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Drugging the ‘undruggable’ cancer targets
Open accessAbstract
The term 'undruggable' was coined to describe proteins that could not be targeted pharmacologically. However, progress is being made to 'drug' many of these targets, and therefore more appropriate terms might be 'difficult to drug' or 'yet to be drugged'. Many desirable targets in cancer fall into this category, including the RAS and MYC oncogenes, and pharmacologically targeting these intractable proteins is now a key challenge in cancer research that requires innovation and the development of new technologies. In this Viewpoint article, we asked four scientists working in this field for their opinions on the most crucial advances, as well as the challenges and what the future holds for this important area of research.
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“Transcription factors have remained challenging drug targets due to the absence of druggable active sites (14).”
From Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN (2018) · cites this paper as [14]
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Cites
Vogelstein, B., Papadopoulos, N., Velculescu, V. E., Zhou, S., Diaz, L. A., & Kinzler, K. W. (2013) · Science · doi:10.1126/science.1235122 · Cited by 7,863
The future of immune checkpoint therapy
Sharma, P., & Allison, J. P. (2015) · Science · doi:10.1126/science.aaa8172 · Cited by 4,878
Selective inhibition of BET bromodomains
Filippakopoulos, P., Qi, J., Picaud, S., Shen, Y., Smith, W. B., Fedorov, O., Morse, E. M., Keates, T., Hickman, T. T., Felletar, I., et al. (2010) · Nature · doi:10.1038/nature09504 · Cited by 4,262
Dang, C. V. (2012) · Cell · doi:10.1016/j.cell.2012.03.003 · Cited by 3,390
Self-citationPeptide therapeutics: current status and future directions
Fosgerau, K., & Hoffmann, T. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.10.003 · Cited by 3,160
AR-V7 and Resistance to Enzalutamide and Abiraterone in Prostate Cancer
Antonarakis, E. S., Lu, C., Wang, H., Luber, B., Nakazawa, M., Roeser, J. C., Chen, Y., Mohammad, T. A., Chen, Y., Fedor, H. L., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1315815 · Cited by 2,710
K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions
Ostrem, J. M., Peters, U., Sos, M. L., Wells, J. A., & Shokat, K. M. (2013) · Nature · doi:10.1038/nature12796 · Cited by 2,557
Self-citationDrugging the undruggable RAS: Mission Possible?
Cox, A. D., Fesik, S. W., Kimmelman, A. C., Luo, J., & Der, C. J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4389 · Cited by 1,997
Macropinocytosis of protein is an amino acid supply route in Ras-transformed cells
Commisso, C., Davidson, S. M., Soydaner-Azeloglu, R. G., Parker, S. J., Kamphorst, J. J., Hackett, S., Grabocka, E., Nofal, M., Drebin, J. A., Thompson, C. B., et al. (2013) · Nature · doi:10.1038/nature12138 · Cited by 1,683
Emerging mechanisms of resistance to androgen receptor inhibitors in prostate cancer
Watson, P. A., Arora, V. K., & Sawyers, C. L. (2015) · Nature Reviews Cancer · doi:10.1038/nrc4016 · Cited by 1,536
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Pandur, E., Schenk, P., Kulcsár, G., Gulyás‐Fekete, G., Sipos, K., & Huber, I. (2025) · Cancer Cell International · doi:10.1186/s12935-025-04077-2 · Cited by 2
Liu, X.-Z., Wang, X.-D., & Hu, M.-H. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.109656 · Cited by 2
Chen, X., Gao, Q., Yang, L., Mou, S., Wang, R., & Han, D. (2026) · Nano Letters · doi:10.1021/acs.nanolett.6c00010 · Cited by 2
Mao, Q., Zhai, S., Cao, S., Zhu, R., Xu, W., Zhang, C., Ning, Z., Guo, J., & Duan, H. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6c00253 · Cited by 2
Lu, X., Qin, J., Dong, S., Yuan, Y., Zhang, Z., Zhang, B., Chen, X., Gan, X., Liang, H., & Liu, F. (2026) · Biomarker Research · doi:10.1186/s40364-026-00937-9 · Cited by 3
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Ding, W. (2026) · Advanced Science · doi:10.1002/advs.77125 · Cited by 2
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Joshi, V., Upadhyay, A., Amanullah, A., Mishra, R., & Mishra, A. (2019) · Springer eBooks · doi:10.1007/978-981-13-5877-7_4 · Cited by 2
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Mao, S., Zeng, L., Yang, Y., Liu, Z., & Zhang, L. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1170942 · Cited by 2
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Ma, Y., Liu, N., Shi, Y., Ma, S., Wang, Y., Zheng, W., Sun, R., Song, Y., Chen, M., Qu, L., et al. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111173 · Cited by 2
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Bennett, G. M., Starczewski, J., & Cerna, M. V. C. D. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101767 · Cited by 2
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Valiuska, S., Elder, K. K., McKay, S. J., Ciudad, C. J., Noé, V., & Brooks, T. A. (2024) · Genes · doi:10.3390/genes15101332 · Cited by 2
Hu, Z., & Martí, J. (2024) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2024.109599 · Cited by 2
Song, X., Pan, Z., Zhang, Y., Yang, W., Zhang, T., Wang, H., Chen, Y., Yu, X., Ding, H., Li, R., et al. (2025) · Advanced Science · doi:10.1002/advs.202403851 · Cited by 2
Hoey, R., Sharpe, E., Kukula, A. K., & Workman, P. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.12.015 · Cited by 2
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Oon, M. L., Hoppe, M. M., Shuangyi, F., Phyu, T., Phuong, H. M., Tan, S., Hue, S. S., Wang, S., Poon, L. M., Chan, H. L. E., et al. (2019) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2019.1633629 · Cited by 2
Selective targeting of KRAS-driven lung tumorigenesis via unresolved ER stress
Shimomura, I., Watanabe, N., Yamamoto, T., Kumazaki, M., Tada, Y., Tatsumi, K., Ochiya, T., & Yamamoto, Y. (2021) · JCI Insight · doi:10.1172/jci.insight.137876 · Cited by 2
Kwon, O., Lee, H., Kong, H., Park, J. E., Lee, W., Kang, S., Kim, S., Kim, W., & Cha, H. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/394163 · Cited by 2
Teo, W. S., Holliday, H., Karthikeyan, N., Cazet, A., Roden, D. L., Harvey, K., Konrad, C. V., Murali, R., Varghese, B. A., Archana, P. T., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/497313 · Cited by 2
Váradi, M., Nagy, N. T., Reis, H., Hadaschik, B. A., Niedworok, C., Módos, O., Szendrői, A., Ablat, J., Black, P. C., Keresztes, D., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1757372/v1 · Cited by 2
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Zeng, X., Hu, Y., Xu, Z. P., Wu, X. O., Xiong, Y., & Liu, S. (2023) · Soft Computing · doi:10.1007/s00500-023-08664-1 · Cited by 1
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Madan, B., Harmston, N., Nallan, G., Montoya, A., Faull, P. A., Petretto, E. G., & Virshup, D. M. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/326819 · Cited by 1
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Alabi, C. A., Ghosal, S., Robertus, C. M., Wang, J., Chan, H., Alamgir, A., & Almonte, J. (2024) · Research Square · doi:10.21203/rs.3.rs-3797623/v1 · Cited by 1
Zhang, L., Deng, T., Liufu, Z., Liu, X., Chen, B., Hu, Z., Liu, C., Tracy, M. E., Lu, X., Wen, H., et al. (2024) · eLife · doi:10.7554/elife.99340.2 · Cited by 1
Zhang, L., Deng, T., Liufu, Z., Chen, X., Wu, S., Liu, X., Shi, C., Chen, B., Hu, Z., Cai, Q., et al. (2024) · eLife · doi:10.7554/elife.99341.2 · Cited by 1
PepCCD: A Contrastive Conditioned Diffusion Framework for Target-Specific Peptide GenerationPreprint
Zhang, J., Zhou, Y., Zhu, T., & Zhu, Z. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.01.673427 · Cited by 1
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Hayward, R. E., Berkeley, R. F., Gao, Z., Garhammer, M., Morizono, M. A., Njomen, E., Li, H., DeMeester, K. E., Cociorva, V., Herzik, M. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.20.683548 · Cited by 1
Louet, A. A. B., Hummer, G., & Vendruscolo, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.19.688850 · Cited by 2
Navigating the Cancer Transcriptome by Decoding Divergent Oncogenic States
Amin, S. B., & Verhaak, R. G. W. (2017) · Cell Systems · doi:10.1016/j.cels.2017.08.006
The USP28-ΔNp63 axis is a vulnerability of squamous tumoursPreprint
Prieto‐Garcia, C., Hartmann, O., Reissland, M., Braun, F., Fischer, T., Walz, S., Fischer, A., Calzado, M. A., Orian, A., Rosenfeldt, M. T., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/683508
MYC’xing it up: zebrafish B ALL models provide insight into MYC-driven disease and relapse
da Bandeira, D. S., & Clements, W. K. (2020) · Oncotarget · doi:10.18632/oncotarget.27644
Chemical Probes to Control RNA Function
François‐Moutal, L., Miranda, V. G., Sandino, M., & Khanna, M. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160745-00214
PANCREATIC CANCER, CURRENT THERAPEUTIC APPROACHES AND POSSIBLE PROSPECTS
Bykova, E. A., Falaleeva, N. A., & Grivtsova, L. Y. (2020) · Russian Journal of Biotherapy · doi:10.17650/1726-9784-2020-19-4-18-28
Small-molecule Inhibitors of Myc–Max Interaction and DNA Binding
Fletcher, S., & Prochownik, E. V. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016544-00302
Ma, L., Gong, Q., Chen, Z., Wang, Y., Tan, X., Liu, Y., Wang, Y., Liu, G., Fu, J., Xie, M., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-421070/v1
Zhao, Y., Wang, Y., Chen, W., Bai, S., Wang, P., Zheng, M., Yang, Y., Cheng, B., & Luan, Z. (2021) · Research Square · doi:10.21203/rs.3.rs-907935/v1
Sahm, B. D. B. (2020) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2020.tde-30092020-102358
Faculty Opinions recommendation of How We Think about Targeting RNA with Small Molecules.
Lowe, J. A., III (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737636298.793572902
Metadata
- Authors
- Dang, C. V., Reddy, E. P., Shokat, K. M., & Soucek, L.
- Affiliations
- The Wistar Institute (US)
- Icahn School of Medicine at Mount Sinai (US)
- Howard Hughes Medical Institute (US)
- Institució Catalana de Recerca i Estudis Avançats (ES)
- Corresponding author
- Dang, Chi V.
- Reddy, E. Premkumar
- Shokat, Kevan M.
- Soucek, Laura
- Venue
- Nature Reviews Cancer
- Published
- 2017-06-23
- Volume
- 17
- Issue
- 8
- Pages
- 502-508
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- PMC
- PMC5945194
- OpenAlex
- W2692768525
- Cited by
- 927
- References
- 57
- Citations by year
- 2026: 93 · 2025: 113 · 2024: 125 · 2023: 110 · 2022: 121 · 2021: 121 · 2020: 113 · 2019: 63 · 2018: 58 · 2017: 10
- FWCI
- 6.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute (R01CA057341, R01CA158209, R01CA051497)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Mechanisms and Therapy
- Keywords
- oncogenic Ras, MYC oncogene, oncogene targeting, anticancer drug development
- MeSH terms
- Antineoplastic Agents, Humans, Neoplasms, Receptors, Androgen, Oncogene Proteins, Fusion, Proto-Oncogene Proteins c-myc, NF-kappa B, ras Proteins, Proto-Oncogene Proteins c-myb, Drug Discovery, Molecular Targeted Therapy
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