., Fuchigami, H., Kawase, T., Hirose, K., Mitani, A., Sumiyoshi, W., Kinoshita, T., Abe, J., et al. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00132 · Cited by 45 · see citing works
Trial watch: Toll-like receptor ligands in cancer therapy
Naour, J. L., & Kroemer, G. (2023) · OncoImmunology · doi:10.1080/2162402x.2023.2180237 · Cited by 45 · see citing works
Recent advances in the search of BCRP- and dual P-gp/BCRP-based multidrug resistance modulators
Dei, S., Braconi, L., Romanelli, M. N., & Teodori, E. (2019) · Cancer Drug Resistance · doi:10.20517/cdr.2019.31 · Cited by 44 · see citing works
Exploiting protease activation for therapy
Bleuez, C., Koch, W. F., Urbach, C., Hollfelder, F., & Jermutus, L. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.03.011 · Cited by 43 · see citing works
Bispecifics and antibody–drug conjugates: A positive synergy
Maruani, A. (2018) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2018.09.003 · Cited by 42 · see citing works
A Biparatopic Antibody That Modulates MET Trafficking Exhibits Enhanced Efficacy Compared with Parental Antibodies in MET-Driven Tumor Models
DaSilva, J. O., Yang, K., Bay, A. E. P., Andreev, J., Ngoi, P., Pyles, E. A., Franklin, M. C., Dudgeon, D., Rafique, A., Dore, A. T., et al. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-19-2428 · Cited by 42 · see citing works
Enfortumab Vedotin in urothelial cancer
Alt, M., Stecca, C., Tobin, S., Jiang, D., & Sridhar, S. S. (2020) · Therapeutic Advances in Urology · doi:10.1177/1756287220980192 · Cited by 42 · see citing works
Nonclinical Efficacy and Safety of CX-2029, an Anti-CD71 Probody–Drug Conjugate
Singh, S., Serwer, L., DuPage, A., Elkins, K., Chauhan, N., Ravn, M., Buchanan, F., Wang, L., Krimm, M., Wong, K., et al. (2022) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0193 · Cited by 41 · see citing works
Targeted Activation of Toll-Like Receptors: Conjugation of a Toll-Like Receptor 7 Agonist to a Monoclonal Antibody Maintains Antigen Binding and Specificity
Gadd, A., Greco, F., Cobb, A. J. A., & Edwards, A. D. (2015) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.5b00302 · Cited by 40 · see citing works
The tumor targeting performance of anti-CD166 Probody drug conjugate CX-2009 and its parental derivatives as monitored by 89Zr-immuno-PET in xenograft bearing mice
Chomet, M., Schreurs, M., Nguyen, M. T. L., Howng, B., Villanueva, R., Krimm, M., Vasiljeva, O. S., van Dongen, G. A. M. S., & Vugts, D. J. (2020) · Theranostics · doi:10.7150/thno.44334 · Cited by 38 · see citing works
Substrate Design Enables Heterobifunctional, Dual “Click” Antibody Modification via Microbial Transglutaminase
Walker, J. A., Bohn, J. J., Ledesma, F., Sorkin, M. R., Kabaria, S. R., Thornlow, D. N., & Alabi, C. A. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00522 · Cited by 36 · see citing works
Targeting BET Bromodomains in Cancer
Trojer, P. (2022) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-070120-103531 · Cited by 36 · see citing works
Amyloid Precursor-Like Protein 2 Increases the Endocytosis, Instability, and Turnover of the H2-Kd MHC Class I Molecule
Tuli, A., Sharma, M., McIlhaney, M. M., Talmadge, J. E., Naslavsky, N., Caplan, S., & Solheim, J. C. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.3.1978 · Cited by 34 · see citing works
An in Vitro Assay Using Cultured Kupffer Cells Can Predict the Impact of Drug Conjugation on in Vivo Antibody Pharmacokinetics
Meyer, D. W., Bou, L., Shum, S., Jonas, M., Anderson, M. E., Hamilton, J. Z., Hunter, J. H., Wo, S., Wong, A., Okeley, N. M., et al. (2020) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.9b00991 · Cited by 33 · see citing works
In Vitro Cytotoxicity Study of Cyclophosphamide, Etoposide and Paclitaxel on Monocyte Macrophage Cell Line Raw 264.7
Yadav, A., Mandal, M. K., & Dubey, K. K. (2020) · Indian Journal of Microbiology · doi:10.1007/s12088-020-00896-1 · Cited by 33 · see citing works
Compact hydrophilic electrophiles enable highly efficacious high DAR ADCs with excellent in vivo PK profile
Ochtrop, P., Jahzerah, J., Machui, P., Mai, I., Schumacher, D., Helma, J., Kasper, M., & Hackenberger, C. P. R. (2023) · Chemical Science · doi:10.1039/d2sc05678j · Cited by 33 · see citing works

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Advance in peptide-based drug development: delivery platforms, therapeutics and vaccines
Xiao, W., Jiang, W., Chen, Z., Huang, Y., Mao, J., Zheng, W., Hu, Y., & Shi, J. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02107-5 · Cited by 449 · see citing works
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 317 · see citing works
Extracellular vesicle-based drug overview: research landscape, quality control and nonclinical evaluation strategies
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 279 · see citing works
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 271 · see citing works
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 · see citing works
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 240 · see citing works
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 · see citing works
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 110 · see citing works
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 109 · see citing works
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 · see citing works
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 92 · see citing works
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 96 · see citing works
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 · see citing works
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 91 · see citing works
Glioblastoma in adults: A Society for Neuro-Oncology (SNO) and European Society of Neuro-Oncology (EANO) consensus review on current management and future directions
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 95 · see citing works
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 · see citing works
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 85 · see citing works
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 85 · see citing works
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 · see citing works
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 · see citing works
Sacituzumab tirumotecan in advanced non-small-cell lung cancer with or without EGFR mutations: phase 1/2 and phase 2 trials
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 61 · see citing works
A pivotal decade for bispecific antibodies?
Surowka, M., & Klein, C. (2024) · mAbs · doi:10.1080/19420862.2024.2321635 · Cited by 64 · see citing works
Antibody–drug conjugates in cancer therapy: mechanisms and clinical studies
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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
ORCID: Tsuchikama, Kyoji
Anami, Yasuaki
Ha, Summer Y. Y.
Yamazaki, Chisato M.
Venue: Nature Reviews Clinical Oncology
Publisher: Springer Science and Business Media LLC
Published: 2024-01-08
Volume: 21
Issue: 3
Pages: 203-223
ISSN: 1759-4774 (ISSN-L)
1759-4782
DOI: 10.1038/s41571-023-00850-2
OpenAlex: W4390673654
Cited by: 659
References: 248
Citations by year: 2026: 282 · 2025: 270 · 2024: 106 · 2023: 1
FWCI: 42.66
Type: journal article
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Nature Reviews Clinical Oncology (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Defense (W81XWH1910598, W81XWH)
National Institutes of Health (W81XWH)
Topics: Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › 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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Exploring the next generation of antibody–drug conjugates

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